Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 00:25, 17 November 2007 (UTC)
[edit]Proteins without matches (14)
[edit]Proteins with a High Potential Match (7)
[edit]Redirected Proteins (4)
[edit]Manual Inspection (Page not found) (21)
[edit]
Protein Status Grid - Date: 00:25, 17 November 2007 (UTC)
[edit]Vebose Log - Date: 00:25, 17 November 2007 (UTC)
[edit]- INFO: Beginning work on ATP1A1... {November 16, 2007 4:03:00 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:03:26 PM PST}
<!-- 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
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ATP1A1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mo7.
| PDB = {{PDB2|1mo7}}, {{PDB2|1mo8}}
| Name = ATPase, Na+/K+ transporting, alpha 1 polypeptide
| HGNCid = 799
| Symbol = ATP1A1
| AltSymbols =; MGC3285; MGC51750
| OMIM = 182310
| ECnumber =
| Homologene = 564
| MGIid = 88105
| GeneAtlas_image1 = PBB_GE_ATP1A1_220948_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003869 |text = 4-nitrophenylphosphatase activity}} {{GNF_GO|id=GO:0005391 |text = sodium:potassium-exchanging ATPase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0015077 |text = monovalent inorganic cation transmembrane transporter activity}} {{GNF_GO|id=GO:0015662 |text = ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016820 |text = hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}} {{GNF_GO|id=GO:0031402 |text = sodium ion binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0005890 |text = sodium:potassium-exchanging ATPase complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016323 |text = basolateral plasma membrane}} {{GNF_GO|id=GO:0042383 |text = sarcolemma}}
| Process = {{GNF_GO|id=GO:0002026 |text = cardiac inotropy}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006812 |text = cation transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}} {{GNF_GO|id=GO:0006814 |text = sodium ion transport}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0008217 |text = blood pressure regulation}} {{GNF_GO|id=GO:0015991 |text = ATP hydrolysis coupled proton transport}} {{GNF_GO|id=GO:0030317 |text = sperm motility}} {{GNF_GO|id=GO:0030641 |text = cellular hydrogen ion homeostasis}} {{GNF_GO|id=GO:0045822 |text = negative regulation of heart contraction}} {{GNF_GO|id=GO:0045823 |text = positive regulation of heart contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 476
| Hs_Ensembl = ENSG00000163399
| Hs_RefseqProtein = NP_000692
| Hs_RefseqmRNA = NM_000701
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 116717359
| Hs_GenLoc_end = 116754301
| Hs_Uniprot = P05023
| Mm_EntrezGene = 11928
| Mm_Ensembl = ENSMUSG00000033161
| Mm_RefseqmRNA = NM_144900
| Mm_RefseqProtein = NP_659149
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 101705286
| Mm_GenLoc_end = 101733745
| Mm_Uniprot = Q3TXF9
}}
}}
'''ATPase, Na+/K+ transporting, alpha 1 polypeptide''', also known as '''ATP1A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP1A1 ATPase, Na+/K+ transporting, alpha 1 polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=476| accessdate = }}</ref>
<!-- 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 belongs to the family of P-type cation transport ATPases, and to the subfamily of Na+/K+ -ATPases. Na+/K+ -ATPase is an integral membrane protein responsible for establishing and maintaining the electrochemical gradients of Na and K ions across the plasma membrane. These gradients are essential for osmoregulation, for sodium-coupled transport of a variety of organic and inorganic molecules, and for electrical excitability of nerve and muscle. This enzyme is composed of two subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The catalytic subunit of Na+/K+ -ATPase is encoded by multiple genes. This gene encodes an alpha 1 subunit. Alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: ATP1A1 ATPase, Na+/K+ transporting, alpha 1 polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=476| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lingrel JB, Orlowski J, Shull MM, Price EM |title=Molecular genetics of Na,K-ATPase. |journal=Prog. Nucleic Acid Res. Mol. Biol. |volume=38 |issue= |pages= 37-89 |year= 1990 |pmid= 2158121 |doi= }}
*{{cite journal | author=Dunbar LA, Caplan MJ |title=Ion pumps in polarized cells: sorting and regulation of the Na+, K+- and H+, K+-ATPases. |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 29617-20 |year= 2001 |pmid= 11404365 |doi= 10.1074/jbc.R100023200 }}
*{{cite journal | author=Wangemann P |title=K+ cycling and the endocochlear potential. |journal=Hear. Res. |volume=165 |issue= 1-2 |pages= 1-9 |year= 2002 |pmid= 12031509 |doi= }}
*{{cite journal | author=Xie Z, Cai T |title=Na+-K+--ATPase-mediated signal transduction: from protein interaction to cellular function. |journal=Mol. Interv. |volume=3 |issue= 3 |pages= 157-68 |year= 2004 |pmid= 14993422 |doi= 10.1124/mi.3.3.157 }}
*{{cite journal | author=Shull MM, Pugh DG, Lingrel JB |title=The human Na, K-ATPase alpha 1 gene: characterization of the 5'-flanking region and identification of a restriction fragment length polymorphism. |journal=Genomics |volume=6 |issue= 3 |pages= 451-60 |year= 1990 |pmid= 1970326 |doi= }}
*{{cite journal | author=Herrera VL, Ruiz-Opazo N |title=Alteration of alpha 1 Na+,K(+)-ATPase 86Rb+ influx by a single amino acid substitution. |journal=Science |volume=249 |issue= 4972 |pages= 1023-6 |year= 1990 |pmid= 1975705 |doi= }}
*{{cite journal | author=Kawakami K, Ohta T, Nojima H, Nagano K |title=Primary structure of the alpha-subunit of human Na,K-ATPase deduced from cDNA sequence. |journal=J. Biochem. |volume=100 |issue= 2 |pages= 389-97 |year= 1986 |pmid= 2430951 |doi= }}
*{{cite journal | author=Yang-Feng TL, Schneider JW, Lindgren V, ''et al.'' |title=Chromosomal localization of human Na+, K+-ATPase alpha- and beta-subunit genes. |journal=Genomics |volume=2 |issue= 2 |pages= 128-38 |year= 1988 |pmid= 2842249 |doi= }}
*{{cite journal | author=Sverdlov ED, Broude NE, Sverdlov VE, ''et al.'' |title=Family of Na+,K+-ATPase genes. Intra-individual tissue-specific restriction fragment length polymorphism. |journal=FEBS Lett. |volume=221 |issue= 1 |pages= 129-33 |year= 1987 |pmid= 2887455 |doi= }}
*{{cite journal | author=Chehab FF, Kan YW, Law ML, ''et al.'' |title=Human placental Na+,K+-ATPase alpha subunit: cDNA cloning, tissue expression, DNA polymorphism, and chromosomal localization. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 22 |pages= 7901-5 |year= 1987 |pmid= 2891135 |doi= }}
*{{cite journal | author=Ovchinnikov YuA , Monastyrskaya GS, Broude NE, ''et al.'' |title=The family of human Na+,K+-ATPase genes. A partial nucleotide sequence related to the alpha-subunit. |journal=FEBS Lett. |volume=213 |issue= 1 |pages= 73-80 |year= 1987 |pmid= 3030810 |doi= }}
*{{cite journal | author=Shull MM, Lingrel JB |title=Multiple genes encode the human Na+,K+-ATPase catalytic subunit. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 12 |pages= 4039-43 |year= 1987 |pmid= 3035563 |doi= }}
*{{cite journal | author=Sverdlov ED, Monastyrskaya GS, Broude NE, ''et al.'' |title=The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit. |journal=FEBS Lett. |volume=217 |issue= 2 |pages= 275-8 |year= 1987 |pmid= 3036582 |doi= }}
*{{cite journal | author=Ruiz A, Bhat SP, Bok D |title=Characterization and quantification of full-length and truncated Na,K-ATPase alpha 1 and beta 1 RNA transcripts expressed in human retinal pigment epithelium. |journal=Gene |volume=155 |issue= 2 |pages= 179-84 |year= 1995 |pmid= 7536695 |doi= }}
*{{cite journal | author=Hundal HS, Maxwell DL, Ahmed A, ''et al.'' |title=Subcellular distribution and immunocytochemical localization of Na,K-ATPase subunit isoforms in human skeletal muscle. |journal=Mol. Membr. Biol. |volume=11 |issue= 4 |pages= 255-62 |year= 1995 |pmid= 7711835 |doi= }}
*{{cite journal | author=Feschenko MS, Sweadner KJ |title=Structural basis for species-specific differences in the phosphorylation of Na,K-ATPase by protein kinase C. |journal=J. Biol. Chem. |volume=270 |issue= 23 |pages= 14072-7 |year= 1995 |pmid= 7775468 |doi= }}
*{{cite journal | author=Ruiz-Opazo N, Barany F, Hirayama K, Herrera VL |title=Confirmation of mutant alpha 1 Na,K-ATPase gene and transcript in Dahl salt-sensitive/JR rats. |journal=Hypertension |volume=24 |issue= 3 |pages= 260-70 |year= 1994 |pmid= 8082931 |doi= }}
*{{cite journal | author=Zahler R, Gilmore-Hebert M, Baldwin JC, ''et al.'' |title=Expression of alpha isoforms of the Na,K-ATPase in human heart. |journal=Biochim. Biophys. Acta |volume=1149 |issue= 2 |pages= 189-94 |year= 1993 |pmid= 8391840 |doi= }}
*{{cite journal | author=Wang J, Schwinger RH, Frank K, ''et al.'' |title=Regional expression of sodium pump subunits isoforms and Na+-Ca++ exchanger in the human heart. |journal=J. Clin. Invest. |volume=98 |issue= 7 |pages= 1650-8 |year= 1996 |pmid= 8833915 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on C4A... {November 16, 2007 4:03:26 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:04:53 PM PST}
<!-- 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
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_C4A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hzf.
| PDB = {{PDB2|1hzf}}
| Name = Complement component 4A (Rodgers blood group)
| HGNCid = 1323
| Symbol = C4A
| AltSymbols =; C4; C4A2; C4A3; C4A4; C4A6; C4B; C4S; CO4; CPAMD2; RG; C4A; C4A13; C4A91; C4B1; C4B12; C4B2; C4B3; C4B5; C4F; CH; CPAMD3
| OMIM = 120810
| ECnumber =
| Homologene = 36030
| MGIid = 88228
| GeneAtlas_image1 = PBB_GE_C4A_208451_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_C4A_214428_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004866 |text = endopeptidase inhibitor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006956 |text = complement activation}} {{GNF_GO|id=GO:0006958 |text = complement activation, classical pathway}} {{GNF_GO|id=GO:0045087 |text = innate immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 720
| Hs_Ensembl = ENSG00000204319
| Hs_RefseqProtein = NP_009224
| Hs_RefseqmRNA = NM_007293
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 32090517
| Hs_GenLoc_end = 32111174
| Hs_Uniprot = P0C0L4
| Mm_EntrezGene = 12268
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_001002697
| Mm_RefseqProtein = XP_001002697
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Complement component 4A (Rodgers blood group)''', also known as '''C4A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: C4A complement component 4A (Rodgers blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=720| accessdate = }}</ref>
<!-- 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 the acidic form of complement factor 4, part of the classical activation pathway. The protein is expressed as a single chain precursor which is proteolytically cleaved into a trimer of alpha, beta, and gamma chains prior to secretion. The trimer provides a surface for interaction between the antigen-antibody complex and other complement components. The alpha chain may be cleaved to release C4 anaphylatoxin, a mediator of local inflammation. Deficiency of this protein is associated with systemic lupus erythematosus and type I diabetes mellitus. This gene localizes to the major histocompatibility complex (MHC) class III region on chromosome 6. Varying haplotypes of this gene cluster exist, such that individuals may have 1, 2, or 3 copies of this gene.<ref name="entrez">{{cite web | title = Entrez Gene: C4A complement component 4A (Rodgers blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=720| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hugli TE |title=Biochemistry and biology of anaphylatoxins. |journal=Complement |volume=3 |issue= 3 |pages= 111-27 |year= 1987 |pmid= 3542363 |doi= }}
*{{cite journal | author=Yu CY |title=Molecular genetics of the human MHC complement gene cluster. |journal=Exp. Clin. Immunogenet. |volume=15 |issue= 4 |pages= 213-30 |year= 1999 |pmid= 10072631 |doi= }}
*{{cite journal | author=Anderson MJ, Milner CM, Cotton RG, Campbell RD |title=The coding sequence of the hemolytically inactive C4A6 allotype of human complement component C4 reveals that a single arginine to tryptophan substitution at beta-chain residue 458 is the likely cause of the defect. |journal=J. Immunol. |volume=148 |issue= 9 |pages= 2795-802 |year= 1992 |pmid= 1573268 |doi= }}
*{{cite journal | author=Hessing M, van 't Veer C, Hackeng TM, ''et al.'' |title=Importance of the alpha 3-fragment of complement C4 for the binding with C4b-binding protein. |journal=FEBS Lett. |volume=271 |issue= 1-2 |pages= 131-6 |year= 1990 |pmid= 1699796 |doi= }}
*{{cite journal | author=Yu CY |title=The complete exon-intron structure of a human complement component C4A gene. DNA sequences, polymorphism, and linkage to the 21-hydroxylase gene. |journal=J. Immunol. |volume=146 |issue= 3 |pages= 1057-66 |year= 1991 |pmid= 1988494 |doi= }}
*{{cite journal | author=Ghiso J, Saball E, Leoni J, ''et al.'' |title=Binding of cystatin C to C4: the importance of sense-antisense peptides in their interaction. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 4 |pages= 1288-91 |year= 1990 |pmid= 2304899 |doi= }}
*{{cite journal | author=Yu CY, Belt KT, Giles CM, ''et al.'' |title=Structural basis of the polymorphism of human complement components C4A and C4B: gene size, reactivity and antigenicity. |journal=EMBO J. |volume=5 |issue= 11 |pages= 2873-81 |year= 1987 |pmid= 2431902 |doi= }}
*{{cite journal | author=Speiser PW, White PC |title=Structure of the human RD gene: a highly conserved gene in the class III region of the major histocompatibility complex. |journal=DNA |volume=8 |issue= 10 |pages= 745-51 |year= 1990 |pmid= 2612324 |doi= }}
*{{cite journal | author=Palsdottir A, Fossdal R, Arnason A, ''et al.'' |title=Heterogeneity of human C4 gene size. A large intron (6.5 kb) is present in all C4A genes and some C4B genes. |journal=Immunogenetics |volume=25 |issue= 5 |pages= 299-304 |year= 1987 |pmid= 2883116 |doi= }}
*{{cite journal | author=Kishore N, Shah D, Skanes VM, Levine RP |title=The fluid-phase binding of human C4 and its genetic variants, C4A3 and C4B1, to immunoglobulins. |journal=Mol. Immunol. |volume=25 |issue= 9 |pages= 811-9 |year= 1989 |pmid= 3264881 |doi= }}
*{{cite journal | author=Chakravarti DN, Campbell RD, Porter RR |title=The chemical structure of the C4d fragment of the human complement component C4. |journal=Mol. Immunol. |volume=24 |issue= 11 |pages= 1187-97 |year= 1988 |pmid= 3696167 |doi= }}
*{{cite journal | author=Belt KT, Yu CY, Carroll MC, Porter RR |title=Polymorphism of human complement component C4. |journal=Immunogenetics |volume=21 |issue= 2 |pages= 173-80 |year= 1985 |pmid= 3838531 |doi= }}
*{{cite journal | author=Hortin G, Sims H, Strauss AW |title=Identification of the site of sulfation of the fourth component of human complement. |journal=J. Biol. Chem. |volume=261 |issue= 4 |pages= 1786-93 |year= 1986 |pmid= 3944109 |doi= }}
*{{cite journal | author=Moon KE, Gorski JP, Hugli TE |title=Complete primary structure of human C4a anaphylatoxin. |journal=J. Biol. Chem. |volume=256 |issue= 16 |pages= 8685-92 |year= 1981 |pmid= 6167582 |doi= }}
*{{cite journal | author=Palsdottir A, Cross SJ, Edwards JH, Carroll MC |title=Correlation between a DNA restriction fragment length polymorphism and C4A6 protein. |journal=Nature |volume=306 |issue= 5943 |pages= 615-6 |year= 1984 |pmid= 6316164 |doi= }}
*{{cite journal | author=Belt KT, Carroll MC, Porter RR |title=The structural basis of the multiple forms of human complement component C4. |journal=Cell |volume=36 |issue= 4 |pages= 907-14 |year= 1984 |pmid= 6546707 |doi= }}
*{{cite journal | author=Carroll MC, Campbell RD, Bentley DR, Porter RR |title=A molecular map of the human major histocompatibility complex class III region linking complement genes C4, C2 and factor B. |journal=Nature |volume=307 |issue= 5948 |pages= 237-41 |year= 1984 |pmid= 6559257 |doi= }}
*{{cite journal | author=Carroll MC, Porter RR |title=Cloning of a human complement component C4 gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 1 |pages= 264-7 |year= 1983 |pmid= 6572000 |doi= }}
*{{cite journal | author=Whitehead AS, Goldberger G, Woods DE, ''et al.'' |title=Use of a cDNA clone for the fourth component of human complement (C4) for analysis of a genetic deficiency of C4 in guinea pig. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 17 |pages= 5387-91 |year= 1983 |pmid= 6577433 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CALM3... {November 16, 2007 4:04:53 PM PST}
- SEARCH REDIRECT: Control Box Found: CALM3 {November 16, 2007 4:05:18 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:05:19 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:05:19 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:05:19 PM PST}
- UPDATED: Updated protein page: CALM3 {November 16, 2007 4:05:26 PM PST}
- INFO: Beginning work on CD82... {November 16, 2007 4:09:29 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:10:14 PM PST}
<!-- 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
}}
<!-- 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 = CD82 molecule
| HGNCid = 6210
| Symbol = CD82
| AltSymbols =; R2; IA4; 4F9; C33; GR15; KAI1; SAR2; ST6; TSPAN27
| OMIM = 600623
| ECnumber =
| Homologene = 20512
| MGIid = 104651
| GeneAtlas_image1 = PBB_GE_CD82_203904_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3732
| Hs_Ensembl = ENSG00000085117
| Hs_RefseqProtein = NP_001020015
| Hs_RefseqmRNA = NM_001024844
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 44543717
| Hs_GenLoc_end = 44597889
| Hs_Uniprot = P27701
| Mm_EntrezGene = 12521
| Mm_Ensembl = ENSMUSG00000027215
| Mm_RefseqmRNA = NM_007656
| Mm_RefseqProtein = NP_031682
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 93219950
| Mm_GenLoc_end = 93263335
| Mm_Uniprot = Q3UII2
}}
}}
'''CD82 molecule''', also known as '''CD82''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CD82 CD82 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3732| accessdate = }}</ref>
<!-- 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 metastasis suppressor gene product is a membrane glycoprotein that is a member of the transmembrane 4 superfamily. Expression of this gene has been shown to be downregulated in tumor progression of human cancers and can be activated by p53 through a consensus binding sequence in the promoter. Its expression and that of p53 are strongly correlated, and the loss of expression of these two proteins is associated with poor survival for prostate cancer patients. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CD82 CD82 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3732| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Baek SH |title=A novel link between SUMO modification and cancer metastasis. |journal=Cell Cycle |volume=5 |issue= 14 |pages= 1492-5 |year= 2006 |pmid= 16861889 |doi= }}
*{{cite journal | author=Imai T, Fukudome K, Takagi S, ''et al.'' |title=C33 antigen recognized by monoclonal antibodies inhibitory to human T cell leukemia virus type 1-induced syncytium formation is a member of a new family of transmembrane proteins including CD9, CD37, CD53, and CD63. |journal=J. Immunol. |volume=149 |issue= 9 |pages= 2879-86 |year= 1992 |pmid= 1401919 |doi= }}
*{{cite journal | author=Ichikawa T, Ichikawa Y, Dong J, ''et al.'' |title=Localization of metastasis suppressor gene(s) for prostatic cancer to the short arm of human chromosome 11. |journal=Cancer Res. |volume=52 |issue= 12 |pages= 3486-90 |year= 1992 |pmid= 1596907 |doi= }}
*{{cite journal | author=Gaugitsch HW, Hofer E, Huber NE, ''et al.'' |title=A new superfamily of lymphoid and melanoma cell proteins with extensive homology to Schistosoma mansoni antigen Sm23. |journal=Eur. J. Immunol. |volume=21 |issue= 2 |pages= 377-83 |year= 1991 |pmid= 1842498 |doi= }}
*{{cite journal | author=Ichikawa T, Ichikawa Y, Isaacs JT |title=Genetic factors and suppression of metastatic ability of prostatic cancer. |journal=Cancer Res. |volume=51 |issue= 14 |pages= 3788-92 |year= 1991 |pmid= 2065333 |doi= }}
*{{cite journal | author=Imai T, Kakizaki M, Nishimura M, Yoshie O |title=Molecular analyses of the association of CD4 with two members of the transmembrane 4 superfamily, CD81 and CD82. |journal=J. Immunol. |volume=155 |issue= 3 |pages= 1229-39 |year= 1995 |pmid= 7636191 |doi= }}
*{{cite journal | author=Dong JT, Lamb PW, Rinker-Schaeffer CW, ''et al.'' |title=KAI1, a metastasis suppressor gene for prostate cancer on human chromosome 11p11.2. |journal=Science |volume=268 |issue= 5212 |pages= 884-6 |year= 1995 |pmid= 7754374 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Mannion BA, Berditchevski F, Kraeft SK, ''et al.'' |title=Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associated with integrin alpha 4 beta 1 (CD49d/CD29). |journal=J. Immunol. |volume=157 |issue= 5 |pages= 2039-47 |year= 1996 |pmid= 8757325 |doi= }}
*{{cite journal | author=Szöllósi J, Horejsí V, Bene L, ''et al.'' |title=Supramolecular complexes of MHC class I, MHC class II, CD20, and tetraspan molecules (CD53, CD81, and CD82) at the surface of a B cell line JY. |journal=J. Immunol. |volume=157 |issue= 7 |pages= 2939-46 |year= 1996 |pmid= 8816400 |doi= }}
*{{cite journal | author=Dong JT, Isaacs WB, Barrett JC, Isaacs JT |title=Genomic organization of the human KAI1 metastasis-suppressor gene. |journal=Genomics |volume=41 |issue= 1 |pages= 25-32 |year= 1997 |pmid= 9126478 |doi= 10.1006/geno.1997.4618 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Hammond C, Denzin LK, Pan M, ''et al.'' |title=The tetraspan protein CD82 is a resident of MHC class II compartments where it associates with HLA-DR, -DM, and -DO molecules. |journal=J. Immunol. |volume=161 |issue= 7 |pages= 3282-91 |year= 1998 |pmid= 9759843 |doi= }}
*{{cite journal | author=Horváth G, Serru V, Clay D, ''et al.'' |title=CD19 is linked to the integrin-associated tetraspans CD9, CD81, and CD82. |journal=J. Biol. Chem. |volume=273 |issue= 46 |pages= 30537-43 |year= 1998 |pmid= 9804823 |doi= }}
*{{cite journal | author=Serru V, Le Naour F, Billard M, ''et al.'' |title=Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions. |journal=Biochem. J. |volume=340 ( Pt 1) |issue= |pages= 103-11 |year= 1999 |pmid= 10229664 |doi= }}
*{{cite journal | author=Lombardi DP, Geradts J, Foley JF, ''et al.'' |title=Loss of KAI1 expression in the progression of colorectal cancer. |journal=Cancer Res. |volume=59 |issue= 22 |pages= 5724-31 |year= 1999 |pmid= 10582691 |doi= }}
*{{cite journal | author=Shibagaki N, Hanada K, Yamashita H, ''et al.'' |title=Overexpression of CD82 on human T cells enhances LFA-1 / ICAM-1-mediated cell-cell adhesion: functional association between CD82 and LFA-1 in T cell activation. |journal=Eur. J. Immunol. |volume=29 |issue= 12 |pages= 4081-91 |year= 2000 |pmid= 10602019 |doi= }}
*{{cite journal | author=Nakamura K, Mitamura T, Takahashi T, ''et al.'' |title=Importance of the major extracellular domain of CD9 and the epidermal growth factor (EGF)-like domain of heparin-binding EGF-like growth factor for up-regulation of binding and activity. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18284-90 |year= 2000 |pmid= 10749879 |doi= 10.1074/jbc.M907971199 }}
*{{cite journal | author=Odintsova E, Sugiura T, Berditchevski F |title=Attenuation of EGF receptor signaling by a metastasis suppressor, the tetraspanin CD82/KAI-1. |journal=Curr. Biol. |volume=10 |issue= 16 |pages= 1009-12 |year= 2001 |pmid= 10985391 |doi= }}
*{{cite journal | author=Ono M, Handa K, Withers DA, Hakomori S |title=Glycosylation effect on membrane domain (GEM) involved in cell adhesion and motility: a preliminary note on functional alpha3, alpha5-CD82 glycosylation complex in ldlD 14 cells. |journal=Biochem. Biophys. Res. Commun. |volume=279 |issue= 3 |pages= 744-50 |year= 2001 |pmid= 11162423 |doi= 10.1006/bbrc.2000.4030 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EZH2... {November 16, 2007 4:05:26 PM PST}
- SEARCH REDIRECT: Control Box Found: EZH2 {November 16, 2007 4:06:03 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:06:06 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:06:06 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:06:06 PM PST}
- UPDATED: Updated protein page: EZH2 {November 16, 2007 4:06:12 PM PST}
- INFO: Beginning work on FCER2... {November 16, 2007 4:06:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:06:54 PM PST}
<!-- 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
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FCER2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1t8c.
