Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Dry Status Log - Date: 21:25, 10 September 2007 (UTC)
[edit]Redirected Proteins (33)
[edit]Protein Status Log - Date: 21:25, 10 September 2007 (UTC)
[edit]Skipped: Tag Parsing Error (23)
[edit]Updated Existing Page (10)
[edit]Condensed Log - Date: 21:25, 10 September 2007 (UTC)
[edit]Updated Protein Pages (10)
[edit]Skipped Proteins (23)
[edit]Redirected Proteins (33)
[edit]Vebose Log - Date: 21:25, 10 September 2007 (UTC)
[edit]AKT1
- REDIRECT: Protein Redirected to: AKT1 {September 10, 2007 2:09:35 PM PDT}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {September 10, 2007 2:09:37 PM PDT}
- UPDATE SUMMARY: Updating Summary, No Errors. {September 10, 2007 2:09:37 PM PDT}
- UPDATE CITATIONS: Updating Citations, No Errors. {September 10, 2007 2:09:37 PM PDT}
- UPDATED: Updated protein page: AKT1 {September 10, 2007 2:09:43 PM PDT}
APOE
- REDIRECT: Protein Redirected to: Apolipoprotein E {September 10, 2007 2:10:00 PM PDT}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {September 10, 2007 2:10:02 PM PDT}
- UPDATE SUMMARY: Updating Summary, No Errors. {September 10, 2007 2:10:02 PM PDT}
- UPDATE CITATIONS: Updating Citations, No Errors. {September 10, 2007 2:10:02 PM PDT}
- UPDATED: Updated protein page: Apolipoprotein E {September 10, 2007 2:10:11 PM PDT}
APP
- REDIRECT: Protein Redirected to: Amyloid_precursor_protein {September 10, 2007 2:10:38 PM PDT}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {September 10, 2007 2:10:40 PM PDT}
- UPDATE SUMMARY: Updating Summary, No Errors. {September 10, 2007 2:10:40 PM PDT}
- UPDATE CITATIONS: Updating Citations, No Errors. {September 10, 2007 2:10:40 PM PDT}
- UPDATED: Updated protein page: Amyloid_precursor_protein {September 10, 2007 2:10:52 PM PDT}
AR
- REDIRECT: Protein Redirected to: Androgen_receptor {September 10, 2007 2:11:27 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: Androgen_receptor. Invoking a Mandantory Inspection. {September 10, 2007 2:11:30 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Androgen receptor (dihydrotestosterone receptor; testicular feminization; spinal and bulbar muscular atrophy; Kennedy disease)''', also known as '''AR''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_AR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1e3g.
| PDB = {{PDB2|1e3g}}, {{PDB2|1gs4}}, {{PDB2|1i37}}, {{PDB2|1i38}}, {{PDB2|1r4i}}, {{PDB2|1t5z}}, {{PDB2|1t63}}, {{PDB2|1t65}}, {{PDB2|1t73}}, {{PDB2|1t74}}, {{PDB2|1t76}}, {{PDB2|1t79}}, {{PDB2|1t7f}}, {{PDB2|1t7m}}, {{PDB2|1t7r}}, {{PDB2|1t7t}}, {{PDB2|1xj7}}, {{PDB2|1xnn}}, {{PDB2|1xow}}, {{PDB2|1xq3}}, {{PDB2|1z95}}, {{PDB2|2am9}}, {{PDB2|2ama}}, {{PDB2|2amb}}, {{PDB2|2ao6}}, {{PDB2|2ax6}}, {{PDB2|2ax7}}, {{PDB2|2ax8}}, {{PDB2|2ax9}}, {{PDB2|2axa}}, {{PDB2|2ihq}}, {{PDB2|2nw4}}, {{PDB2|2oz7}}
| Name = Androgen receptor (dihydrotestosterone receptor; testicular feminization; spinal and bulbar muscular atrophy; Kennedy disease)
| HGNCid = 644
| Symbol = AR
| AltSymbols =; AIS; DHTR; HUMARA; KD; NR3C4; SBMA; SMAX1; TFM
| OMIM = 313700
| ECnumber =
| Homologene = 28
| MGIid = 88064
| GeneAtlas_image1 = PBB_GE_AR_211110_s_at.png
| GeneAtlas_image2 = PBB_GE_AR_211621_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004882 |text = androgen receptor activity}} {{GNF_GO|id=GO:0005496 |text = steroid binding}} {{GNF_GO|id=GO:0005497 |text = androgen binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0046983 |text = protein dimerization activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0001701 |text = in utero embryonic development}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007548 |text = sex differentiation}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008584 |text = male gonad development}} {{GNF_GO|id=GO:0016049 |text = cell growth}} {{GNF_GO|id=GO:0019102 |text = male somatic sex determination}} {{GNF_GO|id=GO:0030521 |text = androgen receptor signaling pathway}} {{GNF_GO|id=GO:0030850 |text = prostate gland development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 367
| Hs_Ensembl = ENSG00000169083
| Hs_RefseqProtein = NP_000035
| Hs_RefseqmRNA = NM_000044
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 66681190
| Hs_GenLoc_end = 66867186
| Hs_Uniprot = P10275
| Mm_EntrezGene = 11835
| Mm_Ensembl = ENSMUSG00000046532
| Mm_RefseqmRNA = NM_013476
| Mm_RefseqProtein = NP_038504
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 94352469
| Mm_GenLoc_end = 94519866
| Mm_Uniprot = P19091
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The androgen receptor gene is more than 90 kb long and codes for a protein that has 3 major functional domains: the N-terminal domain, DNA-binding domain, and androgen-binding domain. The protein functions as a steroid-hormone activated transcription factor. Upon binding the hormone ligand, the receptor dissociates from accessory proteins, translocates into the nucleus, dimerizes, and then stimulates transcription of androgen responsive genes. This gene contains 2 polymorphic trinucleotide repeat segments that encode polyglutamine and polyglycine tracts in the N-terminal transactivation domain of its protein. Expansion of the polyglutamine tract causes spinal bulbar muscular atrophy (Kennedy disease). Mutations in this gene are also associated with complete androgen insensitivity (CAIS). Two alternatively spliced variants encoding distinct isoforms have been described.<ref>{{cite web | title = Entrez Gene: AR androgen receptor (dihydrotestosterone receptor; testicular feminization; spinal and bulbar muscular atrophy; Kennedy disease)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=367| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pinsky L, Trifiro M, Kaufman M, ''et al.'' |title=Androgen resistance due to mutation of the androgen receptor. |journal=Clinical and investigative medicine. Médecine clinique et experimentale |volume=15 |issue= 5 |pages= 456-72 |year= 1993 |pmid= 1458719 |doi= }}
*{{cite journal | author=Veldscholte J, Berrevoets CA, Ris-Stalpers C, ''et al.'' |title=The androgen receptor in LNCaP cells contains a mutation in the ligand binding domain which affects steroid binding characteristics and response to antiandrogens. |journal=J. Steroid Biochem. Mol. Biol. |volume=41 |issue= 3-8 |pages= 665-9 |year= 1992 |pmid= 1562539 |doi= }}
*{{cite journal | author=Brinkmann AO, Jenster G, Ris-Stalpers C, ''et al.'' |title=Androgen receptor mutations. |journal=J. Steroid Biochem. Mol. Biol. |volume=53 |issue= 1-6 |pages= 443-8 |year= 1995 |pmid= 7626493 |doi= }}
*{{cite journal | author=Quigley CA, De Bellis A, Marschke KB, ''et al.'' |title=Androgen receptor defects: historical, clinical, and molecular perspectives. |journal=Endocr. Rev. |volume=16 |issue= 3 |pages= 271-321 |year= 1995 |pmid= 7671849 |doi= }}
*{{cite journal | author=Sultan C, Lumbroso S, Poujol N, ''et al.'' |title=Mutations of androgen receptor gene in androgen insensitivity syndromes. |journal=J. Steroid Biochem. Mol. Biol. |volume=46 |issue= 5 |pages= 519-30 |year= 1994 |pmid= 8240973 |doi= }}
*{{cite journal | author=Yong EL, Tut TG, Ghadessy FJ, ''et al.'' |title=Partial androgen insensitivity and correlations with the predicted three dimensional structure of the androgen receptor ligand-binding domain. |journal=Mol. Cell. Endocrinol. |volume=137 |issue= 1 |pages= 41-50 |year= 1999 |pmid= 9607727 |doi= }}
*{{cite journal | author=Jänne OA, Moilanen AM, Poukka H, ''et al.'' |title=Androgen-receptor-interacting nuclear proteins. |journal=Biochem. Soc. Trans. |volume=28 |issue= 4 |pages= 401-5 |year= 2001 |pmid= 10961928 |doi= }}
*{{cite journal | author=Yeh S, Sampson ER, Lee DK, ''et al.'' |title=Functional analysis of androgen receptor N-terminal and ligand binding domain interacting coregulators in prostate cancer. |journal=J. Formos. Med. Assoc. |volume=99 |issue= 12 |pages= 885-94 |year= 2001 |pmid= 11155740 |doi= }}
*{{cite journal | author=Loy CJ, Yong EL |title=Sex, infertility and the molecular biology of the androgen receptor. |journal=Curr. Opin. Obstet. Gynecol. |volume=13 |issue= 3 |pages= 315-21 |year= 2001 |pmid= 11396657 |doi= }}
*{{cite journal | author=Roy AK, Tyagi RK, Song CS, ''et al.'' |title=Androgen receptor: structural domains and functional dynamics after ligand-receptor interaction. |journal=Ann. N. Y. Acad. Sci. |volume=949 |issue= |pages= 44-57 |year= 2002 |pmid= 11795379 |doi= }}
*{{cite journal | author=He B, Wilson EM |title=The NH(2)-terminal and carboxyl-terminal interaction in the human androgen receptor. |journal=Mol. Genet. Metab. |volume=75 |issue= 4 |pages= 293-8 |year= 2002 |pmid= 12051960 |doi= 10.1016/S1096-7192(02)00009-4 }}
*{{cite journal | author=Culig Z, Klocker H, Bartsch G, Hobisch A |title=Androgen receptor mutations in carcinoma of the prostate: significance for endocrine therapy. |journal=American journal of pharmacogenomics : genomics-related research in drug development and clinical practice |volume=1 |issue= 4 |pages= 241-9 |year= 2002 |pmid= 12083956 |doi= }}
*{{cite journal | author=Ferro P, Catalano MG, Dell'Eva R, ''et al.'' |title=The androgen receptor CAG repeat: a modifier of carcinogenesis? |journal=Mol. Cell. Endocrinol. |volume=193 |issue= 1-2 |pages= 109-20 |year= 2003 |pmid= 12161010 |doi= }}
*{{cite journal | author=Sultan Ch, Gobinet J, Terouanne B, ''et al.'' |title=[The androgen receptor: molecular pathology] |journal=J. Soc. Biol. |volume=196 |issue= 3 |pages= 223-40 |year= 2003 |pmid= 12465595 |doi= }}
*{{cite journal | author=Walcott JL, Merry DE |title=Trinucleotide repeat disease. The androgen receptor in spinal and bulbar muscular atrophy. |journal=Vitam. Horm. |volume=65 |issue= |pages= 127-47 |year= 2003 |pmid= 12481545 |doi= }}
*{{cite journal | author=Bonaccorsi L, Muratori M, Carloni V, ''et al.'' |title=Androgen receptor and prostate cancer invasion. |journal=Int. J. Androl. |volume=26 |issue= 1 |pages= 21-5 |year= 2003 |pmid= 12534934 |doi= }}
*{{cite journal | author=Verrijdt G, Haelens A, Claessens F |title=Selective DNA recognition by the androgen receptor as a mechanism for hormone-specific regulation of gene expression. |journal=Mol. Genet. Metab. |volume=78 |issue= 3 |pages= 175-85 |year= 2004 |pmid= 12649062 |doi= }}
*{{cite journal | author=Santos AF, Huang H, Tindall DJ |title=The androgen receptor: a potential target for therapy of prostate cancer. |journal=Steroids |volume=69 |issue= 2 |pages= 79-85 |year= 2004 |pmid= 15013685 |doi= 10.1016/j.steroids.2003.10.005 }}
*{{cite journal | author=Mazen I, Lumbroso S, Abdel Ghaffar S, ''et al.'' |title=Mutation of the androgen receptor (R840S) in an Egyptian patient with partial androgen insensitivity syndrome: review of the literature on the clinical expression of different R840 substitutions. |journal=J. Endocrinol. Invest. |volume=27 |issue= 1 |pages= 57-60 |year= 2004 |pmid= 15053245 |doi= }}
*{{cite journal | author=Black BE, Paschal BM |title=Intranuclear organization and function of the androgen receptor. |journal=Trends Endocrinol. Metab. |volume=15 |issue= 9 |pages= 411-7 |year= 2005 |pmid= 15519887 |doi= 10.1016/j.tem.2004.09.006 }}
*{{cite journal | author=Tufan AC, Satiroglu-Tufan NL, Aydinuraz B, ''et al.'' |title=No association of the CAG repeat length in exon 1 of the androgen receptor gene with idiopathic infertility in Turkish men: implications and literature review. |journal=Tohoku J. Exp. Med. |volume=206 |issue= 2 |pages= 105-15 |year= 2005 |pmid= 15888966 |doi= }}
*{{cite journal | author=Morel Y, Michel-Calemard L, Mallet D |title=[Genetic anomalies of the androgen receptor and sexual ambiguity with normal testicular function at birth] |journal=Ann. Endocrinol. (Paris) |volume=66 |issue= 3 |pages= 217-24 |year= 2005 |pmid= 15988382 |doi= }}
*{{cite journal | author=Rajender S, Singh L, Thangaraj K |title=Phenotypic heterogeneity of mutations in androgen receptor gene. |journal=Asian J. Androl. |volume=9 |issue= 2 |pages= 147-79 |year= 2007 |pmid= 17334586 |doi= 10.1111/j.1745-7262.2007.00250.x }}
*{{cite journal | author=Comstock CE, Knudsen KE |title=The complex role of AR signaling after cytotoxic insult: implications for cell-cycle-based chemotherapeutics. |journal=Cell Cycle |volume=6 |issue= 11 |pages= 1307-13 |year= 2007 |pmid= 17568191 |doi= }}
}}
{{refend}}
BCL2
- REDIRECT: Protein Redirected to: Bcl-2 {September 10, 2007 2:11:53 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: Bcl-2. Invoking a Mandantory Inspection. {September 10, 2007 2:11:56 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''B-cell CLL/lymphoma 2''', also known as '''BCL2''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_BCL2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2o2f.
| PDB = {{PDB2|2o2f}}
| Name = B-cell CLL/lymphoma 2
| HGNCid = 990
| Symbol = BCL2
| AltSymbols =; Bcl-2
| OMIM = 151430
| ECnumber =
| Homologene = 527
| MGIid = 88138
| GeneAtlas_image1 = PBB_GE_BCL2_203685_at.png
| GeneAtlas_image2 = PBB_GE_BCL2_203684_s_at.png
| GeneAtlas_image3 = PBB_GE_BCL2_207005_s_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005741 |text = mitochondrial outer membrane}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0001836 |text = release of cytochrome c from mitochondria}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0006959 |text = humoral immune response}} {{GNF_GO|id=GO:0051453 |text = regulation of cellular pH}} {{GNF_GO|id=GO:0051902 |text = negative regulation of mitochondrial depolarization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 596
| Hs_Ensembl = ENSG00000171791
| Hs_RefseqProtein = NP_000624
| Hs_RefseqmRNA = NM_000633
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 58941559
| Hs_GenLoc_end = 59137593
| Hs_Uniprot = P10415
| Mm_EntrezGene = 12043
| Mm_Ensembl = ENSMUSG00000057329
| Mm_RefseqmRNA = NM_009741
| Mm_RefseqProtein = NP_033871
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 108365740
| Mm_GenLoc_end = 108541821
| Mm_Uniprot = Q4VBF6
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.<ref>{{cite web | title = Entrez Gene: BCL2 B-cell CLL/lymphoma 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=596| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Reed JC, Zha H, Aime-Sempe C, ''et al.'' |title=Structure-function analysis of Bcl-2 family proteins. Regulators of programmed cell death. |journal=Adv. Exp. Med. Biol. |volume=406 |issue= |pages= 99-112 |year= 1997 |pmid= 8910675 |doi= }}
*{{cite journal | author=Zauli G, Gibellini D |title=The human immunodeficiency virus type-1 (HIV-1) Tat protein and Bcl-2 gene expression. |journal=Leuk. Lymphoma |volume=23 |issue= 5-6 |pages= 551-60 |year= 1997 |pmid= 9031086 |doi= }}
*{{cite journal | author=Deng X, Kornblau SM, Ruvolo PP, May WS |title=Regulation of Bcl2 phosphorylation and potential significance for leukemic cell chemoresistance. |journal=J. Natl. Cancer Inst. Monographs |volume= |issue= 28 |pages= 30-7 |year= 2003 |pmid= 11158204 |doi= }}
*{{cite journal | author=Vieira HL, Haouzi D, El Hamel C, ''et al.'' |title=Permeabilization of the mitochondrial inner membrane during apoptosis: impact of the adenine nucleotide translocator. |journal=Cell Death Differ. |volume=7 |issue= 12 |pages= 1146-54 |year= 2001 |pmid= 11175251 |doi= 10.1038/sj.cdd.4400778 }}
*{{cite journal | author=Ruvolo PP, Deng X, May WS |title=Phosphorylation of Bcl2 and regulation of apoptosis. |journal=Leukemia |volume=15 |issue= 4 |pages= 515-22 |year= 2001 |pmid= 11368354 |doi= }}
*{{cite journal | author=Marone M, Bonanno G, Rutella S, ''et al.'' |title=Survival and cell cycle control in early hematopoiesis: role of bcl-2, and the cyclin dependent kinase inhibitors P27 and P21. |journal=Leuk. Lymphoma |volume=43 |issue= 1 |pages= 51-7 |year= 2003 |pmid= 11908736 |doi= }}
*{{cite journal | author=Irvine AE, McMullin MF, Ong YL |title=Bcl-2 family members as prognostic indicators in AML. |journal=Hematology |volume=7 |issue= 1 |pages= 21-31 |year= 2002 |pmid= 12171774 |doi= 10.1080/10245330290011838 }}
*{{cite journal | author=Cory S, Adams JM |title=The Bcl2 family: regulators of the cellular life-or-death switch. |journal=Nat. Rev. Cancer |volume=2 |issue= 9 |pages= 647-56 |year= 2002 |pmid= 12209154 |doi= 10.1038/nrc883 }}
*{{cite journal | author=Catz SD, Johnson JL |title=BCL-2 in prostate cancer: a minireview. |journal=Apoptosis |volume=8 |issue= 1 |pages= 29-37 |year= 2003 |pmid= 12510149 |doi= }}
*{{cite journal | author=Ouyang YB, Giffard RG |title=Cellular neuroprotective mechanisms in cerebral ischemia: Bcl-2 family proteins and protection of mitochondrial function. |journal=Cell Calcium |volume=36 |issue= 3-4 |pages= 303-11 |year= 2005 |pmid= 15261486 |doi= 10.1016/j.ceca.2004.02.015 }}
*{{cite journal | author=Seelamgari A, Maddukuri A, Berro R, ''et al.'' |title=Role of viral regulatory and accessory proteins in HIV-1 replication. |journal=Front. Biosci. |volume=9 |issue= |pages= 2388-413 |year= 2006 |pmid= 15353294 |doi= }}
*{{cite journal | author=Hadar T, Shvero J, Yaniv E, ''et al.'' |title=Expression of p53, Ki-67 and Bcl-2 in parathyroid adenoma and residual normal tissue. |journal=Pathol. Oncol. Res. |volume=11 |issue= 1 |pages= 45-9 |year= 2005 |pmid= 15800682 |doi= PAOR.2005.11.1.0045 }}
*{{cite journal | author=Muthumani K, Choo AY, Premkumar A, ''et al.'' |title=Human immunodeficiency virus type 1 (HIV-1) Vpr-regulated cell death: insights into mechanism. |journal=Cell Death Differ. |volume=12 Suppl 1 |issue= |pages= 962-70 |year= 2006 |pmid= 15832179 |doi= 10.1038/sj.cdd.4401583 }}
*{{cite journal | author=Soane L, Fiskum G |title=Inhibition of mitochondrial neural cell death pathways by protein transduction of Bcl-2 family proteins. |journal=J. Bioenerg. Biomembr. |volume=37 |issue= 3 |pages= 179-90 |year= 2006 |pmid= 16167175 |doi= 10.1007/s10863-005-6590-8 }}
}}
{{refend}}
BRCA1
- REDIRECT: Protein Redirected to: BRCA1 {September 10, 2007 2:12:27 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: BRCA1. Invoking a Mandantory Inspection. {September 10, 2007 2:12:41 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Breast cancer 1, early onset''', also known as '''BRCA1''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_BRCA1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jm7.
