Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 22:39, 14 November 2007 (UTC)
[edit]Proteins without matches (9)
[edit]Proteins with a High Potential Match (11)
[edit]Redirected Proteins (5)
[edit]Manual Inspection (Page not found) (20)
[edit]
Protein Status Grid - Date: 22:39, 14 November 2007 (UTC)
[edit]Vebose Log - Date: 22:39, 14 November 2007 (UTC)
[edit]- INFO: Beginning work on ACHE... {November 14, 2007 2:14:19 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:14:54 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ACHE_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b41.
| PDB = {{PDB2|1b41}}, {{PDB2|1f8u}}, {{PDB2|1vzj}}
| Name = Acetylcholinesterase (Yt blood group)
| HGNCid = 108
| Symbol = ACHE
| AltSymbols =; ARACHE; N-ACHE; YT
| OMIM = 100740
| ECnumber =
| Homologene = 543
| MGIid = 87876
| GeneAtlas_image1 = PBB_GE_ACHE_205377_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ACHE_205378_s_at_tn.png
| Function = {{GNF_GO|id=GO:0001540 |text = beta-amyloid binding}} {{GNF_GO|id=GO:0003990 |text = acetylcholinesterase activity}} {{GNF_GO|id=GO:0004104 |text = cholinesterase activity}} {{GNF_GO|id=GO:0004759 |text = carboxylesterase activity}} {{GNF_GO|id=GO:0005518 |text = collagen binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0017171 |text = serine hydrolase activity}} {{GNF_GO|id=GO:0042166 |text = acetylcholine binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0043237 |text = laminin-1 binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005605 |text = basal lamina}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0045202 |text = synapse}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}}
| Process = {{GNF_GO|id=GO:0001507 |text = acetylcholine catabolic process in synaptic cleft}} {{GNF_GO|id=GO:0002076 |text = osteoblast development}} {{GNF_GO|id=GO:0006260 |text = DNA replication}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007416 |text = synaptogenesis}} {{GNF_GO|id=GO:0007517 |text = muscle development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0009611 |text = response to wounding}} {{GNF_GO|id=GO:0032223 |text = negative regulation of synaptic transmission, cholinergic}} {{GNF_GO|id=GO:0042982 |text = amyloid precursor protein metabolic process}} {{GNF_GO|id=GO:0050714 |text = positive regulation of protein secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 43
| Hs_Ensembl = ENSG00000087085
| Hs_RefseqProtein = NP_000656
| Hs_RefseqmRNA = NM_000665
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 100325552
| Hs_GenLoc_end = 100331651
| Hs_Uniprot = P22303
| Mm_EntrezGene = 11423
| Mm_Ensembl = ENSMUSG00000023328
| Mm_RefseqmRNA = NM_009599
| Mm_RefseqProtein = NP_033729
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 137518065
| Mm_GenLoc_end = 137524251
| Mm_Uniprot = Q543Z1
}}
}}
'''Acetylcholinesterase (Yt blood group)''', also known as '''ACHE''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Acetylcholinesterase hydrolyzes the neurotransmitter, acetylcholine at neuromuscular junctions and brain cholinergic synapses, and thus terminates signal transmission. It is also found on the red blood cell membranes, where it constitutes the Yt blood group antigen. Acetylcholinesterase exists in multiple molecular forms which possess similar catalytic properties, but differ in their oligomeric assembly and mode of cell attachment to the cell surface. It is encoded by the single ACHE gene, and the structural diversity in the gene products arises from alternative mRNA splicing, and post-translational associations of catalytic and structural subunits. The major form of acetylcholinesterase found in brain, muscle and other tissues is the hydrophilic species, which forms disulfide-linked oligomers with collagenous, or lipid-containing structural subunits. The other, alternatively spliced form, expressed primarily in the erythroid tissues, differs at the C-terminal end, and contains a cleavable hydrophobic peptide with a GPI-anchor site. It associates with the membranes through the phosphoinositide (PI) moieties added post-translationally.<ref>{{cite web | title = Entrez Gene: ACHE acetylcholinesterase (Yt blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=43| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Silman I, Futerman AH |title=Modes of attachment of acetylcholinesterase to the surface membrane. |journal=Eur. J. Biochem. |volume=170 |issue= 1-2 |pages= 11-22 |year= 1988 |pmid= 3319614 |doi= }}
*{{cite journal | author=Soreq H, Seidman S |title=Acetylcholinesterase--new roles for an old actor. |journal=Nat. Rev. Neurosci. |volume=2 |issue= 4 |pages= 294-302 |year= 2001 |pmid= 11283752 |doi= 10.1038/35067589 }}
*{{cite journal | author=Shen T, Tai K, Henchman RH, McCammon JA |title=Molecular dynamics of acetylcholinesterase. |journal=Acc. Chem. Res. |volume=35 |issue= 6 |pages= 332-40 |year= 2003 |pmid= 12069617 |doi= }}
*{{cite journal | author=Pakaski M, Kasa P |title=Role of acetylcholinesterase inhibitors in the metabolism of amyloid precursor protein. |journal=Current drug targets. CNS and neurological disorders |volume=2 |issue= 3 |pages= 163-71 |year= 2003 |pmid= 12769797 |doi= }}
*{{cite journal | author=Meshorer E, Soreq H |title=Virtues and woes of AChE alternative splicing in stress-related neuropathologies. |journal=Trends Neurosci. |volume=29 |issue= 4 |pages= 216-24 |year= 2006 |pmid= 16516310 |doi= 10.1016/j.tins.2006.02.005 }}
*{{cite journal | author=Ehrlich G, Viegas-Pequignot E, Ginzberg D, ''et al.'' |title=Mapping the human acetylcholinesterase gene to chromosome 7q22 by fluorescent in situ hybridization coupled with selective PCR amplification from a somatic hybrid cell panel and chromosome-sorted DNA libraries. |journal=Genomics |volume=13 |issue= 4 |pages= 1192-7 |year= 1992 |pmid= 1380483 |doi= }}