| PDB = {{PDB2|1t8c}}, {{PDB2|1t8d}}, {{PDB2|2h2r}}, {{PDB2|2h2t}}
| Name = Fc fragment of IgE, low affinity II, receptor for (CD23)
| HGNCid = 3612
| Symbol = FCER2
| AltSymbols =; CD23; CD23A; CLEC4J; FCE2; IGEBF
| OMIM = 151445
| ECnumber =
| Homologene = 1517
| MGIid = 95497
| GeneAtlas_image1 = PBB_GE_FCER2_206760_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FCER2_206759_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005057 |text = receptor signaling protein activity}} {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0019863 |text = IgE binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2208
| Hs_Ensembl = ENSG00000104921
| Hs_RefseqProtein = NP_001993
| Hs_RefseqmRNA = NM_002002
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 7659667
| Hs_GenLoc_end = 7673032
| Hs_Uniprot = P06734
| Mm_EntrezGene = 14128
| Mm_Ensembl = ENSMUSG00000005540
| Mm_RefseqmRNA = NM_013517
| Mm_RefseqProtein = NP_038545
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 3681801
| Mm_GenLoc_end = 3694174
| Mm_Uniprot = P20693
}}
}}
'''Fc fragment of IgE, low affinity II, receptor for (CD23)''', also known as '''FCER2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FCER2 Fc fragment of IgE, low affinity II, receptor for (CD23)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2208| accessdate = }}</ref>
<!-- 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 human leukocyte differentiation antigen CD23 (FCE2) is a key molecule for B-cell activation and growth. It is the low-affinity receptor for IgE. The truncated molecule can be secreted, then functioning as a potent mitogenic growth factor.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: FCER2 Fc fragment of IgE, low affinity II, receptor for (CD23)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2208| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kijimoto-Ochiai S |title=CD23 (the low-affinity IgE receptor) as a C-type lectin: a multidomain and multifunctional molecule. |journal=Cell. Mol. Life Sci. |volume=59 |issue= 4 |pages= 648-64 |year= 2002 |pmid= 12022472 |doi= }}
*{{cite journal | author=Schwarzmeier JD, Hubmann R, Düchler M, ''et al.'' |title=Regulation of CD23 expression by Notch2 in B-cell chronic lymphocytic leukemia. |journal=Leuk. Lymphoma |volume=46 |issue= 2 |pages= 157-65 |year= 2005 |pmid= 15621797 |doi= 10.1080/10428190400010742 }}
*{{cite journal | author=Maekawa N, Kawabe T, Sugie K, ''et al.'' |title=Induction of Fc epsilon RII/CD23 on PHA-activated human peripheral blood T lymphocytes and the association of Fyn tyrosine kinase with Fc epsilon RII/CD23. |journal=Res. Immunol. |volume=143 |issue= 4 |pages= 422-5 |year= 1992 |pmid= 1387715 |doi= }}
*{{cite journal | author=Rose K, Turcatti G, Graber P, ''et al.'' |title=Partial characterization of natural and recombinant human soluble CD23. |journal=Biochem. J. |volume=286 ( Pt 3) |issue= |pages= 819-24 |year= 1992 |pmid= 1417742 |doi= }}
*{{cite journal | author=Maekawa N, Kawabe T, Sugie K, ''et al.'' |title=Induction of Fc epsilon RII/CD23 on PHA-activated human peripheral blood T lymphocytes and association of fyn tyrosine kinase with Fc epsilon RII/CD23. |journal=International journal of tissue reactions |volume=14 |issue= 3 |pages= 121-30 |year= 1992 |pmid= 1446976 |doi= }}
*{{cite journal | author=Sugie K, Kawakami T, Maeda Y, ''et al.'' |title=Fyn tyrosine kinase associated with Fc epsilon RII/CD23: possible multiple roles in lymphocyte activation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 20 |pages= 9132-5 |year= 1991 |pmid= 1717997 |doi= }}
*{{cite journal | author=Bettler B, Hofstetter H, Rao M, ''et al.'' |title=Molecular structure and expression of the murine lymphocyte low-affinity receptor for IgE (Fc epsilon RII). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 19 |pages= 7566-70 |year= 1989 |pmid= 2529542 |doi= }}
*{{cite journal | author=Kikutani H, Inui S, Sato R, ''et al.'' |title=Molecular structure of human lymphocyte receptor for immunoglobulin E. |journal=Cell |volume=47 |issue= 5 |pages= 657-65 |year= 1987 |pmid= 2877743 |doi= }}
*{{cite journal | author=Ikuta K, Takami M, Kim CW, ''et al.'' |title=Human lymphocyte Fc receptor for IgE: sequence homology of its cloned cDNA with animal lectins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 3 |pages= 819-23 |year= 1987 |pmid= 2949326 |doi= }}
*{{cite journal | author=Yokota A, Kikutani H, Tanaka T, ''et al.'' |title=Two species of human Fc epsilon receptor II (Fc epsilon RII/CD23): tissue-specific and IL-4-specific regulation of gene expression. |journal=Cell |volume=55 |issue= 4 |pages= 611-8 |year= 1988 |pmid= 2972386 |doi= }}
*{{cite journal | author=Lüdin C, Hofstetter H, Sarfati M, ''et al.'' |title=Cloning and expression of the cDNA coding for a human lymphocyte IgE receptor. |journal=EMBO J. |volume=6 |issue= 1 |pages= 109-14 |year= 1987 |pmid= 3034567 |doi= }}
*{{cite journal | author=Aubry JP, Pochon S, Gauchat JF, ''et al.'' |title=CD23 interacts with a new functional extracytoplasmic domain involving N-linked oligosaccharides on CD21. |journal=J. Immunol. |volume=152 |issue= 12 |pages= 5806-13 |year= 1994 |pmid= 7515913 |doi= }}
*{{cite journal | author=Lecoanet-Henchoz S, Gauchat JF, Aubry JP, ''et al.'' |title=CD23 regulates monocyte activation through a novel interaction with the adhesion molecules CD11b-CD18 and CD11c-CD18. |journal=Immunity |volume=3 |issue= 1 |pages= 119-25 |year= 1995 |pmid= 7621072 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Padlan EA, Helm BA |title=Modeling of the lectin-homology domains of the human and murine low-affinity Fc epsilon receptor (Fc epsilon RII/CD23). |journal=Receptor |volume=3 |issue= 4 |pages= 325-41 |year= 1994 |pmid= 8142907 |doi= }}
*{{cite journal | author=Trask B, Fertitta A, Christensen M, ''et al.'' |title=Fluorescence in situ hybridization mapping of human chromosome 19: cytogenetic band location of 540 cosmids and 70 genes or DNA markers. |journal=Genomics |volume=15 |issue= 1 |pages= 133-45 |year= 1993 |pmid= 8432525 |doi= }}
*{{cite journal | author=Chirmule N, Kalyanaraman VS, Lederman S, ''et al.'' |title=HIV-gp 160-induced T cell-dependent B cell differentiation. Role of T cell-B cell activation molecule and IL-6. |journal=J. Immunol. |volume=150 |issue= 6 |pages= 2478-86 |year= 1993 |pmid= 8450224 |doi= }}
*{{cite journal | author=Förster HH, Wäsch R, Kretschmar T, ''et al.'' |title=Genetic markers on chromosome 19p and prenatal diagnosis of HLA class II-deficient combined immunodeficiency. |journal=Pediatr. Res. |volume=38 |issue= 5 |pages= 812-6 |year= 1996 |pmid= 8552454 |doi= }}
*{{cite journal | author=Bajorath J, Aruffo A |title=Structure-based modeling of the ligand binding domain of the human cell surface receptor CD23 and comparison of two independently derived molecular models. |journal=Protein Sci. |volume=5 |issue= 2 |pages= 240-7 |year= 1996 |pmid= 8745401 |doi= }}
*{{cite journal | author=Frémeaux-Bacchi V, Bernard I, Maillet F, ''et al.'' |title=Human lymphocytes shed a soluble form of CD21 (the C3dg/Epstein-Barr virus receptor, CR2) that binds iC3b and CD23. |journal=Eur. J. Immunol. |volume=26 |issue= 7 |pages= 1497-503 |year= 1996 |pmid= 8766552 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HLA-DRB3... {November 16, 2007 4:06:54 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:07:46 PM PST}
<!-- 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
}}
<!-- 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-DRB3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a6a.
| PDB = {{PDB2|1a6a}}, {{PDB2|1d5m}}, {{PDB2|1d5x}}, {{PDB2|1d5z}}, {{PDB2|1d6e}}, {{PDB2|1j8h}}, {{PDB2|2seb}}
| Name = Major histocompatibility complex, class II, DR beta 3
| HGNCid = 4951
| Symbol = HLA-DRB3
| AltSymbols =; HLA-DR3B; MGC117330
| OMIM =
| ECnumber =
| Homologene =
| MGIid =
| GeneAtlas_image1 = PBB_GE_HLA-DRB3_209312_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_HLA-DRB3_215193_x_at_tn.png
| Function = {{GNF_GO|id=GO:0032395 |text = MHC class II receptor activity}}
| Component = {{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:0042613 |text = MHC class II protein complex}}
| Process = {{GNF_GO|id=GO:0002504 |text = antigen processing and presentation of peptide or polysaccharide antigen via MHC class II}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3125
| Hs_Ensembl = ENSG00000206241
| Hs_RefseqProtein = NP_072049
| Hs_RefseqmRNA = NM_022555
| Hs_GenLoc_db =
| Hs_GenLoc_chr = c6_COX
| Hs_GenLoc_start = 32560298
| Hs_GenLoc_end = 32572205
| Hs_Uniprot = P79483
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Major histocompatibility complex, class II, DR beta 3''', also known as '''HLA-DRB3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HLA-DRB3 major histocompatibility complex, class II, DR beta 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3125| accessdate = }}</ref>
<!-- 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-DRB3 belongs to the HLA class II beta chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DRA) and a beta (DRB) chain, both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26-28 kDa and its gene contains 6 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and exon 5 encodes the cytoplasmic tail. Within the DR molecule the beta chain contains all the polymorphisms specifying the peptide binding specificities. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. DRB1 is expressed at a level five times higher than its paralogues DRB3, DRB4 and DRB5. The presence of DRB3 is linked with allelic variants of DRB1, otherwise it is omitted. There are 4 related pseudogenes: DRB2, DRB6, DRB7, DRB8 and DRB9.<ref name="entrez">{{cite web | title = Entrez Gene: HLA-DRB3 major histocompatibility complex, class II, DR beta 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3125| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Germain RN |title=Binding domain regulation of MHC class II molecule assembly, trafficking, fate, and function. |journal=Semin. Immunol. |volume=7 |issue= 6 |pages= 361-72 |year= 1996 |pmid= 8775462 |doi= 10.1006/smim.1995.0041 }}
*{{cite journal | author=Piatier-Tonneau D, Gastinel LN, Amblard F, ''et al.'' |title=Interaction of CD4 with HLA class II antigens and HIV gp120. |journal=Immunogenetics |volume=34 |issue= 2 |pages= 121-8 |year= 1991 |pmid= 1869305 |doi= }}
*{{cite journal | author=Nong Y, Kandil O, Tobin EH, ''et al.'' |title=The HIV core protein p24 inhibits interferon-gamma-induced increase of HLA-DR and cytochrome b heavy chain mRNA levels in the human monocyte-like cell line THP1. |journal=Cell. Immunol. |volume=132 |issue= 1 |pages= 10-6 |year= 1991 |pmid= 1905983 |doi= }}
*{{cite journal | author=Ress SR, Rousseau J, Ratanjee B, ''et al.'' |title=HLA class II induction by interferon-gamma in K562 variant cell line: inhibition by serum lipid. |journal=Hum. Immunol. |volume=31 |issue= 1 |pages= 57-66 |year= 1991 |pmid= 1908841 |doi= }}
*{{cite journal | author=Rosenstein Y, Burakoff SJ, Herrmann SH |title=HIV-gp120 can block CD4-class II MHC-mediated adhesion. |journal=J. Immunol. |volume=144 |issue= 2 |pages= 526-31 |year= 1990 |pmid= 1967269 |doi= }}
*{{cite journal | author=Callahan KM, Fort MM, Obah EA, ''et al.'' |title=Genetic variability in HIV-1 gp120 affects interactions with HLA molecules and T cell receptor. |journal=J. Immunol. |volume=144 |issue= 9 |pages= 3341-6 |year= 1990 |pmid= 1970352 |doi= }}
*{{cite journal | author=Bowman MR, MacFerrin KD, Schreiber SL, Burakoff SJ |title=Identification and structural analysis of residues in the V1 region of CD4 involved in interaction with human immunodeficiency virus envelope glycoprotein gp120 and class II major histocompatibility complex molecules. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 22 |pages= 9052-6 |year= 1991 |pmid= 1978941 |doi= }}
*{{cite journal | author=Gorski J |title=HLA-DR beta-chain polymorphism. Second domain polymorphism reflects evolutionary relatedness of alleles and may explain public serologic epitopes. |journal=J. Immunol. |volume=143 |issue= 1 |pages= 329-33 |year= 1989 |pmid= 2471740 |doi= }}
*{{cite journal | author=Kao HT, Gregersen PK, Tang JC, ''et al.'' |title=Molecular analysis of the HLA class II genes in two DRw6-related haplotypes, DRw13 DQw1 and DRw14 DQw3. |journal=J. Immunol. |volume=142 |issue= 5 |pages= 1743-7 |year= 1989 |pmid= 2493052 |doi= }}
*{{cite journal | author=Jonsson AK, Andersson L, Rask L |title=A cellular and functional split in the DRw8 haplotype is due to a single amino acid replacement (DR beta ser 57- asp 57). |journal=Immunogenetics |volume=29 |issue= 5 |pages= 308-16 |year= 1989 |pmid= 2497068 |doi= }}
*{{cite journal | author=Clayton LK, Sieh M, Pious DA, Reinherz EL |title=Identification of human CD4 residues affecting class II MHC versus HIV-1 gp120 binding. |journal=Nature |volume=339 |issue= 6225 |pages= 548-51 |year= 1989 |pmid= 2543930 |doi= 10.1038/339548a0 }}
*{{cite journal | author=Diamond DC, Sleckman BP, Gregory T, ''et al.'' |title=Inhibition of CD4+ T cell function by the HIV envelope protein, gp120. |journal=J. Immunol. |volume=141 |issue= 11 |pages= 3715-7 |year= 1988 |pmid= 2846691 |doi= }}
*{{cite journal | author=Angelini G, de Preval C, Gorski J, Mach B |title=High-resolution analysis of the human HLA-DR polymorphism by hybridization with sequence-specific oligonucleotide probes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 12 |pages= 4489-93 |year= 1986 |pmid= 3012569 |doi= }}
*{{cite journal | author=Didier DK, Schiffenbauer J, Shuman S, ''et al.'' |title=Characterization of two distinct DR beta chain alleles at the beta III locus of the DR5 haplotype: beta III alleles are highly conserved. |journal=J. Immunol. |volume=137 |issue= 8 |pages= 2627-31 |year= 1986 |pmid= 3020126 |doi= }}
*{{cite journal | author=Young JA, Wilkinson D, Bodmer WF, Trowsdale J |title=Sequence and evolution of HLA-DR7- and -DRw53-associated beta-chain genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 14 |pages= 4929-33 |year= 1987 |pmid= 3110774 |doi= }}
*{{cite journal | author=Horn GT, Bugawan TL, Long CM, ''et al.'' |title=Sequence analysis of HLA class II genes from insulin-dependent diabetic individuals. |journal=Hum. Immunol. |volume=21 |issue= 4 |pages= 249-63 |year= 1988 |pmid= 3372263 |doi= }}
*{{cite journal | author=Gorski J, Mach B |title=Polymorphism of human Ia antigens: gene conversion between two DR beta loci results in a new HLA-D/DR specificity. |journal=Nature |volume=322 |issue= 6074 |pages= 67-70 |year= 1986 |pmid= 3459965 |doi= 10.1038/322067a0 }}
*{{cite journal | author=Gregersen PK, Moriuchi T, Karr RW, ''et al.'' |title=Polymorphism of HLA-DR beta chains in DR4, -7, and -9 haplotypes: implications for the mechanisms of allelic variation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 23 |pages= 9149-53 |year= 1987 |pmid= 3466180 |doi= }}
*{{cite journal | author=Bell JI, Denney D, Foster L, ''et al.'' |title=Allelic variation in the DR subregion of the human major histocompatibility complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 17 |pages= 6234-8 |year= 1987 |pmid= 3476943 |doi= }}
*{{cite journal | author=Andrieu JM, Even P, Venet A |title=AIDS and related syndromes as a viral-induced autoimmune disease of the immune system: an anti-MHC II disorder. Therapeutic implications. |journal=AIDS research |volume=2 |issue= 3 |pages= 163-74 |year= 1986 |pmid= 3489470 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HSPG2... {November 16, 2007 4:07:46 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:08:19 PM PST}
<!-- 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
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_HSPG2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gl4.