| PDB = {{PDB2|1jm7}}, {{PDB2|1jnx}}, {{PDB2|1n5o}}, {{PDB2|1oqa}}, {{PDB2|1t15}}, {{PDB2|1t29}}, {{PDB2|1t2u}}, {{PDB2|1t2v}}, {{PDB2|1y98}}
| Name = Breast cancer 1, early onset
| HGNCid = 1100
| Symbol = BRCA1
| AltSymbols =; BRCAI; BRCC1; IRIS; PSCP; RNF53
| OMIM = 113705
| ECnumber =
| Homologene = 5276
| MGIid = 104537
| GeneAtlas_image1 = PBB_GE_BRCA1_204531_s_at.png
| GeneAtlas_image2 = PBB_GE_BRCA1_211851_x_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003684 |text = damaged DNA binding}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0015631 |text = tubulin binding}} {{GNF_GO|id=GO:0019899 |text = enzyme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0050681 |text = androgen receptor binding}}
| Component = {{GNF_GO|id=GO:0000151 |text = ubiquitin ligase complex}} {{GNF_GO|id=GO:0000793 |text = condensed chromosome}} {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0008274 |text = gamma-tubulin ring complex}} {{GNF_GO|id=GO:0031436 |text = BRCA1-BARD1 complex}}
| Process = {{GNF_GO|id=GO:0000075 |text = cell cycle checkpoint}} {{GNF_GO|id=GO:0006260 |text = DNA replication}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006359 |text = regulation of transcription from RNA polymerase III promoter}} {{GNF_GO|id=GO:0006633 |text = fatty acid biosynthetic process}} {{GNF_GO|id=GO:0006978 |text = DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007059 |text = chromosome segregation}} {{GNF_GO|id=GO:0007098 |text = centrosome cycle}} {{GNF_GO|id=GO:0008630 |text = DNA damage response, signal transduction resulting in induction of apoptosis}} {{GNF_GO|id=GO:0009048 |text = dosage compensation, by inactivation of X chromosome}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}} {{GNF_GO|id=GO:0016567 |text = protein ubiquitination}} {{GNF_GO|id=GO:0030521 |text = androgen receptor signaling pathway}} {{GNF_GO|id=GO:0031398 |text = positive regulation of protein ubiquitination}} {{GNF_GO|id=GO:0042127 |text = regulation of cell proliferation}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0045717 |text = negative regulation of fatty acid biosynthetic process}} {{GNF_GO|id=GO:0045739 |text = positive regulation of DNA repair}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}} {{GNF_GO|id=GO:0045893 |text = positive regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0046600 |text = negative regulation of centriole replication}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 672
| Hs_Ensembl = ENSG00000012048
| Hs_RefseqProtein = NP_009225
| Hs_RefseqmRNA = NM_007294
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 38449840
| Hs_GenLoc_end = 38530994
| Hs_Uniprot = P38398
| Mm_EntrezGene = 12189
| Mm_Ensembl = ENSMUSG00000017146
| Mm_RefseqmRNA = NM_009764
| Mm_RefseqProtein = NP_033894
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 101305657
| Mm_GenLoc_end = 101367902
| Mm_Uniprot = Q3UMS5
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a nuclear phosphoprotein that plays a role in maintaining genomic stability and acts as a tumor suppressor. The encoded protein combines with other tumor suppressors, DNA damage sensors, and signal transducers to form a large multi-subunit protein complex known as BASC for BRCA1-associated genome surveillance complex. This gene product associates with RNA polymerase II, and through the C-terminal domain, also interacts with histone deacetylase complex. This protein thus plays a role in transcription, DNA repair of double-stranded breaks, and recombination. Mutations in this gene are responsible for approximately 40% of inherited breast cancers and more than 80% of inherited breast and ovarian cancers. Alternative splicing plays a role in modulating the subcellular localization and physiological function of this gene. Many alternatively spliced transcript variants have been described for this gene but only some have had their full-length natures identified.<ref>{{cite web | title = Entrez Gene: BRCA1 breast cancer 1, early onset| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=672| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Paterson JW |title=BRCA1: a review of structure and putative functions. |journal=Dis. Markers |volume=13 |issue= 4 |pages= 261-74 |year= 1998 |pmid= 9553742 |doi= }}
*{{cite journal | author=Yang X, Lippman ME |title=BRCA1 and BRCA2 in breast cancer. |journal=Breast Cancer Res. Treat. |volume=54 |issue= 1 |pages= 1-10 |year= 1999 |pmid= 10369075 |doi= }}
*{{cite journal | author=Deng CX, Brodie SG |title=Roles of BRCA1 and its interacting proteins. |journal=Bioessays |volume=22 |issue= 8 |pages= 728-37 |year= 2000 |pmid= 10918303 |doi= 10.1002/1521-1878(200008)22:8<728::AID-BIES6>3.0.CO;2-B }}
*{{cite journal | author=McGowan CH |title=Checking in on Cds1 (Chk2): A checkpoint kinase and tumor suppressor. |journal=Bioessays |volume=24 |issue= 6 |pages= 502-11 |year= 2002 |pmid= 12111733 |doi= 10.1002/bies.10101 }}
*{{cite journal | author=Deng CX |title=Roles of BRCA1 in centrosome duplication. |journal=Oncogene |volume=21 |issue= 40 |pages= 6222-7 |year= 2002 |pmid= 12214252 |doi= 10.1038/sj.onc.1205713 }}
*{{cite journal | author=Daniel DC |title=Highlight: BRCA1 and BRCA2 proteins in breast cancer. |journal=Microsc. Res. Tech. |volume=59 |issue= 1 |pages= 68-83 |year= 2002 |pmid= 12242698 |doi= 10.1002/jemt.10178 }}
*{{cite journal | author=Kubista M, Rosner M, Miloloza A, ''et al.'' |title=Brca1 and differentiation. |journal=Mutat. Res. |volume=512 |issue= 2-3 |pages= 165-72 |year= 2003 |pmid= 12464350 |doi= }}
*{{cite journal | author=Tutt A, Ashworth A |title=The relationship between the roles of BRCA genes in DNA repair and cancer predisposition. |journal=Trends in molecular medicine |volume=8 |issue= 12 |pages= 571-6 |year= 2003 |pmid= 12470990 |doi= }}
*{{cite journal | author=El-Deiry WS |title=Transactivation of repair genes by BRCA1. |journal=Cancer Biol. Ther. |volume=1 |issue= 5 |pages= 490-1 |year= 2003 |pmid= 12496474 |doi= }}
*{{cite journal | author=Somasundaram K |title=Breast cancer gene 1 (BRCA1): role in cell cycle regulation and DNA repair--perhaps through transcription. |journal=J. Cell. Biochem. |volume=88 |issue= 6 |pages= 1084-91 |year= 2003 |pmid= 12647291 |doi= 10.1002/jcb.10469 }}
*{{cite journal | author=Deng CX, Wang RH |title=Roles of BRCA1 in DNA damage repair: a link between development and cancer. |journal=Hum. Mol. Genet. |volume=12 Spec No 1 |issue= |pages= R113-23 |year= 2003 |pmid= 12668603 |doi= }}
*{{cite journal | author=Lou Z, Chen J |title=BRCA proteins and DNA damage checkpoints. |journal=Front. Biosci. |volume=8 |issue= |pages= s718-21 |year= 2004 |pmid= 12700125 |doi= }}
*{{cite journal | author=Rosen EM, Fan S, Pestell RG, Goldberg ID |title=BRCA1 gene in breast cancer. |journal=J. Cell. Physiol. |volume=196 |issue= 1 |pages= 19-41 |year= 2003 |pmid= 12767038 |doi= 10.1002/jcp.10257 }}
*{{cite journal | author=Mullineaux LG, Castellano TM, Shaw J, ''et al.'' |title=Identification of germline 185delAG BRCA1 mutations in non-Jewish Americans of Spanish ancestry from the San Luis Valley, Colorado. |journal=Cancer |volume=98 |issue= 3 |pages= 597-602 |year= 2003 |pmid= 12879478 |doi= 10.1002/cncr.11533 }}
*{{cite journal | author=Hartman AR, Ford JM |title=BRCA1 and p53: compensatory roles in DNA repair. |journal=J. Mol. Med. |volume=81 |issue= 11 |pages= 700-7 |year= 2004 |pmid= 13679996 |doi= 10.1007/s00109-003-0477-0 }}
*{{cite journal | author=Rosen EM, Fan S, Pestell RG, Goldberg ID |title=BRCA1 in hormone-responsive cancers. |journal=Trends Endocrinol. Metab. |volume=14 |issue= 8 |pages= 378-85 |year= 2004 |pmid= 14516936 |doi= }}
*{{cite journal | author=McCoy ML, Mueller CR, Roskelley CD |title=The role of the breast cancer susceptibility gene 1 (BRCA1) in sporadic epithelial ovarian cancer. |journal=Reprod. Biol. Endocrinol. |volume=1 |issue= |pages= 72 |year= 2004 |pmid= 14613551 |doi= 10.1186/1477-7827-1-72 }}
*{{cite journal | author=Levine DA, Argenta PA, Yee CJ, ''et al.'' |title=Fallopian tube and primary peritoneal carcinomas associated with BRCA mutations. |journal=J. Clin. Oncol. |volume=21 |issue= 22 |pages= 4222-7 |year= 2003 |pmid= 14615451 |doi= 10.1200/JCO.2003.04.131 }}
*{{cite journal | author=Feunteun J |title=[A paradox and three egnimas about the role of BRCA1 in breast and ovarian cancers] |journal=J. Soc. Biol. |volume=198 |issue= 2 |pages= 123-6 |year= 2004 |pmid= 15368961 |doi= }}
*{{cite journal | author=Sunpaweravong S, Sunpaweravong P |title=Recent developments in critical genes in the molecular biology of breast cancer. |journal=Asian journal of surgery / Asian Surgical Association |volume=28 |issue= 1 |pages= 71-5 |year= 2005 |pmid= 15691805 |doi= }}
*{{cite journal | author=Aiyar S, Sun JL, Li R |title=BRCA1: a locus-specific "liaison" in gene expression and genetic integrity. |journal=J. Cell. Biochem. |volume=94 |issue= 6 |pages= 1103-11 |year= 2005 |pmid= 15723343 |doi= 10.1002/jcb.20386 }}
*{{cite journal | author=Dumitrescu RG, Cotarla I |title=Understanding breast cancer risk -- where do we stand in 2005? |journal=J. Cell. Mol. Med. |volume=9 |issue= 1 |pages= 208-21 |year= 2005 |pmid= 15784178 |doi= }}
*{{cite journal | author=Gonçalves A, Viens P, Sobol H, ''et al.'' |title=[Molecular alterations in breast cancer: clinical implications and new analytical tools] |journal=La Revue de médecine interne / fondée ... par la Société nationale francaise de médecine interne |volume=26 |issue= 6 |pages= 470-8 |year= 2005 |pmid= 15936476 |doi= 10.1016/j.revmed.2004.11.012 }}
*{{cite journal | author=Durant ST, Nickoloff JA |title=Good timing in the cell cycle for precise DNA repair by BRCA1. |journal=Cell Cycle |volume=4 |issue= 9 |pages= 1216-22 |year= 2006 |pmid= 16103751 |doi= }}
*{{cite journal | author=Rosen EM, Fan S, Isaacs C |title=BRCA1 in hormonal carcinogenesis: basic and clinical research. |journal=Endocr. Relat. Cancer |volume=12 |issue= 3 |pages= 533-48 |year= 2005 |pmid= 16172191 |doi= 10.1677/erc.1.00972 }}
*{{cite journal | author=Lee Y, Medeiros F, Kindelberger D, ''et al.'' |title=Advances in the recognition of tubal intraepithelial carcinoma: applications to cancer screening and the pathogenesis of ovarian cancer. |journal=Advances in anatomic pathology |volume=13 |issue= 1 |pages= 1-7 |year= 2006 |pmid= 16462151 |doi= 10.1097/01.pap.0000201826.46978.e5 }}
*{{cite journal | author=Starita LM, Parvin JD |title=Substrates of the BRCA1-dependent ubiquitin ligase. |journal=Cancer Biol. Ther. |volume=5 |issue= 2 |pages= 137-41 |year= 2006 |pmid= 16479151 |doi= }}
*{{cite journal | author=Domchek SM, Weber BL |title=Clinical management of BRCA1 and BRCA2 mutation carriers. |journal=Oncogene |volume=25 |issue= 43 |pages= 5825-31 |year= 2006 |pmid= 16998496 |doi= 10.1038/sj.onc.1209881 }}
*{{cite journal | author=Honrado E, Osorio A, Palacios J, Benitez J |title=Pathology and gene expression of hereditary breast tumors associated with BRCA1, BRCA2 and CHEK2 gene mutations. |journal=Oncogene |volume=25 |issue= 43 |pages= 5837-45 |year= 2006 |pmid= 16998498 |doi= 10.1038/sj.onc.1209875 }}
*{{cite journal | author=Turner NC, Reis-Filho JS |title=Basal-like breast cancer and the BRCA1 phenotype. |journal=Oncogene |volume=25 |issue= 43 |pages= 5846-53 |year= 2006 |pmid= 16998499 |doi= 10.1038/sj.onc.1209876 }}
*{{cite journal | author=Mullan PB, Quinn JE, Harkin DP |title=The role of BRCA1 in transcriptional regulation and cell cycle control. |journal=Oncogene |volume=25 |issue= 43 |pages= 5854-63 |year= 2006 |pmid= 16998500 |doi= 10.1038/sj.onc.1209872 }}
}}
{{refend}}
- REDIRECT: Protein Redirected to: Caspase 3 {September 10, 2007 2:12:52 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: Caspase 3. Invoking a Mandantory Inspection. {September 10, 2007 2:12:55 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Caspase 3, apoptosis-related cysteine peptidase''', also known as '''CASP3''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CASP3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cp3.
| PDB = {{PDB2|1cp3}}, {{PDB2|1gfw}}, {{PDB2|1i3o}}, {{PDB2|1nme}}, {{PDB2|1nmq}}, {{PDB2|1nms}}, {{PDB2|1pau}}, {{PDB2|1qx3}}, {{PDB2|1re1}}, {{PDB2|1rhj}}, {{PDB2|1rhk}}, {{PDB2|1rhm}}, {{PDB2|1rhq}}, {{PDB2|1rhr}}, {{PDB2|1rhu}}, {{PDB2|2c1e}}, {{PDB2|2c2k}}, {{PDB2|2c2m}}, {{PDB2|2c2o}}, {{PDB2|2cdr}}, {{PDB2|2cjx}}, {{PDB2|2cjy}}, {{PDB2|2cnk}}, {{PDB2|2cnl}}, {{PDB2|2cnn}}, {{PDB2|2cno}}, {{PDB2|2dko}}, {{PDB2|2h5i}}, {{PDB2|2h5j}}, {{PDB2|2h65}}, {{PDB2|2j30}}, {{PDB2|2j31}}, {{PDB2|2j32}}, {{PDB2|2j33}}
| Name = Caspase 3, apoptosis-related cysteine peptidase
| HGNCid = 1504
| Symbol = CASP3
| AltSymbols =; CPP32; CPP32B; SCA-1
| OMIM = 600636
| ECnumber =
| Homologene = 37912
| MGIid = 107739
| GeneAtlas_image1 = PBB_GE_CASP3_202763_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0004861 |text = cyclin-dependent protein kinase inhibitor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008234 |text = cysteine-type peptidase activity}} {{GNF_GO|id=GO:0030693 |text = caspase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0001782 |text = B cell homeostasis}} {{GNF_GO|id=GO:0001836 |text = release of cytochrome c from mitochondria}} {{GNF_GO|id=GO:0006309 |text = DNA fragmentation during apoptosis}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0008625 |text = induction of apoptosis via death domain receptors}} {{GNF_GO|id=GO:0008631 |text = induction of apoptosis by oxidative stress}} {{GNF_GO|id=GO:0009411 |text = response to UV}} {{GNF_GO|id=GO:0009611 |text = response to wounding}} {{GNF_GO|id=GO:0030216 |text = keratinocyte differentiation}} {{GNF_GO|id=GO:0030889 |text = negative regulation of B cell proliferation}} {{GNF_GO|id=GO:0043029 |text = T cell homeostasis}} {{GNF_GO|id=GO:0045165 |text = cell fate commitment}} {{GNF_GO|id=GO:0045736 |text = negative regulation of cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0046007 |text = negative regulation of activated T cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 836
| Hs_Ensembl = ENSG00000164305
| Hs_RefseqProtein = NP_004337
| Hs_RefseqmRNA = NM_004346
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 185785845
| Hs_GenLoc_end = 185807623
| Hs_Uniprot = P42574
| Mm_EntrezGene = 12367
| Mm_Ensembl = ENSMUSG00000031628
| Mm_RefseqmRNA = XM_991820
| Mm_RefseqProtein = XP_996914
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 48116235
| Mm_GenLoc_end = 48137523
| Mm_Uniprot = Q8BNT4
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. Alternative splicing of this gene results in two transcript variants that encode the same protein.<ref>{{cite web | title = Entrez Gene: CASP3 caspase 3, apoptosis-related cysteine peptidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=836| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Cohen GM |title=Caspases: the executioners of apoptosis. |journal=Biochem. J. |volume=326 ( Pt 1) |issue= |pages= 1-16 |year= 1997 |pmid= 9337844 |doi= }}
*{{cite journal | author=Roig J, Traugh JA |title=Cytostatic p21 G protein-activated protein kinase gamma-PAK. |journal=Vitam. Horm. |volume=62 |issue= |pages= 167-98 |year= 2001 |pmid= 11345898 |doi= }}
*{{cite journal | author=Zhao LJ, Zhu H |title=Structure and function of HIV-1 auxiliary regulatory protein Vpr: novel clues to drug design. |journal=Curr. Drug Targets Immune Endocr. Metabol. Disord. |volume=4 |issue= 4 |pages= 265-75 |year= 2005 |pmid= 15578977 |doi= }}
*{{cite journal | author=Le Rouzic E, Benichou S |title=The Vpr protein from HIV-1: distinct roles along the viral life cycle. |journal=Retrovirology |volume=2 |issue= |pages= 11 |year= 2006 |pmid= 15725353 |doi= 10.1186/1742-4690-2-11 }}
*{{cite journal | author=Sykes MC, Mowbray AL, Jo H |title=Reversible glutathiolation of caspase-3 by glutaredoxin as a novel redox signaling mechanism in tumor necrosis factor-alpha-induced cell death. |journal=Circ. Res. |volume=100 |issue= 2 |pages= 152-4 |year= 2007 |pmid= 17272816 |doi= 10.1161/01.RES.0000258171.08020.72 }}
}}
{{refend}}
CDKN1A
- REDIRECT: Protein Redirected to: p21 {September 10, 2007 2:13:05 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: p21. Invoking a Mandantory Inspection. {September 10, 2007 2:13:19 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Cyclin-dependent kinase inhibitor 1A (p21, Cip1)''', also known as '''CDKN1A''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cyclin-dependent kinase inhibitor 1A (p21, Cip1)
| HGNCid = 1784
| Symbol = CDKN1A
| AltSymbols =; CAP20; CDKN1; CIP1; MDA-6; P21; SDI1; WAF1; p21CIP1
| OMIM = 116899
| ECnumber =
| Homologene = 333
| MGIid = 104556
| GeneAtlas_image1 = PBB_GE_CDKN1A_202284_s_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0004672 |text = protein kinase activity}} {{GNF_GO|id=GO:0004861 |text = cyclin-dependent protein kinase inhibitor activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0030332 |text = cyclin binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0000307 |text = cyclin-dependent protein kinase holoenzyme complex}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006974 |text = response to DNA damage stimulus}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0008629 |text = induction of apoptosis by intracellular signals}} {{GNF_GO|id=GO:0009411 |text = response to UV}} {{GNF_GO|id=GO:0030890 |text = positive regulation of B cell proliferation}} {{GNF_GO|id=GO:0043066 |text = negative regulation of apoptosis}} {{GNF_GO|id=GO:0043071 |text = positive regulation of non-apoptotic programmed cell death}} {{GNF_GO|id=GO:0045736 |text = negative regulation of cyclin-dependent protein kinase activity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1026
| Hs_Ensembl = ENSG00000124762
| Hs_RefseqProtein = NP_000380
| Hs_RefseqmRNA = NM_000389
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 36754413
| Hs_GenLoc_end = 36763094
| Hs_Uniprot = P38936
| Mm_EntrezGene = 12575
| Mm_Ensembl = ENSMUSG00000023067
| Mm_RefseqmRNA = NM_007669
| Mm_RefseqProtein = NP_031695
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 28821439
| Mm_GenLoc_end = 28828386
| Mm_Uniprot = Q4FK34
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a potent cyclin-dependent kinase inhibitor. The encoded protein binds to and inhibits the activity of cyclin-CDK2 or -CDK4 complexes, and thus functions as a regulator of cell cycle progression at G1. The expression of this gene is tightly controlled by the tumor suppressor protein p53, through which this protein mediates the p53-dependent cell cycle G1 phase arrest in response to a variety of stress stimuli. This protein can interact with proliferating cell nuclear antigen (PCNA), a DNA polymerase accessory factor, and plays a regulatory role in S phase DNA replication and DNA damage repair. This protein was reported to be specifically cleaved by CASP3-like caspases, which thus leads to a dramatic activation of CDK2, and may be instrumental in the execution of apoptosis following caspase activation. Two alternatively spliced variants, which encode an identical protein, have been reported.<ref>{{cite web | title = Entrez Gene: CDKN1A cyclin-dependent kinase inhibitor 1A (p21, Cip1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1026| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Marone M, Bonanno G, Rutella S, ''et al.'' |title=Survival and cell cycle control in early hematopoiesis: role of bcl-2, and the cyclin dependent kinase inhibitors P27 and P21. |journal=Leuk. Lymphoma |volume=43 |issue= 1 |pages= 51-7 |year= 2003 |pmid= 11908736 |doi= }}
*{{cite journal | author=Fang JY, Lu YY |title=Effects of histone acetylation and DNA methylation on p21( WAF1) regulation. |journal=World J. Gastroenterol. |volume=8 |issue= 3 |pages= 400-5 |year= 2002 |pmid= 12046058 |doi= }}
*{{cite journal | author=Tokumoto M, Tsuruya K, Fukuda K, ''et al.'' |title=Parathyroid cell growth in patients with advanced secondary hyperparathyroidism: vitamin D receptor and cyclin-dependent kinase inhibitors, p21 and p27. |journal=Nephrol. Dial. Transplant. |volume=18 Suppl 3 |issue= |pages= iii9-12 |year= 2003 |pmid= 12771291 |doi= }}
*{{cite journal | author=Amini S, Khalili K, Sawaya BE |title=Effect of HIV-1 Vpr on cell cycle regulators. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 249-60 |year= 2004 |pmid= 15142382 |doi= 10.1089/104454904773819833 }}
*{{cite journal | author=Zhang Z, Wang H, Li M, ''et al.'' |title=Novel MDM2 p53-independent functions identified through RNA silencing technologies. |journal=Ann. N. Y. Acad. Sci. |volume=1058 |issue= |pages= 205-14 |year= 2006 |pmid= 16394138 |doi= 10.1196/annals.1359.030 }}
}}
{{refend}}
CDKN2A
- REDIRECT: Protein Redirected to: P16INK4a {September 10, 2007 2:13:50 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: P16INK4a. Invoking a Mandantory Inspection. {September 10, 2007 2:13:57 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Cyclin-dependent kinase inhibitor 2A (melanoma, p16, inhibits CDK4)''', also known as '''CDKN2A''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CDKN2A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a5e.