*{{cite journal | author=Spring FA, Gardner B, Anstee DJ |title=Evidence that the antigens of the Yt blood group system are located on human erythrocyte acetylcholinesterase. |journal=Blood |volume=80 |issue= 8 |pages= 2136-41 |year= 1992 |pmid= 1391965 |doi= }}
*{{cite journal | author=Shafferman A, Kronman C, Flashner Y, ''et al.'' |title=Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding. |journal=J. Biol. Chem. |volume=267 |issue= 25 |pages= 17640-8 |year= 1992 |pmid= 1517212 |doi= }}
*{{cite journal | author=Getman DK, Eubanks JH, Camp S, ''et al.'' |title=The human gene encoding acetylcholinesterase is located on the long arm of chromosome 7. |journal=Am. J. Hum. Genet. |volume=51 |issue= 1 |pages= 170-7 |year= 1992 |pmid= 1609795 |doi= }}
*{{cite journal | author=Li Y, Camp S, Rachinsky TL, ''et al.'' |title=Gene structure of mammalian acetylcholinesterase. Alternative exons dictate tissue-specific expression. |journal=J. Biol. Chem. |volume=266 |issue= 34 |pages= 23083-90 |year= 1992 |pmid= 1744105 |doi= }}
*{{cite journal | author=Velan B, Grosfeld H, Kronman C, ''et al.'' |title=The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580----Ala mutant. |journal=J. Biol. Chem. |volume=266 |issue= 35 |pages= 23977-84 |year= 1992 |pmid= 1748670 |doi= }}
*{{cite journal | author=Soreq H, Ben-Aziz R, Prody CA, ''et al.'' |title=Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 24 |pages= 9688-92 |year= 1991 |pmid= 2263619 |doi= }}
*{{cite journal | author=Chhajlani V, Derr D, Earles B, ''et al.'' |title=Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase. |journal=FEBS Lett. |volume=247 |issue= 2 |pages= 279-82 |year= 1989 |pmid= 2714437 |doi= }}
*{{cite journal | author=Lapidot-Lifson Y, Prody CA, Ginzberg D, ''et al.'' |title=Coamplification of human acetylcholinesterase and butyrylcholinesterase genes in blood cells: correlation with various leukemias and abnormal megakaryocytopoiesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 12 |pages= 4715-9 |year= 1989 |pmid= 2734315 |doi= }}
*{{cite journal | author=Bazelyansky M, Robey E, Kirsch JF |title=Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase. |journal=Biochemistry |volume=25 |issue= 1 |pages= 125-30 |year= 1986 |pmid= 3954986 |doi= }}
*{{cite journal | author=Gaston SM, Marchase RB, Jakoi ER |title=Brain ligatin: a membrane lectin that binds acetylcholinesterase. |journal=J. Cell. Biochem. |volume=18 |issue= 4 |pages= 447-59 |year= 1982 |pmid= 7085778 |doi= 10.1002/jcb.1982.240180406 }}
*{{cite journal | author=Ordentlich A, Barak D, Kronman C, ''et al.'' |title=Contribution of aromatic moieties of tyrosine 133 and of the anionic subsite tryptophan 86 to catalytic efficiency and allosteric modulation of acetylcholinesterase. |journal=J. Biol. Chem. |volume=270 |issue= 5 |pages= 2082-91 |year= 1995 |pmid= 7836436 |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=Ben Aziz-Aloya R, Sternfeld M, Soreq H |title=Promoter elements and alternative splicing in the human ACHE gene. |journal=Prog. Brain Res. |volume=98 |issue= |pages= 147-53 |year= 1994 |pmid= 8248502 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BAK1... {November 14, 2007 2:14:54 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:15:40 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
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_BAK1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ims.
| PDB = {{PDB2|2ims}}, {{PDB2|2imt}}, {{PDB2|2jcn}}
| Name = BCL2-antagonist/killer 1
| HGNCid = 949
| Symbol = BAK1
| AltSymbols =; BAK; BAK-LIKE; BCL2L7; CDN1; MGC117255; MGC3887
| OMIM = 600516
| ECnumber =
| Homologene = 917
| MGIid = 1097161
| GeneAtlas_image1 = PBB_GE_BAK1_203728_at_tn.png
| Function = {{GNF_GO|id=GO:0042802 |text = identical protein binding}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0008637 |text = apoptotic mitochondrial changes}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 578
| Hs_Ensembl = ENSG00000030110
| Hs_RefseqProtein = NP_001179
| Hs_RefseqmRNA = NM_001188
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 33648307
| Hs_GenLoc_end = 33655997
| Hs_Uniprot = Q16611
| Mm_EntrezGene = 12018
| Mm_Ensembl = ENSMUSG00000057789
| Mm_RefseqmRNA = NM_007523
| Mm_RefseqProtein = NP_031549
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 26747399
| Mm_GenLoc_end = 26756216
| Mm_Uniprot = Q8C264
}}
}}
'''BCL2-antagonist/killer 1''', also known as '''BAK1''', is a human [[gene]].
<!-- 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 BCL2 protein family. BCL2 family members form oligomers or heterodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein localizes to mitochondria, and functions to induce apoptosis. It interacts with and accelerates the opening of the mitochondrial voltage-dependent anion channel, which leads to a loss in membrane potential and the release of cytochrome c. This protein also interacts with the tumor suppressor P53 after exposure to cell stress.<ref>{{cite web | title = Entrez Gene: BAK1 BCL2-antagonist/killer 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=578| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Buytaert E, Callewaert G, Vandenheede JR, Agostinis P |title=Deficiency in apoptotic effectors Bax and Bak reveals an autophagic cell death pathway initiated by photodamage to the endoplasmic reticulum. |journal=Autophagy |volume=2 |issue= 3 |pages= 238-40 |year= 2007 |pmid= 16874066 |doi= }}
*{{cite journal | author=Farrow SN, White JH, Martinou I, ''et al.'' |title=Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K. |journal=Nature |volume=374 |issue= 6524 |pages= 731-3 |year= 1995 |pmid= 7715729 |doi= 10.1038/374731a0 }}