| PDB = {{PDB2|1gl4}}
| Name = Heparan sulfate proteoglycan 2
| HGNCid = 5273
| Symbol = HSPG2
| AltSymbols =; PLC; PRCAN; SJA; SJS; SJS1
| OMIM = 142461
| ECnumber =
| Homologene = 68473
| MGIid =
| GeneAtlas_image1 = PBB_GE_HSPG2_201655_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_HSPG2_201654_s_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005604 |text = basement membrane}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0008104 |text = protein localization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3339
| Hs_Ensembl = ENSG00000142798
| Hs_RefseqProtein = NP_005520
| Hs_RefseqmRNA = NM_005529
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 22021325
| Hs_GenLoc_end = 22136377
| Hs_Uniprot = P98160
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Heparan sulfate proteoglycan 2''', also known as '''HSPG2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HSPG2 heparan sulfate proteoglycan 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3339| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Heparan sulfate proteoglycan is a major component of basement membranes, where the molecule may be involved in the stabilization of other molecules as well as being involved with glomerular permeability to macromolecules and cell adhesion. This form of HSPG, known as HSPG2 or perlecan, is encoded by a gene that maps to chromosome 1. The gene for the form of HSPG associated with the cell surface of fibroblasts has been mapped to human chromosome 8 (MIM 142460).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: HSPG2 heparan sulfate proteoglycan 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3339| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Olsen BR |title=Life without perlecan has its problems. |journal=J. Cell Biol. |volume=147 |issue= 5 |pages= 909-12 |year= 1999 |pmid= 10579711 |doi= }}
*{{cite journal | author=Murdoch AD, Dodge GR, Cohen I, ''et al.'' |title=Primary structure of the human heparan sulfate proteoglycan from basement membrane (HSPG2/perlecan). A chimeric molecule with multiple domains homologous to the low density lipoprotein receptor, laminin, neural cell adhesion molecules, and epidermal growth factor. |journal=J. Biol. Chem. |volume=267 |issue= 12 |pages= 8544-57 |year= 1992 |pmid= 1569102 |doi= }}
*{{cite journal | author=Dodge GR, Kovalszky I, Chu ML, ''et al.'' |title=Heparan sulfate proteoglycan of human colon: partial molecular cloning, cellular expression, and mapping of the gene (HSPG2) to the short arm of human chromosome 1. |journal=Genomics |volume=10 |issue= 3 |pages= 673-80 |year= 1991 |pmid= 1679749 |doi= }}
*{{cite journal | author=Kallunki P, Eddy RL, Byers MG, ''et al.'' |title=Cloning of human heparan sulfate proteoglycan core protein, assignment of the gene (HSPG2) to 1p36.1----p35 and identification of a BamHI restriction fragment length polymorphism. |journal=Genomics |volume=11 |issue= 2 |pages= 389-96 |year= 1992 |pmid= 1685141 |doi= }}
*{{cite journal | author=Kallunki P, Tryggvason K |title=Human basement membrane heparan sulfate proteoglycan core protein: a 467-kD protein containing multiple domains resembling elements of the low density lipoprotein receptor, laminin, neural cell adhesion molecules, and epidermal growth factor. |journal=J. Cell Biol. |volume=116 |issue= 2 |pages= 559-71 |year= 1992 |pmid= 1730768 |doi= }}
*{{cite journal | author=Heremans A, van der Schueren B, de Cock B, ''et al.'' |title=Matrix-associated heparan sulfate proteoglycan: core protein-specific monoclonal antibodies decorate the pericellular matrix of connective tissue cells and the stromal side of basement membranes. |journal=J. Cell Biol. |volume=109 |issue= 6 Pt 1 |pages= 3199-211 |year= 1990 |pmid= 2687294 |doi= }}
*{{cite journal | author=Sage H, Vernon RB, Funk SE, ''et al.'' |title=SPARC, a secreted protein associated with cellular proliferation, inhibits cell spreading in vitro and exhibits Ca+2-dependent binding to the extracellular matrix. |journal=J. Cell Biol. |volume=109 |issue= 1 |pages= 341-56 |year= 1989 |pmid= 2745554 |doi= }}
*{{cite journal | author=Sasaki T, Göhring W, Pan TC, ''et al.'' |title=Binding of mouse and human fibulin-2 to extracellular matrix ligands. |journal=J. Mol. Biol. |volume=254 |issue= 5 |pages= 892-9 |year= 1996 |pmid= 7500359 |doi= 10.1006/jmbi.1995.0664 }}
*{{cite journal | author=Cohen IR, Grässel S, Murdoch AD, Iozzo RV |title=Structural characterization of the complete human perlecan gene and its promoter. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 21 |pages= 10404-8 |year= 1993 |pmid= 8234307 |doi= }}
*{{cite journal | author=Nicole S, Ben Hamida C, Beighton P, ''et al.'' |title=Localization of the Schwartz-Jampel syndrome (SJS) locus to chromosome 1p34-p36.1 by homozygosity mapping. |journal=Hum. Mol. Genet. |volume=4 |issue= 9 |pages= 1633-6 |year= 1996 |pmid= 8541852 |doi= }}
*{{cite journal | author=Cáceres J, Brandan E |title=Interaction between Alzheimer's disease beta A4 precursor protein (APP) and the extracellular matrix: evidence for the participation of heparan sulfate proteoglycans. |journal=J. Cell. Biochem. |volume=65 |issue= 2 |pages= 145-58 |year= 1997 |pmid= 9136074 |doi= }}
*{{cite journal | author=Smeland S, Kolset SO, Lyon M, ''et al.'' |title=Binding of perlecan to transthyretin in vitro. |journal=Biochem. J. |volume=326 ( Pt 3) |issue= |pages= 829-36 |year= 1997 |pmid= 9307034 |doi= }}
*{{cite journal | author=Hansen PM, Chowdhury T, Deckert T, ''et al.'' |title=Genetic variation of the heparan sulfate proteoglycan gene (perlecan gene). Association with urinary albumin excretion in IDDM patients. |journal=Diabetes |volume=46 |issue= 10 |pages= 1658-9 |year= 1997 |pmid= 9313766 |doi= }}
*{{cite journal | author=Brown JC, Sasaki T, Göhring W, ''et al.'' |title=The C-terminal domain V of perlecan promotes beta1 integrin-mediated cell adhesion, binds heparin, nidogen and fibulin-2 and can be modified by glycosaminoglycans. |journal=Eur. J. Biochem. |volume=250 |issue= 1 |pages= 39-46 |year= 1998 |pmid= 9431988 |doi= }}
*{{cite journal | author=Ettner N, Göhring W, Sasaki T, ''et al.'' |title=The N-terminal globular domain of the laminin alpha1 chain binds to alpha1beta1 and alpha2beta1 integrins and to the heparan sulfate-containing domains of perlecan. |journal=FEBS Lett. |volume=430 |issue= 3 |pages= 217-21 |year= 1998 |pmid= 9688542 |doi= }}
*{{cite journal | author=Göhring W, Sasaki T, Heldin CH, Timpl R |title=Mapping of the binding of platelet-derived growth factor to distinct domains of the basement membrane proteins BM-40 and perlecan and distinction from the BM-40 collagen-binding epitope. |journal=Eur. J. Biochem. |volume=255 |issue= 1 |pages= 60-6 |year= 1998 |pmid= 9692901 |doi= }}
*{{cite journal | author=Kohfeldt E, Sasaki T, Göhring W, Timpl R |title=Nidogen-2: a new basement membrane protein with diverse binding properties. |journal=J. Mol. Biol. |volume=282 |issue= 1 |pages= 99-109 |year= 1998 |pmid= 9733643 |doi= 10.1006/jmbi.1998.2004 }}
*{{cite journal | author=Arikawa-Hirasawa E, Watanabe H, Takami H, ''et al.'' |title=Perlecan is essential for cartilage and cephalic development. |journal=Nat. Genet. |volume=23 |issue= 3 |pages= 354-8 |year= 1999 |pmid= 10545953 |doi= 10.1038/15537 }}
*{{cite journal | author=Mongiat M, Taylor K, Otto J, ''et al.'' |title=The protein core of the proteoglycan perlecan binds specifically to fibroblast growth factor-7. |journal=J. Biol. Chem. |volume=275 |issue= 10 |pages= 7095-100 |year= 2000 |pmid= 10702276 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IL12A... {November 16, 2007 4:08:52 PM PST}
- SEARCH REDIRECT: Control Box Found: IL12A {November 16, 2007 4:09:22 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:09:23 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:09:23 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:09:23 PM PST}
- UPDATED: Updated protein page: IL12A {November 16, 2007 4:09:29 PM PST}
- INFO: Beginning work on IL2RG... {November 16, 2007 4:08:19 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:08:52 PM PST}
<!-- 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
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_IL2RG_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2b5i.
| PDB = {{PDB2|2b5i}}, {{PDB2|2erj}}
| Name = Interleukin 2 receptor, gamma (severe combined immunodeficiency)
| HGNCid = 6010
| Symbol = IL2RG
| AltSymbols =; CD132; IMD4; SCIDX; SCIDX1
| OMIM = 308380
| ECnumber =
| Homologene = 172
| MGIid = 96551
| GeneAtlas_image1 = PBB_GE_IL2RG_204116_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004896 |text = hematopoietin/interferon-class (D200-domain) cytokine receptor activity}} {{GNF_GO|id=GO:0004911 |text = interleukin-2 receptor activity}} {{GNF_GO|id=GO:0004913 |text = interleukin-4 receptor activity}} {{GNF_GO|id=GO:0004917 |text = interleukin-7 receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3561
| Hs_Ensembl = ENSG00000147168
| Hs_RefseqProtein = NP_000197
| Hs_RefseqmRNA = NM_000206
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 70243979
| Hs_GenLoc_end = 70248188
| Hs_Uniprot = P31785
| Mm_EntrezGene = 16186
| Mm_Ensembl = ENSMUSG00000031304
| Mm_RefseqmRNA = NM_013563
| Mm_RefseqProtein = NP_038591
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 97467097
| Mm_GenLoc_end = 97470925
| Mm_Uniprot = Q3UPA9
}}
}}
'''Interleukin 2 receptor, gamma (severe combined immunodeficiency)''', also known as '''IL2RG''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IL2RG interleukin 2 receptor, gamma (severe combined immunodeficiency)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3561| accessdate = }}</ref>
<!-- 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 interleukin 2 (IL2) receptor gamma chain (IL2RG), an important signalling component of many interleukin receptors (IL2,IL4,IL7,IL9, and IL15), is thus referred to as the common gamma chain. Mutations in this X-chromosome-linked gene cause X-linked severe combined immunodeficiency (XSCID).<ref name="entrez">{{cite web | title = Entrez Gene: IL2RG interleukin 2 receptor, gamma (severe combined immunodeficiency)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3561| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ellery JM, Nicholls PJ |title=Alternate signalling pathways from the interleukin-2 receptor. |journal=Cytokine Growth Factor Rev. |volume=13 |issue= 1 |pages= 27-40 |year= 2002 |pmid= 11750878 |doi= }}
*{{cite journal | author=Takeshita T, Asao H, Ohtani K, ''et al.'' |title=Cloning of the gamma chain of the human IL-2 receptor. |journal=Science |volume=257 |issue= 5068 |pages= 379-82 |year= 1992 |pmid= 1631559 |doi= }}
*{{cite journal | author=Burton J, Goldman CK, Rao P, ''et al.'' |title=Association of intercellular adhesion molecule 1 with the multichain high-affinity interleukin 2 receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 18 |pages= 7329-33 |year= 1990 |pmid= 1976256 |doi= }}
*{{cite journal | author=Oyaizu N, Chirmule N, Kalyanaraman VS, ''et al.'' |title=Human immunodeficiency virus type 1 envelope glycoprotein gp120 produces immune defects in CD4+ T lymphocytes by inhibiting interleukin 2 mRNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 6 |pages= 2379-83 |year= 1990 |pmid= 2315327 |doi= }}
*{{cite journal | author=Kornfeld H, Cruikshank WW, Pyle SW, ''et al.'' |title=Lymphocyte activation by HIV-1 envelope glycoprotein. |journal=Nature |volume=335 |issue= 6189 |pages= 445-8 |year= 1988 |pmid= 2843775 |doi= 10.1038/335445a0 }}
*{{cite journal | author=Bamborough P, Hedgecock CJ, Richards WG |title=The interleukin-2 and interleukin-4 receptors studied by molecular modelling. |journal=Structure |volume=2 |issue= 9 |pages= 839-51 |year= 1995 |pmid= 7529123 |doi= }}
*{{cite journal | author=Clark PA, Lester T, Genet S, ''et al.'' |title=Screening for mutations causing X-linked severe combined immunodeficiency in the IL-2R gamma chain gene by single-strand conformation polymorphism analysis. |journal=Hum. Genet. |volume=96 |issue= 4 |pages= 427-32 |year= 1995 |pmid= 7557965 |doi= }}
*{{cite journal | author=Giri JG, Kumaki S, Ahdieh M, ''et al.'' |title=Identification and cloning of a novel IL-15 binding protein that is structurally related to the alpha chain of the IL-2 receptor. |journal=EMBO J. |volume=14 |issue= 15 |pages= 3654-63 |year= 1995 |pmid= 7641685 |doi= }}
*{{cite journal | author=Pepper AE, Buckley RH, Small TN, Puck JM |title=Two mutational hotspots in the interleukin-2 receptor gamma chain gene causing human X-linked severe combined immunodeficiency. |journal=Am. J. Hum. Genet. |volume=57 |issue= 3 |pages= 564-71 |year= 1995 |pmid= 7668284 |doi= }}
*{{cite journal | author=Ohbo K, Takasawa N, Ishii N, ''et al.'' |title=Functional analysis of the human interleukin 2 receptor gamma chain gene promoter. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7479-86 |year= 1995 |pmid= 7706294 |doi= }}
*{{cite journal | author=Puck JM, Pepper AE, Bédard PM, Laframboise R |title=Female germ line mosaicism as the origin of a unique IL-2 receptor gamma-chain mutation causing X-linked severe combined immunodeficiency. |journal=J. Clin. Invest. |volume=95 |issue= 2 |pages= 895-9 |year= 1995 |pmid= 7860773 |doi= }}
*{{cite journal | author=Schmalstieg FC, Leonard WJ, Noguchi M, ''et al.'' |title=Missense mutation in exon 7 of the common gamma chain gene causes a moderate form of X-linked combined immunodeficiency. |journal=J. Clin. Invest. |volume=95 |issue= 3 |pages= 1169-73 |year= 1995 |pmid= 7883965 |doi= }}
*{{cite journal | author=DiSanto JP, Rieux-Laucat F, Dautry-Varsat A, ''et al.'' |title=Defective human interleukin 2 receptor gamma chain in an atypical X chromosome-linked severe combined immunodeficiency with peripheral T cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 20 |pages= 9466-70 |year= 1994 |pmid= 7937790 |doi= }}
*{{cite journal | author=Russell SM, Johnston JA, Noguchi M, ''et al.'' |title=Interaction of IL-2R beta and gamma c chains with Jak1 and Jak3: implications for XSCID and XCID. |journal=Science |volume=266 |issue= 5187 |pages= 1042-5 |year= 1994 |pmid= 7973658 |doi= }}
*{{cite journal | author=Ishii N, Asao H, Kimura Y, ''et al.'' |title=Impairment of ligand binding and growth signaling of mutant IL-2 receptor gamma-chains in patients with X-linked severe combined immunodeficiency. |journal=J. Immunol. |volume=153 |issue= 3 |pages= 1310-7 |year= 1994 |pmid= 8027558 |doi= }}
*{{cite journal | author=Johnson K, Choi Y, Wu Z, ''et al.'' |title=Soluble IL-2 receptor beta and gamma subunits: ligand binding and cooperativity. |journal=Eur. Cytokine Netw. |volume=5 |issue= 1 |pages= 23-34 |year= 1994 |pmid= 8049354 |doi= }}
*{{cite journal | author=Markiewicz S, Subtil A, Dautry-Varsat A, ''et al.'' |title=Detection of three nonsense mutations and one missense mutation in the interleukin-2 receptor gamma chain gene in SCIDX1 that differently affect the mRNA processing. |journal=Genomics |volume=21 |issue= 1 |pages= 291-3 |year= 1994 |pmid= 8088810 |doi= 10.1006/geno.1994.1265 }}
*{{cite journal | author=Kondo M, Takeshita T, Ishii N, ''et al.'' |title=Sharing of the interleukin-2 (IL-2) receptor gamma chain between receptors for IL-2 and IL-4. |journal=Science |volume=262 |issue= 5141 |pages= 1874-7 |year= 1994 |pmid= 8266076 |doi= }}
*{{cite journal | author=Noguchi M, Nakamura Y, Russell SM, ''et al.'' |title=Interleukin-2 receptor gamma chain: a functional component of the interleukin-7 receptor. |journal=Science |volume=262 |issue= 5141 |pages= 1877-80 |year= 1994 |pmid= 8266077 |doi= }}
*{{cite journal | author=Russell SM, Keegan AD, Harada N, ''et al.'' |title=Interleukin-2 receptor gamma chain: a functional component of the interleukin-4 receptor. |journal=Science |volume=262 |issue= 5141 |pages= 1880-3 |year= 1994 |pmid= 8266078 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KCNJ2... {November 16, 2007 4:10:14 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:10:54 PM PST}
<!-- 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
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_KCNJ2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1u4f.