| PDB = {{PDB2|1a5e}}, {{PDB2|1bi7}}, {{PDB2|1dc2}}, {{PDB2|2a5e}}
| Name = Cyclin-dependent kinase inhibitor 2A (melanoma, p16, inhibits CDK4)
| HGNCid = 1787
| Symbol = CDKN2A
| AltSymbols =; ARF; CDK4I; CDKN2; CMM2; INK4; INK4a; MLM; MTS1; TP16; p14; p14ARF; p16; p16INK4; p16INK4a; p19
| OMIM = 600160
| ECnumber =
| Homologene = 55430
| MGIid =
| GeneAtlas_image1 = PBB_GE_CDKN2A_207039_at.png
| GeneAtlas_image2 = PBB_GE_CDKN2A_209644_x_at.png
| GeneAtlas_image3 = PBB_GE_CDKN2A_211156_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004861 |text = cyclin-dependent protein kinase inhibitor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016301 |text = kinase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0005730 |text = nucleolus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000075 |text = cell cycle checkpoint}} {{GNF_GO|id=GO:0000079 |text = regulation of cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006364 |text = rRNA processing}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0007569 |text = cell aging}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0008544 |text = epidermis development}} {{GNF_GO|id=GO:0045736 |text = negative regulation of cyclin-dependent protein kinase activity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1029
| Hs_Ensembl = ENSG00000147889
| Hs_RefseqProtein = NP_000068
| Hs_RefseqmRNA = NM_000077
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 21957751
| Hs_GenLoc_end = 21984490
| Hs_Uniprot = P42771
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene generates several transcript variants which differ in their first exons. At least three alternatively spliced variants encoding distinct proteins have been reported, two of which encode structurally related isoforms known to function as inhibitors of CDK4 kinase. The remaining transcript includes an alternate first exon located 20 Kb upstream of the remainder of the gene; this transcript contains an alternate open reading frame (ARF) that specifies a protein which is structurally unrelated to the products of the other variants. This ARF product functions as a stabilizer of the tumor suppressor protein p53 as it can interact with, and sequester, MDM1, a protein responsible for the degradation of p53. In spite of the structural and functional differences, the CDK inhibitor isoforms and the ARF product encoded by this gene, through the regulatory roles of CDK4 and p53 in cell cycle G1 progression, share a common functionality in cell cycle G1 control. This gene is frequently mutated or deleted in a wide variety of tumors, and is known to be an important tumor suppressor gene.<ref>{{cite web | title = Entrez Gene: CDKN2A cyclin-dependent kinase inhibitor 2A (melanoma, p16, inhibits CDK4)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1029| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Smith-Sørensen B, Hovig E |title=CDKN2A (p16INK4A) somatic and germline mutations. |journal=Hum. Mutat. |volume=7 |issue= 4 |pages= 294-303 |year= 1996 |pmid= 8723678 |doi= 10.1002/(SICI)1098-1004(1996)7:4<294::AID-HUMU2>3.0.CO;2-9 }}
*{{cite journal | author=Dracopoli NC, Fountain JW |title=CDKN2 mutations in melanoma. |journal=Cancer Surv. |volume=26 |issue= |pages= 115-32 |year= 1996 |pmid= 8783570 |doi= }}
*{{cite journal | author=Akita H |title=[Prognostic importance of altered expression of cell cycle regulators in lung cancer] |journal=Nippon Rinsho |volume=60 Suppl 5 |issue= |pages= 267-71 |year= 2003 |pmid= 12101670 |doi= }}
*{{cite journal | author=Kusy S, Larsen CJ, Roche J |title=p14ARF, p15INK4b and p16INK4a methylation status in chronic myelogenous leukemia. |journal=Leuk. Lymphoma |volume=45 |issue= 10 |pages= 1989-94 |year= 2005 |pmid= 15370242 |doi= 10.1080/10428190410001714025 }}
*{{cite journal | author=Gjerset RA |title=DNA damage, p14ARF, nucleophosmin (NPM/B23), and cancer. |journal=J. Mol. Histol. |volume=37 |issue= 5-7 |pages= 239-51 |year= 2007 |pmid= 16855788 |doi= 10.1007/s10735-006-9040-y }}
*{{cite journal | author=Yildiz IZ, Usubütün A, Firat P, ''et al.'' |title=Efficiency of immunohistochemical p16 expression and HPV typing in cervical squamous intraepithelial lesion grading and review of the p16 literature. |journal=Pathol. Res. Pract. |volume=203 |issue= 6 |pages= 445-9 |year= 2007 |pmid= 17543474 |doi= 10.1016/j.prp.2007.03.010 }}
}}
{{refend}}
CTNNB1
- REDIRECT: Protein Redirected to: Beta-catenin {September 10, 2007 2:14:35 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: Beta-catenin. Invoking a Mandantory Inspection. {September 10, 2007 2:14:42 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Catenin (cadherin-associated protein), beta 1, 88kDa''', also known as '''CTNNB1''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CTNNB1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dow.
| PDB = {{PDB2|1dow}}, {{PDB2|1g3j}}, {{PDB2|1i7w}}, {{PDB2|1i7x}}, {{PDB2|1jdh}}, {{PDB2|1jpp}}, {{PDB2|1jpw}}, {{PDB2|1luj}}, {{PDB2|1m1e}}, {{PDB2|1qz7}}, {{PDB2|1t08}}, {{PDB2|1th1}}, {{PDB2|1v18}}, {{PDB2|2bct}}, {{PDB2|2gl7}}, {{PDB2|3bct}}
| Name = Catenin (cadherin-associated protein), beta 1, 88kDa
| HGNCid = 2514
| Symbol = CTNNB1
| AltSymbols =; CTNNB; FLJ25606
| OMIM = 116806
| ECnumber =
| Homologene = 1434
| MGIid = 88276
| GeneAtlas_image1 = PBB_GE_CTNNB1_201533_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0045294 |text = alpha-catenin binding}} {{GNF_GO|id=GO:0045296 |text = cadherin binding}} {{GNF_GO|id=GO:0050681 |text = androgen receptor binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005667 |text = transcription factor complex}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005913 |text = cell-cell adherens junction}} {{GNF_GO|id=GO:0016323 |text = basolateral plasma membrane}} {{GNF_GO|id=GO:0016328 |text = lateral plasma membrane}} {{GNF_GO|id=GO:0030027 |text = lamellipodium}} {{GNF_GO|id=GO:0031528 |text = microvillus membrane}} {{GNF_GO|id=GO:0045177 |text = apical part of cell}}
| Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0000904 |text = cellular morphogenesis during differentiation}} {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0001569 |text = patterning of blood vessels}} {{GNF_GO|id=GO:0001706 |text = endoderm formation}} {{GNF_GO|id=GO:0001708 |text = cell fate specification}} {{GNF_GO|id=GO:0001709 |text = cell fate determination}} {{GNF_GO|id=GO:0001711 |text = endodermal cell fate commitment}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007398 |text = ectoderm development}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0009950 |text = dorsal/ventral axis specification}} {{GNF_GO|id=GO:0009954 |text = proximal/distal pattern formation}} {{GNF_GO|id=GO:0010003 |text = gastrulation (sensu Mammalia)}} {{GNF_GO|id=GO:0016055 |text = Wnt receptor signaling pathway}} {{GNF_GO|id=GO:0016331 |text = morphogenesis of embryonic epithelium}} {{GNF_GO|id=GO:0016337 |text = cell-cell adhesion}} {{GNF_GO|id=GO:0030097 |text = hemopoiesis}} {{GNF_GO|id=GO:0030316 |text = osteoclast differentiation}} {{GNF_GO|id=GO:0030324 |text = lung development}} {{GNF_GO|id=GO:0030521 |text = androgen receptor signaling pathway}} {{GNF_GO|id=GO:0030858 |text = positive regulation of epithelial cell differentiation}} {{GNF_GO|id=GO:0030900 |text = forebrain development}} {{GNF_GO|id=GO:0031016 |text = pancreas development}} {{GNF_GO|id=GO:0035116 |text = embryonic hindlimb morphogenesis}} {{GNF_GO|id=GO:0035117 |text = embryonic arm morphogenesis}} {{GNF_GO|id=GO:0042127 |text = regulation of cell proliferation}} {{GNF_GO|id=GO:0042475 |text = odontogenesis (sensu Vertebrata)}} {{GNF_GO|id=GO:0042733 |text = embryonic digit morphogenesis}} {{GNF_GO|id=GO:0045453 |text = bone resorption}} {{GNF_GO|id=GO:0045596 |text = negative regulation of cell differentiation}} {{GNF_GO|id=GO:0045669 |text = positive regulation of osteoblast differentiation}} {{GNF_GO|id=GO:0045671 |text = negative regulation of osteoclast differentiation}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0048469 |text = cell maturation}} {{GNF_GO|id=GO:0048489 |text = synaptic vesicle transport}} {{GNF_GO|id=GO:0050808 |text = synapse organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1499
| Hs_Ensembl = ENSG00000168036
| Hs_RefseqProtein = XP_001133660
| Hs_RefseqmRNA = XM_001133660
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 41216004
| Hs_GenLoc_end = 41256938
| Hs_Uniprot = P35222
| Mm_EntrezGene = 12387
| Mm_Ensembl = ENSMUSG00000006932
| Mm_RefseqmRNA = NM_007614
| Mm_RefseqProtein = NP_031640
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 120782173
| Mm_GenLoc_end = 120809205
| Mm_Uniprot = Q3UZT7
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Beta-catenin is an adherens junction protein. Adherens junctions (AJs; also called the zonula adherens) are critical for the establishment and maintenance of epithelial layers, such as those lining organ surfaces. AJs mediate adhesion between cells, communicate a signal that neighboring cells are present, and anchor the actin cytoskeleton. In serving these roles, AJs regulate normal cell growth and behavior. At several stages of embryogenesis, wound healing, and tumor cell metastasis, cells form and leave epithelia. This process, which involves the disruption and reestablishment of epithelial cell-cell contacts, may be regulated by the disassembly and assembly of AJs. AJs may also function in the transmission of the 'contact inhibition' signal, which instructs cells to stop dividing once an epithelial sheet is complete.[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: CTNNB1 catenin (cadherin-associated protein), beta 1, 88kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1499| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kikuchi A |title=Regulation of beta-catenin signaling in the Wnt pathway. |journal=Biochem. Biophys. Res. Commun. |volume=268 |issue= 2 |pages= 243-8 |year= 2000 |pmid= 10679188 |doi= 10.1006/bbrc.1999.1860 }}
*{{cite journal | author=Wilson PD |title=Polycystin: new aspects of structure, function, and regulation. |journal=J. Am. Soc. Nephrol. |volume=12 |issue= 4 |pages= 834-45 |year= 2001 |pmid= 11274246 |doi= }}
*{{cite journal | author=Kalluri R, Neilson EG |title=Epithelial-mesenchymal transition and its implications for fibrosis. |journal=J. Clin. Invest. |volume=112 |issue= 12 |pages= 1776-84 |year= 2004 |pmid= 14679171 |doi= 10.1172/JCI200320530 }}
*{{cite journal | author=De Ferrari GV, Moon RT |title=The ups and downs of Wnt signaling in prevalent neurological disorders. |journal=Oncogene |volume=25 |issue= 57 |pages= 7545-53 |year= 2007 |pmid= 17143299 |doi= 10.1038/sj.onc.1210064 }}
}}
{{refend}}
EGFR
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Epidermal growth factor receptor (erythroblastic leukemia viral (v-erb-b) oncogene homolog, avian)''', also known as '''EGFR''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_EGFR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ivo.
| PDB = {{PDB2|1ivo}}, {{PDB2|1m14}}, {{PDB2|1m17}}, {{PDB2|1mox}}, {{PDB2|1nql}}, {{PDB2|1xkk}}, {{PDB2|1yy9}}, {{PDB2|1z9i}}, {{PDB2|2gs2}}, {{PDB2|2gs6}}, {{PDB2|2gs7}}, {{PDB2|2itn}}, {{PDB2|2ito}}, {{PDB2|2itp}}, {{PDB2|2itq}}, {{PDB2|2itt}}, {{PDB2|2itu}}, {{PDB2|2itv}}, {{PDB2|2itw}}, {{PDB2|2itx}}, {{PDB2|2ity}}, {{PDB2|2itz}}, {{PDB2|2j5e}}, {{PDB2|2j5f}}, {{PDB2|2j6m}}
| Name = Epidermal growth factor receptor (erythroblastic leukemia viral (v-erb-b) oncogene homolog, avian)
| HGNCid = 3236
| Symbol = EGFR
| AltSymbols =; ERBB; ERBB1; mENA
| OMIM = 131550
| ECnumber =
| Homologene = 74545
| MGIid = 95294
| GeneAtlas_image1 = PBB_GE_EGFR_201983_s_at.png
| GeneAtlas_image2 = PBB_GE_EGFR_201984_s_at.png
| GeneAtlas_image3 = PBB_GE_EGFR_210984_x_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003690 |text = double-stranded DNA binding}} {{GNF_GO|id=GO:0004710 |text = MAP/ERK kinase kinase activity}} {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005006 |text = epidermal growth factor receptor activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0030235 |text = nitric-oxide synthase regulator activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}} {{GNF_GO|id=GO:0051015 |text = actin filament binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005768 |text = endosome}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0016323 |text = basolateral plasma membrane}} {{GNF_GO|id=GO:0030122 |text = AP-2 adaptor complex}} {{GNF_GO|id=GO:0030139 |text = endocytic vesicle}}
| Process = {{GNF_GO|id=GO:0001503 |text = ossification}} {{GNF_GO|id=GO:0006950 |text = response to stress}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007173 |text = epidermal growth factor receptor signaling pathway}} {{GNF_GO|id=GO:0007202 |text = phospholipase C activation}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0016337 |text = cell-cell adhesion}} {{GNF_GO|id=GO:0030335 |text = positive regulation of cell migration}} {{GNF_GO|id=GO:0042327 |text = positive regulation of phosphorylation}} {{GNF_GO|id=GO:0043006 |text = calcium-dependent phospholipase A2 activation}} {{GNF_GO|id=GO:0043406 |text = positive regulation of MAPK activity}} {{GNF_GO|id=GO:0045429 |text = positive regulation of nitric oxide biosynthetic process}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}} {{GNF_GO|id=GO:0046777 |text = protein amino acid autophosphorylation}} {{GNF_GO|id=GO:0050679 |text = positive regulation of epithelial cell proliferation}} {{GNF_GO|id=GO:0050730 |text = regulation of peptidyl-tyrosine phosphorylation}} {{GNF_GO|id=GO:0050999 |text = regulation of nitric-oxide synthase activity}} {{GNF_GO|id=GO:0051205 |text = protein insertion into membrane}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1956
| Hs_Ensembl = ENSG00000146648
| Hs_RefseqProtein = NP_005219
| Hs_RefseqmRNA = NM_005228
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 55054219
| Hs_GenLoc_end = 55242524
| Hs_Uniprot = P00533
| Mm_EntrezGene = 13649
| Mm_Ensembl = ENSMUSG00000020122
| Mm_RefseqmRNA = NM_007912
| Mm_RefseqProtein = NP_031938
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 16652206
| Mm_GenLoc_end = 16813912
| Mm_Uniprot = Q3TQS6
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Carpenter G |title=Receptors for epidermal growth factor and other polypeptide mitogens. |journal=Annu. Rev. Biochem. |volume=56 |issue= |pages= 881-914 |year= 1987 |pmid= 3039909 |doi= 10.1146/annurev.bi.56.070187.004313 }}
*{{cite journal | author=Boonstra J, Rijken P, Humbel B, ''et al.'' |title=The epidermal growth factor. |journal=Cell Biol. Int. |volume=19 |issue= 5 |pages= 413-30 |year= 1995 |pmid= 7640657 |doi= }}
*{{cite journal | author=Carpenter G |title=The EGF receptor: a nexus for trafficking and signaling. |journal=Bioessays |volume=22 |issue= 8 |pages= 697-707 |year= 2000 |pmid= 10918300 |doi= 10.1002/1521-1878(200008)22:8<697::AID-BIES3>3.0.CO;2-1 }}
*{{cite journal | author=Filardo EJ |title=Epidermal growth factor receptor (EGFR) transactivation by estrogen via the G-protein-coupled receptor, GPR30: a novel signaling pathway with potential significance for breast cancer. |journal=J. Steroid Biochem. Mol. Biol. |volume=80 |issue= 2 |pages= 231-8 |year= 2002 |pmid= 11897506 |doi= }}
*{{cite journal | author=Tiganis T |title=Protein tyrosine phosphatases: dephosphorylating the epidermal growth factor receptor. |journal=IUBMB Life |volume=53 |issue= 1 |pages= 3-14 |year= 2002 |pmid= 12018405 |doi= }}
*{{cite journal | author=Di Fiore PP, Scita G |title=Eps8 in the midst of GTPases. |journal=Int. J. Biochem. Cell Biol. |volume=34 |issue= 10 |pages= 1178-83 |year= 2002 |pmid= 12127568 |doi= }}
*{{cite journal | author=Benaim G, Villalobo A |title=Phosphorylation of calmodulin. Functional implications. |journal=Eur. J. Biochem. |volume=269 |issue= 15 |pages= 3619-31 |year= 2002 |pmid= 12153558 |doi= }}
*{{cite journal | author=Leu TH, Maa MC |title=Functional implication of the interaction between EGF receptor and c-Src. |journal=Front. Biosci. |volume=8 |issue= |pages= s28-38 |year= 2004 |pmid= 12456372 |doi= }}
*{{cite journal | author=Anderson NL, Anderson NG |title=The human plasma proteome: history, character, and diagnostic prospects. |journal=Mol. Cell Proteomics |volume=1 |issue= 11 |pages= 845-67 |year= 2003 |pmid= 12488461 |doi= }}
*{{cite journal | author=Kari C, Chan TO, Rocha de Quadros M, Rodeck U |title=Targeting the epidermal growth factor receptor in cancer: apoptosis takes center stage. |journal=Cancer Res. |volume=63 |issue= 1 |pages= 1-5 |year= 2003 |pmid= 12517767 |doi= }}
*{{cite journal | author=Bonaccorsi L, Muratori M, Carloni V, ''et al.'' |title=Androgen receptor and prostate cancer invasion. |journal=Int. J. Androl. |volume=26 |issue= 1 |pages= 21-5 |year= 2003 |pmid= 12534934 |doi= }}
*{{cite journal | author=Reiter JL, Maihle NJ |title=Characterization and expression of novel 60-kDa and 110-kDa EGFR isoforms in human placenta. |journal=Ann. N. Y. Acad. Sci. |volume=995 |issue= |pages= 39-47 |year= 2003 |pmid= 12814937 |doi= }}
*{{cite journal | author=Adams TE, McKern NM, Ward CW |title=Signalling by the type 1 insulin-like growth factor receptor: interplay with the epidermal growth factor receptor. |journal=Growth Factors |volume=22 |issue= 2 |pages= 89-95 |year= 2005 |pmid= 15253384 |doi= }}
*{{cite journal | author=Ferguson KM |title=Active and inactive conformations of the epidermal growth factor receptor. |journal=Biochem. Soc. Trans. |volume=32 |issue= Pt 5 |pages= 742-5 |year= 2005 |pmid= 15494003 |doi= 10.1042/BST0320742 }}
*{{cite journal | author=Chao C, Hellmich MR |title=Bi-directional signaling between gastrointestinal peptide hormone receptors and epidermal growth factor receptor. |journal=Growth Factors |volume=22 |issue= 4 |pages= 261-8 |year= 2005 |pmid= 15621729 |doi= 10.1080/08977190412331286900 }}
*{{cite journal | author=Carlsson J, Ren ZP, Wester K, ''et al.'' |title=Planning for intracavitary anti-EGFR radionuclide therapy of gliomas. Literature review and data on EGFR expression. |journal=J. Neurooncol. |volume=77 |issue= 1 |pages= 33-45 |year= 2006 |pmid= 16200342 |doi= 10.1007/s11060-005-7410-z }}
*{{cite journal | author=Scartozzi M, Pierantoni C, Berardi R, ''et al.'' |title=Epidermal growth factor receptor: a promising therapeutic target for colorectal cancer. |journal=Anal. Quant. Cytol. Histol. |volume=28 |issue= 2 |pages= 61-8 |year= 2006 |pmid= 16637508 |doi= }}
*{{cite journal | author=Prudkin L, Wistuba II |title=Epidermal growth factor receptor abnormalities in lung cancer. Pathogenetic and clinical implications. |journal=Annals of diagnostic pathology |volume=10 |issue= 5 |pages= 306-15 |year= 2006 |pmid= 16979526 |doi= 10.1016/j.anndiagpath.2006.06.011 }}
*{{cite journal | author=Ahmed SM, Salgia R |title=Epidermal growth factor receptor mutations and susceptibility to targeted therapy in lung cancer. |journal=Respirology |volume=11 |issue= 6 |pages= 687-92 |year= 2007 |pmid= 17052295 |doi= 10.1111/j.1440-1843.2006.00887.x }}
*{{cite journal | author=Zhang X, Chang A |title=Somatic mutations of the epidermal growth factor receptor and non-small-cell lung cancer. |journal=J. Med. Genet. |volume=44 |issue= 3 |pages= 166-72 |year= 2007 |pmid= 17158592 |doi= 10.1136/jmg.2006.046102 }}
*{{cite journal | author=Cohenuram M, Saif MW |title=Epidermal growth factor receptor inhibition strategies in pancreatic cancer: past, present and the future. |journal=JOP |volume=8 |issue= 1 |pages= 4-15 |year= 2007 |pmid= 17228128 |doi= }}
*{{cite journal | author=Mellinghoff IK, Cloughesy TF, Mischel PS |title=PTEN-mediated resistance to epidermal growth factor receptor kinase inhibitors. |journal=Clin. Cancer Res. |volume=13 |issue= 2 Pt 1 |pages= 378-81 |year= 2007 |pmid= 17255257 |doi= 10.1158/1078-0432.CCR-06-1992 }}
*{{cite journal | author=Nakamura JL |title=The epidermal growth factor receptor in malignant gliomas: pathogenesis and therapeutic implications. |journal=Expert Opin. Ther. Targets |volume=11 |issue= 4 |pages= 463-72 |year= 2007 |pmid= 17373877 |doi= 10.1517/14728222.11.4.463 }}
}}
{{refend}}
ERBB2
- REDIRECT: Protein Redirected to: HER2 {September 10, 2007 2:15:44 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: HER2. Invoking a Mandantory Inspection. {September 10, 2007 2:15:47 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''V-erb-b2 erythroblastic leukemia viral oncogene homolog 2, neuro/glioblastoma derived oncogene homolog (avian)''', also known as '''ERBB2''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ERBB2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1n8z.