*{{cite journal | author=Chittenden T, Harrington EA, O'Connor R, ''et al.'' |title=Induction of apoptosis by the Bcl-2 homologue Bak. |journal=Nature |volume=374 |issue= 6524 |pages= 733-6 |year= 1995 |pmid= 7715730 |doi= 10.1038/374733a0 }}
*{{cite journal | author=Kiefer MC, Brauer MJ, Powers VC, ''et al.'' |title=Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak. |journal=Nature |volume=374 |issue= 6524 |pages= 736-9 |year= 1995 |pmid= 7715731 |doi= 10.1038/374736a0 }}
*{{cite journal | author=Chittenden T, Flemington C, Houghton AB, ''et al.'' |title=A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions. |journal=EMBO J. |volume=14 |issue= 22 |pages= 5589-96 |year= 1996 |pmid= 8521816 |doi= }}
*{{cite journal | author=Sattler M, Liang H, Nettesheim D, ''et al.'' |title=Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis. |journal=Science |volume=275 |issue= 5302 |pages= 983-6 |year= 1997 |pmid= 9020082 |doi= }}
*{{cite journal | author=Diaz JL, Oltersdorf T, Horne W, ''et al.'' |title=A common binding site mediates heterodimerization and homodimerization of Bcl-2 family members. |journal=J. Biol. Chem. |volume=272 |issue= 17 |pages= 11350-5 |year= 1997 |pmid= 9111042 |doi= }}
*{{cite journal | author=Huang DC, Adams JM, Cory S |title=The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4. |journal=EMBO J. |volume=17 |issue= 4 |pages= 1029-39 |year= 1998 |pmid= 9463381 |doi= 10.1093/emboj/17.4.1029 }}
*{{cite journal | author=Herberg JA, Phillips S, Beck S, ''et al.'' |title=Genomic structure and domain organisation of the human Bak gene. |journal=Gene |volume=211 |issue= 1 |pages= 87-94 |year= 1998 |pmid= 9573342 |doi= }}
*{{cite journal | author=Narita M, Shimizu S, Ito T, ''et al.'' |title=Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 25 |pages= 14681-6 |year= 1999 |pmid= 9843949 |doi= }}
*{{cite journal | author=Song Q, Kuang Y, Dixit VM, Vincenz C |title=Boo, a novel negative regulator of cell death, interacts with Apaf-1. |journal=EMBO J. |volume=18 |issue= 1 |pages= 167-78 |year= 1999 |pmid= 9878060 |doi= 10.1093/emboj/18.1.167 }}
*{{cite journal | author=Griffiths GJ, Dubrez L, Morgan CP, ''et al.'' |title=Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis. |journal=J. Cell Biol. |volume=144 |issue= 5 |pages= 903-14 |year= 1999 |pmid= 10085290 |doi= }}
*{{cite journal | author=Shimizu S, Narita M, Tsujimoto Y |title=Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. |journal=Nature |volume=399 |issue= 6735 |pages= 483-7 |year= 1999 |pmid= 10365962 |doi= 10.1038/20959 }}
*{{cite journal | author=Ohi N, Tokunaga A, Tsunoda H, ''et al.'' |title=A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region. |journal=Cell Death Differ. |volume=6 |issue= 4 |pages= 314-25 |year= 1999 |pmid= 10381623 |doi= 10.1038/sj.cdd.4400493 }}
*{{cite journal | author=Holmgreen SP, Huang DC, Adams JM, Cory S |title=Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members. |journal=Cell Death Differ. |volume=6 |issue= 6 |pages= 525-32 |year= 1999 |pmid= 10381646 |doi= 10.1038/sj.cdd.4400519 }}
*{{cite journal | author=Leo CP, Hsu SY, Chun SY, ''et al.'' |title=Characterization of the antiapoptotic Bcl-2 family member myeloid cell leukemia-1 (Mcl-1) and the stimulation of its message by gonadotropins in the rat ovary. |journal=Endocrinology |volume=140 |issue= 12 |pages= 5469-77 |year= 1999 |pmid= 10579309 |doi= }}
*{{cite journal | author=Shimizu S, Tsujimoto Y |title=Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 2 |pages= 577-82 |year= 2000 |pmid= 10639121 |doi= }}
*{{cite journal | author=Bae J, Leo CP, Hsu SY, Hsueh AJ |title=MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain. |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25255-61 |year= 2000 |pmid= 10837489 |doi= 10.1074/jbc.M909826199 }}
*{{cite journal | author=Wei MC, Lindsten T, Mootha VK, ''et al.'' |title=tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. |journal=Genes Dev. |volume=14 |issue= 16 |pages= 2060-71 |year= 2000 |pmid= 10950869 |doi= }}
*{{cite journal | author=Degterev A, Lugovskoy A, Cardone M, ''et al.'' |title=Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL. |journal=Nat. Cell Biol. |volume=3 |issue= 2 |pages= 173-82 |year= 2001 |pmid= 11175750 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BLM... {November 14, 2007 2:15:40 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:16:30 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
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<!-- 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 = Bloom syndrome
| HGNCid = 1058
| Symbol = BLM
| AltSymbols =; BS; MGC126616; MGC131618; MGC131620; RECQ2; RECQL2; RECQL3
| OMIM = 604610
| ECnumber =
| Homologene = 47902
| MGIid = 1328362
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004003 |text = ATP-dependent DNA helicase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016818 |text = hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006260 |text = DNA replication}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006310 |text = DNA recombination}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 641
| Hs_Ensembl = ENSG00000197299
| Hs_RefseqProtein = NP_000048
| Hs_RefseqmRNA = NM_000057
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 89061639
| Hs_GenLoc_end = 89159688
| Hs_Uniprot = P54132
| Mm_EntrezGene = 12144
| Mm_Ensembl = ENSMUSG00000030528
| Mm_RefseqmRNA = NM_001042527
| Mm_RefseqProtein = NP_001035992
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 80328605
| Mm_GenLoc_end = 80408610
| Mm_Uniprot = O88700
}}
}}
'''Bloom syndrome''', also known as '''BLM''', is a human [[gene]].