| PDB = {{PDB2|1u4f}}, {{PDB2|2gix}}
| Name = Potassium inwardly-rectifying channel, subfamily J, member 2
| HGNCid = 6263
| Symbol = KCNJ2
| AltSymbols =; HHBIRK1; HHIRK1; IRK1; KIR2.1; LQT7; SQT3
| OMIM = 600681
| ECnumber =
| Homologene = 20249
| MGIid = 104744
| GeneAtlas_image1 = PBB_GE_KCNJ2_206765_at_tn.png
| Function = {{GNF_GO|id=GO:0005242 |text = inward rectifier potassium channel activity}} {{GNF_GO|id=GO:0005244 |text = voltage-gated ion channel activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3759
| Hs_Ensembl = ENSG00000123700
| Hs_RefseqProtein = NP_000882
| Hs_RefseqmRNA = NM_000891
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 65677271
| Hs_GenLoc_end = 65687755
| Hs_Uniprot = P63252
| Mm_EntrezGene = 16518
| Mm_Ensembl = ENSMUSG00000041695
| Mm_RefseqmRNA = NM_008425
| Mm_RefseqProtein = NP_032451
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 110882254
| Mm_GenLoc_end = 110891741
| Mm_Uniprot = Q543W5
}}
}}
'''Potassium inwardly-rectifying channel, subfamily J, member 2''', also known as '''KCNJ2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KCNJ2 potassium inwardly-rectifying channel, subfamily J, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3759| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded protein, which has a greater tendency to allow potassium to flow into a cell rather than out of a cell, probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Mutations in this gene have been associated with Andersen syndrome, which is characterized by periodic paralysis, cardiac arrhythmias, and dysmorphic features.<ref name="entrez">{{cite web | title = Entrez Gene: KCNJ2 potassium inwardly-rectifying channel, subfamily J, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3759| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kubo Y, Adelman JP, Clapham DE, ''et al.'' |title=International Union of Pharmacology. LIV. Nomenclature and molecular relationships of inwardly rectifying potassium channels. |journal=Pharmacol. Rev. |volume=57 |issue= 4 |pages= 509-26 |year= 2006 |pmid= 16382105 |doi= 10.1124/pr.57.4.11 }}
*{{cite journal | author=Wood LS, Tsai TD, Lee KS, Vogeli G |title=Cloning and functional expression of a human gene, hIRK1, encoding the heart inward rectifier K+-channel. |journal=Gene |volume=163 |issue= 2 |pages= 313-7 |year= 1995 |pmid= 7590287 |doi= }}
*{{cite journal | author=Kubo Y, Baldwin TJ, Jan YN, Jan LY |title=Primary structure and functional expression of a mouse inward rectifier potassium channel. |journal=Nature |volume=362 |issue= 6416 |pages= 127-33 |year= 1993 |pmid= 7680768 |doi= 10.1038/362127a0 }}
*{{cite journal | author=Raab-Graham KF, Radeke CM, Vandenberg CA |title=Molecular cloning and expression of a human heart inward rectifier potassium channel. |journal=Neuroreport |volume=5 |issue= 18 |pages= 2501-5 |year= 1995 |pmid= 7696590 |doi= }}
*{{cite journal | author=Ashen MD, O'Rourke B, Kluge KA, ''et al.'' |title=Inward rectifier K+ channel from human heart and brain: cloning and stable expression in a human cell line. |journal=Am. J. Physiol. |volume=268 |issue= 1 Pt 2 |pages= H506-11 |year= 1995 |pmid= 7840300 |doi= }}
*{{cite journal | author=Tang W, Qin CL, Yang XC |title=Cloning, localization, and functional expression of a human brain inward rectifier potassium channel (hIRK1). |journal=Recept. Channels |volume=3 |issue= 3 |pages= 175-83 |year= 1996 |pmid= 8821791 |doi= }}
*{{cite journal | author=Tare M, Prestwich SA, Gordienko DV, ''et al.'' |title=Inwardly rectifying whole cell potassium current in human blood eosinophils. |journal=J. Physiol. (Lond.) |volume=506 ( Pt 2) |issue= |pages= 303-18 |year= 1998 |pmid= 9490857 |doi= }}
*{{cite journal | author=Rae JL, Shepard AR |title=Inwardly rectifying potassium channels in lens epithelium are from the IRK1 (Kir 2.1) family. |journal=Exp. Eye Res. |volume=66 |issue= 3 |pages= 347-59 |year= 1998 |pmid= 9533862 |doi= 10.1006/exer.1997.0432 }}
*{{cite journal | author=Kurschner C, Yuzaki M |title=Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein. |journal=J. Neurosci. |volume=19 |issue= 18 |pages= 7770-80 |year= 1999 |pmid= 10479680 |doi= }}
*{{cite journal | author=Tucker SJ, Ashcroft FM |title=Mapping of the physical interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2. |journal=J. Biol. Chem. |volume=274 |issue= 47 |pages= 33393-7 |year= 1999 |pmid= 10559219 |doi= }}
*{{cite journal | author=Nehring RB, Wischmeyer E, Döring F, ''et al.'' |title=Neuronal inwardly rectifying K(+) channels differentially couple to PDZ proteins of the PSD-95/SAP90 family. |journal=J. Neurosci. |volume=20 |issue= 1 |pages= 156-62 |year= 2000 |pmid= 10627592 |doi= }}
*{{cite journal | author=Leonoudakis D, Mailliard W, Wingerd K, ''et al.'' |title=Inward rectifier potassium channel Kir2.2 is associated with synapse-associated protein SAP97. |journal=J. Cell. Sci. |volume=114 |issue= Pt 5 |pages= 987-98 |year= 2001 |pmid= 11181181 |doi= }}
*{{cite journal | author=Derst C, Karschin C, Wischmeyer E, ''et al.'' |title=Genetic and functional linkage of Kir5.1 and Kir2.1 channel subunits. |journal=FEBS Lett. |volume=491 |issue= 3 |pages= 305-11 |year= 2001 |pmid= 11240146 |doi= }}
*{{cite journal | author=Stockklausner C, Ludwig J, Ruppersberg JP, Klöcker N |title=A sequence motif responsible for ER export and surface expression of Kir2.0 inward rectifier K(+) channels. |journal=FEBS Lett. |volume=493 |issue= 2-3 |pages= 129-33 |year= 2001 |pmid= 11287009 |doi= }}
*{{cite journal | author=Dart C, Leyland ML |title=Targeting of an A kinase-anchoring protein, AKAP79, to an inwardly rectifying potassium channel, Kir2.1. |journal=J. Biol. Chem. |volume=276 |issue= 23 |pages= 20499-505 |year= 2001 |pmid= 11287423 |doi= 10.1074/jbc.M101425200 }}
*{{cite journal | author=Plaster NM, Tawil R, Tristani-Firouzi M, ''et al.'' |title=Mutations in Kir2.1 cause the developmental and episodic electrical phenotypes of Andersen's syndrome. |journal=Cell |volume=105 |issue= 4 |pages= 511-9 |year= 2001 |pmid= 11371347 |doi= }}
*{{cite journal | author=Jeong JS, Lee HJ, Jung JS, ''et al.'' |title=Characterization of inwardly rectifying K(+) conductance across the basolateral membrane of rat tracheal epithelia. |journal=Biochem. Biophys. Res. Commun. |volume=288 |issue= 4 |pages= 914-20 |year= 2001 |pmid= 11688996 |doi= 10.1006/bbrc.2001.5831 }}
*{{cite journal | author=Giovannardi S, Forlani G, Balestrini M, ''et al.'' |title=Modulation of the inward rectifier potassium channel IRK1 by the Ras signaling pathway. |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 12158-63 |year= 2002 |pmid= 11809752 |doi= 10.1074/jbc.M110466200 }}
*{{cite journal | author=Preisig-Müller R, Schlichthörl G, Goerge T, ''et al.'' |title=Heteromerization of Kir2.x potassium channels contributes to the phenotype of Andersen's syndrome. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 11 |pages= 7774-9 |year= 2002 |pmid= 12032359 |doi= 10.1073/pnas.102609499 }}
*{{cite journal | author=Ai T, Fujiwara Y, Tsuji K, ''et al.'' |title=Novel KCNJ2 mutation in familial periodic paralysis with ventricular dysrhythmia. |journal=Circulation |volume=105 |issue= 22 |pages= 2592-4 |year= 2002 |pmid= 12045162 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KRT14... {November 16, 2007 4:10:54 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:11:23 PM PST}
<!-- 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
}}
<!-- 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 = Keratin 14 (epidermolysis bullosa simplex, Dowling-Meara, Koebner)
| HGNCid = 6416
| Symbol = KRT14
| AltSymbols =; CK14; EBS3; EBS4; K14
| OMIM = 148066
| ECnumber =
| Homologene = 81522
| MGIid = 96688
| GeneAtlas_image1 = PBB_GE_KRT14_209351_at_tn.png
| Function = {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0030280 |text = structural constituent of epidermis}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005882 |text = intermediate filament}} {{GNF_GO|id=GO:0045095 |text = keratin filament}}
| Process = {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0008544 |text = epidermis development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3861
| Hs_Ensembl = ENSG00000186847
| Hs_RefseqProtein = NP_000517
| Hs_RefseqmRNA = NM_000526
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 36992070
| Hs_GenLoc_end = 36996699
| Hs_Uniprot = P02533
| Mm_EntrezGene = 16664
| Mm_Ensembl = ENSMUSG00000045545
| Mm_RefseqmRNA = NM_016958
| Mm_RefseqProtein = NP_058654
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 100019252
| Mm_GenLoc_end = 100023600
| Mm_Uniprot = Q61782
}}
}}
'''Keratin 14 (epidermolysis bullosa simplex, Dowling-Meara, Koebner)''', also known as '''KRT14''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KRT14 keratin 14 (epidermolysis bullosa simplex, Dowling-Meara, Koebner)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3861| accessdate = }}</ref>
<!-- 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 keratin family, the most diverse group of intermediate filaments. This gene product, a type I keratin, is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells. Mutations in the genes for these keratins are associated with epidermolysis bullosa simplex. At least one pseudogene has been identified at 17p12-p11.<ref name="entrez">{{cite web | title = Entrez Gene: KRT14 keratin 14 (epidermolysis bullosa simplex, Dowling-Meara, Koebner)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3861| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schuilenga-Hut PH, Vlies P, Jonkman MF, ''et al.'' |title=Mutation analysis of the entire keratin 5 and 14 genes in patients with epidermolysis bullosa simplex and identification of novel mutations. |journal=Hum. Mutat. |volume=21 |issue= 4 |pages= 447 |year= 2003 |pmid= 12655565 |doi= 10.1002/humu.9124 }}
*{{cite journal | author=Rosenberg M, Fuchs E, Le Beau MM, ''et al.'' |title=Three epidermal and one simple epithelial type II keratin genes map to human chromosome 12. |journal=Cytogenet. Cell Genet. |volume=57 |issue= 1 |pages= 33-8 |year= 1991 |pmid= 1713141 |doi= }}
*{{cite journal | author=Coulombe PA, Hutton ME, Letai A, ''et al.'' |title=Point mutations in human keratin 14 genes of epidermolysis bullosa simplex patients: genetic and functional analyses. |journal=Cell |volume=66 |issue= 6 |pages= 1301-11 |year= 1991 |pmid= 1717157 |doi= }}
*{{cite journal | author=Bonifas JM, Rothman AL, Epstein EH |title=Epidermolysis bullosa simplex: evidence in two families for keratin gene abnormalities. |journal=Science |volume=254 |issue= 5035 |pages= 1202-5 |year= 1991 |pmid= 1720261 |doi= }}
*{{cite journal | author=Albers K, Fuchs E |title=The expression of mutant epidermal keratin cDNAs transfected in simple epithelial and squamous cell carcinoma lines. |journal=J. Cell Biol. |volume=105 |issue= 2 |pages= 791-806 |year= 1987 |pmid= 2442174 |doi= }}
*{{cite journal | author=Rosenberg M, RayChaudhury A, Shows TB, ''et al.'' |title=A group of type I keratin genes on human chromosome 17: characterization and expression. |journal=Mol. Cell. Biol. |volume=8 |issue= 2 |pages= 722-36 |year= 1988 |pmid= 2451124 |doi= }}
*{{cite journal | author=Marchuk D, McCrohon S, Fuchs E |title=Complete sequence of a gene encoding a human type I keratin: sequences homologous to enhancer elements in the regulatory region of the gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 6 |pages= 1609-13 |year= 1985 |pmid= 2580298 |doi= }}
*{{cite journal | author=Hanukoglu I, Fuchs E |title=The cDNA sequence of a human epidermal keratin: divergence of sequence but conservation of structure among intermediate filament proteins. |journal=Cell |volume=31 |issue= 1 |pages= 243-52 |year= 1983 |pmid= 6186381 |doi= }}
*{{cite journal | author=Marchuk D, McCrohon S, Fuchs E |title=Remarkable conservation of structure among intermediate filament genes. |journal=Cell |volume=39 |issue= 3 Pt 2 |pages= 491-8 |year= 1985 |pmid= 6210150 |doi= }}
*{{cite journal | author=Rugg EL, Morley SM, Smith FJ, ''et al.'' |title=Missing links: Weber-Cockayne keratin mutations implicate the L12 linker domain in effective cytoskeleton function. |journal=Nat. Genet. |volume=5 |issue= 3 |pages= 294-300 |year= 1994 |pmid= 7506097 |doi= 10.1038/ng1193-294 }}
*{{cite journal | author=Chen MA, Bonifas JM, Matsumura K, ''et al.'' |title=A novel three-nucleotide deletion in the helix 2B region of keratin 14 in epidermolysis bullosa simplex: delta E375. |journal=Hum. Mol. Genet. |volume=2 |issue= 11 |pages= 1971-2 |year= 1994 |pmid= 7506606 |doi= }}
*{{cite journal | author=Chan Y, Anton-Lamprecht I, Yu QC, ''et al.'' |title=A human keratin 14 "knockout": the absence of K14 leads to severe epidermolysis bullosa simplex and a function for an intermediate filament protein. |journal=Genes Dev. |volume=8 |issue= 21 |pages= 2574-87 |year= 1994 |pmid= 7525408 |doi= }}
*{{cite journal | author=Yamanishi K, Matsuki M, Konishi K, Yasuno H |title=A novel mutation of Leu122 to Phe at a highly conserved hydrophobic residue in the helix initiation motif of keratin 14 in epidermolysis bullosa simplex. |journal=Hum. Mol. Genet. |volume=3 |issue= 7 |pages= 1171-2 |year= 1995 |pmid= 7526926 |doi= }}
*{{cite journal | author=Hovnanian A, Pollack E, Hilal L, ''et al.'' |title=A missense mutation in the rod domain of keratin 14 associated with recessive epidermolysis bullosa simplex. |journal=Nat. Genet. |volume=3 |issue= 4 |pages= 327-32 |year= 1995 |pmid= 7526933 |doi= 10.1038/ng0493-327 }}
*{{cite journal | author=Chen H, Bonifas JM, Matsumura K, ''et al.'' |title=Keratin 14 gene mutations in patients with epidermolysis bullosa simplex. |journal=J. Invest. Dermatol. |volume=105 |issue= 4 |pages= 629-32 |year= 1995 |pmid= 7561171 |doi= }}
*{{cite journal | author=Humphries MM, Sheils DM, Farrar GJ, ''et al.'' |title=A mutation (Met-->Arg) in the type I keratin (K14) gene responsible for autosomal dominant epidermolysis bullosa simplex. |journal=Hum. Mutat. |volume=2 |issue= 1 |pages= 37-42 |year= 1993 |pmid= 7682883 |doi= 10.1002/humu.1380020107 }}
*{{cite journal | author=Stephens K, Sybert VP, Wijsman EM, ''et al.'' |title=A keratin 14 mutational hot spot for epidermolysis bullosa simplex, Dowling-Meara: implications for diagnosis. |journal=J. Invest. Dermatol. |volume=101 |issue= 2 |pages= 240-3 |year= 1993 |pmid= 7688405 |doi= }}
*{{cite journal | author=Chan YM, Cheng J, Gedde-Dahl T, ''et al.'' |title=Genetic analysis of a severe case of Dowling-Meara epidermolysis bullosa simplex. |journal=J. Invest. Dermatol. |volume=106 |issue= 2 |pages= 327-34 |year= 1996 |pmid= 8601736 |doi= }}
*{{cite journal | author=Paladini RD, Takahashi K, Bravo NS, Coulombe PA |title=Onset of re-epithelialization after skin injury correlates with a reorganization of keratin filaments in wound edge keratinocytes: defining a potential role for keratin 16. |journal=J. Cell Biol. |volume=132 |issue= 3 |pages= 381-97 |year= 1996 |pmid= 8636216 |doi= }}
*{{cite journal | author=Jonkman MF, Heeres K, Pas HH, ''et al.'' |title=Effects of keratin 14 ablation on the clinical and cellular phenotype in a kindred with recessive epidermolysis bullosa simplex. |journal=J. Invest. Dermatol. |volume=107 |issue= 5 |pages= 764-9 |year= 1996 |pmid= 8875963 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LIF... {November 16, 2007 4:11:23 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:11:50 PM PST}
<!-- 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
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_LIF_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1emr.
| PDB = {{PDB2|1emr}}, {{PDB2|1pvh}}
| Name = Leukemia inhibitory factor (cholinergic differentiation factor)
| HGNCid = 6596
| Symbol = LIF
| AltSymbols =; CDF; D-FACTOR; HILDA
| OMIM = 159540
| ECnumber =
| Homologene = 1734
| MGIid = 96787
| GeneAtlas_image1 = PBB_GE_LIF_205266_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005146 |text = leukemia inhibitory factor receptor binding}} {{GNF_GO|id=GO:0005147 |text = oncostatin-M receptor binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006955 |text = 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:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0042503 |text = tyrosine phosphorylation of Stat3 protein}} {{GNF_GO|id=GO:0048644 |text = muscle morphogenesis}} {{GNF_GO|id=GO:0048666 |text = neuron development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3976
| Hs_Ensembl = ENSG00000128342
| Hs_RefseqProtein = NP_002300
| Hs_RefseqmRNA = NM_002309
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 28966441
| Hs_GenLoc_end = 28972748
| Hs_Uniprot = P15018
| Mm_EntrezGene = 16878
| Mm_Ensembl = ENSMUSG00000034394
| Mm_RefseqmRNA = NM_001039537
| Mm_RefseqProtein = NP_001034626
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 4157571
| Mm_GenLoc_end = 4172517
| Mm_Uniprot = Q3U1H5
}}
}}
'''Leukemia inhibitory factor (cholinergic differentiation factor)''', also known as '''LIF''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LIF leukemia inhibitory factor (cholinergic differentiation factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3976| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Leukaemia inhibitory factor is a cytokine that induces macrophage differentiation. Neurotransmitters and neuropeptides, well known for their role in the communication between neurons, are also capable of activating monocytes and macrophages and inducing chemotaxis in immune cells. LIF signals through different receptors and transcription factors. LIF in conjunction with BMP2 acts in synergy on primary fetal neural progenitor cells to induce astrocytes.<ref name="entrez">{{cite web | title = Entrez Gene: LIF leukemia inhibitory factor (cholinergic differentiation factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3976| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Patterson PH |title=Leukemia inhibitory factor, a cytokine at the interface between neurobiology and immunology. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 17 |pages= 7833-5 |year= 1994 |pmid= 8058719 |doi= }}
*{{cite journal | author=Aghajanova L |title=Leukemia inhibitory factor and human embryo implantation. |journal=Ann. N. Y. Acad. Sci. |volume=1034 |issue= |pages= 176-83 |year= 2005 |pmid= 15731310 |doi= 10.1196/annals.1335.020 }}
*{{cite journal | author=Králícková M, Síma P, Rokyta Z |title=Role of the leukemia-inhibitory factor gene mutations in infertile women: the embryo-endometrial cytokine cross talk during implantation--a delicate homeostatic equilibrium. |journal=Folia Microbiol. (Praha) |volume=50 |issue= 3 |pages= 179-86 |year= 2005 |pmid= 16295654 |doi= }}
*{{cite journal | author=Stahl J, Gearing DP, Willson TA, ''et al.'' |title=Structural organization of the genes for murine and human leukemia inhibitory factor. Evolutionary conservation of coding and non-coding regions. |journal=J. Biol. Chem. |volume=265 |issue= 15 |pages= 8833-41 |year= 1990 |pmid= 1692837 |doi= }}
*{{cite journal | author=Bazan JF |title=Neuropoietic cytokines in the hematopoietic fold. |journal=Neuron |volume=7 |issue= 2 |pages= 197-208 |year= 1991 |pmid= 1714745 |doi= }}
*{{cite journal | author=Lowe DG, Nunes W, Bombara M, ''et al.'' |title=Genomic cloning and heterologous expression of human differentiation-stimulating factor. |journal=DNA |volume=8 |issue= 5 |pages= 351-9 |year= 1989 |pmid= 2475312 |doi= }}
*{{cite journal | author=Sutherland GR, Baker E, Hyland VJ, ''et al.'' |title=The gene for human leukemia inhibitory factor (LIF) maps to 22q12. |journal=Leukemia |volume=3 |issue= 1 |pages= 9-13 |year= 1989 |pmid= 2491897 |doi= }}
*{{cite journal | author=Mori M, Yamaguchi K, Abe K |title=Purification of a lipoprotein lipase-inhibiting protein produced by a melanoma cell line associated with cancer cachexia. |journal=Biochem. Biophys. Res. Commun. |volume=160 |issue= 3 |pages= 1085-92 |year= 1989 |pmid= 2730639 |doi= }}
*{{cite journal | author=Gough NM, Gearing DP, King JA, ''et al.'' |title=Molecular cloning and expression of the human homologue of the murine gene encoding myeloid leukemia-inhibitory factor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 8 |pages= 2623-7 |year= 1988 |pmid= 3128791 |doi= }}
*{{cite journal | author=Williams RL, Hilton DJ, Pease S, ''et al.'' |title=Myeloid leukaemia inhibitory factor maintains the developmental potential of embryonic stem cells. |journal=Nature |volume=336 |issue= 6200 |pages= 684-7 |year= 1989 |pmid= 3143916 |doi= 10.1038/336684a0 }}
*{{cite journal | author=Moreau JF, Donaldson DD, Bennett F, ''et al.'' |title=Leukaemia inhibitory factor is identical to the myeloid growth factor human interleukin for DA cells. |journal=Nature |volume=336 |issue= 6200 |pages= 690-2 |year= 1989 |pmid= 3143918 |doi= 10.1038/336690a0 }}
*{{cite journal | author=Yamaguchi M, Miki N, Ono M, ''et al.'' |title=Inhibition of growth hormone-releasing factor production in mouse placenta by cytokines using gp130 as a signal transducer. |journal=Endocrinology |volume=136 |issue= 3 |pages= 1072-8 |year= 1995 |pmid= 7867561 |doi= }}
*{{cite journal | author=Schmelzer CH, Harris RJ, Butler D, ''et al.'' |title=Glycosylation pattern and disulfide assignments of recombinant human differentiation-stimulating factor. |journal=Arch. Biochem. Biophys. |volume=302 |issue= 2 |pages= 484-9 |year= 1993 |pmid= 8489250 |doi= 10.1006/abbi.1993.1243 }}