| PDB = {{PDB2|1n8z}}, {{PDB2|1s78}}, {{PDB2|2a91}}
| Name = V-erb-b2 erythroblastic leukemia viral oncogene homolog 2, neuro/glioblastoma derived oncogene homolog (avian)
| HGNCid = 3430
| Symbol = ERBB2
| AltSymbols =; HER-2; HER-2/neu; HER2; NEU; NGL; TKR1; c-erb B2
| OMIM = 164870
| ECnumber =
| Homologene = 3273
| MGIid = 95410
| GeneAtlas_image1 = PBB_GE_ERBB2_216836_s_at.png
| GeneAtlas_image2 = PBB_GE_ERBB2_210930_s_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004715 |text = non-membrane spanning protein tyrosine kinase activity}} {{GNF_GO|id=GO:0004716 |text = receptor signaling protein tyrosine kinase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005006 |text = epidermal growth factor receptor activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}} {{GNF_GO|id=GO:0043125 |text = ErbB-3 class receptor binding}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0016324 |text = apical plasma membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0007422 |text = peripheral nervous system development}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0030879 |text = mammary gland development}} {{GNF_GO|id=GO:0042552 |text = myelination}} {{GNF_GO|id=GO:0043406 |text = positive regulation of MAPK activity}} {{GNF_GO|id=GO:0045765 |text = regulation of angiogenesis}} {{GNF_GO|id=GO:0048015 |text = phosphoinositide-mediated signaling}} {{GNF_GO|id=GO:0050679 |text = positive regulation of epithelial cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2064
| Hs_Ensembl = ENSG00000141736
| Hs_RefseqProtein = NP_001005862
| Hs_RefseqmRNA = NM_001005862
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 35104766
| Hs_GenLoc_end = 35138441
| Hs_Uniprot = P04626
| Mm_EntrezGene = 13866
| Mm_Ensembl = ENSMUSG00000062312
| Mm_RefseqmRNA = NM_001003817
| Mm_RefseqProtein = NP_001003817
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 98228574
| Mm_GenLoc_end = 98253806
| Mm_Uniprot = Q80Y89
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the epidermal growth factor (EGF) receptor family of receptor tyrosine kinases. This protein has no ligand binding domain of its own and therefore cannot bind growth factors. However, it does bind tightly to other ligand-bound EGF receptor family members to form a heterodimer, stabilizing ligand binding and enhancing kinase-mediated activation of downstream signalling pathways, such as those involving mitogen-activated protein kinase and phosphatidylinositol-3 kinase. Allelic variations at amino acid positions 654 and 655 of isoform a (positions 624 and 625 of isoform b) have been reported, with the most common allele, Ile654/Ile655, shown here. Amplification and/or overexpression of this gene has been reported in numerous cancers, including breast and ovarian tumors. Alternative splicing results in several additional transcript variants, some encoding different isoforms and others that have not been fully characterized.<ref>{{cite web | title = Entrez Gene: ERBB2 v-erb-b2 erythroblastic leukemia viral oncogene homolog 2, neuro/glioblastoma derived oncogene homolog (avian)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2064| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ross JS, Fletcher JA, Linette GP, ''et al.'' |title=The Her-2/neu gene and protein in breast cancer 2003: biomarker and target of therapy. |journal=Oncologist |volume=8 |issue= 4 |pages= 307-25 |year= 2003 |pmid= 12897328 |doi= }}
*{{cite journal | author=Zhou BP, Hung MC |title=Dysregulation of cellular signaling by HER2/neu in breast cancer. |journal=Semin. Oncol. |volume=30 |issue= 5 Suppl 16 |pages= 38-48 |year= 2003 |pmid= 14613025 |doi= }}
*{{cite journal | author=Ménard S, Casalini P, Campiglio M, ''et al.'' |title=Role of HER2/neu in tumor progression and therapy. |journal=Cell. Mol. Life Sci. |volume=61 |issue= 23 |pages= 2965-78 |year= 2005 |pmid= 15583858 |doi= 10.1007/s00018-004-4277-7 }}
*{{cite journal | author=Becker JC, Muller-Tidow C, Serve H, ''et al.'' |title=Role of receptor tyrosine kinases in gastric cancer: new targets for a selective therapy. |journal=World J. Gastroenterol. |volume=12 |issue= 21 |pages= 3297-305 |year= 2006 |pmid= 16733844 |doi= }}
*{{cite journal | author=Laudadio J, Quigley DI, Tubbs R, Wolff DJ |title=HER2 testing: a review of detection methodologies and their clinical performance. |journal=Expert Rev. Mol. Diagn. |volume=7 |issue= 1 |pages= 53-64 |year= 2007 |pmid= 17187484 |doi= 10.1586/14737159.7.1.53 }}
*{{cite journal | author=Bianchi F, Tagliabue E, Ménard S, Campiglio M |title=Fhit expression protects against HER2-driven breast tumor development: unraveling the molecular interconnections. |journal=Cell Cycle |volume=6 |issue= 6 |pages= 643-6 |year= 2007 |pmid= 17374991 |doi= }}
}}
{{refend}}
ESR1
- REDIRECT: Protein Redirected to: Estrogen receptor {September 10, 2007 2:15:56 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: Estrogen receptor. Invoking a Mandantory Inspection. {September 10, 2007 2:16:00 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Estrogen receptor 1''', also known as '''ESR1''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ESR1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a52.
| PDB = {{PDB2|1a52}}, {{PDB2|1ere}}, {{PDB2|1err}}, {{PDB2|1g50}}, {{PDB2|1gwq}}, {{PDB2|1gwr}}, {{PDB2|1hcp}}, {{PDB2|1hcq}}, {{PDB2|1l2i}}, {{PDB2|1pcg}}, {{PDB2|1qkt}}, {{PDB2|1qku}}, {{PDB2|1r5k}}, {{PDB2|1sj0}}, {{PDB2|1uom}}, {{PDB2|1x7e}}, {{PDB2|1x7r}}, {{PDB2|1xp1}}, {{PDB2|1xp6}}, {{PDB2|1xp9}}, {{PDB2|1xpc}}, {{PDB2|1xqc}}, {{PDB2|1yim}}, {{PDB2|1yin}}, {{PDB2|1zky}}, {{PDB2|2ayr}}, {{PDB2|2b1v}}, {{PDB2|2b1z}}, {{PDB2|2b23}}, {{PDB2|2bj4}}, {{PDB2|2fai}}, {{PDB2|2g44}}, {{PDB2|2g5o}}, {{PDB2|2i0j}}, {{PDB2|2jf9}}, {{PDB2|2jfa}}, {{PDB2|2ouz}}, {{PDB2|2p15}}, {{PDB2|3erd}}, {{PDB2|3ert}}
| Name = Estrogen receptor 1
| HGNCid = 3467
| Symbol = ESR1
| AltSymbols =; ER; DKFZp686N23123; ESR; ESRA; Era; NR3A1
| OMIM = 133430
| ECnumber =
| Homologene = 47906
| MGIid = 1352467
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005496 |text = steroid binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0030235 |text = nitric-oxide synthase regulator activity}} {{GNF_GO|id=GO:0030284 |text = estrogen receptor activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016585 |text = chromatin remodeling complex}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0016049 |text = cell growth}} {{GNF_GO|id=GO:0030520 |text = estrogen receptor signaling pathway}} {{GNF_GO|id=GO:0045839 |text = negative regulation of mitosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2099
| Hs_Ensembl = ENSG00000091831
| Hs_RefseqProtein = NP_000116
| Hs_RefseqmRNA = NM_000125
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 152170379
| Hs_GenLoc_end = 152466099
| Hs_Uniprot = P03372
| Mm_EntrezGene = 13982
| Mm_Ensembl = ENSMUSG00000019768
| Mm_RefseqmRNA = XM_985634
| Mm_RefseqProtein = XP_990728
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 5342780
| Mm_GenLoc_end = 5734495
| Mm_Uniprot = Q3UT58
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The estrogen receptor (ESR) is a ligand-activated transcription factor composed of several domains important for hormone binding, DNA binding, and activation of transcription. Alternative splicing results in several ESR1 mRNA transcripts, which differ primarily in their 5-prime untranslated regions. The translated receptors show less variability.[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: ESR1 estrogen receptor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2099| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=McDonnell DP, Norris JD |title=Connections and regulation of the human estrogen receptor. |journal=Science |volume=296 |issue= 5573 |pages= 1642-4 |year= 2002 |pmid= 12040178 |doi= 10.1126/science.1071884 }}
*{{cite journal | author=Simoncini T, Fornari L, Mannella P, ''et al.'' |title=Novel non-transcriptional mechanisms for estrogen receptor signaling in the cardiovascular system. Interaction of estrogen receptor alpha with phosphatidylinositol 3-OH kinase. |journal=Steroids |volume=67 |issue= 12 |pages= 935-9 |year= 2003 |pmid= 12398989 |doi= }}
*{{cite journal | author=Lannigan DA |title=Estrogen receptor phosphorylation. |journal=Steroids |volume=68 |issue= 1 |pages= 1-9 |year= 2003 |pmid= 12475718 |doi= }}
*{{cite journal | author=Herrington DM |title=Role of estrogen receptor-alpha in pharmacogenetics of estrogen action. |journal=Curr. Opin. Lipidol. |volume=14 |issue= 2 |pages= 145-50 |year= 2003 |pmid= 12642782 |doi= 10.1097/01.mol.0000064045.68936.23 }}
*{{cite journal | author=Tanaka Y, Sasaki M, Kaneuchi M, ''et al.'' |title=Estrogen receptor alpha polymorphisms and renal cell carcinoma--a possible risk. |journal=Mol. Cell. Endocrinol. |volume=202 |issue= 1-2 |pages= 109-16 |year= 2004 |pmid= 12770739 |doi= }}
*{{cite journal | author=Ali S, Coombes RC |title=Estrogen receptor alpha in human breast cancer: occurrence and significance. |journal=Journal of mammary gland biology and neoplasia |volume=5 |issue= 3 |pages= 271-81 |year= 2004 |pmid= 14973389 |doi= }}
*{{cite journal | author=Olsson H |title=Estrogen receptor content in malignant breast tumors in men--a review. |journal=Journal of mammary gland biology and neoplasia |volume=5 |issue= 3 |pages= 283-7 |year= 2004 |pmid= 14973390 |doi= }}
*{{cite journal | author=Surmacz E, Bartucci M |title=Role of estrogen receptor alpha in modulating IGF-I receptor signaling and function in breast cancer. |journal=J. Exp. Clin. Cancer Res. |volume=23 |issue= 3 |pages= 385-94 |year= 2005 |pmid= 15595626 |doi= }}
*{{cite journal | author=Evinger AJ, Levin ER |title=Requirements for estrogen receptor alpha membrane localization and function. |journal=Steroids |volume=70 |issue= 5-7 |pages= 361-3 |year= 2005 |pmid= 15862818 |doi= 10.1016/j.steroids.2005.02.015 }}
*{{cite journal | author=Wang CL, Tang XY, Chen WQ, ''et al.'' |title=Association of estrogen receptor alpha gene polymorphisms with bone mineral density in Chinese women: a meta-analysis. |journal=Osteoporosis international : a journal established as result of cooperation between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA |volume=18 |issue= 3 |pages= 295-305 |year= 2007 |pmid= 17089081 |doi= 10.1007/s00198-006-0239-2 }}
}}
{{refend}}
HIF1A
- REDIRECT: Protein Redirected to: HIF1A {September 10, 2007 2:16:17 PM PDT}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {September 10, 2007 2:16:21 PM PDT}
- UPDATE SUMMARY: Updating Summary, No Errors. {September 10, 2007 2:16:21 PM PDT}
- UPDATE CITATIONS: Updating Citations, No Errors. {September 10, 2007 2:16:21 PM PDT}
- UPDATED: Updated protein page: HIF1A {September 10, 2007 2:16:28 PM PDT}
HLA-B
- REDIRECT: Protein Redirected to: HLA-B {September 10, 2007 2:16:43 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: HLA-B. Invoking a Mandantory Inspection. {September 10, 2007 2:16:46 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Major histocompatibility complex, class I, B''', also known as '''HLA-B''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_HLA-B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a1n.
| PDB = {{PDB2|1a1n}}, {{PDB2|1a9b}}, {{PDB2|1a9e}}, {{PDB2|1agb}}, {{PDB2|1agc}}, {{PDB2|1agd}}, {{PDB2|1age}}, {{PDB2|1agf}}, {{PDB2|1cg9}}, {{PDB2|1e27}}, {{PDB2|1e28}}, {{PDB2|1efx}}, {{PDB2|1hsa}}, {{PDB2|1jgd}}, {{PDB2|1jge}}, {{PDB2|1k5n}}, {{PDB2|1m05}}, {{PDB2|1mi5}}, {{PDB2|1of2}}, {{PDB2|1ogt}}, {{PDB2|1uxs}}, {{PDB2|1uxw}}, {{PDB2|1w0v}}, {{PDB2|1w0w}}, {{PDB2|1xh3}}, {{PDB2|1xr8}}, {{PDB2|1xr9}}, {{PDB2|1zhk}}, {{PDB2|1zhl}}, {{PDB2|1zsd}}, {{PDB2|2a83}}, {{PDB2|2ak4}}, {{PDB2|2axf}}, {{PDB2|2axg}}, {{PDB2|2bsr}}, {{PDB2|2bss}}, {{PDB2|2bst}}, {{PDB2|2cik}}, {{PDB2|2fyy}}, {{PDB2|2fz3}}, {{PDB2|2h6p}}, {{PDB2|2nw3}}, {{PDB2|2nx5}}
| Name = Major histocompatibility complex, class I, B
| HGNCid = 4932
| Symbol = HLA-B
| AltSymbols =; HLA B; SPDA1
| OMIM = 142830
| ECnumber =
| Homologene = 83181
| MGIid =
| GeneAtlas_image1 = PBB_GE_HLA-B_209140_x_at.png
| GeneAtlas_image2 = PBB_GE_HLA-B_208729_x_at.png
| GeneAtlas_image3 = PBB_GE_HLA-B_211911_x_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0032393 |text = MHC class I receptor activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042612 |text = MHC class I protein complex}}
| Process = {{GNF_GO|id=GO:0002474 |text = antigen processing and presentation of peptide antigen via MHC class I}} {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0019882 |text = antigen processing and presentation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3106
| Hs_Ensembl = ENSG00000204523
| Hs_RefseqProtein = NP_005505
| Hs_RefseqmRNA = NM_005514
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 31429622
| Hs_GenLoc_end = 31433001
| Hs_Uniprot = P01889
| Mm_EntrezGene = 547349
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_001025208
| Mm_RefseqProtein = NP_001020379
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = HLA-B belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45 kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exon 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-B alleles have been described<ref>{{cite web | title = Entrez Gene: HLA-B major histocompatibility complex, class I, B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3106| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Parham P, Benjamin RJ, Chen BP, ''et al.'' |title=Diversity of class I HLA molecules: functional and evolutionary interactions with T cells. |journal=Cold Spring Harb. Symp. Quant. Biol. |volume=54 Pt 1 |issue= |pages= 529-43 |year= 1990 |pmid= 2700944 |doi= }}
*{{cite journal | author=Geyer M, Fackler OT, Peterlin BM |title=Structure--function relationships in HIV-1 Nef. |journal=EMBO Rep. |volume=2 |issue= 7 |pages= 580-5 |year= 2001 |pmid= 11463741 |doi= 10.1093/embo-reports/kve141 }}
*{{cite journal | author=Greenway AL, Holloway G, McPhee DA, ''et al.'' |title=HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication. |journal=J. Biosci. |volume=28 |issue= 3 |pages= 323-35 |year= 2004 |pmid= 12734410 |doi= }}
*{{cite journal | author=Bénichou S, Benmerah A |title=[The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: "parasites"of the endocytosis pathway] |journal=Med Sci (Paris) |volume=19 |issue= 1 |pages= 100-6 |year= 2003 |pmid= 12836198 |doi= }}
*{{cite journal | author=Piancatelli D, Canossi A, Aureli A, ''et al.'' |title=Human leukocyte antigen-A, -B, and -Cw polymorphism in a Berber population from North Morocco using sequence-based typing. |journal=Tissue Antigens |volume=63 |issue= 2 |pages= 158-72 |year= 2004 |pmid= 14705987 |doi= }}
*{{cite journal | author=Leavitt SA, SchOn A, Klein JC, ''et al.'' |title=Interactions of HIV-1 proteins gp120 and Nef with cellular partners define a novel allosteric paradigm. |journal=Curr. Protein Pept. Sci. |volume=5 |issue= 1 |pages= 1-8 |year= 2004 |pmid= 14965316 |doi= }}
*{{cite journal | author=Arayssi T, Hamdan A |title=New insights into the pathogenesis and therapy of Behçet's disease. |journal=Current opinion in pharmacology |volume=4 |issue= 2 |pages= 183-8 |year= 2004 |pmid= 15063364 |doi= 10.1016/j.coph.2003.10.009 }}
*{{cite journal | author=Tolstrup M, Ostergaard L, Laursen AL, ''et al.'' |title=HIV/SIV escape from immune surveillance: focus on Nef. |journal=Curr. HIV Res. |volume=2 |issue= 2 |pages= 141-51 |year= 2004 |pmid= 15078178 |doi= }}
*{{cite journal | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87-94 |year= 2005 |pmid= 15638726 |doi= }}
*{{cite journal | author=Anderson JL, Hope TJ |title=HIV accessory proteins and surviving the host cell. |journal=Current HIV/AIDS reports |volume=1 |issue= 1 |pages= 47-53 |year= 2005 |pmid= 16091223 |doi= }}
*{{cite journal | author=Grubić Z |title=[Hla-B27 gene: polymorphism, evolution, distribution, and association with spondyloartopathies] |journal=Reumatizam |volume=53 |issue= 1 |pages= 5-10 |year= 2007 |pmid= 17580542 |doi= }}
}}
{{refend}}
IGF1
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Insulin-like growth factor 1 (somatomedin C)''', also known as '''IGF1''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_IGF1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bqt.
| PDB = {{PDB2|1bqt}}, {{PDB2|1gzr}}, {{PDB2|1gzy}}, {{PDB2|1gzz}}, {{PDB2|1h02}}, {{PDB2|1h59}}, {{PDB2|1imx}}, {{PDB2|1pmx}}, {{PDB2|1wqj}}, {{PDB2|2dsp}}, {{PDB2|2dsq}}, {{PDB2|2dsr}}, {{PDB2|2gf1}}, {{PDB2|3gf1}}, {{PDB2|3lri}}
| Name = Insulin-like growth factor 1 (somatomedin C)
| HGNCid = 5464
| Symbol = IGF1
| AltSymbols =; IGFI
| OMIM = 147440
| ECnumber =
| Homologene = 515
| MGIid = 96432
| GeneAtlas_image1 = PBB_GE_IGF1_209541_at.png
| GeneAtlas_image2 = PBB_GE_IGF1_209540_at.png
| GeneAtlas_image3 = PBB_GE_IGF1_209542_x_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0005159 |text = insulin-like growth factor receptor binding}} {{GNF_GO|id=GO:0005179 |text = hormone activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0018445 |text = prothoracicotrophic hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0006260 |text = DNA replication}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007265 |text = Ras protein signal transduction}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007517 |text = muscle development}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0009441 |text = glycolate metabolic process}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0010001 |text = glial cell differentiation}} {{GNF_GO|id=GO:0048009 |text = insulin-like growth factor receptor signaling pathway}} {{GNF_GO|id=GO:0048468 |text = cell development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3479
| Hs_Ensembl = ENSG00000017427
| Hs_RefseqProtein = NP_000609
| Hs_RefseqmRNA = NM_000618
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 101313809
| Hs_GenLoc_end = 101398471
| Hs_Uniprot = P01343
| Mm_EntrezGene = 16000
| Mm_Ensembl = ENSMUSG00000020053
| Mm_RefseqmRNA = NM_010512
| Mm_RefseqProtein = NP_034642
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 87288867
| Mm_GenLoc_end = 87361600
| Mm_Uniprot = Q4VJC0
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: IGF1 insulin-like growth factor 1 (somatomedin C)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3479| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Butler AA, Yakar S, LeRoith D |title=Insulin-like growth factor-I: compartmentalization within the somatotropic axis? |journal=News Physiol. Sci. |volume=17 |issue= |pages= 82-5 |year= 2002 |pmid= 11909998 |doi= }}
*{{cite journal | author=Maccario M, Tassone F, Grottoli S, ''et al.'' |title=Neuroendocrine and metabolic determinants of the adaptation of GH/IGF-I axis to obesity. |journal=Ann. Endocrinol. (Paris) |volume=63 |issue= 2 Pt 1 |pages= 140-4 |year= 2002 |pmid= 11994678 |doi= }}
*{{cite journal | author=Camacho-Hübner C, Woods KA, Clark AJ, Savage MO |title=Insulin-like growth factor (IGF)-I gene deletion. |journal=Reviews in endocrine & metabolic disorders |volume=3 |issue= 4 |pages= 357-61 |year= 2003 |pmid= 12424437 |doi= }}
*{{cite journal | author=Trojan LA, Kopinski P, Wei MX, ''et al.'' |title=IGF-I: from diagnostic to triple-helix gene therapy of solid tumors. |journal=Acta Biochim. Pol. |volume=49 |issue= 4 |pages= 979-90 |year= 2004 |pmid= 12545204 |doi= 024904979 }}
*{{cite journal | author=Winn N, Paul A, Musaró A, Rosenthal N |title=Insulin-like growth factor isoforms in skeletal muscle aging, regeneration, and disease. |journal=Cold Spring Harb. Symp. Quant. Biol. |volume=67 |issue= |pages= 507-18 |year= 2003 |pmid= 12858577 |doi= }}
*{{cite journal | author=Delafontaine P, Song YH, Li Y |title=Expression, regulation, and function of IGF-1, IGF-1R, and IGF-1 binding proteins in blood vessels. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 3 |pages= 435-44 |year= 2005 |pmid= 14604834 |doi= 10.1161/01.ATV.0000105902.89459.09 }}
*{{cite journal | author=Trejo JL, Carro E, Garcia-Galloway E, Torres-Aleman I |title=Role of insulin-like growth factor I signaling in neurodegenerative diseases. |journal=J. Mol. Med. |volume=82 |issue= 3 |pages= 156-62 |year= 2004 |pmid= 14647921 |doi= 10.1007/s00109-003-0499-7 }}
*{{cite journal | author=Rabinovsky ED |title=The multifunctional role of IGF-1 in peripheral nerve regeneration. |journal=Neurol. Res. |volume=26 |issue= 2 |pages= 204-10 |year= 2004 |pmid= 15072640 |doi= 10.1179/016164104225013851 }}
*{{cite journal | author=Rincon M, Muzumdar R, Atzmon G, Barzilai N |title=The paradox of the insulin/IGF-1 signaling pathway in longevity. |journal=Mech. Ageing Dev. |volume=125 |issue= 6 |pages= 397-403 |year= 2005 |pmid= 15272501 |doi= }}
*{{cite journal | author=Conti E, Carrozza C, Capoluongo E, ''et al.'' |title=Insulin-like growth factor-1 as a vascular protective factor. |journal=Circulation |volume=110 |issue= 15 |pages= 2260-5 |year= 2005 |pmid= 15477425 |doi= 10.1161/01.CIR.0000144309.87183.FB }}
*{{cite journal | author=Wood AW, Duan C, Bern HA |title=Insulin-like growth factor signaling in fish. |journal=Int. Rev. Cytol. |volume=243 |issue= |pages= 215-85 |year= 2005 |pmid= 15797461 |doi= 10.1016/S0074-7696(05)43004-1 }}
*{{cite journal | author=Sandhu MS |title=Insulin-like growth factor-I and risk of type 2 diabetes and coronary heart disease: molecular epidemiology. |journal=Endocrine development |volume=9 |issue= |pages= 44-54 |year= 2005 |pmid= 15879687 |doi= 10.1159/000085755 }}
*{{cite journal | author=Ye P, D'Ercole AJ |title=Insulin-like growth factor actions during development of neural stem cells and progenitors in the central nervous system. |journal=J. Neurosci. Res. |volume=83 |issue= 1 |pages= 1-6 |year= 2006 |pmid= 16294334 |doi= 10.1002/jnr.20688 }}
*{{cite journal | author=Gómez JM |title=The role of insulin-like growth factor I components in the regulation of vitamin D. |journal=Current pharmaceutical biotechnology |volume=7 |issue= 2 |pages= 125-32 |year= 2006 |pmid= 16724947 |doi= }}
*{{cite journal | author=Federico G, Street ME, Maghnie M, ''et al.'' |title=Assessment of serum IGF-I concentrations in the diagnosis of isolated childhood-onset GH deficiency: a proposal of the Italian Society for Pediatric Endocrinology and Diabetes (SIEDP/ISPED). |journal=J. Endocrinol. Invest. |volume=29 |issue= 8 |pages= 732-7 |year= 2006 |pmid= 17033263 |doi= }}
*{{cite journal | author=Zakula Z, Koricanac G, Putnikovic B, ''et al.'' |title=Regulation of the inducible nitric oxide synthase and sodium pump in type 1 diabetes. |journal=Med. Hypotheses |volume=69 |issue= 2 |pages= 302-6 |year= 2007 |pmid= 17289286 |doi= 10.1016/j.mehy.2006.11.045 }}
*{{cite journal | author=Trojan J, Cloix JF, Ardourel MY, ''et al.'' |title=Insulin-like growth factor type I biology and targeting in malignant gliomas. |journal=Neuroscience |volume=145 |issue= 3 |pages= 795-811 |year= 2007 |pmid= 17320297 |doi= 10.1016/j.neuroscience.2007.01.021 }}
}}
{{refend}}
IL10
- REDIRECT: Protein Redirected to: Interleukin_10 {September 10, 2007 2:18:19 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: Interleukin_10. Invoking a Mandantory Inspection. {September 10, 2007 2:18:25 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Interleukin 10''', also known as '''IL10''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_IL10_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ilk.