<!-- 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 Bloom syndrome gene product is related to the RecQ subset of DExH box-containing DNA helicases and has both DNA-stimulated ATPase and ATP-dependent DNA helicase activities. Mutations causing Bloom syndrome delete or alter helicase motifs and may disable the 3'-5' helicase activity. The normal protein may act to suppress inappropriate recombination.<ref>{{cite web | title = Entrez Gene: BLM Bloom syndrome| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=641| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Woo LL, Onel K, Ellis NA |title=The broken genome: genetic and pharmacologic approaches to breaking DNA. |journal=Ann. Med. |volume=39 |issue= 3 |pages= 208-18 |year= 2007 |pmid= 17457718 |doi= 10.1080/08035250601167136 }}
*{{cite journal | author=McDaniel LD, Schultz RA |title=Elevated sister chromatid exchange phenotype of Bloom syndrome cells is complemented by human chromosome 15. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 17 |pages= 7968-72 |year= 1992 |pmid= 1518822 |doi= }}
*{{cite journal | author=Ellis NA, Groden J, Ye TZ, ''et al.'' |title=The Bloom's syndrome gene product is homologous to RecQ helicases. |journal=Cell |volume=83 |issue= 4 |pages= 655-66 |year= 1995 |pmid= 7585968 |doi= }}
*{{cite journal | author=German J, Roe AM, Leppert MF, Ellis NA |title=Bloom syndrome: an analysis of consanguineous families assigns the locus mutated to chromosome band 15q26.1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6669-73 |year= 1994 |pmid= 8022833 |doi= }}
*{{cite journal | author=Foucault F, Vaury C, Barakat A, ''et al.'' |title=Characterization of a new BLM mutation associated with a topoisomerase II alpha defect in a patient with Bloom's syndrome. |journal=Hum. Mol. Genet. |volume=6 |issue= 9 |pages= 1427-34 |year= 1998 |pmid= 9285778 |doi= }}
*{{cite journal | author=Karow JK, Chakraverty RK, Hickson ID |title=The Bloom's syndrome gene product is a 3'-5' DNA helicase. |journal=J. Biol. Chem. |volume=272 |issue= 49 |pages= 30611-4 |year= 1998 |pmid= 9388193 |doi= }}
*{{cite journal | author=Kaneko H, Orii KO, Matsui E, ''et al.'' |title=BLM (the causative gene of Bloom syndrome) protein translocation into the nucleus by a nuclear localization signal. |journal=Biochem. Biophys. Res. Commun. |volume=240 |issue= 2 |pages= 348-53 |year= 1997 |pmid= 9388480 |doi= 10.1006/bbrc.1997.7648 }}
*{{cite journal | author=Wu L, Davies SL, North PS, ''et al.'' |title=The Bloom's syndrome gene product interacts with topoisomerase III. |journal=J. Biol. Chem. |volume=275 |issue= 13 |pages= 9636-44 |year= 2000 |pmid= 10734115 |doi= }}
*{{cite journal | author=Yankiwski V, Marciniak RA, Guarente L, Neff NF |title=Nuclear structure in normal and Bloom syndrome cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 10 |pages= 5214-9 |year= 2000 |pmid= 10779560 |doi= 10.1073/pnas.090525897 }}
*{{cite journal | author=Wang Y, Cortez D, Yazdi P, ''et al.'' |title=BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures. |journal=Genes Dev. |volume=14 |issue= 8 |pages= 927-39 |year= 2000 |pmid= 10783165 |doi= }}
*{{cite journal | author=Karow JK, Constantinou A, Li JL, ''et al.'' |title=The Bloom's syndrome gene product promotes branch migration of holliday junctions. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 12 |pages= 6504-8 |year= 2000 |pmid= 10823897 |doi= 10.1073/pnas.100448097 }}
*{{cite journal | author=Brosh RM, Li JL, Kenny MK, ''et al.'' |title=Replication protein A physically interacts with the Bloom's syndrome protein and stimulates its helicase activity. |journal=J. Biol. Chem. |volume=275 |issue= 31 |pages= 23500-8 |year= 2000 |pmid= 10825162 |doi= 10.1074/jbc.M001557200 }}
*{{cite journal | author=Dutertre S, Ababou M, Onclercq R, ''et al.'' |title=Cell cycle regulation of the endogenous wild type Bloom's syndrome DNA helicase. |journal=Oncogene |volume=19 |issue= 23 |pages= 2731-8 |year= 2000 |pmid= 10851073 |doi= 10.1038/sj.onc.1203595 }}
*{{cite journal | author=Barakat A, Ababou M, Onclercq R, ''et al.'' |title=Identification of a novel BLM missense mutation (2706T>C) in a Moroccan patient with Bloom's syndrome. |journal=Hum. Mutat. |volume=15 |issue= 6 |pages= 584-5 |year= 2000 |pmid= 10862105 |doi= 10.1002/1098-1004(200006)15:6<584::AID-HUMU28>3.0.CO;2-I }}
*{{cite journal | author=Brosh RM, Karow JK, White EJ, ''et al.'' |title=Potent inhibition of werner and bloom helicases by DNA minor groove binding drugs. |journal=Nucleic Acids Res. |volume=28 |issue= 12 |pages= 2420-30 |year= 2000 |pmid= 10871376 |doi= }}
*{{cite journal | author=Wu L, Davies SL, Levitt NC, Hickson ID |title=Potential role for the BLM helicase in recombinational repair via a conserved interaction with RAD51. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19375-81 |year= 2001 |pmid= 11278509 |doi= 10.1074/jbc.M009471200 }}
*{{cite journal | author=Langland G, Kordich J, Creaney J, ''et al.'' |title=The Bloom's syndrome protein (BLM) interacts with MLH1 but is not required for DNA mismatch repair. |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 30031-5 |year= 2001 |pmid= 11325959 |doi= 10.1074/jbc.M009664200 }}
*{{cite journal | author=Wang XW, Tseng A, Ellis NA, ''et al.'' |title=Functional interaction of p53 and BLM DNA helicase in apoptosis. |journal=J. Biol. Chem. |volume=276 |issue= 35 |pages= 32948-55 |year= 2001 |pmid= 11399766 |doi= 10.1074/jbc.M103298200 }}
*{{cite journal | author=Hu P, Beresten SF, van Brabant AJ, ''et al.'' |title=Evidence for BLM and Topoisomerase IIIalpha interaction in genomic stability. |journal=Hum. Mol. Genet. |volume=10 |issue= 12 |pages= 1287-98 |year= 2001 |pmid= 11406610 |doi= }}
*{{cite journal | author=Freire R, d'Adda Di Fagagna F, Wu L, ''et al.'' |title=Cleavage of the Bloom's syndrome gene product during apoptosis by caspase-3 results in an impaired interaction with topoisomerase IIIalpha. |journal=Nucleic Acids Res. |volume=29 |issue= 15 |pages= 3172-80 |year= 2001 |pmid= 11470874 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BMP4... {November 14, 2007 2:16:30 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:17:04 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_BMP4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1reu.