*{{cite journal | author=Aikawa J, Ikeda-Naiki S, Ohgane J, ''et al.'' |title=Molecular cloning of rat leukemia inhibitory factor receptor alpha-chain gene and its expression during pregnancy. |journal=Biochim. Biophys. Acta |volume=1353 |issue= 3 |pages= 266-76 |year= 1997 |pmid= 9349722 |doi= }}
*{{cite journal | author=Hinds MG, Maurer T, Zhang JG, ''et al.'' |title=Solution structure of leukemia inhibitory factor. |journal=J. Biol. Chem. |volume=273 |issue= 22 |pages= 13738-45 |year= 1998 |pmid= 9593715 |doi= }}
*{{cite journal | author= |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097-108 |year= 1999 |pmid= 9847074 |doi= }}
*{{cite journal | author=Tanaka M, Hara T, Copeland NG, ''et al.'' |title=Reconstitution of the functional mouse oncostatin M (OSM) receptor: molecular cloning of the mouse OSM receptor beta subunit. |journal=Blood |volume=93 |issue= 3 |pages= 804-15 |year= 1999 |pmid= 9920829 |doi= }}
*{{cite journal | author=Nakashima K, Yanagisawa M, Arakawa H, ''et al.'' |title=Synergistic signaling in fetal brain by STAT3-Smad1 complex bridged by p300. |journal=Science |volume=284 |issue= 5413 |pages= 479-82 |year= 1999 |pmid= 10205054 |doi= }}
*{{cite journal | author=Dunham I, Shimizu N, Roe BA, ''et al.'' |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489-95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LIPE... {November 16, 2007 4:11:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:12:19 PM PST}
<!-- 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
}}
<!-- 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 = Lipase, hormone-sensitive
| HGNCid = 6621
| Symbol = LIPE
| AltSymbols =; HSL; LHS
| OMIM = 151750
| ECnumber =
| Homologene = 3912
| MGIid = 96790
| GeneAtlas_image1 = PBB_GE_LIPE_208186_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_LIPE_213855_s_at_tn.png
| Function = {{GNF_GO|id=GO:0016788 |text = hydrolase activity, acting on ester bonds}} {{GNF_GO|id=GO:0047372 |text = acylglycerol lipase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006631 |text = fatty acid metabolic process}} {{GNF_GO|id=GO:0007565 |text = female pregnancy}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0008202 |text = steroid metabolic process}} {{GNF_GO|id=GO:0008203 |text = cholesterol metabolic process}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}} {{GNF_GO|id=GO:0019433 |text = triacylglycerol catabolic process}} {{GNF_GO|id=GO:0042493 |text = response to drug}} {{GNF_GO|id=GO:0046340 |text = diacylglycerol catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3991
| Hs_Ensembl = ENSG00000079435
| Hs_RefseqProtein = NP_005348
| Hs_RefseqmRNA = NM_005357
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 47597499
| Hs_GenLoc_end = 47623418
| Hs_Uniprot = Q05469
| Mm_EntrezGene = 16890
| Mm_Ensembl = ENSMUSG00000003123
| Mm_RefseqmRNA = NM_001039507
| Mm_RefseqProtein = NP_001034596
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 25088287
| Mm_GenLoc_end = 25104747
| Mm_Uniprot = Q6LCY9
}}
}}
'''Lipase, hormone-sensitive''', also known as '''LIPE''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LIPE lipase, hormone-sensitive| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3991| accessdate = }}</ref>
<!-- 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 has a long and a short form, generated by use of alternative translational start codons. The long form is expressed in steroidogenic tissues such as testis, where it converts cholesteryl esters to free cholesterol for steroid hormone production. The short form is expressed in adipose tissue, among others, where it hydrolyzes stored triglycerides to free fatty acids.<ref name="entrez">{{cite web | title = Entrez Gene: LIPE lipase, hormone-sensitive| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3991| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kraemer FB, Shen WJ |title=Hormone-sensitive lipase: control of intracellular tri-(di-)acylglycerol and cholesteryl ester hydrolysis. |journal=J. Lipid Res. |volume=43 |issue= 10 |pages= 1585-94 |year= 2003 |pmid= 12364542 |doi= }}
*{{cite journal | author=Langfort J, Donsmark M, Ploug T, ''et al.'' |title=Hormone-sensitive lipase in skeletal muscle: regulatory mechanisms. |journal=Acta Physiol. Scand. |volume=178 |issue= 4 |pages= 397-403 |year= 2003 |pmid= 12864745 |doi= }}
*{{cite journal | author=Holm C |title=Molecular mechanisms regulating hormone-sensitive lipase and lipolysis. |journal=Biochem. Soc. Trans. |volume=31 |issue= Pt 6 |pages= 1120-4 |year= 2004 |pmid= 14641008 |doi= 10.1042/ }}
*{{cite journal | author=Holm C, Kirchgessner TG, Svenson KL, ''et al.'' |title=Hormone-sensitive lipase: sequence, expression, and chromosomal localization to 19 cent-q13.3. |journal=Science |volume=241 |issue= 4872 |pages= 1503-6 |year= 1988 |pmid= 3420405 |doi= }}
*{{cite journal | author=Levitt RC, Liu Z, Nouri N, ''et al.'' |title=Mapping of the gene for hormone sensitive lipase (LIPE) to chromosome 19q13.1-->q13.2. |journal=Cytogenet. Cell Genet. |volume=69 |issue= 3-4 |pages= 211-4 |year= 1995 |pmid= 7698015 |doi= }}
*{{cite journal | author=Langin D, Laurell H, Holst LS, ''et al.'' |title=Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 11 |pages= 4897-901 |year= 1993 |pmid= 8506334 |doi= }}
*{{cite journal | author=Holst LS, Langin D, Mulder H, ''et al.'' |title=Molecular cloning, genomic organization, and expression of a testicular isoform of hormone-sensitive lipase. |journal=Genomics |volume=35 |issue= 3 |pages= 441-7 |year= 1996 |pmid= 8812477 |doi= }}
*{{cite journal | author=Anthonsen MW, Rönnstrand L, Wernstedt C, ''et al.'' |title=Identification of novel phosphorylation sites in hormone-sensitive lipase that are phosphorylated in response to isoproterenol and govern activation properties in vitro. |journal=J. Biol. Chem. |volume=273 |issue= 1 |pages= 215-21 |year= 1998 |pmid= 9417067 |doi= }}
*{{cite journal | author=Shen WJ, Sridhar K, Bernlohr DA, Kraemer FB |title=Interaction of rat hormone-sensitive lipase with adipocyte lipid-binding protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 10 |pages= 5528-32 |year= 1999 |pmid= 10318917 |doi= }}
*{{cite journal | author=Syu LJ, Saltiel AR |title=Lipotransin: a novel docking protein for hormone-sensitive lipase. |journal=Mol. Cell |volume=4 |issue= 1 |pages= 109-15 |year= 1999 |pmid= 10445032 |doi= }}
*{{cite journal | author=Shen WJ, Patel S, Hong R, Kraemer FB |title=Hormone-sensitive lipase functions as an oligomer. |journal=Biochemistry |volume=39 |issue= 9 |pages= 2392-8 |year= 2000 |pmid= 10694408 |doi= }}
*{{cite journal | author=Johnson WJ, Jang SY, Bernard DW |title=Hormone sensitive lipase mRNA in both monocyte and macrophage forms of the human THP-1 cell line. |journal=Comp. Biochem. Physiol. B, Biochem. Mol. Biol. |volume=126 |issue= 4 |pages= 543-52 |year= 2001 |pmid= 11026666 |doi= }}
*{{cite journal | author=Laurin NN, Wang SP, Mitchell GA |title=The hormone-sensitive lipase gene is transcribed from at least five alternative first exons in mouse adipose tissue. |journal=Mamm. Genome |volume=11 |issue= 11 |pages= 972-8 |year= 2001 |pmid= 11063252 |doi= }}
*{{cite journal | author=Greenberg AS, Shen WJ, Muliro K, ''et al.'' |title=Stimulation of lipolysis and hormone-sensitive lipase via the extracellular signal-regulated kinase pathway. |journal=J. Biol. Chem. |volume=276 |issue= 48 |pages= 45456-61 |year= 2002 |pmid= 11581251 |doi= 10.1074/jbc.M104436200 }}
*{{cite journal | author=Talmud PJ, Palmen J, Luan J, ''et al.'' |title=Variation in the promoter of the human hormone sensitive lipase gene shows gender specific effects on insulin and lipid levels: results from the Ely study. |journal=Biochim. Biophys. Acta |volume=1537 |issue= 3 |pages= 239-44 |year= 2002 |pmid= 11731226 |doi= }}
*{{cite journal | author=Kolehmainen M, Vidal H, Ohisalo JJ, ''et al.'' |title=Hormone sensitive lipase expression and adipose tissue metabolism show gender difference in obese subjects after weight loss. |journal=Int. J. Obes. Relat. Metab. Disord. |volume=26 |issue= 1 |pages= 6-16 |year= 2002 |pmid= 11791141 |doi= 10.1038/sj.ijo.0801858 }}
*{{cite journal | author=Smih F, Rouet P, Lucas S, ''et al.'' |title=Transcriptional regulation of adipocyte hormone-sensitive lipase by glucose. |journal=Diabetes |volume=51 |issue= 2 |pages= 293-300 |year= 2002 |pmid= 11812735 |doi= }}
*{{cite journal | author=Mairal A, Melaine N, Laurell H, ''et al.'' |title=Characterization of a novel testicular form of human hormone-sensitive lipase. |journal=Biochem. Biophys. Res. Commun. |volume=291 |issue= 2 |pages= 286-90 |year= 2002 |pmid= 11846402 |doi= 10.1006/bbrc.2002.6427 }}
*{{cite journal | author=Ylitalo K, Nuotio I, Viikari J, ''et al.'' |title=C3, hormone-sensitive lipase, and peroxisome proliferator-activated receptor gamma expression in adipose tissue of familial combined hyperlipidemia patients. |journal=Metab. Clin. Exp. |volume=51 |issue= 5 |pages= 664-70 |year= 2002 |pmid= 11979403 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LPA... {November 16, 2007 4:12:19 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:12:50 PM PST}
<!-- 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
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_LPA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1i71.
| PDB = {{PDB2|1i71}}, {{PDB2|1jfn}}, {{PDB2|1kiv}}, {{PDB2|2feb}}, {{PDB2|3kiv}}, {{PDB2|4kiv}}
| Name = Lipoprotein, Lp(a)
| HGNCid = 6667
| Symbol = LPA
| AltSymbols =; AK38; APOA; LP
| OMIM = 152200
| ECnumber =
| Homologene = 87856
| MGIid =
| GeneAtlas_image1 = PBB_GE_LPA_207584_at_tn.png
| GeneAtlas_image2 = PBB_GE_LPA_209978_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0004866 |text = endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0005319 |text = lipid transporter activity}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006869 |text = lipid transport}} {{GNF_GO|id=GO:0008015 |text = circulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4018
| Hs_Ensembl = ENSG00000198670
| Hs_RefseqProtein = XP_946885
| Hs_RefseqmRNA = XM_941792
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 160872505
| Hs_GenLoc_end = 161005281
| Hs_Uniprot = P08519
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Lipoprotein, Lp(a)''', also known as '''LPA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LPA lipoprotein, Lp(a)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4018| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Utermann G |title=The mysteries of lipoprotein(a). |journal=Science |volume=246 |issue= 4932 |pages= 904-10 |year= 1989 |pmid= 2530631 |doi= }}
*{{cite journal | author=Salonen EM, Jauhiainen M, Zardi L, ''et al.'' |title=Lipoprotein(a) binds to fibronectin and has serine proteinase activity capable of cleaving it. |journal=EMBO J. |volume=8 |issue= 13 |pages= 4035-40 |year= 1990 |pmid= 2531657 |doi= }}
*{{cite journal | author=Frank SL, Klisak I, Sparkes RS, ''et al.'' |title=The apolipoprotein(a) gene resides on human chromosome 6q26-27, in close proximity to the homologous gene for plasminogen. |journal=Hum. Genet. |volume=79 |issue= 4 |pages= 352-6 |year= 1988 |pmid= 3410459 |doi= }}
*{{cite journal | author=McLean JW, Tomlinson JE, Kuang WJ, ''et al.'' |title=cDNA sequence of human apolipoprotein(a) is homologous to plasminogen. |journal=Nature |volume=330 |issue= 6144 |pages= 132-7 |year= 1987 |pmid= 3670400 |doi= 10.1038/330132a0 }}
*{{cite journal | author=Scanu AM, Pfaffinger D, Lee JC, Hinman J |title=A single point mutation (Trp72-->Arg) in human apo(a) kringle 4-37 associated with a lysine binding defect in Lp(a). |journal=Biochim. Biophys. Acta |volume=1227 |issue= 1-2 |pages= 41-5 |year= 1994 |pmid= 7918682 |doi= }}
*{{cite journal | author=Grainger DJ, Kemp PR, Liu AC, ''et al.'' |title=Activation of transforming growth factor-beta is inhibited in transgenic apolipoprotein(a) mice. |journal=Nature |volume=370 |issue= 6489 |pages= 460-2 |year= 1994 |pmid= 8047165 |doi= 10.1038/370460a0 }}
*{{cite journal | author=Mikol V, LoGrasso PV, Boettcher BR |title=Crystal structures of apolipoprotein(a) kringle IV37 free and complexed with 6-aminohexanoic acid and with p-aminomethylbenzoic acid: existence of novel and expected binding modes. |journal=J. Mol. Biol. |volume=256 |issue= 4 |pages= 751-61 |year= 1996 |pmid= 8642595 |doi= 10.1006/jmbi.1996.0122 }}
*{{cite journal | author=Edelstein C, Italia JA, Klezovitch O, Scanu AM |title=Functional and metabolic differences between elastase-generated fragments of human lipoprotein[a] and apolipoprotein[a] |journal=J. Lipid Res. |volume=37 |issue= 8 |pages= 1786-801 |year= 1997 |pmid= 8864963 |doi= }}
*{{cite journal | author=Edelstein C, Italia JA, Scanu AM |title=Polymorphonuclear cells isolated from human peripheral blood cleave lipoprotein(a) and apolipoprotein(a) at multiple interkringle sites via the enzyme elastase. Generation of mini-Lp(a) particles and apo(a) fragments. |journal=J. Biol. Chem. |volume=272 |issue= 17 |pages= 11079-87 |year= 1997 |pmid= 9111002 |doi= }}
*{{cite journal | author=Köchl S, Fresser F, Lobentanz E, ''et al.'' |title=Novel interaction of apolipoprotein(a) with beta-2 glycoprotein I mediated by the kringle IV domain. |journal=Blood |volume=90 |issue= 4 |pages= 1482-9 |year= 1997 |pmid= 9269765 |doi= }}
*{{cite journal | author=Bonen DK, Nassir F, Hausman AM, Davidson NO |title=Inhibition of N-linked glycosylation results in retention of intracellular apo[a] in hepatoma cells, although nonglycosylated and immature forms of apolipoprotein[a] are competent to associate with apolipoprotein B-100 in vitro. |journal=J. Lipid Res. |volume=39 |issue= 8 |pages= 1629-40 |year= 1998 |pmid= 9717723 |doi= }}
*{{cite journal | author=Niemeier A, Willnow T, Dieplinger H, ''et al.'' |title=Identification of megalin/gp330 as a receptor for lipoprotein(a) in vitro. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=19 |issue= 3 |pages= 552-61 |year= 1999 |pmid= 10073957 |doi= }}
*{{cite journal | author=Edelstein C, Shapiro SD, Klezovitch O, Scanu AM |title=Macrophage metalloelastase, MMP-12, cleaves human apolipoprotein(a) in the linker region between kringles IV-4 and IV-5. Potential relevance to lipoprotein(a) biology. |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 10019-23 |year= 1999 |pmid= 10187779 |doi= }}
*{{cite journal | author=Ogorelkova M, Gruber A, Utermann G |title=Molecular basis of congenital lp(a) deficiency: a frequent apo(a) 'null' mutation in caucasians. |journal=Hum. Mol. Genet. |volume=8 |issue= 11 |pages= 2087-96 |year= 1999 |pmid= 10484779 |doi= }}
*{{cite journal | author=Røsby O, Berg K |title=LPA gene: interaction between the apolipoprotein(a) size ('kringle IV' repeat) polymorphism and a pentanucleotide repeat polymorphism influences Lp(a) lipoprotein level. |journal=J. Intern. Med. |volume=247 |issue= 1 |pages= 139-52 |year= 2000 |pmid= 10672142 |doi= }}
*{{cite journal | author=Klose R, Fresser F, Kochl S, ''et al.'' |title=Mapping of a minimal apolipoprotein(a) interaction motif conserved in fibrin(ogen) beta - and gamma -chains. |journal=J. Biol. Chem. |volume=275 |issue= 49 |pages= 38206-12 |year= 2001 |pmid= 10980194 |doi= 10.1074/jbc.M003640200 }}
*{{cite journal | author=Ogorelkova M, Kraft HG, Ehnholm C, Utermann G |title=Single nucleotide polymorphisms in exons of the apo(a) kringles IV types 6 to 10 domain affect Lp(a) plasma concentrations and have different patterns in Africans and Caucasians. |journal=Hum. Mol. Genet. |volume=10 |issue= 8 |pages= 815-24 |year= 2001 |pmid= 11285247 |doi= }}
*{{cite journal | author=Garner B, Merry AH, Royle L, ''et al.'' |title=Structural elucidation of the N- and O-glycans of human apolipoprotein(a): role of o-glycans in conferring protease resistance. |journal=J. Biol. Chem. |volume=276 |issue= 25 |pages= 22200-8 |year= 2001 |pmid= 11294842 |doi= 10.1074/jbc.M102150200 }}
*{{cite journal | author=Xue S, Madison EL, Miles LA |title=The Kringle V-protease domain is a fibrinogen binding region within Apo(a). |journal=Thromb. Haemost. |volume=86 |issue= 5 |pages= 1229-37 |year= 2003 |pmid= 11816712 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LRP5... {November 16, 2007 4:12:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:13:56 PM PST}
<!-- 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
}}
<!-- 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 = Low density lipoprotein receptor-related protein 5
| HGNCid = 6697
| Symbol = LRP5
| AltSymbols =; HBM; BMND1; EVR1; EVR4; LR3; LRP7; OPPG; OPS; OPTA1; VBCH2
| OMIM = 603506
| ECnumber =
| Homologene = 1746
| MGIid = 1278315
| GeneAtlas_image1 = PBB_GE_LRP5_209468_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006897 |text = endocytosis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0016055 |text = Wnt receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4041
| Hs_Ensembl = ENSG00000162337
| Hs_RefseqProtein = NP_002326
| Hs_RefseqmRNA = NM_002335
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 67836674
| Hs_GenLoc_end = 67973301
| Hs_Uniprot = O75197
| Mm_EntrezGene = 16973
| Mm_Ensembl = ENSMUSG00000024913
| Mm_RefseqmRNA = NM_008513
| Mm_RefseqProtein = NP_032539
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 3584836
| Mm_GenLoc_end = 3686546
| Mm_Uniprot = Q3UI55
}}
}}
'''Low density lipoprotein receptor-related protein 5''', also known as '''LRP5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LRP5 low density lipoprotein receptor-related protein 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4041| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=He X, Semenov M, Tamai K, Zeng X |title=LDL receptor-related proteins 5 and 6 in Wnt/beta-catenin signaling: arrows point the way. |journal=Development |volume=131 |issue= 8 |pages= 1663-77 |year= 2004 |pmid= 15084453 |doi= 10.1242/dev.01117 }}
*{{cite journal | author=Godyna S, Liau G, Popa I, ''et al.'' |title=Identification of the low density lipoprotein receptor-related protein (LRP) as an endocytic receptor for thrombospondin-1. |journal=J. Cell Biol. |volume=129 |issue= 5 |pages= 1403-10 |year= 1995 |pmid= 7775583 |doi= }}
*{{cite journal | author=Gong Y, Vikkula M, Boon L, ''et al.'' |title=Osteoporosis-pseudoglioma syndrome, a disorder affecting skeletal strength and vision, is assigned to chromosome region 11q12-13. |journal=Am. J. Hum. Genet. |volume=59 |issue= 1 |pages= 146-51 |year= 1996 |pmid= 8659519 |doi= }}
*{{cite journal | author=Johnson ML, Gong G, Kimberling W, ''et al.'' |title=Linkage of a gene causing high bone mass to human chromosome 11 (11q12-13) |journal=Am. J. Hum. Genet. |volume=60 |issue= 6 |pages= 1326-32 |year= 1997 |pmid= 9199553 |doi= }}
*{{cite journal | author=Hey PJ, Twells RC, Phillips MS, ''et al.'' |title=Cloning of a novel member of the low-density lipoprotein receptor family. |journal=Gene |volume=216 |issue= 1 |pages= 103-11 |year= 1998 |pmid= 9714764 |doi= }}
*{{cite journal | author=Dong Y, Lathrop W, Weaver D, ''et al.'' |title=Molecular cloning and characterization of LR3, a novel LDL receptor family protein with mitogenic activity. |journal=Biochem. Biophys. Res. Commun. |volume=251 |issue= 3 |pages= 784-90 |year= 1998 |pmid= 9790987 |doi= 10.1006/bbrc.1998.9545 }}
*{{cite journal | author=de Crecchio G, Simonelli F, Nunziata G, ''et al.'' |title=Autosomal recessive familial exudative vitreoretinopathy: evidence for genetic heterogeneity. |journal=Clin. Genet. |volume=54 |issue= 4 |pages= 315-20 |year= 1999 |pmid= 9831343 |doi= }}
*{{cite journal | author=Chen D, Lathrop W, Dong Y |title=Molecular cloning of mouse Lrp7(Lr3) cDNA and chromosomal mapping of orthologous genes in mouse and human. |journal=Genomics |volume=55 |issue= 3 |pages= 314-21 |year= 1999 |pmid= 10049586 |doi= 10.1006/geno.1998.5688 }}
*{{cite journal | author=Mao J, Wang J, Liu B, ''et al.'' |title=Low-density lipoprotein receptor-related protein-5 binds to Axin and regulates the canonical Wnt signaling pathway. |journal=Mol. Cell |volume=7 |issue= 4 |pages= 801-9 |year= 2001 |pmid= 11336703 |doi= }}
*{{cite journal | author=Twells RC, Metzker ML, Brown SD, ''et al.'' |title=The sequence and gene characterization of a 400-kb candidate region for IDDM4 on chromosome 11q13. |journal=Genomics |volume=72 |issue= 3 |pages= 231-42 |year= 2001 |pmid= 11401438 |doi= 10.1006/geno.2000.6492 }}
*{{cite journal | author=Semënov MV, Tamai K, Brott BK, ''et al.'' |title=Head inducer Dickkopf-1 is a ligand for Wnt coreceptor LRP6. |journal=Curr. Biol. |volume=11 |issue= 12 |pages= 951-61 |year= 2001 |pmid= 11448771 |doi= }}
*{{cite journal | author=Zorn AM |title=Wnt signalling: antagonistic Dickkopfs. |journal=Curr. Biol. |volume=11 |issue= 15 |pages= R592-5 |year= 2001 |pmid= 11516963 |doi= }}
*{{cite journal | author=Gong Y, Slee RB, Fukai N, ''et al.'' |title=LDL receptor-related protein 5 (LRP5) affects bone accrual and eye development. |journal=Cell |volume=107 |issue= 4 |pages= 513-23 |year= 2002 |pmid= 11719191 |doi= }}
*{{cite journal | author=Little RD, Carulli JP, Del Mastro RG, ''et al.'' |title=A mutation in the LDL receptor-related protein 5 gene results in the autosomal dominant high-bone-mass trait. |journal=Am. J. Hum. Genet. |volume=70 |issue= 1 |pages= 11-9 |year= 2002 |pmid= 11741193 |doi= }}
*{{cite journal | author=Okubo M, Horinishi A, Kim DH, ''et al.'' |title=Seven novel sequence variants in the human low density lipoprotein receptor related protein 5 (LRP5) gene. |journal=Hum. Mutat. |volume=19 |issue= 2 |pages= 186 |year= 2002 |pmid= 11793484 |doi= 10.1002/humu.9012 }}