| PDB = {{PDB2|1ilk}}, {{PDB2|1inr}}, {{PDB2|1j7v}}, {{PDB2|1lk3}}, {{PDB2|1vlk}}, {{PDB2|1y6k}}, {{PDB2|1y6m}}, {{PDB2|1y6n}}, {{PDB2|2h24}}, {{PDB2|2ilk}}
| Name = Interleukin 10
| HGNCid = 5962
| Symbol = IL10
| AltSymbols =; CSIF; IL-10; IL10A; MGC126450; MGC126451; TGIF
| OMIM = 124092
| ECnumber =
| Homologene = 478
| MGIid = 96537
| GeneAtlas_image1 = PBB_GE_IL10_207433_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005141 |text = interleukin-10 receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007253 |text = cytoplasmic sequestering of NF-kappaB}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0030097 |text = hemopoiesis}} {{GNF_GO|id=GO:0030183 |text = B cell differentiation}} {{GNF_GO|id=GO:0030595 |text = leukocyte chemotaxis}} {{GNF_GO|id=GO:0042092 |text = T-helper 2 type immune response}} {{GNF_GO|id=GO:0042100 |text = B cell proliferation}} {{GNF_GO|id=GO:0042130 |text = negative regulation of T cell proliferation}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}} {{GNF_GO|id=GO:0045019 |text = negative regulation of nitric oxide biosynthetic process}} {{GNF_GO|id=GO:0045077 |text = negative regulation of interferon-gamma biosynthetic process}} {{GNF_GO|id=GO:0045191 |text = regulation of isotype switching}} {{GNF_GO|id=GO:0045347 |text = negative regulation of MHC class II biosynthetic process}} {{GNF_GO|id=GO:0045348 |text = positive regulation of MHC class II biosynthetic process}} {{GNF_GO|id=GO:0045355 |text = negative regulation of interferon-alpha biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3586
| Hs_Ensembl = ENSG00000136634
| Hs_RefseqProtein = NP_000563
| Hs_RefseqmRNA = NM_000572
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 205007570
| Hs_GenLoc_end = 205012462
| Hs_Uniprot = P22301
| Mm_EntrezGene = 16153
| Mm_Ensembl = ENSMUSG00000016529
| Mm_RefseqmRNA = NM_010548
| Mm_RefseqProtein = NP_034678
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 132847393
| Mm_GenLoc_end = 132852516
| Mm_Uniprot = Q0VBJ1
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a cytokine produced primarily by monocytes and to a lesser extent by lymphocytes. This cytokine has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. This cytokine can block NF-kappa B activity, and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract.<ref>{{cite web | title = Entrez Gene: IL10 interleukin 10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3586| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Moore KW, de Waal Malefyt R, Coffman RL, O'Garra A |title=Interleukin-10 and the interleukin-10 receptor. |journal=Annu. Rev. Immunol. |volume=19 |issue= |pages= 683-765 |year= 2001 |pmid= 11244051 |doi= 10.1146/annurev.immunol.19.1.683 }}
*{{cite journal | author=Girndt M |title=Humoral immune responses in uremia and the role of IL-10. |journal=Blood Purif. |volume=20 |issue= 5 |pages= 485-8 |year= 2003 |pmid= 12207099 |doi= }}
*{{cite journal | author=Beebe AM, Cua DJ, de Waal Malefyt R |title=The role of interleukin-10 in autoimmune disease: systemic lupus erythematosus (SLE) and multiple sclerosis (MS). |journal=Cytokine Growth Factor Rev. |volume=13 |issue= 4-5 |pages= 403-12 |year= 2003 |pmid= 12220553 |doi= }}
*{{cite journal | author=Mocellin S, Panelli MC, Wang E, ''et al.'' |title=The dual role of IL-10. |journal=Trends Immunol. |volume=24 |issue= 1 |pages= 36-43 |year= 2004 |pmid= 12495723 |doi= }}
*{{cite journal | author=Roncarolo MG, Battaglia M, Gregori S |title=The role of interleukin 10 in the control of autoimmunity. |journal=J. Autoimmun. |volume=20 |issue= 4 |pages= 269-72 |year= 2004 |pmid= 12791310 |doi= }}
*{{cite journal | author=Groux H, Cottrez F |title=The complex role of interleukin-10 in autoimmunity. |journal=J. Autoimmun. |volume=20 |issue= 4 |pages= 281-5 |year= 2004 |pmid= 12791313 |doi= }}
*{{cite journal | author=Llorente L, Richaud-Patin Y |title=The role of interleukin-10 in systemic lupus erythematosus. |journal=J. Autoimmun. |volume=20 |issue= 4 |pages= 287-9 |year= 2004 |pmid= 12791314 |doi= }}
*{{cite journal | author=Asadullah K, Sabat R, Friedrich M, ''et al.'' |title=Interleukin-10: an important immunoregulatory cytokine with major impact on psoriasis. |journal=Current drug targets. Inflammation and allergy |volume=3 |issue= 2 |pages= 185-92 |year= 2004 |pmid= 15180472 |doi= }}
*{{cite journal | author=Stenvinkel P, Ketteler M, Johnson RJ, ''et al.'' |title=IL-10, IL-6, and TNF-alpha: central factors in the altered cytokine network of uremia--the good, the bad, and the ugly. |journal=Kidney Int. |volume=67 |issue= 4 |pages= 1216-33 |year= 2005 |pmid= 15780075 |doi= 10.1111/j.1523-1755.2005.00200.x }}
*{{cite journal | author=Copeland KF |title=Modulation of HIV-1 transcription by cytokines and chemokines. |journal=Mini reviews in medicinal chemistry |volume=5 |issue= 12 |pages= 1093-101 |year= 2006 |pmid= 16375755 |doi= }}
}}
{{refend}}
IL1B
- REDIRECT: Protein Redirected to: IL1B {September 10, 2007 2:17:30 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: IL1B. Invoking a Mandantory Inspection. {September 10, 2007 2:17:33 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Interleukin 1, beta''', also known as '''IL1B''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_IL1B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hib.
| PDB = {{PDB2|1hib}}, {{PDB2|1i1b}}, {{PDB2|1iob}}, {{PDB2|1itb}}, {{PDB2|1l2h}}, {{PDB2|1s0l}}, {{PDB2|1t4q}}, {{PDB2|1too}}, {{PDB2|1tp0}}, {{PDB2|1twe}}, {{PDB2|1twm}}, {{PDB2|21bi}}, {{PDB2|2i1b}}, {{PDB2|2nvh}}, {{PDB2|31bi}}, {{PDB2|41bi}}, {{PDB2|4i1b}}, {{PDB2|5i1b}}, {{PDB2|6i1b}}, {{PDB2|7i1b}}, {{PDB2|9ilb}}
| Name = Interleukin 1, beta
| HGNCid = 5992
| Symbol = IL1B
| AltSymbols =; IL-1; IL1-BETA; IL1F2
| OMIM = 147720
| ECnumber =
| Homologene = 481
| MGIid = 96543
| GeneAtlas_image1 = PBB_GE_IL1B_39402_at.png
| GeneAtlas_image2 = PBB_GE_IL1B_205067_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005149 |text = interleukin-1 receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0001660 |text = fever}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}} {{GNF_GO|id=GO:0030593 |text = neutrophil chemotaxis}} {{GNF_GO|id=GO:0045080 |text = positive regulation of chemokine biosynthetic process}} {{GNF_GO|id=GO:0045410 |text = positive regulation of interleukin-6 biosynthetic process}} {{GNF_GO|id=GO:0050900 |text = leukocyte migration}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3553
| Hs_Ensembl = ENSG00000125538
| Hs_RefseqProtein = NP_000567
| Hs_RefseqmRNA = NM_000576
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 113303808
| Hs_GenLoc_end = 113310827
| Hs_Uniprot = P01584
| Mm_EntrezGene = 16176
| Mm_Ensembl = ENSMUSG00000027398
| Mm_RefseqmRNA = NM_008361
| Mm_RefseqProtein = NP_032387
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 129056011
| Mm_GenLoc_end = 129062561
| Mm_Uniprot = Q2M4J6
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the interleukin 1 cytokine family. This cytokine is produced by activated macrophages as a proprotein, which is proteolytically processed to its active form by caspase 1 (CASP1/ICE). This cytokine is an important mediator of the inflammatory response, and is involved in a variety of cellular activities, including cell proliferation, differentiation, and apoptosis. The induction of cyclooxygenase-2 (PTGS2/COX2) by this cytokine in the central nervous system (CNS) is found to contribute to inflammatory pain hypersensitivity. This gene and eight other interleukin 1 family genes form a cytokine gene cluster on chromosome 2.<ref>{{cite web | title = Entrez Gene: IL1B interleukin 1, beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3553| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Smirnova MG, Kiselev SL, Gnuchev NV, ''et al.'' |title=Role of the pro-inflammatory cytokines tumor necrosis factor-alpha, interleukin-1 beta, interleukin-6 and interleukin-8 in the pathogenesis of the otitis media with effusion. |journal=Eur. Cytokine Netw. |volume=13 |issue= 2 |pages= 161-72 |year= 2003 |pmid= 12101072 |doi= }}
*{{cite journal | author=Griffin WS, Mrak RE |title=Interleukin-1 in the genesis and progression of and risk for development of neuronal degeneration in Alzheimer's disease. |journal=J. Leukoc. Biol. |volume=72 |issue= 2 |pages= 233-8 |year= 2002 |pmid= 12149413 |doi= }}
*{{cite journal | author=Arend WP |title=The balance between IL-1 and IL-1Ra in disease. |journal=Cytokine Growth Factor Rev. |volume=13 |issue= 4-5 |pages= 323-40 |year= 2003 |pmid= 12220547 |doi= }}
*{{cite journal | author=Chakravorty M, Ghosh A, Choudhury A, ''et al.'' |title=Ethnic differences in allele distribution for the IL8 and IL1B genes in populations from eastern India. |journal=Hum. Biol. |volume=76 |issue= 1 |pages= 153-9 |year= 2004 |pmid= 15222686 |doi= }}
*{{cite journal | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87-94 |year= 2005 |pmid= 15638726 |doi= }}
*{{cite journal | author=Maruyama Y, Stenvinkel P, Lindholm B |title=Role of interleukin-1beta in the development of malnutrition in chronic renal failure patients. |journal=Blood Purif. |volume=23 |issue= 4 |pages= 275-81 |year= 2005 |pmid= 15925866 |doi= 10.1159/000086012 }}
*{{cite journal | author=Roy D, Sarkar S, Felty Q |title=Levels of IL-1 beta control stimulatory/inhibitory growth of cancer cells. |journal=Front. Biosci. |volume=11 |issue= |pages= 889-98 |year= 2006 |pmid= 16146780 |doi= }}
*{{cite journal | author=Copeland KF |title=Modulation of HIV-1 transcription by cytokines and chemokines. |journal=Mini reviews in medicinal chemistry |volume=5 |issue= 12 |pages= 1093-101 |year= 2006 |pmid= 16375755 |doi= }}
*{{cite journal | author=Prinz C, Schwendy S, Voland P |title=H pylori and gastric cancer: shifting the global burden. |journal=World J. Gastroenterol. |volume=12 |issue= 34 |pages= 5458-64 |year= 2006 |pmid= 17006981 |doi= }}
*{{cite journal | author=Kamangar F, Cheng C, Abnet CC, Rabkin CS |title=Interleukin-1B polymorphisms and gastric cancer risk--a meta-analysis. |journal=Cancer Epidemiol. Biomarkers Prev. |volume=15 |issue= 10 |pages= 1920-8 |year= 2007 |pmid= 17035400 |doi= 10.1158/1055-9965.EPI-06-0267 }}
}}
{{refend}}
IL6
- REDIRECT: Protein Redirected to: Interleukin-6 {September 10, 2007 2:17:45 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: Interleukin-6. Invoking a Mandantory Inspection. {September 10, 2007 2:17:48 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Interleukin 6 (interferon, beta 2)''', also known as '''IL6''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_IL6_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1alu.
| PDB = {{PDB2|1alu}}, {{PDB2|1il6}}, {{PDB2|1p9m}}, {{PDB2|2il6}}
| Name = Interleukin 6 (interferon, beta 2)
| HGNCid = 6018
| Symbol = IL6
| AltSymbols =; HGF; BSF2; HSF; IFNB2; IL-6
| OMIM = 147620
| ECnumber =
| Homologene = 502
| MGIid = 96559
| GeneAtlas_image1 = PBB_GE_IL6_205207_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005138 |text = interleukin-6 receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0001781 |text = neutrophil apoptosis}} {{GNF_GO|id=GO:0006953 |text = acute-phase response}} {{GNF_GO|id=GO:0006959 |text = humoral immune response}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0043066 |text = negative regulation of apoptosis}} {{GNF_GO|id=GO:0045079 |text = negative regulation of chemokine biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3569
| Hs_Ensembl = ENSG00000136244
| Hs_RefseqProtein = NP_000591
| Hs_RefseqmRNA = NM_000600
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 22732028
| Hs_GenLoc_end = 22738091
| Hs_Uniprot = P05231
| Mm_EntrezGene = 16193
| Mm_Ensembl = ENSMUSG00000025746
| Mm_RefseqmRNA = NM_031168
| Mm_RefseqProtein = NP_112445
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 30343948
| Mm_GenLoc_end = 30350755
| Mm_Uniprot = Q0PMN1
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=De Kloet ER, Oitzl MS, Schöbitz B |title=Cytokines and the brain corticosteroid receptor balance: relevance to pathophysiology of neuroendocrine-immune communication. |journal=Psychoneuroendocrinology |volume=19 |issue= 2 |pages= 121-34 |year= 1994 |pmid= 8190832 |doi= }}
*{{cite journal | author=Morishita R, Aoki M, Yo Y, Ogihara T |title=Hepatocyte growth factor as cardiovascular hormone: role of HGF in the pathogenesis of cardiovascular disease. |journal=Endocr. J. |volume=49 |issue= 3 |pages= 273-84 |year= 2003 |pmid= 12201209 |doi= }}
*{{cite journal | author=Ishihara K, Hirano T |title=IL-6 in autoimmune disease and chronic inflammatory proliferative disease. |journal=Cytokine Growth Factor Rev. |volume=13 |issue= 4-5 |pages= 357-68 |year= 2003 |pmid= 12220549 |doi= }}
*{{cite journal | author=Culig Z, Bartsch G, Hobisch A |title=Interleukin-6 regulates androgen receptor activity and prostate cancer cell growth. |journal=Mol. Cell. Endocrinol. |volume=197 |issue= 1-2 |pages= 231-8 |year= 2003 |pmid= 12431817 |doi= }}
*{{cite journal | author=Rattazzi M, Puato M, Faggin E, ''et al.'' |title=C-reactive protein and interleukin-6 in vascular disease: culprits or passive bystanders? |journal=J. Hypertens. |volume=21 |issue= 10 |pages= 1787-803 |year= 2004 |pmid= 14508181 |doi= 10.1097/01.hjh.0000084735.53355.44 }}
*{{cite journal | author=Tackey E, Lipsky PE, Illei GG |title=Rationale for interleukin-6 blockade in systemic lupus erythematosus. |journal=Lupus |volume=13 |issue= 5 |pages= 339-43 |year= 2005 |pmid= 15230289 |doi= }}
*{{cite journal | author=Berger FG |title=The interleukin-6 gene: a susceptibility factor that may contribute to racial and ethnic disparities in breast cancer mortality. |journal=Breast Cancer Res. Treat. |volume=88 |issue= 3 |pages= 281-5 |year= 2005 |pmid= 15609131 |doi= 10.1007/s10549-004-0726-0 }}
*{{cite journal | author=Stenvinkel P, Ketteler M, Johnson RJ, ''et al.'' |title=IL-10, IL-6, and TNF-alpha: central factors in the altered cytokine network of uremia--the good, the bad, and the ugly. |journal=Kidney Int. |volume=67 |issue= 4 |pages= 1216-33 |year= 2005 |pmid= 15780075 |doi= 10.1111/j.1523-1755.2005.00200.x }}
*{{cite journal | author=Vgontzas AN, Bixler EO, Lin HM, ''et al.'' |title=IL-6 and its circadian secretion in humans. |journal=Neuroimmunomodulation |volume=12 |issue= 3 |pages= 131-40 |year= 2005 |pmid= 15905620 |doi= 10.1159/000084844 }}
*{{cite journal | author=Jones SA |title=Directing transition from innate to acquired immunity: defining a role for IL-6. |journal=J. Immunol. |volume=175 |issue= 6 |pages= 3463-8 |year= 2005 |pmid= 16148087 |doi= }}
*{{cite journal | author=Kristiansen OP, Mandrup-Poulsen T |title=Interleukin-6 and diabetes: the good, the bad, or the indifferent? |journal=Diabetes |volume=54 Suppl 2 |issue= |pages= S114-24 |year= 2006 |pmid= 16306329 |doi= }}
*{{cite journal | author=Copeland KF |title=Modulation of HIV-1 transcription by cytokines and chemokines. |journal=Mini reviews in medicinal chemistry |volume=5 |issue= 12 |pages= 1093-101 |year= 2006 |pmid= 16375755 |doi= }}
*{{cite journal | author=Mastorakos G, Ilias I |title=Interleukin-6: a cytokine and/or a major modulator of the response to somatic stress. |journal=Ann. N. Y. Acad. Sci. |volume=1088 |issue= |pages= 373-81 |year= 2007 |pmid= 17192581 |doi= 10.1196/annals.1366.021 }}
*{{cite journal | author=Dubiński A, Zdrojewicz Z |title=[The role of interleukin-6 in development and progression of atherosclerosis] |journal=Pol. Merkur. Lekarski |volume=22 |issue= 130 |pages= 291-4 |year= 2007 |pmid= 17684929 |doi= }}
}}
{{refend}}
IL8
- REDIRECT: Protein Redirected to: Interleukin_8 {September 10, 2007 2:18:01 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: Interleukin_8. Invoking a Mandantory Inspection. {September 10, 2007 2:18:08 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Interleukin 8''', also known as '''IL8''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_IL8_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1icw.