| PDB = {{PDB2|1reu}}
| Name = Bone morphogenetic protein 4
| HGNCid = 1071
| Symbol = BMP4
| AltSymbols =; BMP2B; BMP2B1; ZYME
| OMIM = 112262
| ECnumber =
| Homologene = 7247
| MGIid = 88180
| GeneAtlas_image1 = PBB_GE_BMP4_211518_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0001649 |text = osteoblast differentiation}} {{GNF_GO|id=GO:0001657 |text = ureteric bud development}} {{GNF_GO|id=GO:0001934 |text = positive regulation of protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007281 |text = germ cell development}} {{GNF_GO|id=GO:0007500 |text = mesodermal cell fate determination}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0021904 |text = dorsoventral neural tube patterning}} {{GNF_GO|id=GO:0021978 |text = telencephalon regionalization}} {{GNF_GO|id=GO:0030218 |text = erythrocyte differentiation}} {{GNF_GO|id=GO:0030324 |text = lung development}} {{GNF_GO|id=GO:0030501 |text = positive regulation of bone mineralization}} {{GNF_GO|id=GO:0030509 |text = BMP signaling pathway}} {{GNF_GO|id=GO:0030900 |text = forebrain development}} {{GNF_GO|id=GO:0040007 |text = growth}} {{GNF_GO|id=GO:0042475 |text = odontogenesis (sensu Vertebrata)}} {{GNF_GO|id=GO:0045165 |text = cell fate commitment}} {{GNF_GO|id=GO:0045662 |text = negative regulation of myoblast differentiation}} {{GNF_GO|id=GO:0045669 |text = positive regulation of osteoblast differentiation}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}} {{GNF_GO|id=GO:0045843 |text = negative regulation of striated muscle development}} {{GNF_GO|id=GO:0051145 |text = smooth muscle cell differentiation}} {{GNF_GO|id=GO:0051216 |text = cartilage development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 652
| Hs_Ensembl = ENSG00000125378
| Hs_RefseqProtein = NP_001193
| Hs_RefseqmRNA = NM_001202
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 53486207
| Hs_GenLoc_end = 53493362
| Hs_Uniprot = P12644
| Mm_EntrezGene = 12159
| Mm_Ensembl = ENSMUSG00000021835
| Mm_RefseqmRNA = NM_007554
| Mm_RefseqProtein = NP_031580
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 45305599
| Mm_GenLoc_end = 45312453
| Mm_Uniprot = Q3ULR1
}}
}}
'''Bone morphogenetic protein 4''', also known as '''BMP4''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.<ref>{{cite web | title = Entrez Gene: BMP4 bone morphogenetic protein 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=652| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wozney JM, Rosen V, Celeste AJ, ''et al.'' |title=Novel regulators of bone formation: molecular clones and activities. |journal=Science |volume=242 |issue= 4885 |pages= 1528-34 |year= 1989 |pmid= 3201241 |doi= }}
*{{cite journal | author=van den Wijngaard A, Weghuis DO, Boersma CJ, ''et al.'' |title=Fine mapping of the human bone morphogenetic protein-4 gene (BMP4) to chromosome 14q22-q23 by in situ hybridization. |journal=Genomics |volume=27 |issue= 3 |pages= 559-60 |year= 1995 |pmid= 7558046 |doi= }}
*{{cite journal | author=Oida S, Iimura T, Maruoka Y, ''et al.'' |title=Cloning and sequence of bone morphogenetic protein 4 (BMP-4) from a human placental cDNA library. |journal=DNA Seq. |volume=5 |issue= 5 |pages= 273-5 |year= 1995 |pmid= 7579580 |doi= }}
*{{cite journal | author=Rosenzweig BL, Imamura T, Okadome T, ''et al.'' |title=Cloning and characterization of a human type II receptor for bone morphogenetic proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 17 |pages= 7632-6 |year= 1995 |pmid= 7644468 |doi= }}
*{{cite journal | author=Nohno T, Ishikawa T, Saito T, ''et al.'' |title=Identification of a human type II receptor for bone morphogenetic protein-4 that forms differential heteromeric complexes with bone morphogenetic protein type I receptors. |journal=J. Biol. Chem. |volume=270 |issue= 38 |pages= 22522-6 |year= 1995 |pmid= 7673243 |doi= }}
*{{cite journal | author=Yamaji N, Celeste AJ, Thies RS, ''et al.'' |title=A mammalian serine/threonine kinase receptor specifically binds BMP-2 and BMP-4. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 3 |pages= 1944-51 |year= 1995 |pmid= 7811286 |doi= 10.1006/bbrc.1994.2898 }}
*{{cite journal | author=Harris SE, Harris MA, Mahy P, ''et al.'' |title=Expression of bone morphogenetic protein messenger RNAs by normal rat and human prostate and prostate cancer cells. |journal=Prostate |volume=24 |issue= 4 |pages= 204-11 |year= 1994 |pmid= 8146069 |doi= }}
*{{cite journal | author=van den Wijngaard A, van Kraay M, van Zoelen EJ, ''et al.'' |title=Genomic organization of the human bone morphogenetic protein-4 gene: molecular basis for multiple transcripts. |journal=Biochem. Biophys. Res. Commun. |volume=219 |issue= 3 |pages= 789-94 |year= 1996 |pmid= 8645259 |doi= 10.1006/bbrc.1996.0312 }}
*{{cite journal | author=Nishitoh H, Ichijo H, Kimura M, ''et al.'' |title=Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5. |journal=J. Biol. Chem. |volume=271 |issue= 35 |pages= 21345-52 |year= 1996 |pmid= 8702914 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Shore EM, Xu M, Shah PB, ''et al.'' |title=The human bone morphogenetic protein 4 (BMP-4) gene: molecular structure and transcriptional regulation. |journal=Calcif. Tissue Int. |volume=63 |issue= 3 |pages= 221-9 |year= 1998 |pmid= 9701626 |doi= }}
*{{cite journal | author=Tucker AS, Matthews KL, Sharpe PT |title=Transformation of tooth type induced by inhibition of BMP signaling. |journal=Science |volume=282 |issue= 5391 |pages= 1136-8 |year= 1998 |pmid= 9804553 |doi= }}
*{{cite journal | author=Van den Wijngaard A, Pijpers MA, Joosten PH, ''et al.'' |title=Functional characterization of two promoters in the human bone morphogenetic protein-4 gene. |journal=J. Bone Miner. Res. |volume=14 |issue= 8 |pages= 1432-41 |year= 1999 |pmid= 10457277 |doi= }}
*{{cite journal | author=Li W, LoTurco JJ |title=Noggin is a negative regulator of neuronal differentiation in developing neocortex. |journal=Dev. Neurosci. |volume=22 |issue= 1-2 |pages= 68-73 |year= 2000 |pmid= 10657699 |doi= }}