*{{cite journal | author=Boyden LM, Mao J, Belsky J, ''et al.'' |title=High bone density due to a mutation in LDL-receptor-related protein 5. |journal=N. Engl. J. Med. |volume=346 |issue= 20 |pages= 1513-21 |year= 2002 |pmid= 12015390 |doi= 10.1056/NEJMoa013444 }}
*{{cite journal | author=Van Hul E, Gram J, Bollerslev J, ''et al.'' |title=Localization of the gene causing autosomal dominant osteopetrosis type I to chromosome 11q12-13. |journal=J. Bone Miner. Res. |volume=17 |issue= 6 |pages= 1111-7 |year= 2002 |pmid= 12054167 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Fujino T, Asaba H, Kang MJ, ''et al.'' |title=Low-density lipoprotein receptor-related protein 5 (LRP5) is essential for normal cholesterol metabolism and glucose-induced insulin secretion. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 1 |pages= 229-34 |year= 2003 |pmid= 12509515 |doi= 10.1073/pnas.0133792100 }}
*{{cite journal | author=Van Wesenbeeck L, Cleiren E, Gram J, ''et al.'' |title=Six novel missense mutations in the LDL receptor-related protein 5 (LRP5) gene in different conditions with an increased bone density. |journal=Am. J. Hum. Genet. |volume=72 |issue= 3 |pages= 763-71 |year= 2003 |pmid= 12579474 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MX1... {November 16, 2007 4:13:56 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:14:25 PM PST}
<!-- 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
}}
<!-- 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 = Myxovirus (influenza virus) resistance 1, interferon-inducible protein p78 (mouse)
| HGNCid = 7532
| Symbol = MX1
| AltSymbols =; IFI-78K; IFI78; MX; MxA
| OMIM = 147150
| ECnumber =
| Homologene = 1844
| MGIid = 97244
| GeneAtlas_image1 = PBB_GE_MX1_202086_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0009615 |text = response to virus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4599
| Hs_Ensembl = ENSG00000157601
| Hs_RefseqProtein = NP_002453
| Hs_RefseqmRNA = NM_002462
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 41725838
| Hs_GenLoc_end = 41753008
| Hs_Uniprot = P20591
| Mm_EntrezGene = 17858
| Mm_Ensembl = ENSMUSG00000023341
| Mm_RefseqmRNA = NM_013606
| Mm_RefseqProtein = NP_038634
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 97690999
| Mm_GenLoc_end = 97715817
| Mm_Uniprot = Q61924
}}
}}
'''Myxovirus (influenza virus) resistance 1, interferon-inducible protein p78 (mouse)''', also known as '''MX1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MX1 myxovirus (influenza virus) resistance 1, interferon-inducible protein p78 (mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4599| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = In mouse, the interferon-inducible Mx protein is responsible for a specific antiviral state against influenza virus infection. The protein encoded by this gene is similar to the mouse protein as determined by its antigenic relatedness, induction conditions, physicochemical properties, and amino acid analysis. This cytoplasmic protein is a member of both the dynamin family and the family of large GTPases.<ref name="entrez">{{cite web | title = Entrez Gene: MX1 myxovirus (influenza virus) resistance 1, interferon-inducible protein p78 (mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4599| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pavlovic J, Haller O, Staeheli P |title=Human and mouse Mx proteins inhibit different steps of the influenza virus multiplication cycle. |journal=J. Virol. |volume=66 |issue= 4 |pages= 2564-9 |year= 1992 |pmid= 1548781 |doi= }}
*{{cite journal | author=Horisberger MA |title=Interferon-induced human protein MxA is a GTPase which binds transiently to cellular proteins. |journal=J. Virol. |volume=66 |issue= 8 |pages= 4705-9 |year= 1992 |pmid= 1629950 |doi= }}
*{{cite journal | author=Petersen MB, Slaugenhaupt SA, Lewis JG, ''et al.'' |title=A genetic linkage map of 27 markers on human chromosome 21. |journal=Genomics |volume=9 |issue= 3 |pages= 407-19 |year= 1991 |pmid= 1674496 |doi= }}
*{{cite journal | author=Horisberger MA, McMaster GK, Zeller H, ''et al.'' |title=Cloning and sequence analyses of cDNAs for interferon- and virus-induced human Mx proteins reveal that they contain putative guanine nucleotide-binding sites: functional study of the corresponding gene promoter. |journal=J. Virol. |volume=64 |issue= 3 |pages= 1171-81 |year= 1990 |pmid= 2154602 |doi= }}
*{{cite journal | author=Pavlovic J, Zürcher T, Haller O, Staeheli P |title=Resistance to influenza virus and vesicular stomatitis virus conferred by expression of human MxA protein. |journal=J. Virol. |volume=64 |issue= 7 |pages= 3370-5 |year= 1990 |pmid= 2161946 |doi= }}
*{{cite journal | author=Aebi M, Fäh J, Hurt N, ''et al.'' |title=cDNA structures and regulation of two interferon-induced human Mx proteins. |journal=Mol. Cell. Biol. |volume=9 |issue= 11 |pages= 5062-72 |year= 1990 |pmid= 2481229 |doi= }}
*{{cite journal | author=Weitz G, Bekisz J, Zoon K, Arnheiter H |title=Purification and characterization of a human Mx protein. |journal=J. Interferon Res. |volume=9 |issue= 6 |pages= 679-89 |year= 1990 |pmid= 2607176 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Melén K, Keskinen P, Ronni T, ''et al.'' |title=Human MxB protein, an interferon-alpha-inducible GTPase, contains a nuclear targeting signal and is localized in the heterochromatin region beneath the nuclear envelope. |journal=J. Biol. Chem. |volume=271 |issue= 38 |pages= 23478-86 |year= 1996 |pmid= 8798556 |doi= }}
*{{cite journal | author=Ponten A, Sick C, Weeber M, ''et al.'' |title=Dominant-negative mutants of human MxA protein: domains in the carboxy-terminal moiety are important for oligomerization and antiviral activity. |journal=J. Virol. |volume=71 |issue= 4 |pages= 2591-9 |year= 1997 |pmid= 9060610 |doi= }}
*{{cite journal | author=Fernández M, Quiroga JA, Martín J, ''et al.'' |title=Impaired interferon induction of human MxA protein in chronic hepatitis B virus infection. |journal=J. Med. Virol. |volume=51 |issue= 4 |pages= 332-7 |year= 1997 |pmid= 9093949 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Li Y, Youssoufian H |title=MxA overexpression reveals a common genetic link in four Fanconi anemia complementation groups. |journal=J. Clin. Invest. |volume=100 |issue= 11 |pages= 2873-80 |year= 1998 |pmid= 9389754 |doi= }}
*{{cite journal | author=Kochs G, Trost M, Janzen C, Haller O |title=MxA GTPase: oligomerization and GTP-dependent interaction with viral RNP target structures. |journal=Methods |volume=15 |issue= 3 |pages= 255-63 |year= 1998 |pmid= 9735310 |doi= 10.1006/meth.1998.0629 }}
*{{cite journal | author=Weber F, Haller O, Kochs G |title=MxA GTPase blocks reporter gene expression of reconstituted Thogoto virus ribonucleoprotein complexes. |journal=J. Virol. |volume=74 |issue= 1 |pages= 560-3 |year= 2000 |pmid= 10590150 |doi= }}
*{{cite journal | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
*{{cite journal | author=Hijikata M, Ohta Y, Mishiro S |title=Identification of a single nucleotide polymorphism in the MxA gene promoter (G/T at nt -88) correlated with the response of hepatitis C patients to interferon. |journal=Intervirology |volume=43 |issue= 2 |pages= 124-7 |year= 2000 |pmid= 10971132 |doi= }}
*{{cite journal | author=Engelhardt OG, Ullrich E, Kochs G, Haller O |title=Interferon-induced antiviral Mx1 GTPase is associated with components of the SUMO-1 system and promyelocytic leukemia protein nuclear bodies. |journal=Exp. Cell Res. |volume=271 |issue= 2 |pages= 286-95 |year= 2002 |pmid= 11716541 |doi= 10.1006/excr.2001.5380 }}
*{{cite journal | author=Hijikata M, Mishiro S, Miyamoto C, ''et al.'' |title=Genetic polymorphism of the MxA gene promoter and interferon responsiveness of hepatitis C patients: revisited by analyzing two SNP sites (-123 and -88) in vivo and in vitro. |journal=Intervirology |volume=44 |issue= 6 |pages= 379-82 |year= 2002 |pmid= 11805446 |doi= }}
*{{cite journal | author=Kochs G, Haener M, Aebi U, Haller O |title=Self-assembly of human MxA GTPase into highly ordered dynamin-like oligomers. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 14172-6 |year= 2002 |pmid= 11847228 |doi= 10.1074/jbc.M200244200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NDRG1... {November 16, 2007 4:17:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:18:11 PM PST}
<!-- 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
}}
<!-- 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 = N-myc downstream regulated gene 1
| HGNCid = 7679
| Symbol = NDRG1
| AltSymbols =; DRG1; CAP43; CMT4D; GC4; HMSNL; NDR1; NMSL; PROXY1; RIT42; RTP; TARG1; TDD5
| OMIM = 605262
| ECnumber =
| Homologene = 55953
| MGIid = 1341799
| GeneAtlas_image1 = PBB_GE_NDRG1_200632_s_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0010038 |text = response to metal ion}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10397
| Hs_Ensembl = ENSG00000104419
| Hs_RefseqProtein = NP_006087
| Hs_RefseqmRNA = NM_006096
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 134318601
| Hs_GenLoc_end = 134379011
| Hs_Uniprot = Q92597
| Mm_EntrezGene = 17988
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_008681
| Mm_RefseqProtein = NP_032707
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''N-myc downstream regulated gene 1''', also known as '''NDRG1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NDRG1 N-myc downstream regulated gene 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10397| accessdate = }}</ref>
<!-- 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 N-myc downregulated gene family which belongs to the alpha/beta hydrolase superfamily. The protein encoded by this gene is a cytoplasmic protein involved in stress responses, hormone responses, cell growth, and differentiation. Mutation in this gene has been reported to be causative for hereditary motor and sensory neuropathy-Lom.<ref name="entrez">{{cite web | title = Entrez Gene: NDRG1 N-myc downstream regulated gene 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10397| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kovacevic Z, Richardson DR |title=The metastasis suppressor, Ndrg-1: a new ally in the fight against cancer. |journal=Carcinogenesis |volume=27 |issue= 12 |pages= 2355-66 |year= 2007 |pmid= 16920733 |doi= 10.1093/carcin/bgl146 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Kalaydjieva L, Hallmayer J, Chandler D, ''et al.'' |title=Gene mapping in Gypsies identifies a novel demyelinating neuropathy on chromosome 8q24. |journal=Nat. Genet. |volume=14 |issue= 2 |pages= 214-7 |year= 1996 |pmid= 8841199 |doi= 10.1038/ng1096-214 }}
*{{cite journal | author=Kokame K, Kato H, Miyata T |title=Homocysteine-respondent genes in vascular endothelial cells identified by differential display analysis. GRP78/BiP and novel genes. |journal=J. Biol. Chem. |volume=271 |issue= 47 |pages= 29659-65 |year= 1997 |pmid= 8939898 |doi= }}
*{{cite journal | author=van Belzen N, Dinjens WN, Diesveld MP, ''et al.'' |title=A novel gene which is up-regulated during colon epithelial cell differentiation and down-regulated in colorectal neoplasms. |journal=Lab. Invest. |volume=77 |issue= 1 |pages= 85-92 |year= 1997 |pmid= 9251681 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Zhou D, Salnikow K, Costa M |title=Cap43, a novel gene specifically induced by Ni2+ compounds. |journal=Cancer Res. |volume=58 |issue= 10 |pages= 2182-9 |year= 1998 |pmid= 9605764 |doi= }}
*{{cite journal | author=Kurdistani SK, Arizti P, Reimer CL, ''et al.'' |title=Inhibition of tumor cell growth by RTP/rit42 and its responsiveness to p53 and DNA damage. |journal=Cancer Res. |volume=58 |issue= 19 |pages= 4439-44 |year= 1998 |pmid= 9766676 |doi= }}
*{{cite journal | author=Piquemal D, Joulia D, Balaguer P, ''et al.'' |title=Differential expression of the RTP/Drg1/Ndr1 gene product in proliferating and growth arrested cells. |journal=Biochim. Biophys. Acta |volume=1450 |issue= 3 |pages= 364-73 |year= 1999 |pmid= 10395947 |doi= }}
*{{cite journal | author=Guan RJ, Ford HL, Fu Y, ''et al.'' |title=Drg-1 as a differentiation-related, putative metastatic suppressor gene in human colon cancer. |journal=Cancer Res. |volume=60 |issue= 3 |pages= 749-55 |year= 2000 |pmid= 10676663 |doi= }}
*{{cite journal | author=Kalaydjieva L, Gresham D, Gooding R, ''et al.'' |title=N-myc downstream-regulated gene 1 is mutated in hereditary motor and sensory neuropathy-Lom. |journal=Am. J. Hum. Genet. |volume=67 |issue= 1 |pages= 47-58 |year= 2000 |pmid= 10831399 |doi= }}
*{{cite journal | author=Park H, Adams MA, Lachat P, ''et al.'' |title=Hypoxia induces the expression of a 43-kDa protein (PROXY-1) in normal and malignant cells. |journal=Biochem. Biophys. Res. Commun. |volume=276 |issue= 1 |pages= 321-8 |year= 2000 |pmid= 11006124 |doi= 10.1006/bbrc.2000.3475 }}
*{{cite journal | author=Rutherford MN, Bayly GR, Matthews BP, ''et al.'' |title=The leukemogenic transcription factor E2a-Pbx1 induces expression of the putative N-myc and p53 target gene NDRG1 in Ba/F3 cells. |journal=Leukemia |volume=15 |issue= 3 |pages= 362-70 |year= 2001 |pmid= 11237058 |doi= }}
*{{cite journal | author=Zhou RH, Kokame K, Tsukamoto Y, ''et al.'' |title=Characterization of the human NDRG gene family: a newly identified member, NDRG4, is specifically expressed in brain and heart. |journal=Genomics |volume=73 |issue= 1 |pages= 86-97 |year= 2001 |pmid= 11352569 |doi= 10.1006/geno.2000.6496 }}
*{{cite journal | author=Qu X, Zhai Y, Wei H, ''et al.'' |title=Characterization and expression of three novel differentiation-related genes belong to the human NDRG gene family. |journal=Mol. Cell. Biochem. |volume=229 |issue= 1-2 |pages= 35-44 |year= 2002 |pmid= 11936845 |doi= }}
*{{cite journal | author=Cangul H, Salnikow K, Yee H, ''et al.'' |title=Enhanced expression of a novel protein in human cancer cells: a potential aid to cancer diagnosis. |journal=Cell Biol. Toxicol. |volume=18 |issue= 2 |pages= 87-96 |year= 2002 |pmid= 12046693 |doi= }}
*{{cite journal | author=Cangul H, Salnikow K, Yee H, ''et al.'' |title=Enhanced overexpression of an HIF-1/hypoxia-related protein in cancer cells. |journal=Environ. Health Perspect. |volume=110 Suppl 5 |issue= |pages= 783-8 |year= 2002 |pmid= 12429530 |doi= }}
*{{cite journal | author=Lachat P, Shaw P, Gebhard S, ''et al.'' |title=Expression of NDRG1, a differentiation-related gene, in human tissues. |journal=Histochem. Cell Biol. |volume=118 |issue= 5 |pages= 399-408 |year= 2003 |pmid= 12432451 |doi= 10.1007/s00418-002-0460-9 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Segawa T, Nau ME, Xu LL, ''et al.'' |title=Androgen-induced expression of endoplasmic reticulum (ER) stress response genes in prostate cancer cells. |journal=Oncogene |volume=21 |issue= 57 |pages= 8749-58 |year= 2003 |pmid= 12483528 |doi= 10.1038/sj.onc.1205992 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NMT1... {November 16, 2007 4:14:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:14:52 PM PST}
<!-- 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
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_NMT1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1rxt.
| PDB = {{PDB2|1rxt}}
| Name = N-myristoyltransferase 1
| HGNCid = 7857
| Symbol = NMT1
| AltSymbols =; NMT
| OMIM = 160993
| ECnumber =
| Homologene = 69027
| MGIid = 102579
| GeneAtlas_image1 = PBB_GE_NMT1_201157_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_NMT1_201158_at_tn.png
| GeneAtlas_image3 = PBB_GE_NMT1_201159_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004379 |text = glycylpeptide N-tetradecanoyltransferase activity}} {{GNF_GO|id=GO:0008415 |text = acyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0006498 |text = N-terminal protein lipidation}} {{GNF_GO|id=GO:0006499 |text = N-terminal protein myristoylation}} {{GNF_GO|id=GO:0009249 |text = protein lipoylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4836
| Hs_Ensembl = ENSG00000136448
| Hs_RefseqProtein = NP_066565
| Hs_RefseqmRNA = NM_021079
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 40494206
| Hs_GenLoc_end = 40541903
| Hs_Uniprot = P30419
| Mm_EntrezGene = 18107
| Mm_Ensembl = ENSMUSG00000020936
| Mm_RefseqmRNA = XM_906274
| Mm_RefseqProtein = XP_911367
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 102844436
| Mm_GenLoc_end = 102885002
| Mm_Uniprot = Q3UJC3
}}
}}
'''N-myristoyltransferase 1''', also known as '''NMT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NMT1 N-myristoyltransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4836| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rajala RV, Datla RS, Moyana TN, ''et al.'' |title=N-myristoyltransferase. |journal=Mol. Cell. Biochem. |volume=204 |issue= 1-2 |pages= 135-55 |year= 2000 |pmid= 10718634 |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=Wice BM, Gordon JI |title=A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexin. |journal=J. Cell Biol. |volume=116 |issue= 2 |pages= 405-22 |year= 1992 |pmid= 1530946 |doi= }}
*{{cite journal | author=Duronio RJ, Reed SI, Gordon JI |title=Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 9 |pages= 4129-33 |year= 1992 |pmid= 1570339 |doi= }}
*{{cite journal | author=Mumby SM, Heukeroth RO, Gordon JI, Gilman AG |title=G-protein alpha-subunit expression, myristoylation, and membrane association in COS cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 2 |pages= 728-32 |year= 1990 |pmid= 2153964 |doi= }}
*{{cite journal | author=Pal R, Reitz MS, Tschachler E, ''et al.'' |title=Myristoylation of gag proteins of HIV-1 plays an important role in virus assembly. |journal=AIDS Res. Hum. Retroviruses |volume=6 |issue= 6 |pages= 721-30 |year= 1990 |pmid= 2194551 |doi= }}
*{{cite journal | author=Bryant M, Ratner L |title=Myristoylation-dependent replication and assembly of human immunodeficiency virus 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 2 |pages= 523-7 |year= 1990 |pmid= 2405382 |doi= }}
*{{cite journal | author=Tashiro A, Shoji S, Kubota Y |title=Antimyristoylation of the gag proteins in the human immunodeficiency virus-infected cells with N-myristoyl glycinal diethylacetal resulted in inhibition of virus production. |journal=Biochem. Biophys. Res. Commun. |volume=165 |issue= 3 |pages= 1145-54 |year= 1990 |pmid= 2692561 |doi= }}
*{{cite journal | author=Goddard C, Aquino A, Glazer RI, Felsted RL |title=Chemical characterization of p17gag from human immunodeficiency virus as an N-terminally myristoylated protein. |journal=Eur. J. Biochem. |volume=182 |issue= 2 |pages= 323-6 |year= 1989 |pmid= 2737204 |doi= }}
*{{cite journal | author=Göttlinger HG, Sodroski JG, Haseltine WA |title=Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 15 |pages= 5781-5 |year= 1989 |pmid= 2788277 |doi= }}
*{{cite journal | author=Schultz AM, Henderson LE, Oroszlan S, ''et al.'' |title=Amino terminal myristylation of the protein kinase p60src, a retroviral transforming protein. |journal=Science |volume=227 |issue= 4685 |pages= 427-9 |year= 1985 |pmid= 3917576 |doi= }}
*{{cite journal | author=Liu J, Sessa WC |title=Identification of covalently bound amino-terminal myristic acid in endothelial nitric oxide synthase. |journal=J. Biol. Chem. |volume=269 |issue= 16 |pages= 11691-4 |year= 1994 |pmid= 7512951 |doi= }}
*{{cite journal | author=Lee PP, Linial ML |title=Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signal. |journal=J. Virol. |volume=68 |issue= 10 |pages= 6644-54 |year= 1994 |pmid= 7521919 |doi= }}
*{{cite journal | author=Sigal CT, Zhou W, Buser CA, ''et al.'' |title=Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 25 |pages= 12253-7 |year= 1995 |pmid= 7527558 |doi= }}
*{{cite journal | author=Zhou W, Parent LJ, Wills JW, Resh MD |title=Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids. |journal=J. Virol. |volume=68 |issue= 4 |pages= 2556-69 |year= 1994 |pmid= 8139035 |doi= }}
*{{cite journal | author=Kobayashi M, Takamatsu K, Saitoh S, Noguchi T |title=Myristoylation of hippocalcin is linked to its calcium-dependent membrane association properties. |journal=J. Biol. Chem. |volume=268 |issue= 25 |pages= 18898-904 |year= 1993 |pmid= 8360179 |doi= }}
*{{cite journal | author=Morikawa Y, Hinata S, Tomoda H, ''et al.'' |title=Complete inhibition of human immunodeficiency virus Gag myristoylation is necessary for inhibition of particle budding. |journal=J. Biol. Chem. |volume=271 |issue= 5 |pages= 2868-73 |year= 1996 |pmid= 8576268 |doi= }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Zhou W, Resh MD |title=Differential membrane binding of the human immunodeficiency virus type 1 matrix protein. |journal=J. Virol. |volume=70 |issue= 12 |pages= 8540-8 |year= 1997 |pmid= 8970978 |doi= }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NR1H3... {November 16, 2007 4:16:46 PM PST}
- SEARCH REDIRECT: Control Box Found: NR1H3 {November 16, 2007 4:17:20 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:17:21 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:17:21 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:17:21 PM PST}
- UPDATED: Updated protein page: NR1H3 {November 16, 2007 4:17:27 PM PST}
- INFO: Beginning work on OCLN... {November 16, 2007 4:14:52 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:15:11 PM PST}
<!-- 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
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_OCLN_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wpa.