| PDB = {{PDB2|1icw}}, {{PDB2|1ikl}}, {{PDB2|1ikm}}, {{PDB2|1il8}}, {{PDB2|1ilp}}, {{PDB2|1ilq}}, {{PDB2|1qe6}}, {{PDB2|2il8}}, {{PDB2|3il8}}
| Name = Interleukin 8
| HGNCid = 6025
| Symbol = IL8
| AltSymbols =; 3-10C; AMCF-I; CXCL8; GCP-1; GCP1; K60; LECT; LUCT; LYNAP; MDNCF; MONAP; NAF; NAP-1; NAP1; SCYB8; TSG-1; b-ENAP
| OMIM = 146930
| ECnumber =
| Homologene = 47937
| MGIid =
| GeneAtlas_image1 = PBB_GE_IL8_211506_s_at.png
| GeneAtlas_image2 = PBB_GE_IL8_202859_x_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0005153 |text = interleukin-8 receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008009 |text = chemokine activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0019722 |text = calcium-mediated signaling}} {{GNF_GO|id=GO:0030155 |text = regulation of cell adhesion}} {{GNF_GO|id=GO:0030593 |text = neutrophil chemotaxis}} {{GNF_GO|id=GO:0042119 |text = neutrophil activation}} {{GNF_GO|id=GO:0045091 |text = regulation of retroviral genome replication}} {{GNF_GO|id=GO:0050930 |text = induction of positive chemotaxis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3576
| Hs_Ensembl = ENSG00000169429
| Hs_RefseqProtein = NP_000575
| Hs_RefseqmRNA = NM_000584
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 74825139
| Hs_GenLoc_end = 74828295
| Hs_Uniprot = P10145
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the CXC chemokine family. This chemokine is one of the major mediators of the inflammatory response. This chemokine is secreted by several cell types. It functions as a chemoattractant, and is also a potent angiogenic factor. This gene is believed to play a role in the pathogenesis of bronchiolitis, a common respiratory tract disease caused by viral infection. This gene and other ten members of the CXC chemokine gene family form a chemokine gene cluster in a region mapped to chromosome 4q.<ref>{{cite web | title = Entrez Gene: IL8 interleukin 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3576| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Baggiolini M, Clark-Lewis I |title=Interleukin-8, a chemotactic and inflammatory cytokine. |journal=FEBS Lett. |volume=307 |issue= 1 |pages= 97-101 |year= 1992 |pmid= 1639201 |doi= }}
*{{cite journal | author=Wahl SM, Greenwell-Wild T, Hale-Donze H, ''et al.'' |title=Permissive factors for HIV-1 infection of macrophages. |journal=J. Leukoc. Biol. |volume=68 |issue= 3 |pages= 303-10 |year= 2000 |pmid= 10985244 |doi= }}
*{{cite journal | author=Starckx S, Van den Steen PE, Wuyts A, ''et al.'' |title=Neutrophil gelatinase B and chemokines in leukocytosis and stem cell mobilization. |journal=Leuk. Lymphoma |volume=43 |issue= 2 |pages= 233-41 |year= 2003 |pmid= 11999552 |doi= }}
*{{cite journal | author=Smirnova MG, Kiselev SL, Gnuchev NV, ''et al.'' |title=Role of the pro-inflammatory cytokines tumor necrosis factor-alpha, interleukin-1 beta, interleukin-6 and interleukin-8 in the pathogenesis of the otitis media with effusion. |journal=Eur. Cytokine Netw. |volume=13 |issue= 2 |pages= 161-72 |year= 2003 |pmid= 12101072 |doi= }}
*{{cite journal | author=Struyf S, Proost P, Van Damme J |title=Regulation of the immune response by the interaction of chemokines and proteases. |journal=Adv. Immunol. |volume=81 |issue= |pages= 1-44 |year= 2004 |pmid= 14711052 |doi= }}
*{{cite journal | author=Chakravorty M, Ghosh A, Choudhury A, ''et al.'' |title=Ethnic differences in allele distribution for the IL8 and IL1B genes in populations from eastern India. |journal=Hum. Biol. |volume=76 |issue= 1 |pages= 153-9 |year= 2004 |pmid= 15222686 |doi= }}
*{{cite journal | author=Yuan A, Chen JJ, Yao PL, Yang PC |title=The role of interleukin-8 in cancer cells and microenvironment interaction. |journal=Front. Biosci. |volume=10 |issue= |pages= 853-65 |year= 2006 |pmid= 15569594 |doi= }}
*{{cite journal | author=Copeland KF |title=Modulation of HIV-1 transcription by cytokines and chemokines. |journal=Mini reviews in medicinal chemistry |volume=5 |issue= 12 |pages= 1093-101 |year= 2006 |pmid= 16375755 |doi= }}
}}
{{refend}}
ITGB1
- REDIRECT: Protein Redirected to: CD29 {September 10, 2007 2:18:40 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: CD29. Invoking a Mandantory Inspection. {September 10, 2007 2:18:43 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12)''', also known as '''ITGB1''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12)
| HGNCid = 6153
| Symbol = ITGB1
| AltSymbols =; CD29; FNRB; GPIIA; MDF2; MSK12; VLAB
| OMIM = 135630
| ECnumber =
| Homologene = 22999
| MGIid = 96610
| GeneAtlas_image1 = PBB_GE_ITGB1_211945_s_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0001726 |text = ruffle}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007156 |text = homophilic cell adhesion}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0016477 |text = cell migration}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3688
| Hs_Ensembl = ENSG00000150093
| Hs_RefseqProtein = NP_002202
| Hs_RefseqmRNA = NM_002211
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 33229326
| Hs_GenLoc_end = 33287204
| Hs_Uniprot = P05556
| Mm_EntrezGene = 16412
| Mm_Ensembl = ENSMUSG00000025809
| Mm_RefseqmRNA = NM_010578
| Mm_RefseqProtein = NP_034708
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 131591503
| Mm_GenLoc_end = 131618179
| Mm_Uniprot = Q3TIW5
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Integrins are heterodimeric proteins made up of alpha and beta subunits. At least 18 alpha and 8 beta subunits have been described in mammals. Integrin family members are membrane receptors involved in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metatastatic diffusion of tumor cells. The protein encoded by this gene is a beta subunit. Six alternatively spliced variants have been found for this gene which encode five proteins with alternate carboxy termini.<ref>{{cite web | title = Entrez Gene: ITGB1 integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3688| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Evans JP |title=Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization. |journal=Bioessays |volume=23 |issue= 7 |pages= 628-39 |year= 2001 |pmid= 11462216 |doi= 10.1002/bies.1088 }}
*{{cite journal | author=Armulik A |title=Splice variants of human beta 1 integrins: origin, biosynthesis and functions. |journal=Front. Biosci. |volume=7 |issue= |pages= d219-27 |year= 2002 |pmid= 11779688 |doi= }}
*{{cite journal | author=Brakebusch C, Fässler R |title=beta 1 integrin function in vivo: adhesion, migration and more. |journal=Cancer Metastasis Rev. |volume=24 |issue= 3 |pages= 403-11 |year= 2006 |pmid= 16258728 |doi= 10.1007/s10555-005-5132-5 }}
}}
{{refend}}
MAPK1
- REDIRECT: Protein Redirected to: MAPK1 {September 10, 2007 2:20:30 PM PDT}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {September 10, 2007 2:20:31 PM PDT}
- UPDATE SUMMARY: Updating Summary, No Errors. {September 10, 2007 2:20:31 PM PDT}
- UPDATE CITATIONS: Updating Citations, No Errors. {September 10, 2007 2:20:31 PM PDT}
- UPDATED: Updated protein page: MAPK1 {September 10, 2007 2:20:41 PM PDT}
MMP9
- REDIRECT: Protein Redirected to: MMP9 {September 10, 2007 2:18:54 PM PDT}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {September 10, 2007 2:18:55 PM PDT}
- UPDATE SUMMARY: Updating Summary, No Errors. {September 10, 2007 2:18:55 PM PDT}
- UPDATE CITATIONS: Updating Citations, No Errors. {September 10, 2007 2:18:55 PM PDT}
- UPDATED: Updated protein page: MMP9 {September 10, 2007 2:19:02 PM PDT}
NFKB1
- REDIRECT: Protein Redirected to: NFKB1 {September 10, 2007 2:19:26 PM PDT}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {September 10, 2007 2:19:27 PM PDT}
- UPDATE SUMMARY: Updating Summary, No Errors. {September 10, 2007 2:19:27 PM PDT}
- UPDATE CITATIONS: Updating Citations, No Errors. {September 10, 2007 2:19:27 PM PDT}
- UPDATED: Updated protein page: NFKB1 {September 10, 2007 2:19:36 PM PDT}
PPARG
- REDIRECT: Protein Redirected to: PPARG {September 10, 2007 2:19:48 PM PDT}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {September 10, 2007 2:19:50 PM PDT}
- UPDATE SUMMARY: Updating Summary, No Errors. {September 10, 2007 2:19:50 PM PDT}
- UPDATE CITATIONS: Updating Citations, No Errors. {September 10, 2007 2:19:50 PM PDT}
- UPDATED: Updated protein page: PPARG {September 10, 2007 2:19:59 PM PDT}
PRKCA
- REDIRECT: Protein Redirected to: PKC-alpha {September 10, 2007 2:20:06 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: PKC-alpha. Invoking a Mandantory Inspection. {September 10, 2007 2:20:09 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Protein kinase C, alpha''', also known as '''PRKCA''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PRKCA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dsy.
| PDB = {{PDB2|1dsy}}
| Name = Protein kinase C, alpha
| HGNCid = 9393
| Symbol = PRKCA
| AltSymbols =; PRKACA; AAG6; MGC129900; MGC129901; PKC-alpha; PKCA
| OMIM = 176960
| ECnumber =
| Homologene = 55679
| MGIid = 97595
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004698 |text = calcium-dependent protein kinase C activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019992 |text = diacylglycerol binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0000188 |text = inactivation of MAPK activity}} {{GNF_GO|id=GO:0001933 |text = negative regulation of protein amino acid phosphorylation}} {{GNF_GO|id=GO:0001934 |text = positive regulation of protein amino acid phosphorylation}} {{GNF_GO|id=GO:0002026 |text = cardiac inotropy}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006469 |text = negative regulation of protein kinase activity}} {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0006937 |text = regulation of muscle contraction}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0008624 |text = induction of apoptosis by extracellular signals}} {{GNF_GO|id=GO:0008629 |text = induction of apoptosis by intracellular signals}} {{GNF_GO|id=GO:0030593 |text = neutrophil chemotaxis}} {{GNF_GO|id=GO:0046325 |text = negative regulation of glucose import}} {{GNF_GO|id=GO:0046627 |text = negative regulation of insulin receptor signaling pathway}} {{GNF_GO|id=GO:0050729 |text = positive regulation of inflammatory response}} {{GNF_GO|id=GO:0050730 |text = regulation of peptidyl-tyrosine phosphorylation}} {{GNF_GO|id=GO:0050930 |text = induction of positive chemotaxis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5578
| Hs_Ensembl = ENSG00000154229
| Hs_RefseqProtein = NP_002728
| Hs_RefseqmRNA = NM_002737
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 61729388
| Hs_GenLoc_end = 62237324
| Hs_Uniprot = P17252
| Mm_EntrezGene = 18750
| Mm_Ensembl = ENSMUSG00000050965
| Mm_RefseqmRNA = NM_011101
| Mm_RefseqProtein = NP_035231
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 107754338
| Mm_GenLoc_end = 108159844
| Mm_Uniprot = Q4VA93
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This kinase has been reported to play roles in many different cellular processes, such as cell adhesion, cell transformation, cell cycle checkpoint, and cell volume control. Knockout studies in mice suggest that this kinase may be a fundamental regulator of cardiac contractility and Ca(2+) handling in myocytes.<ref>{{cite web | title = Entrez Gene: PRKCA protein kinase C, alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5578| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=O'Brian CA |title=Protein kinase C-alpha: a novel target for the therapy of androgen-independent prostate cancer? (Review-hypothesis). |journal=Oncol. Rep. |volume=5 |issue= 2 |pages= 305-9 |year= 1998 |pmid= 9468546 |doi= }}
*{{cite journal | author=Ali A, Hoeflich KP, Woodgett JR |title=Glycogen synthase kinase-3: properties, functions, and regulation. |journal=Chem. Rev. |volume=101 |issue= 8 |pages= 2527-40 |year= 2002 |pmid= 11749387 |doi= }}
*{{cite journal | author=Slater SJ, Ho C, Stubbs CD |title=The use of fluorescent phorbol esters in studies of protein kinase C-membrane interactions. |journal=Chem. Phys. Lipids |volume=116 |issue= 1-2 |pages= 75-91 |year= 2003 |pmid= 12093536 |doi= }}
}}
{{refend}}
PTGS2
- REDIRECT: Protein Redirected to: PTGS2 {September 10, 2007 2:20:55 PM PDT}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {September 10, 2007 2:21:00 PM PDT}
- UPDATE SUMMARY: Updating Summary, No Errors. {September 10, 2007 2:21:00 PM PDT}
- UPDATE CITATIONS: Updating Citations, No Errors. {September 10, 2007 2:21:00 PM PDT}
- UPDATED: Updated protein page: PTGS2 {September 10, 2007 2:21:06 PM PDT}
RB1
- REDIRECT: Protein Redirected to: Retinoblastoma protein {September 10, 2007 2:21:22 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: Retinoblastoma protein. Invoking a Mandantory Inspection. {September 10, 2007 2:21:25 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Retinoblastoma 1 (including osteosarcoma)''', also known as '''RB1''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_RB1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ad6.
| PDB = {{PDB2|1ad6}}, {{PDB2|1gh6}}, {{PDB2|1gux}}, {{PDB2|1o9k}}, {{PDB2|2aze}}
| Name = Retinoblastoma 1 (including osteosarcoma)
| HGNCid = 9884
| Symbol = RB1
| AltSymbols =; OSRC; RB
| OMIM = 180200
| ECnumber =
| Homologene = 272
| MGIid = 97874
| GeneAtlas_image1 = PBB_GE_RB1_203132_at.png
| GeneAtlas_image2 = PBB_GE_RB1_211540_s_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0008134 |text = transcription factor binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0019900 |text = kinase binding}} {{GNF_GO|id=GO:0050681 |text = androgen receptor binding}}
| Component = {{GNF_GO|id=GO:0000785 |text = chromatin}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005667 |text = transcription factor complex}} {{GNF_GO|id=GO:0005819 |text = spindle}}
| Process = {{GNF_GO|id=GO:0000075 |text = cell cycle checkpoint}} {{GNF_GO|id=GO:0000082 |text = G1/S transition of mitotic cell cycle}} {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0000279 |text = M phase}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006469 |text = negative regulation of protein kinase activity}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0030308 |text = negative regulation of cell growth}} {{GNF_GO|id=GO:0030521 |text = androgen receptor signaling pathway}} {{GNF_GO|id=GO:0043550 |text = regulation of lipid kinase activity}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0051146 |text = striated muscle cell differentiation}} {{GNF_GO|id=GO:0051301 |text = cell division}} {{GNF_GO|id=GO:0051318 |text = G1 phase}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5925
| Hs_Ensembl = ENSG00000139687
| Hs_RefseqProtein = NP_000312
| Hs_RefseqmRNA = NM_000321
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 47775912
| Hs_GenLoc_end = 47954123
| Hs_Uniprot = P06400
| Mm_EntrezGene = 19645
| Mm_Ensembl = ENSMUSG00000022105
| Mm_RefseqmRNA = NM_009029
| Mm_RefseqProtein = NP_033055
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 71929657
| Mm_GenLoc_end = 72059946
| Mm_Uniprot = Q3UFM7
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Retinoblastoma (RB) is an embryonic malignant neoplasm of retinal origin. It almost always presents in early childhood and is often bilateral. Spontaneous regression ('cure') occurs in some cases.[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: RB1 retinoblastoma 1 (including osteosarcoma)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5925| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Momand J, Wu HH, Dasgupta G |title=MDM2--master regulator of the p53 tumor suppressor protein. |journal=Gene |volume=242 |issue= 1-2 |pages= 15-29 |year= 2000 |pmid= 10721693 |doi= }}
*{{cite journal | author=Zheng L, Lee WH |title=Retinoblastoma tumor suppressor and genome stability. |journal=Adv. Cancer Res. |volume=85 |issue= |pages= 13-50 |year= 2003 |pmid= 12374284 |doi= }}
*{{cite journal | author=Classon M, Harlow E |title=The retinoblastoma tumour suppressor in development and cancer. |journal=Nat. Rev. Cancer |volume=2 |issue= 12 |pages= 910-7 |year= 2003 |pmid= 12459729 |doi= 10.1038/nrc950 }}
*{{cite journal | author=Lai H, Ma F, Lai S |title=Identification of the novel role of pRB in eye cancer. |journal=J. Cell. Biochem. |volume=88 |issue= 1 |pages= 121-7 |year= 2003 |pmid= 12461781 |doi= 10.1002/jcb.10283 }}
*{{cite journal | author=Simin K, Wu H, Lu L, ''et al.'' |title=pRb inactivation in mammary cells reveals common mechanisms for tumor initiation and progression in divergent epithelia. |journal=PLoS Biol. |volume=2 |issue= 2 |pages= E22 |year= 2006 |pmid= 14966529 |doi= 10.1371/journal.pbio.0020022 }}
*{{cite journal | author=Lohmann DR, Gallie BL |title=Retinoblastoma: revisiting the model prototype of inherited cancer. |journal=American journal of medical genetics. Part C, Seminars in medical genetics |volume=129 |issue= 1 |pages= 23-8 |year= 2004 |pmid= 15264269 |doi= 10.1002/ajmg.c.30024 }}
*{{cite journal | author=Clemo NK, Arhel NJ, Barnes JD, ''et al.'' |title=The role of the retinoblastoma protein (Rb) in the nuclear localization of BAG-1: implications for colorectal tumour cell survival. |journal=Biochem. Soc. Trans. |volume=33 |issue= Pt 4 |pages= 676-8 |year= 2005 |pmid= 16042572 |doi= 10.1042/BST0330676 }}
*{{cite journal | author=RodrÃguez-Cruz M, del Prado M, Salcedo M |title=[Genomic retinoblastoma perspectives: implications of tumor supressor gene RB1] |journal=Rev. Invest. Clin. |volume=57 |issue= 4 |pages= 572-81 |year= 2006 |pmid= 16315642 |doi= }}
*{{cite journal | author=Knudsen ES, Knudsen KE |title=Retinoblastoma tumor suppressor: where cancer meets the cell cycle. |journal=Exp. Biol. Med. (Maywood) |volume=231 |issue= 7 |pages= 1271-81 |year= 2006 |pmid= 16816134 |doi= }}
}}
{{refend}}
SRC
- REDIRECT: Protein Redirected to: Src_(gene) {September 10, 2007 2:21:47 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: Src_(gene). Invoking a Mandantory Inspection. {September 10, 2007 2:21:53 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''V-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog (avian)''', also known as '''SRC''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SRC_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a07.