*{{cite journal | author=Raatikainen-Ahokas A, Hytönen M, Tenhunen A, ''et al.'' |title=BMP-4 affects the differentiation of metanephric mesenchyme and reveals an early anterior-posterior axis of the embryonic kidney. |journal=Dev. Dyn. |volume=217 |issue= 2 |pages= 146-58 |year= 2000 |pmid= 10706139 |doi= 10.1002/(SICI)1097-0177(200002)217:2<146::AID-DVDY2>3.0.CO;2-I }}
*{{cite journal | author=van den Wijngaard A, Mulder WR, Dijkema R, ''et al.'' |title=Antiestrogens specifically up-regulate bone morphogenetic protein-4 promoter activity in human osteoblastic cells. |journal=Mol. Endocrinol. |volume=14 |issue= 5 |pages= 623-33 |year= 2000 |pmid= 10809227 |doi= }}
*{{cite journal | author=Ying Y, Liu XM, Marble A, ''et al.'' |title=Requirement of Bmp8b for the generation of primordial germ cells in the mouse. |journal=Mol. Endocrinol. |volume=14 |issue= 7 |pages= 1053-63 |year= 2000 |pmid= 10894154 |doi= }}
*{{cite journal | author=Nakade O, Takahashi K, Takuma T, ''et al.'' |title=Effect of extracellular calcium on the gene expression of bone morphogenetic protein-2 and -4 of normal human bone cells. |journal=J. Bone Miner. Metab. |volume=19 |issue= 1 |pages= 13-9 |year= 2001 |pmid= 11156467 |doi= }}
*{{cite journal | author=Hatta T, Konishi H, Katoh E, ''et al.'' |title=Identification of the ligand-binding site of the BMP type IA receptor for BMP-4. |journal=Biopolymers |volume=55 |issue= 5 |pages= 399-406 |year= 2001 |pmid= 11241215 |doi= 10.1002/1097-0282(2000)55:5<399::AID-BIP1014>3.0.CO;2-9 }}
*{{cite journal | author=Aoki H, Fujii M, Imamura T, ''et al.'' |title=Synergistic effects of different bone morphogenetic protein type I receptors on alkaline phosphatase induction. |journal=J. Cell. Sci. |volume=114 |issue= Pt 8 |pages= 1483-9 |year= 2001 |pmid= 11282024 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BSG... {November 14, 2007 2:17:04 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:17:54 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 =
| image_source =
| PDB =
| Name = Basigin (Ok blood group)
| HGNCid = 1116
| Symbol = BSG
| AltSymbols =; 5F7; CD147; EMMPRIN; M6; OK; TCSF
| OMIM = 109480
| ECnumber =
| Homologene = 1308
| MGIid = 88208
| GeneAtlas_image1 = PBB_GE_BSG_208677_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0005537 |text = mannose binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 682
| Hs_Ensembl = ENSG00000172270
| Hs_RefseqProtein = NP_001719
| Hs_RefseqmRNA = NM_001728
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 462896
| Hs_GenLoc_end = 534492
| Hs_Uniprot = P35613
| Mm_EntrezGene = 12215
| Mm_Ensembl = ENSMUSG00000023175
| Mm_RefseqmRNA = NM_001077184
| Mm_RefseqProtein = NP_001070652
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 79107635
| Mm_GenLoc_end = 79115097
| Mm_Uniprot = O55107
}}
}}
'''Basigin (Ok blood group)''', also known as '''BSG''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Basigin is a member of the immunoglobulin superfamily, with a structure related to the putative primordial form of the family. As members of the immunoglobulin superfamily play fundamental roles in intercellular recognition involved in various immunologic phenomena, differentiation, and development, basigin is thought also to play a role in intercellular recognition (Miyauchi et al., 1991; Kanekura et al., 1991).[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: BSG basigin (Ok blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=682| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Muramatsu T, Miyauchi T |title=Basigin (CD147): a multifunctional transmembrane protein involved in reproduction, neural function, inflammation and tumor invasion. |journal=Histol. Histopathol. |volume=18 |issue= 3 |pages= 981-7 |year= 2004 |pmid= 12792908 |doi= }}
*{{cite journal | author=Yan L, Zucker S, Toole BP |title=Roles of the multifunctional glycoprotein, emmprin (basigin; CD147), in tumour progression. |journal=Thromb. Haemost. |volume=93 |issue= 2 |pages= 199-204 |year= 2005 |pmid= 15711733 |doi= 10.1267/THRO05020199 }}
*{{cite journal | author=Kasinrerk W, Fiebiger E, Stefanová I, ''et al.'' |title=Human leukocyte activation antigen M6, a member of the Ig superfamily, is the species homologue of rat OX-47, mouse basigin, and chicken HT7 molecule. |journal=J. Immunol. |volume=149 |issue= 3 |pages= 847-54 |year= 1992 |pmid= 1634773 |doi= }}
*{{cite journal | author=Miyauchi T, Masuzawa Y, Muramatsu T |title=The basigin group of the immunoglobulin superfamily: complete conservation of a segment in and around transmembrane domains of human and mouse basigin and chicken HT7 antigen. |journal=J. Biochem. |volume=110 |issue= 5 |pages= 770-4 |year= 1992 |pmid= 1783610 |doi= }}
*{{cite journal | author=Nabeshima K, Lane WS, Biswas C |title=Partial sequencing and characterization of the tumor cell-derived collagenase stimulatory factor. |journal=Arch. Biochem. Biophys. |volume=285 |issue= 1 |pages= 90-6 |year= 1991 |pmid= 1846736 |doi= }}
*{{cite journal | author=Biswas C, Zhang Y, DeCastro R, ''et al.'' |title=The human tumor cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily. |journal=Cancer Res. |volume=55 |issue= 2 |pages= 434-9 |year= 1995 |pmid= 7812975 |doi= }}
*{{cite journal | author=Kaname T, Miyauchi T, Kuwano A, ''et al.'' |title=Mapping basigin (BSG), a member of the immunoglobulin superfamily, to 19p13.3. |journal=Cytogenet. Cell Genet. |volume=64 |issue= 3-4 |pages= 195-7 |year= 1993 |pmid= 8404035 |doi= }}
*{{cite journal | author=DeCastro R, Zhang Y, Guo H, ''et al.'' |title=Human keratinocytes express EMMPRIN, an extracellular matrix metalloproteinase inducer. |journal=J. Invest. Dermatol. |volume=106 |issue= 6 |pages= 1260-5 |year= 1996 |pmid= 8752667 |doi= }}
*{{cite journal | author=Spring FA, Holmes CH, Simpson KL, ''et al.'' |title=The Oka blood group antigen is a marker for the M6 leukocyte activation antigen, the human homolog of OX-47 antigen, basigin and neurothelin, an immunoglobulin superfamily molecule that is widely expressed in human cells and tissues. |journal=Eur. J. Immunol. |volume=27 |issue= 4 |pages= 891-7 |year= 1997 |pmid= 9130641 |doi= }}
*{{cite journal | author=Berditchevski F, Chang S, Bodorova J, Hemler ME |title=Generation of monoclonal antibodies to integrin-associated proteins. Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6. |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 29174-80 |year= 1997 |pmid= 9360995 |doi= }}