| PDB = {{PDB2|1wpa}}, {{PDB2|1xaw}}
| Name = Occludin
| HGNCid = 8104
| Symbol = OCLN
| AltSymbols =;
| OMIM = 602876
| ECnumber =
| Homologene = 1905
| MGIid = 106183
| Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005923 |text = tight junction}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006461 |text = protein complex assembly}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4950
| Hs_Ensembl =
| Hs_RefseqProtein = XP_001128133
| Hs_RefseqmRNA = XM_001128133
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 18260
| Mm_Ensembl = ENSMUSG00000021638
| Mm_RefseqmRNA = NM_008756
| Mm_RefseqProtein = NP_032782
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 101597574
| Mm_GenLoc_end = 101652864
| Mm_Uniprot = Q3UKZ5
}}
}}
'''Occludin''', also known as '''OCLN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: OCLN occludin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4950| accessdate = }}</ref>
<!-- 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 membrane protein which is located at tight junctions. This protein may be involved in the formation and maintenance of the tight junction. The possibility of several alternatively spliced products has been suggested but the full nature of these products has not been described.<ref name="entrez">{{cite web | title = Entrez Gene: OCLN occludin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4950| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Furuse M, Itoh M, Hirase T, ''et al.'' |title=Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. |journal=J. Cell Biol. |volume=127 |issue= 6 Pt 1 |pages= 1617-26 |year= 1995 |pmid= 7798316 |doi= }}
*{{cite journal | author=Ando-Akatsuka Y, Saitou M, Hirase T, ''et al.'' |title=Interspecies diversity of the occludin sequence: cDNA cloning of human, mouse, dog, and rat-kangaroo homologues. |journal=J. Cell Biol. |volume=133 |issue= 1 |pages= 43-7 |year= 1996 |pmid= 8601611 |doi= }}
*{{cite journal | author=Van Itallie CM, Anderson JM |title=Occludin confers adhesiveness when expressed in fibroblasts. |journal=J. Cell. Sci. |volume=110 ( Pt 9) |issue= |pages= 1113-21 |year= 1997 |pmid= 9175707 |doi= }}
*{{cite journal | author=Kimura Y, Shiozaki H, Hirao M, ''et al.'' |title=Expression of occludin, tight-junction-associated protein, in human digestive tract. |journal=Am. J. Pathol. |volume=151 |issue= 1 |pages= 45-54 |year= 1997 |pmid= 9212730 |doi= }}
*{{cite journal | author=Saitou M, Ando-Akatsuka Y, Itoh M, ''et al.'' |title=Mammalian occludin in epithelial cells: its expression and subcellular distribution. |journal=Eur. J. Cell Biol. |volume=73 |issue= 3 |pages= 222-31 |year= 1997 |pmid= 9243183 |doi= }}
*{{cite journal | author=Haskins J, Gu L, Wittchen ES, ''et al.'' |title=ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin. |journal=J. Cell Biol. |volume=141 |issue= 1 |pages= 199-208 |year= 1998 |pmid= 9531559 |doi= }}
*{{cite journal | author=Fanning AS, Jameson BJ, Jesaitis LA, Anderson JM |title=The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton. |journal=J. Biol. Chem. |volume=273 |issue= 45 |pages= 29745-53 |year= 1998 |pmid= 9792688 |doi= }}
*{{cite journal | author=Itoh M, Morita K, Tsukita S |title=Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin. |journal=J. Biol. Chem. |volume=274 |issue= 9 |pages= 5981-6 |year= 1999 |pmid= 10026224 |doi= }}
*{{cite journal | author=Jiang WG, Martin TA, Matsumoto K, ''et al.'' |title=Hepatocyte growth factor/scatter factor decreases the expression of occludin and transendothelial resistance (TER) and increases paracellular permeability in human vascular endothelial cells. |journal=J. Cell. Physiol. |volume=181 |issue= 2 |pages= 319-29 |year= 1999 |pmid= 10497311 |doi= 10.1002/(SICI)1097-4652(199911)181:2<319::AID-JCP14>3.0.CO;2-S }}
*{{cite journal | author=Wittchen ES, Haskins J, Stevenson BR |title=Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3. |journal=J. Biol. Chem. |volume=274 |issue= 49 |pages= 35179-85 |year= 2000 |pmid= 10575001 |doi= }}
*{{cite journal | author=Kojima T, Sawada N, Chiba H, ''et al.'' |title=Induction of tight junctions in human connexin 32 (hCx32)-transfected mouse hepatocytes: connexin 32 interacts with occludin. |journal=Biochem. Biophys. Res. Commun. |volume=266 |issue= 1 |pages= 222-9 |year= 2000 |pmid= 10581193 |doi= 10.1006/bbrc.1999.1778 }}
*{{cite journal | author=Burns AR, Bowden RA, MacDonell SD, ''et al.'' |title=Analysis of tight junctions during neutrophil transendothelial migration. |journal=J. Cell. Sci. |volume=113 ( Pt 1) |issue= |pages= 45-57 |year= 2000 |pmid= 10591624 |doi= }}
*{{cite journal | author=Itoh M, Furuse M, Morita K, ''et al.'' |title=Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. |journal=J. Cell Biol. |volume=147 |issue= 6 |pages= 1351-63 |year= 2000 |pmid= 10601346 |doi= }}
*{{cite journal | author=Singh U, Van Itallie CM, Mitic LL, ''et al.'' |title=CaCo-2 cells treated with Clostridium perfringens enterotoxin form multiple large complex species, one of which contains the tight junction protein occludin. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18407-17 |year= 2000 |pmid= 10749869 |doi= 10.1074/jbc.M001530200 }}
*{{cite journal | author=Marzioni D, Banita M, Felici A, ''et al.'' |title=Expression of ZO-1 and occludin in normal human placenta and in hydatidiform moles. |journal=Mol. Hum. Reprod. |volume=7 |issue= 3 |pages= 279-85 |year= 2001 |pmid= 11228248 |doi= }}
*{{cite journal | author=Andreeva AY, Krause E, Müller EC, ''et al.'' |title=Protein kinase C regulates the phosphorylation and cellular localization of occludin. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 38480-6 |year= 2001 |pmid= 11502742 |doi= 10.1074/jbc.M104923200 }}
*{{cite journal | author=Papadopoulos MC, Saadoun S, Woodrow CJ, ''et al.'' |title=Occludin expression in microvessels of neoplastic and non-neoplastic human brain. |journal=Neuropathol. Appl. Neurobiol. |volume=27 |issue= 5 |pages= 384-95 |year= 2001 |pmid= 11679090 |doi= }}
*{{cite journal | author=Schmidt A, Utepbergenov DI, Krause G, Blasig IE |title=Use of surface plasmon resonance for real-time analysis of the interaction of ZO-1 and occludin. |journal=Biochem. Biophys. Res. Commun. |volume=288 |issue= 5 |pages= 1194-9 |year= 2001 |pmid= 11700038 |doi= 10.1006/bbrc.2001.5914 }}
*{{cite journal | author=Pummi K, Malminen M, Aho H, ''et al.'' |title=Epidermal tight junctions: ZO-1 and occludin are expressed in mature, developing, and affected skin and in vitro differentiating keratinocytes. |journal=J. Invest. Dermatol. |volume=117 |issue= 5 |pages= 1050-8 |year= 2001 |pmid= 11710912 |doi= 10.1046/j.0022-202x.2001.01493.x }}
*{{cite journal | author=Traweger A, Fang D, Liu YC, ''et al.'' |title=The tight junction-specific protein occludin is a functional target of the E3 ubiquitin-protein ligase itch. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10201-8 |year= 2002 |pmid= 11782481 |doi= 10.1074/jbc.M111384200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PKN1... {November 16, 2007 4:15:11 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:15:48 PM PST}
<!-- 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
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PKN1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cxz.
| PDB = {{PDB2|1cxz}}, {{PDB2|1urf}}
| Name = Protein kinase N1
| HGNCid = 9405
| Symbol = PKN1
| AltSymbols =; PAK1; DBK; MGC46204; PKN; PRK1; PRKCL1
| OMIM = 601032
| ECnumber =
| Homologene = 48130
| MGIid = 108022
| GeneAtlas_image1 = PBB_GE_PKN1_202161_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase 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}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007257 |text = activation of JNK activity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5585
| Hs_Ensembl = ENSG00000123143
| Hs_RefseqProtein = NP_002732
| Hs_RefseqmRNA = NM_002741
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 14405135
| Hs_GenLoc_end = 14443678
| Hs_Uniprot = Q16512
| Mm_EntrezGene = 320795
| Mm_Ensembl = ENSMUSG00000057672
| Mm_RefseqmRNA = NM_177262
| Mm_RefseqProtein = NP_796236
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 86560199
| Mm_GenLoc_end = 86589231
| Mm_Uniprot = P70268
}}
}}
'''Protein kinase N1''', also known as '''PKN1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PKN1 protein kinase N1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5585| accessdate = }}</ref>
<!-- 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 belongs to the protein kinase C superfamily. This kinase is activated by Rho family of small G proteins and may mediate the Rho-dependent signaling pathway. This kinase can be activated by phospholipids and by limited proteolysis. The 3-phosphoinositide dependent protein kinase-1 (PDPK1/PDK1) is reported to phosphorylate this kinase, which may mediate insulin signals to the actin cytoskeleton. The proteolytic activation of this kinase by caspase-3 or related proteases during apoptosis suggests its role in signal transduction related to apoptosis. Alternatively spliced transcript variants encoding distinct isoforms have been observed.<ref name="entrez">{{cite web | title = Entrez Gene: PKN1 protein kinase N1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5585| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Palmer RH, Ridden J, Parker PJ |title=Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family. |journal=Eur. J. Biochem. |volume=227 |issue= 1-2 |pages= 344-51 |year= 1995 |pmid= 7851406 |doi= }}
*{{cite journal | author=Chu W, Presky DH, Danho W, ''et al.'' |title=Identification and characterization of DBK, a novel putative serine/threonine protein kinase from human endothelial cells. |journal=Eur. J. Biochem. |volume=225 |issue= 2 |pages= 695-702 |year= 1994 |pmid= 7957185 |doi= }}
*{{cite journal | author=Palmer RH, Ridden J, Parker PJ |title=Identification of multiple, novel, protein kinase C-related gene products. |journal=FEBS Lett. |volume=356 |issue= 1 |pages= 5-8 |year= 1995 |pmid= 7988719 |doi= }}
*{{cite journal | author=Mukai H, Ono Y |title=A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C. |journal=Biochem. Biophys. Res. Commun. |volume=199 |issue= 2 |pages= 897-904 |year= 1994 |pmid= 8135837 |doi= 10.1006/bbrc.1994.1313 }}
*{{cite journal | author=Palmer RH, Schönwasser DC, Rahman D, ''et al.'' |title=PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |journal=FEBS Lett. |volume=378 |issue= 3 |pages= 281-5 |year= 1996 |pmid= 8557118 |doi= }}
*{{cite journal | author=Amano M, Mukai H, Ono Y, ''et al.'' |title=Identification of a putative target for Rho as the serine-threonine kinase protein kinase N. |journal=Science |volume=271 |issue= 5249 |pages= 648-50 |year= 1996 |pmid= 8571127 |doi= }}
*{{cite journal | author=Mukai H, Toshimori M, Shibata H, ''et al.'' |title=PKN associates and phosphorylates the head-rod domain of neurofilament protein. |journal=J. Biol. Chem. |volume=271 |issue= 16 |pages= 9816-22 |year= 1996 |pmid= 8621664 |doi= }}
*{{cite journal | author=Brown JL, Stowers L, Baer M, ''et al.'' |title=Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway. |journal=Curr. Biol. |volume=6 |issue= 5 |pages= 598-605 |year= 1997 |pmid= 8805275 |doi= }}
*{{cite journal | author=Mukai H, Miyahara M, Sunakawa H, ''et al.'' |title=Translocation of PKN from the cytosol to the nucleus induced by stresses. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 19 |pages= 10195-9 |year= 1996 |pmid= 8816775 |doi= }}
*{{cite journal | author=Mukai H, Toshimori M, Shibata H, ''et al.'' |title=Interaction of PKN with alpha-actinin. |journal=J. Biol. Chem. |volume=272 |issue= 8 |pages= 4740-6 |year= 1997 |pmid= 9030526 |doi= }}
*{{cite journal | author=Matsuzawa K, Kosako H, Inagaki N, ''et al.'' |title=Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN. |journal=Biochem. Biophys. Res. Commun. |volume=234 |issue= 3 |pages= 621-5 |year= 1997 |pmid= 9175763 |doi= 10.1006/bbrc.1997.6669 }}
*{{cite journal | author=Goedert M, Hasegawa M, Jakes R, ''et al.'' |title=Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases. |journal=FEBS Lett. |volume=409 |issue= 1 |pages= 57-62 |year= 1997 |pmid= 9199504 |doi= }}
*{{cite journal | author=Flynn P, Mellor H, Palmer R, ''et al.'' |title=Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif. |journal=J. Biol. Chem. |volume=273 |issue= 5 |pages= 2698-705 |year= 1998 |pmid= 9446575 |doi= }}
*{{cite journal | author=Bekri S, Adélaïde J, Merscher S, ''et al.'' |title=Detailed map of a region commonly amplified at 11q13-->q14 in human breast carcinoma. |journal=Cytogenet. Cell Genet. |volume=79 |issue= 1-2 |pages= 125-31 |year= 1998 |pmid= 9533029 |doi= }}
*{{cite journal | author=Zheng-Fischhöfer Q, Biernat J, Mandelkow EM, ''et al.'' |title=Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation. |journal=Eur. J. Biochem. |volume=252 |issue= 3 |pages= 542-52 |year= 1998 |pmid= 9546672 |doi= }}
*{{cite journal | author=Bartsch JW, Mukai H, Takahashi N, ''et al.'' |title=The protein kinase N (PKN) gene PRKCL1/Prkcl1 maps to human chromosome 19p12-p13.1 and mouse chromosome 8 with close linkage to the myodystrophy (myd) mutation. |journal=Genomics |volume=49 |issue= 1 |pages= 129-32 |year= 1998 |pmid= 9570957 |doi= 10.1006/geno.1997.5208 }}
*{{cite journal | author=Takanaga H, Mukai H, Shibata H, ''et al.'' |title=PKN interacts with a paraneoplastic cerebellar degeneration-associated antigen, which is a potential transcription factor. |journal=Exp. Cell Res. |volume=241 |issue= 2 |pages= 363-72 |year= 1998 |pmid= 9637778 |doi= 10.1006/excr.1998.4060 }}
*{{cite journal | author=Takahashi M, Mukai H, Toshimori M, ''et al.'' |title=Proteolytic activation of PKN by caspase-3 or related protease during apoptosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 20 |pages= 11566-71 |year= 1998 |pmid= 9751706 |doi= }}
*{{cite journal | author=Hanger DP, Betts JC, Loviny TL, ''et al.'' |title=New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. |journal=J. Neurochem. |volume=71 |issue= 6 |pages= 2465-76 |year= 1998 |pmid= 9832145 |doi= }}
*{{cite journal | author=Takahashi M, Shibata H, Shimakawa M, ''et al.'' |title=Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the golgi apparatus. |journal=J. Biol. Chem. |volume=274 |issue= 24 |pages= 17267-74 |year= 1999 |pmid= 10358086 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RTN4... {November 16, 2007 4:18:11 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:19:00 PM PST}
<!-- 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
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_RTN4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2g31.