| PDB = {{PDB2|1a07}}, {{PDB2|1a08}}, {{PDB2|1a09}}, {{PDB2|1a1a}}, {{PDB2|1a1b}}, {{PDB2|1a1c}}, {{PDB2|1a1e}}, {{PDB2|1bkl}}, {{PDB2|1bkm}}, {{PDB2|1f1w}}, {{PDB2|1f2f}}, {{PDB2|1fmk}}, {{PDB2|1hcs}}, {{PDB2|1hct}}, {{PDB2|1is0}}, {{PDB2|1kc2}}, {{PDB2|1ksw}}, {{PDB2|1nlo}}, {{PDB2|1nlp}}, {{PDB2|1nzl}}, {{PDB2|1nzv}}, {{PDB2|1o41}}, {{PDB2|1o42}}, {{PDB2|1o43}}, {{PDB2|1o44}}, {{PDB2|1o45}}, {{PDB2|1o46}}, {{PDB2|1o47}}, {{PDB2|1o48}}, {{PDB2|1o49}}, {{PDB2|1o4a}}, {{PDB2|1o4b}}, {{PDB2|1o4c}}, {{PDB2|1o4d}}, {{PDB2|1o4e}}, {{PDB2|1o4f}}, {{PDB2|1o4g}}, {{PDB2|1o4h}}, {{PDB2|1o4i}}, {{PDB2|1o4j}}, {{PDB2|1o4k}}, {{PDB2|1o4l}}, {{PDB2|1o4m}}, {{PDB2|1o4n}}, {{PDB2|1o4o}}, {{PDB2|1o4p}}, {{PDB2|1o4q}}, {{PDB2|1o4r}}, {{PDB2|1p13}}, {{PDB2|1prl}}, {{PDB2|1prm}}, {{PDB2|1qwe}}, {{PDB2|1qwf}}, {{PDB2|1rlp}}, {{PDB2|1rlq}}, {{PDB2|1sha}}, {{PDB2|1shb}}, {{PDB2|1shd}}, {{PDB2|1skj}}, {{PDB2|1spr}}, {{PDB2|1sps}}, {{PDB2|1srl}}, {{PDB2|1srm}}, {{PDB2|1y57}}, {{PDB2|1yi6}}, {{PDB2|1yoj}}, {{PDB2|1yol}}, {{PDB2|1yom}}, {{PDB2|2bdf}}, {{PDB2|2bdj}}, {{PDB2|2h8h}}, {{PDB2|2hwo}}, {{PDB2|2hwp}}, {{PDB2|2oiq}}, {{PDB2|2ptk}}, {{PDB2|2src}}
| Name = V-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog (avian)
| HGNCid = 11283
| Symbol = SRC
| AltSymbols =; ASV; SRC1; c-SRC; p60-Src
| OMIM = 190090
| ECnumber =
| Homologene = 21120
| MGIid = 98397
| GeneAtlas_image1 = PBB_GE_SRC_213324_at.png
| GeneAtlas_image2 = PBB_GE_SRC_221284_s_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0005070 |text = SH3/SH2 adaptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0042169 |text = SH2 domain binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007172 |text = signal complex assembly}} {{GNF_GO|id=GO:0007243 |text = protein kinase cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6714
| Hs_Ensembl = ENSG00000197122
| Hs_RefseqProtein = NP_005408
| Hs_RefseqmRNA = NM_005417
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 35406502
| Hs_GenLoc_end = 35467239
| Hs_Uniprot = P12931
| Mm_EntrezGene = 20779
| Mm_Ensembl = ENSMUSG00000027646
| Mm_RefseqmRNA = NM_001025395
| Mm_RefseqProtein = NP_001020566
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 157115730
| Mm_GenLoc_end = 157163279
| Mm_Uniprot = Q2M4I4
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is highly similar to the v-src gene of Rous sarcoma virus. This proto-oncogene may play a role in the regulation of embryonic development and cell growth. The protein encoded by this gene is a tyrosine-protein kinase whose activity can be inhibited by phosphorylation by c-SRC kinase. Mutations in this gene could be involved in the malignant progression of colon cancer. Two transcript variants encoding the same protein have been found for this gene.<ref>{{cite web | title = Entrez Gene: SRC v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog (avian)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6714| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Frame MC, Fincham VJ, Carragher NO, Wyke JA |title=v-Src's hold over actin and cell adhesions. |journal=Nat. Rev. Mol. Cell Biol. |volume=3 |issue= 4 |pages= 233-45 |year= 2002 |pmid= 11994743 |doi= 10.1038/nrm779 }}
*{{cite journal | author=Benaim G, Villalobo A |title=Phosphorylation of calmodulin. Functional implications. |journal=Eur. J. Biochem. |volume=269 |issue= 15 |pages= 3619-31 |year= 2002 |pmid= 12153558 |doi= }}
*{{cite journal | author=Simeonova PP, Luster MI |title=Arsenic carcinogenicity: relevance of c-Src activation. |journal=Mol. Cell. Biochem. |volume=234-235 |issue= 1-2 |pages= 277-82 |year= 2003 |pmid= 12162444 |doi= }}
*{{cite journal | author=Leu TH, Maa MC |title=Functional implication of the interaction between EGF receptor and c-Src. |journal=Front. Biosci. |volume=8 |issue= |pages= s28-38 |year= 2004 |pmid= 12456372 |doi= }}
*{{cite journal | author=Greenway AL, Holloway G, McPhee DA, ''et al.'' |title=HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication. |journal=J. Biosci. |volume=28 |issue= 3 |pages= 323-35 |year= 2004 |pmid= 12734410 |doi= }}
*{{cite journal | author=Dehm SM, Bonham K |title=SRC gene expression in human cancer: the role of transcriptional activation. |journal=Biochem. Cell Biol. |volume=82 |issue= 2 |pages= 263-74 |year= 2004 |pmid= 15060621 |doi= 10.1139/o03-077 }}
*{{cite journal | author=Tolstrup M, Ostergaard L, Laursen AL, ''et al.'' |title=HIV/SIV escape from immune surveillance: focus on Nef. |journal=Curr. HIV Res. |volume=2 |issue= 2 |pages= 141-51 |year= 2004 |pmid= 15078178 |doi= }}
*{{cite journal | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87-94 |year= 2005 |pmid= 15638726 |doi= }}
*{{cite journal | author=Roskoski R |title=Src kinase regulation by phosphorylation and dephosphorylation. |journal=Biochem. Biophys. Res. Commun. |volume=331 |issue= 1 |pages= 1-14 |year= 2005 |pmid= 15845350 |doi= 10.1016/j.bbrc.2005.03.012 }}
*{{cite journal | author=Alper O, Bowden ET |title=Novel insights into c-Src. |journal=Curr. Pharm. Des. |volume=11 |issue= 9 |pages= 1119-30 |year= 2005 |pmid= 15853660 |doi= }}
}}
{{refend}}
TGFB1
- REDIRECT: Protein Redirected to: TGFB1 {September 10, 2007 2:22:11 PM PDT}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {September 10, 2007 2:22:12 PM PDT}
- UPDATE SUMMARY: Updating Summary, No Errors. {September 10, 2007 2:22:12 PM PDT}
- UPDATE CITATIONS: Updating Citations, No Errors. {September 10, 2007 2:22:12 PM PDT}
- UPDATED: Updated protein page: TGFB1 {September 10, 2007 2:22:20 PM PDT}
TNF
- REDIRECT: Protein Redirected to: TNF-alpha {September 10, 2007 2:22:46 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: TNF-alpha. Invoking a Mandantory Inspection. {September 10, 2007 2:22:49 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Tumor necrosis factor (TNF superfamily, member 2)''', also known as '''TNF''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_TNF_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a8m.
| PDB = {{PDB2|1a8m}}, {{PDB2|1tnf}}, {{PDB2|2az5}}, {{PDB2|2tun}}, {{PDB2|4tsv}}, {{PDB2|5tsw}}
| Name = Tumor necrosis factor (TNF superfamily, member 2)
| HGNCid = 11892
| Symbol = TNF
| AltSymbols =; DIF; TNF-alpha; TNFA; TNFSF2
| OMIM = 191160
| ECnumber =
| Homologene = 496
| MGIid = 104798
| GeneAtlas_image1 = PBB_GE_TNF_207113_s_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005164 |text = tumor necrosis factor receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0000060 |text = protein import into nucleus, translocation}} {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0001932 |text = regulation of protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006006 |text = glucose metabolic process}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0006959 |text = humoral immune response}} {{GNF_GO|id=GO:0007159 |text = leukocyte adhesion}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008625 |text = induction of apoptosis via death domain receptors}} {{GNF_GO|id=GO:0009615 |text = response to virus}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0042127 |text = regulation of cell proliferation}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}} {{GNF_GO|id=GO:0045123 |text = cellular extravasation}} {{GNF_GO|id=GO:0045670 |text = regulation of osteoclast differentiation}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0045994 |text = positive regulation of translational initiation by iron}} {{GNF_GO|id=GO:0046325 |text = negative regulation of glucose import}} {{GNF_GO|id=GO:0046330 |text = positive regulation of JNK cascade}} {{GNF_GO|id=GO:0051023 |text = regulation of immunoglobulin secretion}} {{GNF_GO|id=GO:0051092 |text = activation of NF-kappaB transcription factor}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7124
| Hs_Ensembl = ENSG00000204490
| Hs_RefseqProtein = NP_000585
| Hs_RefseqmRNA = NM_000594
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 31651314
| Hs_GenLoc_end = 31654092
| Hs_Uniprot = P01375
| Mm_EntrezGene = 21926
| Mm_Ensembl = ENSMUSG00000024401
| Mm_RefseqmRNA = NM_013693
| Mm_RefseqProtein = NP_038721
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 34807442
| Mm_GenLoc_end = 34810048
| Mm_Uniprot = Q0X0E6
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a multifunctional proinflammatory cytokine that belongs to the tumor necrosis factor (TNF) superfamily. This cytokine is mainly secreted by macrophages. It can bind to, and thus functions through its receptors TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. This cytokine is involved in the regulation of a wide spectrum of biological processes including cell proliferation, differentiation, apoptosis, lipid metabolism, and coagulation. This cytokine has been implicated in a variety of diseases, including autoimmune diseases, insulin resistance, and cancer. Knockout studies in mice also suggested the neuroprotective function of this cytokine.<ref>{{cite web | title = Entrez Gene: TNF tumor necrosis factor (TNF superfamily, member 2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7124| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Spriggs DR, Deutsch S, Kufe DW |title=Genomic structure, induction, and production of TNF-alpha. |journal=Immunol. Ser. |volume=56 |issue= |pages= 3-34 |year= 1992 |pmid= 1550865 |doi= }}
*{{cite journal | author=Taylor PC |title=Anti-TNF therapy for rheumatoid arthritis and other inflammatory diseases. |journal=Mol. Biotechnol. |volume=19 |issue= 2 |pages= 153-68 |year= 2002 |pmid= 11725485 |doi= }}
*{{cite journal | author=Kollias G, Kontoyiannis D, Douni E, Kassiotis G |title=The role of TNF/TNFR in organ-specific and systemic autoimmunity: implications for the design of optimized 'anti-TNF' therapies. |journal=Curr. Dir. Autoimmun. |volume=5 |issue= |pages= 30-50 |year= 2002 |pmid= 11826759 |doi= }}
*{{cite journal | author=Ghezzi P, Mennini T |title=Tumor necrosis factor and motoneuronal degeneration: an open problem. |journal=Neuroimmunomodulation |volume=9 |issue= 4 |pages= 178-82 |year= 2002 |pmid= 11847479 |doi= }}
*{{cite journal | author=Smirnova MG, Kiselev SL, Gnuchev NV, ''et al.'' |title=Role of the pro-inflammatory cytokines tumor necrosis factor-alpha, interleukin-1 beta, interleukin-6 and interleukin-8 in the pathogenesis of the otitis media with effusion. |journal=Eur. Cytokine Netw. |volume=13 |issue= 2 |pages= 161-72 |year= 2003 |pmid= 12101072 |doi= }}
*{{cite journal | author=Gupta S |title=A decision between life and death during TNF-alpha-induced signaling. |journal=J. Clin. Immunol. |volume=22 |issue= 4 |pages= 185-94 |year= 2003 |pmid= 12148593 |doi= }}
*{{cite journal | author=Yucesoy B, Vallyathan V, Landsittel DP, ''et al.'' |title=Cytokine polymorphisms in silicosis and other pneumoconioses. |journal=Mol. Cell. Biochem. |volume=234-235 |issue= 1-2 |pages= 219-24 |year= 2003 |pmid= 12162437 |doi= }}
*{{cite journal | author=Kollias G, Kontoyiannis D |title=Role of TNF/TNFR in autoimmunity: specific TNF receptor blockade may be advantageous to anti-TNF treatments. |journal=Cytokine Growth Factor Rev. |volume=13 |issue= 4-5 |pages= 315-21 |year= 2003 |pmid= 12220546 |doi= }}
*{{cite journal | author=Satoh J, Yagihashi S, Toyota T |title=The possible role of tumor necrosis factor-alpha in diabetic polyneuropathy. |journal=Exp. Diabesity Res. |volume=4 |issue= 2 |pages= 65-71 |year= 2004 |pmid= 14630568 |doi= }}
*{{cite journal | author=Ceconi C, Boraso A, Mele D, ''et al.'' |title=TNFalpha in patients with congestive heart failure. |journal=Basic Res. Cardiol. |volume=99 |issue= 1 |pages= 12-7 |year= 2004 |pmid= 14685701 |doi= 10.1007/s00395-003-0443-6 }}
*{{cite journal | author=Meyer O |title=[Role of TNF-alpha and cytokines in the physiopathology of rheumatoid arthritis. Therapeutic perspectives] |journal=Bull. Acad. Natl. Med. |volume=187 |issue= 5 |pages= 935-54; discussion 954-5 |year= 2004 |pmid= 14979058 |doi= }}
*{{cite journal | author=Muthumani K, Desai BM, Hwang DS, ''et al.'' |title=HIV-1 Vpr and anti-inflammatory activity. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 239-47 |year= 2004 |pmid= 15142381 |doi= 10.1089/104454904773819824 }}
*{{cite journal | author=Aringer M, Smolen JS |title=Tumour necrosis factor and other proinflammatory cytokines in systemic lupus erythematosus: a rationale for therapeutic intervention. |journal=Lupus |volume=13 |issue= 5 |pages= 344-7 |year= 2005 |pmid= 15230290 |doi= }}
*{{cite journal | author=Rogliani P, Amicosante M, Berretta F, ''et al.'' |title=Role of the HLA-DP Glu 69 and the TNF-alpha TNF-alpha 2 gene markers in susceptibility to beryllium hypersensitivity. |journal=International journal of immunopathology and pharmacology |volume=17 |issue= 2 Suppl |pages= 3-10 |year= 2006 |pmid= 15345185 |doi= }}
*{{cite journal | author=Stenvinkel P, Ketteler M, Johnson RJ, ''et al.'' |title=IL-10, IL-6, and TNF-alpha: central factors in the altered cytokine network of uremia--the good, the bad, and the ugly. |journal=Kidney Int. |volume=67 |issue= 4 |pages= 1216-33 |year= 2005 |pmid= 15780075 |doi= 10.1111/j.1523-1755.2005.00200.x }}
*{{cite journal | author=Zhao RY, Elder RT |title=Viral infections and cell cycle G2/M regulation. |journal=Cell Res. |volume=15 |issue= 3 |pages= 143-9 |year= 2005 |pmid= 15780175 |doi= 10.1038/sj.cr.7290279 }}
*{{cite journal | author=Zhao RY, Bukrinsky M, Elder RT |title=HIV-1 viral protein R (Vpr) & host cellular responses. |journal=Indian J. Med. Res. |volume=121 |issue= 4 |pages= 270-86 |year= 2005 |pmid= 15817944 |doi= }}
*{{cite journal | author=Anderson JL, Hope TJ |title=HIV accessory proteins and surviving the host cell. |journal=Current HIV/AIDS reports |volume=1 |issue= 1 |pages= 47-53 |year= 2005 |pmid= 16091223 |doi= }}
*{{cite journal | author=Lin WJ, Yeh WC |title=Implication of Toll-like receptor and tumor necrosis factor alpha signaling in septic shock. |journal=Shock |volume=24 |issue= 3 |pages= 206-9 |year= 2005 |pmid= 16135957 |doi= }}
*{{cite journal | author=Copeland KF |title=Modulation of HIV-1 transcription by cytokines and chemokines. |journal=Mini reviews in medicinal chemistry |volume=5 |issue= 12 |pages= 1093-101 |year= 2006 |pmid= 16375755 |doi= }}
*{{cite journal | author=Stove V, Verhasselt B |title=Modelling thymic HIV-1 Nef effects. |journal=Curr. HIV Res. |volume=4 |issue= 1 |pages= 57-64 |year= 2006 |pmid= 16454711 |doi= }}
*{{cite journal | author=Langin D, Arner P |title=Importance of TNFalpha and neutral lipases in human adipose tissue lipolysis. |journal=Trends Endocrinol. Metab. |volume=17 |issue= 8 |pages= 314-20 |year= 2007 |pmid= 16938460 |doi= 10.1016/j.tem.2006.08.003 }}
*{{cite journal | author=Mukhopadhyay S, Hoidal JR, Mukherjee TK |title=Role of TNFalpha in pulmonary pathophysiology. |journal=Respir. Res. |volume=7 |issue= |pages= 125 |year= 2006 |pmid= 17034639 |doi= 10.1186/1465-9921-7-125 }}
*{{cite journal | author=Sykes MC, Mowbray AL, Jo H |title=Reversible glutathiolation of caspase-3 by glutaredoxin as a novel redox signaling mechanism in tumor necrosis factor-alpha-induced cell death. |journal=Circ. Res. |volume=100 |issue= 2 |pages= 152-4 |year= 2007 |pmid= 17272816 |doi= 10.1161/01.RES.0000258171.08020.72 }}
*{{cite journal | author=Pereira TV, Rudnicki M, Franco RF, ''et al.'' |title=Effect of the G-308A polymorphism of the tumor necrosis factor alpha gene on the risk of ischemic heart disease and ischemic stroke: a meta-analysis. |journal=Am. Heart J. |volume=153 |issue= 5 |pages= 821-30 |year= 2007 |pmid= 17452160 |doi= 10.1016/j.ahj.2007.02.031 }}
*{{cite journal | author=Clark IA |title=How TNF was recognized as a key mechanism of disease. |journal=Cytokine Growth Factor Rev. |volume=18 |issue= 3-4 |pages= 335-43 |year= 2007 |pmid= 17493863 |doi= 10.1016/j.cytogfr.2007.04.002 }}
}}
{{refend}}
TP53
- REDIRECT: Protein Redirected to: TP53 {September 10, 2007 2:23:56 PM PDT}
- BAD FORMAT: There is a problem with the BOT commands for this protein: TP53. Invoking a Mandantory Inspection. {September 10, 2007 2:23:59 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Tumor protein p53 (Li-Fraumeni syndrome)''', also known as '''TP53''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_TP53_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a1u.
| PDB = {{PDB2|1a1u}}, {{PDB2|1aie}}, {{PDB2|1c26}}, {{PDB2|1gzh}}, {{PDB2|1hs5}}, {{PDB2|1kzy}}, {{PDB2|1olg}}, {{PDB2|1olh}}, {{PDB2|1pes}}, {{PDB2|1pet}}, {{PDB2|1sae}}, {{PDB2|1saf}}, {{PDB2|1sag}}, {{PDB2|1sah}}, {{PDB2|1sai}}, {{PDB2|1saj}}, {{PDB2|1sak}}, {{PDB2|1sal}}, {{PDB2|1tsr}}, {{PDB2|1tup}}, {{PDB2|1uol}}, {{PDB2|1ycs}}, {{PDB2|2ac0}}, {{PDB2|2ady}}, {{PDB2|2ahi}}, {{PDB2|2ata}}, {{PDB2|2b3g}}, {{PDB2|2bim}}, {{PDB2|2bin}}, {{PDB2|2bio}}, {{PDB2|2bip}}, {{PDB2|2biq}}, {{PDB2|2fej}}, {{PDB2|2gs0}}, {{PDB2|2h1l}}, {{PDB2|2j1w}}, {{PDB2|2j1x}}, {{PDB2|2j1y}}, {{PDB2|2j1z}}, {{PDB2|2j20}}, {{PDB2|2j21}}, {{PDB2|2ocj}}, {{PDB2|3sak}}
| Name = Tumor protein p53 (Li-Fraumeni syndrome)
| HGNCid = 11998
| Symbol = TP53
| AltSymbols =; LFS1; TRP53; p53
| OMIM = 191170
| ECnumber =
| Homologene = 460
| MGIid = 98834
| GeneAtlas_image1 = PBB_GE_TP53_201746_at.png
| GeneAtlas_image2 = PBB_GE_TP53_211300_s_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0000739 |text = DNA strand annealing activity}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0004518 |text = nuclease activity}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0019899 |text = enzyme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}} {{GNF_GO|id=GO:0047485 |text = protein N-terminus binding}}
| Component = {{GNF_GO|id=GO:0005626 |text = insoluble fraction}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0005657 |text = replication fork}} {{GNF_GO|id=GO:0005730 |text = nucleolus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0016363 |text = nuclear matrix}}
| Process = {{GNF_GO|id=GO:0000060 |text = protein import into nucleus, translocation}} {{GNF_GO|id=GO:0001701 |text = in utero embryonic development}} {{GNF_GO|id=GO:0006284 |text = base-excision repair}} {{GNF_GO|id=GO:0006289 |text = nucleotide-excision repair}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006974 |text = response to DNA damage stimulus}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007569 |text = cell aging}} {{GNF_GO|id=GO:0008104 |text = protein localization}} {{GNF_GO|id=GO:0008156 |text = negative regulation of DNA replication}} {{GNF_GO|id=GO:0008635 |text = caspase activation via cytochrome c}} {{GNF_GO|id=GO:0009411 |text = response to UV}} {{GNF_GO|id=GO:0009792 |text = embryonic development ending in birth or egg hatching}} {{GNF_GO|id=GO:0010165 |text = response to X-ray}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030308 |text = negative regulation of cell growth}} {{GNF_GO|id=GO:0031571 |text = G1 DNA damage checkpoint}} {{GNF_GO|id=GO:0042127 |text = regulation of cell proliferation}} {{GNF_GO|id=GO:0042771 |text = DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis}} {{GNF_GO|id=GO:0043066 |text = negative regulation of apoptosis}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0046902 |text = regulation of mitochondrial membrane permeability}} {{GNF_GO|id=GO:0048147 |text = negative regulation of fibroblast proliferation}} {{GNF_GO|id=GO:0051097 |text = negative regulation of helicase activity}} {{GNF_GO|id=GO:0051262 |text = protein tetramerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7157
| Hs_Ensembl = ENSG00000141510
| Hs_RefseqProtein = NP_000537
| Hs_RefseqmRNA = NM_000546
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 7512464
| Hs_GenLoc_end = 7531642
| Hs_Uniprot = P04637
| Mm_EntrezGene = 22059
| Mm_Ensembl = ENSMUSG00000059552
| Mm_RefseqmRNA = NM_011640
| Mm_RefseqProtein = NP_035770
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 69396600
| Mm_GenLoc_end = 69407992
| Mm_Uniprot = O70366
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Tumor protein p53, a nuclear protein, plays an essential role in the regulation of cell cycle, specifically in the transition from G0 to G1. It is found in very low levels in normal cells, however, in a variety of transformed cell lines, it is expressed in high amounts, and believed to contribute to transformation and malignancy. p53 is a DNA-binding protein containing DNA-binding, oligomerization and transcription activation domains. It is postulated to bind as a tetramer to a p53-binding site and activate expression of downstream genes that inhibit growth and/or invasion, and thus function as a tumor suppressor. Mutants of p53 that frequently occur in a number of different human cancers fail to bind the consensus DNA binding site, and hence cause the loss of tumor suppressor activity. Alterations of the TP53 gene occur not only as somatic mutations in human malignancies, but also as germline mutations in some cancer-prone families with Li-Fraumeni syndrome.<ref>{{cite web | title = Entrez Gene: TP53 tumor protein p53 (Li-Fraumeni syndrome)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7157| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hollstein M, Sidransky D, Vogelstein B, Harris CC |title=p53 mutations in human cancers. |journal=Science |volume=253 |issue= 5015 |pages= 49-53 |year= 1991 |pmid= 1905840 |doi= }}