*{{cite journal | author=Guo H, Majmudar G, Jensen TC, ''et al.'' |title=Characterization of the gene for human EMMPRIN, a tumor cell surface inducer of matrix metalloproteinases. |journal=Gene |volume=220 |issue= 1-2 |pages= 99-108 |year= 1998 |pmid= 9767135 |doi= }}
*{{cite journal | author=Guo H, Li R, Zucker S, Toole BP |title=EMMPRIN (CD147), an inducer of matrix metalloproteinase synthesis, also binds interstitial collagenase to the tumor cell surface. |journal=Cancer Res. |volume=60 |issue= 4 |pages= 888-91 |year= 2000 |pmid= 10706100 |doi= }}
*{{cite journal | author=Kirk P, Wilson MC, Heddle C, ''et al.'' |title=CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expression. |journal=EMBO J. |volume=19 |issue= 15 |pages= 3896-904 |year= 2000 |pmid= 10921872 |doi= 10.1093/emboj/19.15.3896 }}
*{{cite journal | author=Yurchenko V, O'Connor M, Dai WW, ''et al.'' |title=CD147 is a signaling receptor for cyclophilin B. |journal=Biochem. Biophys. Res. Commun. |volume=288 |issue= 4 |pages= 786-8 |year= 2001 |pmid= 11688976 |doi= 10.1006/bbrc.2001.5847 }}
*{{cite journal | author=Yurchenko V, Zybarth G, O'Connor M, ''et al.'' |title=Active site residues of cyclophilin A are crucial for its signaling activity via CD147. |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 22959-65 |year= 2002 |pmid= 11943775 |doi= 10.1074/jbc.M201593200 }}
*{{cite journal | author=Kanekura T, Chen X, Kanzaki T |title=Basigin (CD147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts. |journal=Int. J. Cancer |volume=99 |issue= 4 |pages= 520-8 |year= 2002 |pmid= 11992541 |doi= 10.1002/ijc.10390 }}
*{{cite journal | author=Major TC, Liang L, Lu X, ''et al.'' |title=Extracellular matrix metalloproteinase inducer (EMMPRIN) is induced upon monocyte differentiation and is expressed in human atheroma. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=22 |issue= 7 |pages= 1200-7 |year= 2002 |pmid= 12117738 |doi= }}
*{{cite journal | author=Taylor PM, Woodfield RJ, Hodgkin MN, ''et al.'' |title=Breast cancer cell-derived EMMPRIN stimulates fibroblast MMP2 release through a phospholipase A(2) and 5-lipoxygenase catalyzed pathway. |journal=Oncogene |volume=21 |issue= 37 |pages= 5765-72 |year= 2002 |pmid= 12173047 |doi= 10.1038/sj.onc.1205702 }}
*{{cite journal | author=Thorns C, Feller AC, Merz H |title=EMMPRIN (CD 174) is expressed in Hodgkin's lymphoma and anaplastic large cell lymphoma. An immunohistochemical study of 60 cases. |journal=Anticancer Res. |volume=22 |issue= 4 |pages= 1983-6 |year= 2002 |pmid= 12174874 |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 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CBS... {November 14, 2007 2:17:54 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:18:26 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
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CBS_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jbq.
| PDB = {{PDB2|1jbq}}, {{PDB2|1m54}}
| Name = Cystathionine-beta-synthase
| HGNCid = 1550
| Symbol = CBS
| AltSymbols =; HIP4
| OMIM = 236200
| ECnumber =
| Homologene = 37258
| MGIid = 88285
| Function = {{GNF_GO|id=GO:0004122 |text = cystathionine beta-synthase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006535 |text = cysteine biosynthetic process from serine}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0008652 |text = amino acid biosynthetic process}} {{GNF_GO|id=GO:0019343 |text = cysteine biosynthetic process via cystathionine}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 875
| Hs_Ensembl = ENSG00000160200
| Hs_RefseqProtein = NP_000062
| Hs_RefseqmRNA = NM_000071
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 43346374
| Hs_GenLoc_end = 43369541
| Hs_Uniprot = P35520
| Mm_EntrezGene = 12411
| Mm_Ensembl = ENSMUSG00000024039
| Mm_RefseqmRNA = NM_144855
| Mm_RefseqProtein = NP_659104
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 31341351
| Mm_GenLoc_end = 31365875
| Mm_Uniprot = Q91WT9
}}
}}
'''Cystathionine-beta-synthase''', also known as '''CBS''', is a human [[gene]].
<!-- 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 involved in the transsulfuration pathway. The first step of this pathway, from homocysteine to cystathionine, is catalyzed by this protein. CBS deficiency can cause homocystinuria which affects many organs and tissues, including the eyes and the skeletal, vascular and central nervous systems.<ref>{{cite web | title = Entrez Gene: CBS cystathionine-beta-synthase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=875| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kraus JP |title=Komrower Lecture. Molecular basis of phenotype expression in homocystinuria. |journal=J. Inherit. Metab. Dis. |volume=17 |issue= 4 |pages= 383-90 |year= 1994 |pmid= 7967489 |doi= }}
*{{cite journal | author=Kraus JP, Janosík M, Kozich V, ''et al.'' |title=Cystathionine beta-synthase mutations in homocystinuria. |journal=Hum. Mutat. |volume=13 |issue= 5 |pages= 362-75 |year= 1999 |pmid= 10338090 |doi= 10.1002/(SICI)1098-1004(1999)13:5<362::AID-HUMU4>3.0.CO;2-K }}
*{{cite journal | author=Jones AL |title=The localization and interactions of huntingtin. |journal=Philos. Trans. R. Soc. Lond., B, Biol. Sci. |volume=354 |issue= 1386 |pages= 1021-7 |year= 1999 |pmid= 10434301 |doi= 10.1098/rstb.1999.0454 }}
*{{cite journal | author=Griffiths R, Tudball N |title=The molecular defect in a case of (cystathionine beta-synthase)-deficient homocystinuria. |journal=Eur. J. Biochem. |volume=74 |issue= 2 |pages= 269-73 |year= 1977 |pmid= 404147 |doi= }}
*{{cite journal | author=Kraus J, Packman S, Fowler B, Rosenberg LE |title=Purification and properties of cystathionine beta-synthase from human liver. Evidence for identical subunits. |journal=J. Biol. Chem. |volume=253 |issue= 18 |pages= 6523-8 |year= 1978 |pmid= 681363 |doi= }}
*{{cite journal | author=Longhi RC, Fleisher LD, Tallan HH, Gaull GE |title=Cystathionine beta-synthase deficiency: a qualitative abnormality of the deficient enzyme modified by vitamin B6 therapy. |journal=Pediatr. Res. |volume=11 |issue= 2 |pages= 100-3 |year= 1977 |pmid= 840498 |doi= }}