| PDB = {{PDB2|2g31}}
| Name = Reticulon 4
| HGNCid = 14085
| Symbol = RTN4
| AltSymbols =; NSP; ASY; NI220/250; NOGO; NOGO-A; NSP-CL; Nbla00271; Nbla10545; RTN-X; RTN4-A; RTN4-B1; RTN4-B2; RTN4-C
| OMIM = 604475
| ECnumber =
| Homologene = 10743
| MGIid = 1915835
| GeneAtlas_image1 = PBB_GE_RTN4_211509_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_RTN4_210968_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_RTN4_214629_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005635 |text = nuclear envelope}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030176 |text = integral to endoplasmic reticulum membrane}}
| Process = {{GNF_GO|id=GO:0019987 |text = negative regulation of anti-apoptosis}} {{GNF_GO|id=GO:0030517 |text = negative regulation of axon extension}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 57142
| Hs_Ensembl = ENSG00000115310
| Hs_RefseqProtein = NP_008939
| Hs_RefseqmRNA = NM_007008
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 55052829
| Hs_GenLoc_end = 55131468
| Hs_Uniprot = Q9NQC3
| Mm_EntrezGene = 68585
| Mm_Ensembl = ENSMUSG00000020458
| Mm_RefseqmRNA = NM_024226
| Mm_RefseqProtein = NP_077188
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 29592947
| Mm_GenLoc_end = 29644255
| Mm_Uniprot = Q99P72
}}
}}
'''Reticulon 4''', also known as '''RTN4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RTN4 reticulon 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57142| accessdate = }}</ref>
<!-- 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 belongs to the family of reticulon encoding genes. Reticulons are associated with the endoplasmic reticulum, and are involved in neuroendocrine secretion or in membrane trafficking in neuroendocrine cells. The product of this gene is a potent neurite outgrowth inhibitor which may also help block the regeneration of the central nervous system in higher vertebrates. Alternatively spliced transcript variants derived both from differential splicing and differential promoter usage and encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: RTN4 reticulon 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57142| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ng CE, Tang BL |title=Nogos and the Nogo-66 receptor: factors inhibiting CNS neuron regeneration. |journal=J. Neurosci. Res. |volume=67 |issue= 5 |pages= 559-65 |year= 2002 |pmid= 11891768 |doi= }}
*{{cite journal | author=Watari A, Yutsudo M |title=Multi-functional gene ASY/Nogo/RTN-X/RTN4: apoptosis, tumor suppression, and inhibition of neuronal regeneration. |journal=Apoptosis |volume=8 |issue= 1 |pages= 5-9 |year= 2003 |pmid= 12510146 |doi= }}
*{{cite journal | author=Schweigreiter R, Bandtlow CE |title=Nogo in the injured spinal cord. |journal=J. Neurotrauma |volume=23 |issue= 3-4 |pages= 384-96 |year= 2006 |pmid= 16629624 |doi= 10.1089/neu.2006.23.384 }}
*{{cite journal | author=Nagase T, Ishikawa K, Suyama M, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=5 |issue= 6 |pages= 355-64 |year= 1999 |pmid= 10048485 |doi= }}
*{{cite journal | author=Prinjha R, Moore SE, Vinson M, ''et al.'' |title=Inhibitor of neurite outgrowth in humans. |journal=Nature |volume=403 |issue= 6768 |pages= 383-4 |year= 2000 |pmid= 10667780 |doi= 10.1038/35000287 }}
*{{cite journal | author=Chen MS, Huber AB, van der Haar ME, ''et al.'' |title=Nogo-A is a myelin-associated neurite outgrowth inhibitor and an antigen for monoclonal antibody IN-1. |journal=Nature |volume=403 |issue= 6768 |pages= 434-9 |year= 2000 |pmid= 10667796 |doi= 10.1038/35000219 }}
*{{cite journal | author=GrandPré T, Nakamura F, Vartanian T, Strittmatter SM |title=Identification of the Nogo inhibitor of axon regeneration as a Reticulon protein. |journal=Nature |volume=403 |issue= 6768 |pages= 439-44 |year= 2000 |pmid= 10667797 |doi= 10.1038/35000226 }}
*{{cite journal | author=Yang J, Yu L, Bi AD, Zhao SY |title=Assignment of the human reticulon 4 gene (RTN4) to chromosome 2p14-->2p13 by radiation hybrid mapping. |journal=Cytogenet. Cell Genet. |volume=88 |issue= 1-2 |pages= 101-2 |year= 2000 |pmid= 10773680 |doi= }}
*{{cite journal | author=Zhang QH, Ye M, Wu XY, ''et al.'' |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546-60 |year= 2001 |pmid= 11042152 |doi= }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Tagami S, Eguchi Y, Kinoshita M, ''et al.'' |title=A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity. |journal=Oncogene |volume=19 |issue= 50 |pages= 5736-46 |year= 2001 |pmid= 11126360 |doi= 10.1038/sj.onc.1203948 }}
*{{cite journal | author=Fournier AE, GrandPre T, Strittmatter SM |title=Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration. |journal=Nature |volume=409 |issue= 6818 |pages= 341-6 |year= 2001 |pmid= 11201742 |doi= 10.1038/35053072 }}
*{{cite journal | author=Josephson A, Widenfalk J, Widmer HW, ''et al.'' |title=NOGO mRNA expression in adult and fetal human and rat nervous tissue and in weight drop injury. |journal=Exp. Neurol. |volume=169 |issue= 2 |pages= 319-28 |year= 2001 |pmid= 11358445 |doi= 10.1006/exnr.2001.7659 }}
*{{cite journal | author=Zhou ZM, Sha JH, Li JM, ''et al.'' |title=Expression of a novel reticulon-like gene in human testis. |journal=Reproduction |volume=123 |issue= 2 |pages= 227-34 |year= 2002 |pmid= 11866689 |doi= }}
*{{cite journal | author=GrandPré T, Li S, Strittmatter SM |title=Nogo-66 receptor antagonist peptide promotes axonal regeneration. |journal=Nature |volume=417 |issue= 6888 |pages= 547-51 |year= 2002 |pmid= 12037567 |doi= 10.1038/417547a }}
*{{cite journal | author=Hu WH, Hausmann ON, Yan MS, ''et al.'' |title=Identification and characterization of a novel Nogo-interacting mitochondrial protein (NIMP). |journal=J. Neurochem. |volume=81 |issue= 1 |pages= 36-45 |year= 2002 |pmid= 12067236 |doi= }}
*{{cite journal | author=Liu BP, Fournier A, GrandPré T, Strittmatter SM |title=Myelin-associated glycoprotein as a functional ligand for the Nogo-66 receptor. |journal=Science |volume=297 |issue= 5584 |pages= 1190-3 |year= 2002 |pmid= 12089450 |doi= 10.1126/science.1073031 }}
*{{cite journal | author=Dupuis L, Gonzalez de Aguilar JL, di Scala F, ''et al.'' |title=Nogo provides a molecular marker for diagnosis of amyotrophic lateral sclerosis. |journal=Neurobiol. Dis. |volume=10 |issue= 3 |pages= 358-65 |year= 2002 |pmid= 12270696 |doi= }}
*{{cite journal | author=Taketomi M, Kinoshita N, Kimura K, ''et al.'' |title=Nogo-A expression in mature oligodendrocytes of rat spinal cord in association with specific molecules. |journal=Neurosci. Lett. |volume=332 |issue= 1 |pages= 37-40 |year= 2002 |pmid= 12377379 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TGM1... {November 16, 2007 4:15:48 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:16:24 PM PST}
<!-- 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
}}
<!-- 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 = Transglutaminase 1 (K polypeptide epidermal type I, protein-glutamine-gamma-glutamyltransferase)
| HGNCid = 11777
| Symbol = TGM1
| AltSymbols =; ICR2; KTG; LI; LI1; TGASE; TGK
| OMIM = 190195
| ECnumber =
| Homologene = 306
| MGIid = 98730
| GeneAtlas_image1 = PBB_GE_TGM1_206008_at_tn.png
| Function = {{GNF_GO|id=GO:0003810 |text = protein-glutamine gamma-glutamyltransferase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008415 |text = acyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0001533 |text = cornified envelope}} {{GNF_GO|id=GO:0005913 |text = cell-cell adherens junction}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0031224 |text = intrinsic to membrane}}
| Process = {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0018149 |text = peptide cross-linking}} {{GNF_GO|id=GO:0030216 |text = keratinocyte differentiation}} {{GNF_GO|id=GO:0031424 |text = keratinization}} {{GNF_GO|id=GO:0043163 |text = cell envelope organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7051
| Hs_Ensembl = ENSG00000092295
| Hs_RefseqProtein = NP_000350
| Hs_RefseqmRNA = NM_000359
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 23788162
| Hs_GenLoc_end = 23802217
| Hs_Uniprot = P22735
| Mm_EntrezGene = 21816
| Mm_Ensembl = ENSMUSG00000022218
| Mm_RefseqmRNA = NM_019984
| Mm_RefseqProtein = NP_064368
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 54654090
| Mm_GenLoc_end = 54667546
| Mm_Uniprot = Q9JLF6
}}
}}
'''Transglutaminase 1 (K polypeptide epidermal type I, protein-glutamine-gamma-glutamyltransferase)''', also known as '''TGM1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TGM1 transglutaminase 1 (K polypeptide epidermal type I, protein-glutamine-gamma-glutamyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7051| accessdate = }}</ref>
<!-- 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 membrane protein that catalyzes the addition of an alkyl group from an akylamine to a glutamine residue of a protein, forming an alkylglutamine in the protein. This protein alkylation leads to crosslinking of proteins and catenation of polyamines to proteins. This gene contains either one or two copies of a 22 nt repeat unit in its 3' UTR. Mutations in this gene have been associated with autosomal recessive lamellar ichthyosis (LI) and nonbullous congenital ichthyosiform erythroderma (NCIE).<ref name="entrez">{{cite web | title = Entrez Gene: TGM1 transglutaminase 1 (K polypeptide epidermal type I, protein-glutamine-gamma-glutamyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7051| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Phillips MA, Stewart BE, Rice RH |title=Genomic structure of keratinocyte transglutaminase. Recruitment of new exon for modified function. |journal=J. Biol. Chem. |volume=267 |issue= 4 |pages= 2282-6 |year= 1992 |pmid= 1346394 |doi= }}
*{{cite journal | author=Kim IG, McBride OW, Wang M, ''et al.'' |title=Structure and organization of the human transglutaminase 1 gene. |journal=J. Biol. Chem. |volume=267 |issue= 11 |pages= 7710-7 |year= 1992 |pmid= 1348508 |doi= }}
*{{cite journal | author=Polakowska RR, Eickbush T, Falciano V, ''et al.'' |title=Organization and evolution of the human epidermal keratinocyte transglutaminase I gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 10 |pages= 4476-80 |year= 1992 |pmid= 1350092 |doi= }}
*{{cite journal | author=Schroeder WT, Thacher SM, Stewart-Galetka S, ''et al.'' |title=Type I keratinocyte transglutaminase: expression in human skin and psoriasis. |journal=J. Invest. Dermatol. |volume=99 |issue= 1 |pages= 27-34 |year= 1992 |pmid= 1351505 |doi= }}
*{{cite journal | author=Yamanishi K, Inazawa J, Liew FM, ''et al.'' |title=Structure of the gene for human transglutaminase 1. |journal=J. Biol. Chem. |volume=267 |issue= 25 |pages= 17858-63 |year= 1992 |pmid= 1381356 |doi= }}
*{{cite journal | author=Kim HC, Idler WW, Kim IG, ''et al.'' |title=The complete amino acid sequence of the human transglutaminase K enzyme deduced from the nucleic acid sequences of cDNA clones. |journal=J. Biol. Chem. |volume=266 |issue= 1 |pages= 536-9 |year= 1991 |pmid= 1670769 |doi= }}
*{{cite journal | author=Yamanishi K, Liew FM, Konishi K, ''et al.'' |title=Molecular cloning of human epidermal transglutaminase cDNA from keratinocytes in culture. |journal=Biochem. Biophys. Res. Commun. |volume=175 |issue= 3 |pages= 906-13 |year= 1991 |pmid= 1673840 |doi= }}
*{{cite journal | author=Polakowska R, Herting E, Goldsmith LA |title=Isolation of cDNA for human epidermal type I transglutaminase. |journal=J. Invest. Dermatol. |volume=96 |issue= 2 |pages= 285-8 |year= 1991 |pmid= 1704039 |doi= }}
*{{cite journal | author=Phillips MA, Stewart BE, Qin Q, ''et al.'' |title=Primary structure of keratinocyte transglutaminase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 23 |pages= 9333-7 |year= 1991 |pmid= 1979171 |doi= }}
*{{cite journal | author=Candi E, Melino G, Mei G, ''et al.'' |title=Biochemical, structural, and transglutaminase substrate properties of human loricrin, the major epidermal cornified cell envelope protein. |journal=J. Biol. Chem. |volume=270 |issue= 44 |pages= 26382-90 |year= 1995 |pmid= 7592852 |doi= }}
*{{cite journal | author=Mariniello L, Esposito C, Di Pierro P, ''et al.'' |title=Human-immunodeficiency-virus transmembrane glycoprotein gp41 is an amino acceptor and donor substrate for transglutaminase in vitro. |journal=Eur. J. Biochem. |volume=215 |issue= 1 |pages= 99-104 |year= 1993 |pmid= 7688299 |doi= }}
*{{cite journal | author=Russell LJ, DiGiovanna JJ, Rogers GR, ''et al.'' |title=Mutations in the gene for transglutaminase 1 in autosomal recessive lamellar ichthyosis. |journal=Nat. Genet. |volume=9 |issue= 3 |pages= 279-83 |year= 1995 |pmid= 7773290 |doi= 10.1038/ng0395-279 }}
*{{cite journal | author=Huber M, Rettler I, Bernasconi K, ''et al.'' |title=Mutations of keratinocyte transglutaminase in lamellar ichthyosis. |journal=Science |volume=267 |issue= 5197 |pages= 525-8 |year= 1995 |pmid= 7824952 |doi= }}
*{{cite journal | author=Amendola A, Lombardi G, Oliverio S, ''et al.'' |title=HIV-1 gp120-dependent induction of apoptosis in antigen-specific human T cell clones is characterized by 'tissue' transglutaminase expression and prevented by cyclosporin A. |journal=FEBS Lett. |volume=339 |issue= 3 |pages= 258-64 |year= 1994 |pmid= 7906657 |doi= }}
*{{cite journal | author=Kim SY, Kim IG, Chung SI, Steinert PM |title=The structure of the transglutaminase 1 enzyme. Deletion cloning reveals domains that regulate its specific activity and substrate specificity. |journal=J. Biol. Chem. |volume=269 |issue= 45 |pages= 27979-86 |year= 1994 |pmid= 7961731 |doi= }}
*{{cite journal | author=Steinert PM, Kim SY, Chung SI, Marekov LN |title=The transglutaminase 1 enzyme is variably acylated by myristate and palmitate during differentiation in epidermal keratinocytes. |journal=J. Biol. Chem. |volume=271 |issue= 42 |pages= 26242-50 |year= 1996 |pmid= 8824274 |doi= }}
*{{cite journal | author=Laiho E, Ignatius J, Mikkola H, ''et al.'' |title=Transglutaminase 1 mutations in autosomal recessive congenital ichthyosis: private and recurrent mutations in an isolated population. |journal=Am. J. Hum. Genet. |volume=61 |issue= 3 |pages= 529-38 |year= 1997 |pmid= 9326318 |doi= }}
*{{cite journal | author=Tarcsa E, Marekov LN, Andreoli J, ''et al.'' |title=The fate of trichohyalin. Sequential post-translational modifications by peptidyl-arginine deiminase and transglutaminases. |journal=J. Biol. Chem. |volume=272 |issue= 44 |pages= 27893-901 |year= 1997 |pmid= 9346937 |doi= }}
*{{cite journal | author=Petit E, Huber M, Rochat A, ''et al.'' |title=Three novel point mutations in the keratinocyte transglutaminase (TGK) gene in lamellar ichthyosis: significance for mutant transcript level, TGK immunodetection and activity. |journal=Eur. J. Hum. Genet. |volume=5 |issue= 4 |pages= 218-28 |year= 1998 |pmid= 9359043 |doi= }}
*{{cite journal | author=Iwasaki W, Nagata K, Hatanaka H, ''et al.'' |title=Solution structure of midkine, a new heparin-binding growth factor. |journal=EMBO J. |volume=16 |issue= 23 |pages= 6936-46 |year= 1998 |pmid= 9384573 |doi= 10.1093/emboj/16.23.6936 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TPMT... {November 16, 2007 4:16:24 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:16:46 PM PST}
<!-- 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
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_TPMT_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2bzg.
| PDB = {{PDB2|2bzg}}, {{PDB2|2h11}}
| Name = Thiopurine S-methyltransferase
| HGNCid = 12014
| Symbol = TPMT
| AltSymbols =;
| OMIM = 187680
| ECnumber =
| Homologene = 313
| MGIid = 98812
| GeneAtlas_image1 = PBB_GE_TPMT_203671_at_tn.png
| GeneAtlas_image2 = PBB_GE_TPMT_203672_x_at_tn.png
| Function = {{GNF_GO|id=GO:0008119 |text = thiopurine S-methyltransferase activity}} {{GNF_GO|id=GO:0008168 |text = methyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006139 |text = nucleobase, nucleoside, nucleotide and nucleic acid metabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7172
| Hs_Ensembl = ENSG00000137364
| Hs_RefseqProtein = NP_000358
| Hs_RefseqmRNA = NM_000367
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 18236526
| Hs_GenLoc_end = 18263353
| Hs_Uniprot = P51580
| Mm_EntrezGene = 22017
| Mm_Ensembl = ENSMUSG00000021376
| Mm_RefseqmRNA = NM_016785
| Mm_RefseqProtein = NP_058065
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 47036149
| Mm_GenLoc_end = 47054175
| Mm_Uniprot = O55060
}}
}}
'''Thiopurine S-methyltransferase''', also known as '''TPMT''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TPMT thiopurine S-methyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7172| accessdate = }}</ref>
<!-- 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 the enzyme that metabolizes thiopurine drugs via S-adenosyl-L-methionine as the S-methyl donor and S-adenosyl-L-homocysteine as a byproduct. Thiopurine drugs such as 6-mercaptopurine are used as chemotherapeutic agents. Genetic polymorphisms that affect this enzymatic activity are correlated with variations in sensitivity and toxicity to such drugs within individuals. A pseudogene for this locus is located on chromosome 18q.<ref name="entrez">{{cite web | title = Entrez Gene: TPMT thiopurine S-methyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7172| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Krynetski EY, Tai HL, Yates CR, ''et al.'' |title=Genetic polymorphism of thiopurine S-methyltransferase: clinical importance and molecular mechanisms. |journal=Pharmacogenetics |volume=6 |issue= 4 |pages= 279-90 |year= 1997 |pmid= 8873214 |doi= }}
*{{cite journal | author=Krynetski E, Evans WE |title=Drug methylation in cancer therapy: lessons from the TPMT polymorphism. |journal=Oncogene |volume=22 |issue= 47 |pages= 7403-13 |year= 2003 |pmid= 14576848 |doi= 10.1038/sj.onc.1206944 }}
*{{cite journal | author=Corominas H, Baiget M |title=Clinical utility of thiopurine S-methyltransferase genotyping. |journal=American journal of pharmacogenomics : genomics-related research in drug development and clinical practice |volume=4 |issue= 1 |pages= 1-8 |year= 2004 |pmid= 14987117 |doi= }}
*{{cite journal | author=Krynetskiy EY, Evans WE |title=Closing the gap between science and clinical practice: the thiopurine S-methyltransferase polymorphism moves forward. |journal=Pharmacogenetics |volume=14 |issue= 7 |pages= 395-6 |year= 2005 |pmid= 15226671 |doi= }}
*{{cite journal | author=Coulthard SA, Matheson EC, Hall AG, Hogarth LA |title=The clinical impact of thiopurine methyltransferase polymorphisms on thiopurine treatment. |journal=Nucleosides Nucleotides Nucleic Acids |volume=23 |issue= 8-9 |pages= 1385-91 |year= 2005 |pmid= 15571264 |doi= }}
*{{cite journal | author=Lee W, Lockhart AC, Kim RB, Rothenberg ML |title=Cancer pharmacogenomics: powerful tools in cancer chemotherapy and drug development. |journal=Oncologist |volume=10 |issue= 2 |pages= 104-11 |year= 2005 |pmid= 15709212 |doi= 10.1634/theoncologist.10-2-104 }}
*{{cite journal | author=Pierik M, Rutgeerts P, Vlietinck R, Vermeire S |title=Pharmacogenetics in inflammatory bowel disease. |journal=World J. Gastroenterol. |volume=12 |issue= 23 |pages= 3657-67 |year= 2006 |pmid= 16773681 |doi= }}
*{{cite journal | author=Lee D, Szumlanski C, Houtman J, ''et al.'' |title=Thiopurine methyltransferase pharmacogenetics. Cloning of human liver cDNA and a processed pseudogene on human chromosome 18q21.1. |journal=Drug Metab. Dispos. |volume=23 |issue= 3 |pages= 398-405 |year= 1995 |pmid= 7628307 |doi= }}
*{{cite journal | author=Krynetski EY, Schuetz JD, Galpin AJ, ''et al.'' |title=A single point mutation leading to loss of catalytic activity in human thiopurine S-methyltransferase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 4 |pages= 949-53 |year= 1995 |pmid= 7862671 |doi= }}
*{{cite journal | author=Honchel R, Aksoy IA, Szumlanski C, ''et al.'' |title=Human thiopurine methyltransferase: molecular cloning and expression of T84 colon carcinoma cell cDNA. |journal=Mol. Pharmacol. |volume=43 |issue= 6 |pages= 878-87 |year= 1993 |pmid= 8316220 |doi= }}
*{{cite journal | author=Glauser TA, Nelson AN, Zembower DE, ''et al.'' |title=Diethyldithiocarbamate S-methylation: evidence for catalysis by human liver thiol methyltransferase and thiopurine methyltransferase. |journal=J. Pharmacol. Exp. Ther. |volume=266 |issue= 1 |pages= 23-32 |year= 1993 |pmid= 8392551 |doi= }}
*{{cite journal | author=Szumlanski C, Otterness D, Her C, ''et al.'' |title=Thiopurine methyltransferase pharmacogenetics: human gene cloning and characterization of a common polymorphism. |journal=DNA Cell Biol. |volume=15 |issue= 1 |pages= 17-30 |year= 1996 |pmid= 8561894 |doi= }}
*{{cite journal | author=Tai HL, Krynetski EY, Yates CR, ''et al.'' |title=Thiopurine S-methyltransferase deficiency: two nucleotide transitions define the most prevalent mutant allele associated with loss of catalytic activity in Caucasians. |journal=Am. J. Hum. Genet. |volume=58 |issue= 4 |pages= 694-702 |year= 1996 |pmid= 8644731 |doi= }}
*{{cite journal | author=Yates CR, Krynetski EY, Loennechen T, ''et al.'' |title=Molecular diagnosis of thiopurine S-methyltransferase deficiency: genetic basis for azathioprine and mercaptopurine intolerance. |journal=Ann. Intern. Med. |volume=126 |issue= 8 |pages= 608-14 |year= 1997 |pmid= 9103127 |doi= }}
*{{cite journal | author=Tai HL, Krynetski EY, Schuetz EG, ''et al.'' |title=Enhanced proteolysis of thiopurine S-methyltransferase (TPMT) encoded by mutant alleles in humans (TPMT*3A, TPMT*2): mechanisms for the genetic polymorphism of TPMT activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 12 |pages= 6444-9 |year= 1997 |pmid= 9177237 |doi= }}
*{{cite journal | author=Otterness D, Szumlanski C, Lennard L, ''et al.'' |title=Human thiopurine methyltransferase pharmacogenetics: gene sequence polymorphisms. |journal=Clin. Pharmacol. Ther. |volume=62 |issue= 1 |pages= 60-73 |year= 1997 |pmid= 9246020 |doi= 10.1016/S0009-9236(97)90152-1 }}
*{{cite journal | author=Leipold G, Schütz E, Haas JP, Oellerich M |title=Azathioprine-induced severe pancytopenia due to a homozygous two-point mutation of the thiopurine methyltransferase gene in a patient with juvenile HLA-B27-associated spondylarthritis. |journal=Arthritis Rheum. |volume=40 |issue= 10 |pages= 1896-8 |year= 1997 |pmid= 9336428 |doi= 10.1002/1529-0131(199710)40:10<1896::AID-ART26>3.0.CO;2-A }}
*{{cite journal | author=Krynetski EY, Fessing MY, Yates CR, ''et al.'' |title=Promoter and intronic sequences of the human thiopurine S-methyltransferase (TPMT) gene isolated from a human PAC1 genomic library. |journal=Pharm. Res. |volume=14 |issue= 12 |pages= 1672-8 |year= 1998 |pmid= 9453052 |doi= }}
*{{cite journal | author=Spire-Vayron de la Moureyre C, Debuysère H, Sabbagh N, ''et al.'' |title=Detection of known and new mutations in the thiopurine S-methyltransferase gene by single-strand conformation polymorphism analysis. |journal=Hum. Mutat. |volume=12 |issue= 3 |pages= 177-85 |year= 1998 |pmid= 9711875 |doi= 10.1002/(SICI)1098-1004(1998)12:3<177::AID-HUMU5>3.0.CO;2-E }}
}}
{{refend}}
{{protein-stub}}
end log.