*{{cite journal | author=Harris CC |title=p53: at the crossroads of molecular carcinogenesis and risk assessment. |journal=Science |volume=262 |issue= 5142 |pages= 1980-1 |year= 1994 |pmid= 8266092 |doi= }}
*{{cite journal | author=Giaccia AJ, Kastan MB |title=The complexity of p53 modulation: emerging patterns from divergent signals. |journal=Genes Dev. |volume=12 |issue= 19 |pages= 2973-83 |year= 1998 |pmid= 9765199 |doi= }}
*{{cite journal | author=Choi J, Donehower LA |title=p53 in embryonic development: maintaining a fine balance. |journal=Cell. Mol. Life Sci. |volume=55 |issue= 1 |pages= 38-47 |year= 1999 |pmid= 10065150 |doi= }}
*{{cite journal | author=Jayaraman L, Prives C |title=Covalent and noncovalent modifiers of the p53 protein. |journal=Cell. Mol. Life Sci. |volume=55 |issue= 1 |pages= 76-87 |year= 1999 |pmid= 10065153 |doi= }}
*{{cite journal | author=Shaul Y |title=c-Abl: activation and nuclear targets. |journal=Cell Death Differ. |volume=7 |issue= 1 |pages= 10-6 |year= 2000 |pmid= 10713716 |doi= 10.1038/sj.cdd.4400626 }}
*{{cite journal | author=Momand J, Wu HH, Dasgupta G |title=MDM2--master regulator of the p53 tumor suppressor protein. |journal=Gene |volume=242 |issue= 1-2 |pages= 15-29 |year= 2000 |pmid= 10721693 |doi= }}
*{{cite journal | author=Tortora V, Bontempo P, Verdicchio M, ''et al.'' |title=Regulation of p53 function in normal and malignant cells. |journal=Adv. Exp. Med. Biol. |volume=472 |issue= |pages= 89-100 |year= 2000 |pmid= 10736619 |doi= }}
*{{cite journal | author=Hainaut P, Mann K |title=Zinc binding and redox control of p53 structure and function. |journal=Antioxid. Redox Signal. |volume=3 |issue= 4 |pages= 611-23 |year= 2002 |pmid= 11554448 |doi= 10.1089/15230860152542961 }}
*{{cite journal | author=Pearson M, Pelicci PG |title=PML interaction with p53 and its role in apoptosis and replicative senescence. |journal=Oncogene |volume=20 |issue= 49 |pages= 7250-6 |year= 2001 |pmid= 11704853 |doi= 10.1038/sj.onc.1204856 }}
*{{cite journal | author=Chang NS |title=A potential role of p53 and WOX1 in mitochondrial apoptosis (review). |journal=Int. J. Mol. Med. |volume=9 |issue= 1 |pages= 19-24 |year= 2002 |pmid= 11744990 |doi= }}
*{{cite journal | author=Lopez-Martinez M, Anzola M, Cuevas N, ''et al.'' |title=Clinical applications of the diagnosis of p53 alterations in squamous cell carcinoma of the head and neck. |journal=Medicina oral : órgano oficial de la Sociedad Española de Medicina Oral y de la Academia Iberoamericana de PatologÃa y Medicina Bucal |volume=7 |issue= 2 |pages= 108-20 |year= 2002 |pmid= 11887018 |doi= }}
*{{cite journal | author=Zupanska A, Kaminska B |title=The diversity of p53 mutations among human brain tumors and their functional consequences. |journal=Neurochem. Int. |volume=40 |issue= 7 |pages= 637-45 |year= 2002 |pmid= 11900859 |doi= }}
*{{cite journal | author=Nakashima S, Sawada M |title=[Involvement of p53 in ceramide signaling cascade] |journal=Tanpakushitsu Kakusan Koso |volume=47 |issue= 4 Suppl |pages= 449-54 |year= 2002 |pmid= 11915341 |doi= }}
*{{cite journal | author=Alarcon-Vargas D, Ronai Z |title=p53-Mdm2--the affair that never ends. |journal=Carcinogenesis |volume=23 |issue= 4 |pages= 541-7 |year= 2002 |pmid= 11960904 |doi= }}
*{{cite journal | author=Le NT, Richardson DR |title=The role of iron in cell cycle progression and the proliferation of neoplastic cells. |journal=Biochim. Biophys. Acta |volume=1603 |issue= 1 |pages= 31-46 |year= 2002 |pmid= 12242109 |doi= }}
*{{cite journal | author=El-Deiry WS |title=Transactivation of repair genes by BRCA1. |journal=Cancer Biol. Ther. |volume=1 |issue= 5 |pages= 490-1 |year= 2003 |pmid= 12496474 |doi= }}
*{{cite journal | author=Michael D, Oren M |title=The p53-Mdm2 module and the ubiquitin system. |journal=Semin. Cancer Biol. |volume=13 |issue= 1 |pages= 49-58 |year= 2003 |pmid= 12507556 |doi= }}
*{{cite journal | author=Greenway AL, Holloway G, McPhee DA, ''et al.'' |title=HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication. |journal=J. Biosci. |volume=28 |issue= 3 |pages= 323-35 |year= 2004 |pmid= 12734410 |doi= }}
*{{cite journal | author=Horiike S, Kita-Sasai Y, Nakao M, Taniwaki M |title=Configuration of the TP53 gene as an independent prognostic parameter of myelodysplastic syndrome. |journal=Leuk. Lymphoma |volume=44 |issue= 6 |pages= 915-22 |year= 2003 |pmid= 12854888 |doi= }}
*{{cite journal | author=Hartman AR, Ford JM |title=BRCA1 and p53: compensatory roles in DNA repair. |journal=J. Mol. Med. |volume=81 |issue= 11 |pages= 700-7 |year= 2004 |pmid= 13679996 |doi= 10.1007/s00109-003-0477-0 }}
*{{cite journal | author=Vecil GG, Lang FF |title=Clinical trials of adenoviruses in brain tumors: a review of Ad-p53 and oncolytic adenoviruses. |journal=J. Neurooncol. |volume=65 |issue= 3 |pages= 237-46 |year= 2004 |pmid= 14682374 |doi= }}
*{{cite journal | author=Tolstrup M, Ostergaard L, Laursen AL, ''et al.'' |title=HIV/SIV escape from immune surveillance: focus on Nef. |journal=Curr. HIV Res. |volume=2 |issue= 2 |pages= 141-51 |year= 2004 |pmid= 15078178 |doi= }}
*{{cite journal | author=Hofseth LJ, Hussain SP, Harris CC |title=p53: 25 years after its discovery. |journal=Trends Pharmacol. Sci. |volume=25 |issue= 4 |pages= 177-81 |year= 2004 |pmid= 15116721 |doi= }}
*{{cite journal | author=Amini S, Khalili K, Sawaya BE |title=Effect of HIV-1 Vpr on cell cycle regulators. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 249-60 |year= 2004 |pmid= 15142382 |doi= 10.1089/104454904773819833 }}
*{{cite journal | author=Halazonetis TD |title=Constitutively active DNA damage checkpoint pathways as the driving force for the high frequency of p53 mutations in human cancer. |journal=DNA Repair (Amst.) |volume=3 |issue= 8-9 |pages= 1057-62 |year= 2005 |pmid= 15279793 |doi= 10.1016/j.dnarep.2004.03.036 }}
*{{cite journal | author=Selivanova G |title=p53: fighting cancer. |journal=Current cancer drug targets |volume=4 |issue= 5 |pages= 385-402 |year= 2005 |pmid= 15320716 |doi= }}
*{{cite journal | author=Seelamgari A, Maddukuri A, Berro R, ''et al.'' |title=Role of viral regulatory and accessory proteins in HIV-1 replication. |journal=Front. Biosci. |volume=9 |issue= |pages= 2388-413 |year= 2006 |pmid= 15353294 |doi= }}
*{{cite journal | author=Jacobs WB, Walsh GS, Miller FD |title=Neuronal survival and p73/p63/p53: a family affair. |journal=The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry |volume=10 |issue= 5 |pages= 443-55 |year= 2005 |pmid= 15359011 |doi= 10.1177/1073858404263456 }}
*{{cite journal | author=Bode AM, Dong Z |title=Post-translational modification of p53 in tumorigenesis. |journal=Nat. Rev. Cancer |volume=4 |issue= 10 |pages= 793-805 |year= 2004 |pmid= 15510160 |doi= 10.1038/nrc1455 }}
*{{cite journal | author=Pise-Masison CA, Brady JN |title=Setting the stage for transformation: HTLV-1 Tax inhibition of p53 function. |journal=Front. Biosci. |volume=10 |issue= |pages= 919-30 |year= 2006 |pmid= 15569630 |doi= }}
*{{cite journal | author=Xu Y |title=A new role for p53 in maintaining genetic stability in embryonic stem cells. |journal=Cell Cycle |volume=4 |issue= 3 |pages= 363-4 |year= 2006 |pmid= 15701975 |doi= }}
*{{cite journal | author=Ho JW, Song JZ, Leung YK |title=Activation of p53 by specific agents in potential cancer therapy. |journal=Current medicinal chemistry. Anti-cancer agents |volume=5 |issue= 2 |pages= 131-5 |year= 2005 |pmid= 15777220 |doi= }}
*{{cite journal | author=Duensing A, Duensing S |title=Guilt by association? p53 and the development of aneuploidy in cancer. |journal=Biochem. Biophys. Res. Commun. |volume=331 |issue= 3 |pages= 694-700 |year= 2005 |pmid= 15865924 |doi= 10.1016/j.bbrc.2005.03.157 }}
*{{cite journal | author=Castedo M, Perfettini JL, Piacentini M, Kroemer G |title=p53-A pro-apoptotic signal transducer involved in AIDS. |journal=Biochem. Biophys. Res. Commun. |volume=331 |issue= 3 |pages= 701-6 |year= 2005 |pmid= 15865925 |doi= 10.1016/j.bbrc.2005.03.188 }}
*{{cite journal | author=Asher G, Shaul Y |title=p53 proteasomal degradation: poly-ubiquitination is not the whole story. |journal=Cell Cycle |volume=4 |issue= 8 |pages= 1015-8 |year= 2006 |pmid= 16082197 |doi= }}
*{{cite journal | author=Meulmeester E, Pereg Y, Shiloh Y, Jochemsen AG |title=ATM-mediated phosphorylations inhibit Mdmx/Mdm2 stabilization by HAUSP in favor of p53 activation. |journal=Cell Cycle |volume=4 |issue= 9 |pages= 1166-70 |year= 2006 |pmid= 16082221 |doi= }}
*{{cite journal | author=Pise-Masison CA, Jeong SJ, Brady JN |title=Human T cell leukemia virus type 1: the role of Tax in leukemogenesis. |journal=Arch. Immunol. Ther. Exp. (Warsz.) |volume=53 |issue= 4 |pages= 283-96 |year= 2005 |pmid= 16088313 |doi= }}
*{{cite journal | author=Lacroix M, Toillon RA, Leclercq G |title=p53 and breast cancer, an update. |journal=Endocr. Relat. Cancer |volume=13 |issue= 2 |pages= 293-325 |year= 2006 |pmid= 16728565 |doi= 10.1677/erc.1.01172 }}
*{{cite journal | author=Matsumoto M, Furihata M, Ohtsuki Y |title=Posttranslational phosphorylation of mutant p53 protein in tumor development. |journal=Medical molecular morphology |volume=39 |issue= 2 |pages= 79-87 |year= 2006 |pmid= 16821145 |doi= 10.1007/s00795-006-0320-0 }}
*{{cite journal | author=Liebermann DA, Hoffman B, Vesely D |title=p53 induced growth arrest versus apoptosis and its modulation by survival cytokines. |journal=Cell Cycle |volume=6 |issue= 2 |pages= 166-70 |year= 2007 |pmid= 17264673 |doi= }}
*{{cite journal | author=Huang CL, Yokomise H, Miyatake A |title=Clinical significance of the p53 pathway and associated gene therapy in non-small cell lung cancers. |journal=Future oncology (London, England) |volume=3 |issue= 1 |pages= 83-93 |year= 2007 |pmid= 17280505 |doi= 10.2217/14796694.3.1.83 }}
*{{cite journal | author=Soussi T |title=p53 alterations in human cancer: more questions than answers. |journal=Oncogene |volume=26 |issue= 15 |pages= 2145-56 |year= 2007 |pmid= 17401423 |doi= 10.1038/sj.onc.1210280 }}
*{{cite journal | author=Petitjean A, Achatz MI, Borresen-Dale AL, ''et al.'' |title=TP53 mutations in human cancers: functional selection and impact on cancer prognosis and outcomes. |journal=Oncogene |volume=26 |issue= 15 |pages= 2157-65 |year= 2007 |pmid= 17401424 |doi= 10.1038/sj.onc.1210302 }}
*{{cite journal | author=Hussain SP, Schwank J, Staib F, ''et al.'' |title=TP53 mutations and hepatocellular carcinoma: insights into the etiology and pathogenesis of liver cancer. |journal=Oncogene |volume=26 |issue= 15 |pages= 2166-76 |year= 2007 |pmid= 17401425 |doi= 10.1038/sj.onc.1210279 }}
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*{{cite journal | author=Mellert H, Sykes SM, Murphy ME, McMahon SB |title=The ARF/oncogene pathway activates p53 acetylation within the DNA binding domain. |journal=Cell Cycle |volume=6 |issue= 11 |pages= 1304-6 |year= 2007 |pmid= 17534149 |doi= }}
}}
{{refend}}
VEGFA
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Vascular endothelial growth factor A''', also known as '''VEGFA''', is a human [[gene]].
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_VEGFA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bj1.
| PDB = {{PDB2|1bj1}}, {{PDB2|1cz8}}, {{PDB2|1flt}}, {{PDB2|1kat}}, {{PDB2|1kmx}}, {{PDB2|1mjv}}, {{PDB2|1mkg}}, {{PDB2|1mkk}}, {{PDB2|1qty}}, {{PDB2|1tzh}}, {{PDB2|1tzi}}, {{PDB2|1vgh}}, {{PDB2|1vpf}}, {{PDB2|1vpp}}, {{PDB2|2fjg}}, {{PDB2|2fjh}}, {{PDB2|2vgh}}, {{PDB2|2vpf}}
| Name = Vascular endothelial growth factor A
| HGNCid = 12680
| Symbol = VEGFA
| AltSymbols =; MGC70609; VEGF; VEGF-A; VPF
| OMIM = 192240
| ECnumber =
| Homologene = 2534
| MGIid = 103178
| GeneAtlas_image1 = PBB_GE_VEGFA_210512_s_at.png
| GeneAtlas_image2 = PBB_GE_VEGFA_210513_s_at.png
| GeneAtlas_image3 = PBB_GE_VEGFA_211527_x_at.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0005172 |text = vascular endothelial growth factor receptor binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0050840 |text = extracellular matrix binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0001570 |text = vasculogenesis}} {{GNF_GO|id=GO:0001666 |text = response to hypoxia}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007498 |text = mesoderm development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0016477 |text = cell migration}} {{GNF_GO|id=GO:0030324 |text = lung development}} {{GNF_GO|id=GO:0030855 |text = epithelial cell differentiation}} {{GNF_GO|id=GO:0030949 |text = positive regulation of vascular endothelial growth factor receptor signaling pathway}} {{GNF_GO|id=GO:0042462 |text = eye photoreceptor cell development}} {{GNF_GO|id=GO:0050679 |text = positive regulation of epithelial cell proliferation}} {{GNF_GO|id=GO:0050930 |text = induction of positive chemotaxis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7422
| Hs_Ensembl = ENSG00000112715
| Hs_RefseqProtein = NP_001020537
| Hs_RefseqmRNA = NM_001025366
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 43845924
| Hs_GenLoc_end = 43862202
| Hs_Uniprot = P15692
| Mm_EntrezGene = 22339
| Mm_Ensembl = ENSMUSG00000023951
| Mm_RefseqmRNA = NM_001025250
| Mm_RefseqProtein = NP_001020421
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 45480574
| Mm_GenLoc_end = 45495331
| Mm_Uniprot = A0FKR4
}}
}}
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the PDGF/VEGF growth factor family and encodes a protein that is often found as a disulfide linked homodimer. This protein is a glycosylated mitogen that specifically acts on endothelial cells and has various effects, including mediating increased vascular permeability, inducing angiogenesis, vasculogenesis and endothelial cell growth, promoting cell migration, and inhibiting apoptosis. Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. Alternate transcriptional splice variants, encoding either freely secreted or cell-associated isoforms, have been characterized. There is also evidence for the use of non-AUG (CUG) translation initiation sites upstream of, and in-frame with the first AUG, leading to additional isoforms.<ref>{{cite web | title = Entrez Gene: VEGFA vascular endothelial growth factor A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7422| accessdate = 2007-09-05}}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ferrara N, Gerber HP |title=The role of vascular endothelial growth factor in angiogenesis. |journal=Acta Haematol. |volume=106 |issue= 4 |pages= 148-56 |year= 2002 |pmid= 11815711 |doi= }}
*{{cite journal | author=Orpana A, Salven P |title=Angiogenic and lymphangiogenic molecules in hematological malignancies. |journal=Leuk. Lymphoma |volume=43 |issue= 2 |pages= 219-24 |year= 2003 |pmid= 11999550 |doi= }}
*{{cite journal | author=Afuwape AO, Kiriakidis S, Paleolog EM |title=The role of the angiogenic molecule VEGF in the pathogenesis of rheumatoid arthritis. |journal=Histol. Histopathol. |volume=17 |issue= 3 |pages= 961-72 |year= 2003 |pmid= 12168808 |doi= }}
*{{cite journal | author=de Bont ES, Neefjes VM, Rosati S, ''et al.'' |title=New vessel formation and aberrant VEGF/VEGFR signaling in acute leukemia: does it matter? |journal=Leuk. Lymphoma |volume=43 |issue= 10 |pages= 1901-9 |year= 2003 |pmid= 12481883 |doi= }}
*{{cite journal | author=Ria R, Roccaro AM, Merchionne F, ''et al.'' |title=Vascular endothelial growth factor and its receptors in multiple myeloma. |journal=Leukemia |volume=17 |issue= 10 |pages= 1961-6 |year= 2003 |pmid= 14513045 |doi= 10.1038/sj.leu.2403076 }}
*{{cite journal | author=Caldwell RB, Bartoli M, Behzadian MA, ''et al.'' |title=Vascular endothelial growth factor and diabetic retinopathy: pathophysiological mechanisms and treatment perspectives. |journal=Diabetes Metab. Res. Rev. |volume=19 |issue= 6 |pages= 442-55 |year= 2004 |pmid= 14648803 |doi= 10.1002/dmrr.415 }}
*{{cite journal | author=Patan S |title=Vasculogenesis and angiogenesis. |journal=Cancer Treat. Res. |volume=117 |issue= |pages= 3-32 |year= 2004 |pmid= 15015550 |doi= }}
*{{cite journal | author=Machein MR, Plate KH |title=Role of VEGF in developmental angiogenesis and in tumor angiogenesis in the brain. |journal=Cancer Treat. Res. |volume=117 |issue= |pages= 191-218 |year= 2004 |pmid= 15015562 |doi= }}
*{{cite journal | author=Eremina V, Quaggin SE |title=The role of VEGF-A in glomerular development and function. |journal=Curr. Opin. Nephrol. Hypertens. |volume=13 |issue= 1 |pages= 9-15 |year= 2004 |pmid= 15090854 |doi= }}
*{{cite journal | author=Storkebaum E, Lambrechts D, Carmeliet P |title=VEGF: once regarded as a specific angiogenic factor, now implicated in neuroprotection. |journal=Bioessays |volume=26 |issue= 9 |pages= 943-54 |year= 2004 |pmid= 15351965 |doi= 10.1002/bies.20092 }}
*{{cite journal | author=Ribatti D |title=The crucial role of vascular permeability factor/vascular endothelial growth factor in angiogenesis: a historical review. |journal=Br. J. Haematol. |volume=128 |issue= 3 |pages= 303-9 |year= 2005 |pmid= 15667531 |doi= 10.1111/j.1365-2141.2004.05291.x }}
*{{cite journal | author=Loureiro RM, D'Amore PA |title=Transcriptional regulation of vascular endothelial growth factor in cancer. |journal=Cytokine Growth Factor Rev. |volume=16 |issue= 1 |pages= 77-89 |year= 2005 |pmid= 15733833 |doi= 10.1016/j.cytogfr.2005.01.005 }}
*{{cite journal | author=Rini BI |title=VEGF-targeted therapy in metastatic renal cell carcinoma. |journal=Oncologist |volume=10 |issue= 3 |pages= 191-7 |year= 2005 |pmid= 15793222 |doi= 10.1634/theoncologist.10-3-191 }}
*{{cite journal | author=Herbst RS, Onn A, Sandler A |title=Angiogenesis and lung cancer: prognostic and therapeutic implications. |journal=J. Clin. Oncol. |volume=23 |issue= 14 |pages= 3243-56 |year= 2005 |pmid= 15886312 |doi= 10.1200/JCO.2005.18.853 }}
*{{cite journal | author=Pufe T, Kurz B, Petersen W, ''et al.'' |title=The influence of biomechanical parameters on the expression of VEGF and endostatin in the bone and joint system. |journal=Ann. Anat. |volume=187 |issue= 5-6 |pages= 461-72 |year= 2006 |pmid= 16320826 |doi= }}
*{{cite journal | author=Tong JP, Yao YF |title=Contribution of VEGF and PEDF to choroidal angiogenesis: a need for balanced expressions. |journal=Clin. Biochem. |volume=39 |issue= 3 |pages= 267-76 |year= 2006 |pmid= 16409998 |doi= 10.1016/j.clinbiochem.2005.11.013 }}
*{{cite journal | author=Lambrechts D, Carmeliet P |title=VEGF at the neurovascular interface: therapeutic implications for motor neuron disease. |journal=Biochim. Biophys. Acta |volume=1762 |issue= 11-12 |pages= 1109-21 |year= 2007 |pmid= 16784838 |doi= 10.1016/j.bbadis.2006.04.005 }}
*{{cite journal | author=Matsumoto T, Mugishima H |title=Signal transduction via vascular endothelial growth factor (VEGF) receptors and their roles in atherogenesis. |journal=J. Atheroscler. Thromb. |volume=13 |issue= 3 |pages= 130-5 |year= 2006 |pmid= 16835467 |doi= }}
*{{cite journal | author=Bogaert E, Van Damme P, Van Den Bosch L, Robberecht W |title=Vascular endothelial growth factor in amyotrophic lateral sclerosis and other neurodegenerative diseases. |journal=Muscle Nerve |volume=34 |issue= 4 |pages= 391-405 |year= 2006 |pmid= 16856151 |doi= 10.1002/mus.20609 }}
*{{cite journal | author=Mercurio AM, Lipscomb EA, Bachelder RE |title=Non-angiogenic functions of VEGF in breast cancer. |journal=Journal of mammary gland biology and neoplasia |volume=10 |issue= 4 |pages= 283-90 |year= 2006 |pmid= 16924371 |doi= 10.1007/s10911-006-9001-9 }}
*{{cite journal | author=Makinde T, Murphy RF, Agrawal DK |title=Immunomodulatory role of vascular endothelial growth factor and angiopoietin-1 in airway remodeling. |journal=Curr. Mol. Med. |volume=6 |issue= 8 |pages= 831-41 |year= 2007 |pmid= 17168735 |doi= }}
*{{cite journal | author=Rini BI, Rathmell WK |title=Biological aspects and binding strategies of vascular endothelial growth factor in renal cell carcinoma. |journal=Clin. Cancer Res. |volume=13 |issue= 2 Pt 2 |pages= 741s-746s |year= 2007 |pmid= 17255303 |doi= 10.1158/1078-0432.CCR-06-2110 }}
}}
{{refend}}
end log.