*{{cite journal | author=Kozich V, Kraus JP |title=Screening for mutations by expressing patient cDNA segments in E. coli: homocystinuria due to cystathionine beta-synthase deficiency. |journal=Hum. Mutat. |volume=1 |issue= 2 |pages= 113-23 |year= 1993 |pmid= 1301198 |doi= 10.1002/humu.1380010206 }}
*{{cite journal | author=Münke M, Kraus JP, Ohura T, Francke U |title=The gene for cystathionine beta-synthase (CBS) maps to the subtelomeric region on human chromosome 21q and to proximal mouse chromosome 17. |journal=Am. J. Hum. Genet. |volume=42 |issue= 4 |pages= 550-9 |year= 1988 |pmid= 2894761 |doi= }}
*{{cite journal | author=Hu FL, Gu Z, Kozich V, ''et al.'' |title=Molecular basis of cystathionine beta-synthase deficiency in pyridoxine responsive and nonresponsive homocystinuria. |journal=Hum. Mol. Genet. |volume=2 |issue= 11 |pages= 1857-60 |year= 1994 |pmid= 7506602 |doi= }}
*{{cite journal | author=Sperandeo MP, Panico M, Pepe A, ''et al.'' |title=Molecular analysis of patients affected by homocystinuria due to cystathionine beta-synthase deficiency: report of a new mutation in exon 8 and a deletion in intron 11. |journal=J. Inherit. Metab. Dis. |volume=18 |issue= 2 |pages= 211-4 |year= 1995 |pmid= 7564249 |doi= }}
*{{cite journal | author=Chassé JF, Paly E, Paris D, ''et al.'' |title=Genomic organization of the human cystathionine beta-synthase gene: evidence for various cDNAs. |journal=Biochem. Biophys. Res. Commun. |volume=211 |issue= 3 |pages= 826-32 |year= 1995 |pmid= 7598711 |doi= 10.1006/bbrc.1995.1886 }}
*{{cite journal | author=Shih VE, Fringer JM, Mandell R, ''et al.'' |title=A missense mutation (I278T) in the cystathionine beta-synthase gene prevalent in pyridoxine-responsive homocystinuria and associated with mild clinical phenotype. |journal=Am. J. Hum. Genet. |volume=57 |issue= 1 |pages= 34-9 |year= 1995 |pmid= 7611293 |doi= }}
*{{cite journal | author=Kluijtmans LA, Blom HJ, Boers GH, ''et al.'' |title=Two novel missense mutations in the cystathionine beta-synthase gene in homocystinuric patients. |journal=Hum. Genet. |volume=96 |issue= 2 |pages= 249-50 |year= 1995 |pmid= 7635485 |doi= }}
*{{cite journal | author=Sebastio G, Sperandeo MP, Panico M, ''et al.'' |title=The molecular basis of homocystinuria due to cystathionine beta-synthase deficiency in Italian families, and report of four novel mutations. |journal=Am. J. Hum. Genet. |volume=56 |issue= 6 |pages= 1324-33 |year= 1995 |pmid= 7762555 |doi= }}
*{{cite journal | author=Marble M, Geraghty MT, de Franchis R, ''et al.'' |title=Characterization of a cystathionine beta-synthase allele with three mutations in cis in a patient with B6 nonresponsive homocystinuria. |journal=Hum. Mol. Genet. |volume=3 |issue= 10 |pages= 1883-6 |year= 1995 |pmid= 7849717 |doi= }}
*{{cite journal | author=Kraus JP, Le K, Swaroop M, ''et al.'' |title=Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells. |journal=Hum. Mol. Genet. |volume=2 |issue= 10 |pages= 1633-8 |year= 1994 |pmid= 7903580 |doi= }}
*{{cite journal | author=de Franchis R, Kozich V, McInnes RR, Kraus JP |title=Identical genotypes in siblings with different homocystinuric phenotypes: identification of three mutations in cystathionine beta-synthase using an improved bacterial expression system. |journal=Hum. Mol. Genet. |volume=3 |issue= 7 |pages= 1103-8 |year= 1995 |pmid= 7981678 |doi= }}
*{{cite journal | author=Kruger WD, Cox DR |title=A yeast system for expression of human cystathionine beta-synthase: structural and functional conservation of the human and yeast genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6614-8 |year= 1994 |pmid= 8022826 |doi= }}
*{{cite journal | author=Kozich V, de Franchis R, Kraus JP |title=Molecular defect in a patient with pyridoxine-responsive homocystinuria. |journal=Hum. Mol. Genet. |volume=2 |issue= 6 |pages= 815-6 |year= 1993 |pmid= 8353501 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CST3... {November 14, 2007 2:19:11 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:19:36 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_CST3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1g96.
| PDB = {{PDB2|1g96}}, {{PDB2|1r4c}}, {{PDB2|1tij}}
| Name = Cystatin C (amyloid angiopathy and cerebral hemorrhage)
| HGNCid = 2475
| Symbol = CST3
| AltSymbols =; MGC117328
| OMIM = 604312
| ECnumber =
| Homologene = 78
| MGIid = 102519
| GeneAtlas_image1 = PBB_GE_CST3_201360_at_tn.png
| Function = {{GNF_GO|id=GO:0004869 |text = cysteine protease inhibitor activity}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component =
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1471
| Hs_Ensembl = ENSG00000101439
| Hs_RefseqProtein = NP_000090
| Hs_RefseqmRNA = NM_000099
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 23562297
| Hs_GenLoc_end = 23566631
| Hs_Uniprot = P01034
| Mm_EntrezGene = 13010
| Mm_Ensembl = ENSMUSG00000027447
| Mm_RefseqmRNA = NM_009976
| Mm_RefseqProtein = NP_034106
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 148563189
| Mm_GenLoc_end = 148566928
| Mm_Uniprot = Q3U5K7
}}
}}
'''Cystatin C (amyloid angiopathy and cerebral hemorrhage)''', also known as '''CST3''', is a human [[gene]].
<!-- 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 cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions, where they appear to provide protective functions. The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in the cystatin locus and encodes the most abundant extracellular inhibitor of cysteine proteases, which is found in high concentrations in biological fluids and is expressed in virtually all organs of the body. A mutation in this gene has been associated with amyloid angiopathy. Expression of this protein in vascular wall smooth muscle cells is severely reduced in both atherosclerotic and aneurysmal aortic lesions, establishing its role in vascular disease.<ref>{{cite web | title = Entrez Gene: CST3 cystatin C (amyloid angiopathy and cerebral hemorrhage)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1471| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Jensson O, Palsdottir A, Thorsteinsson L, Arnason A |title=The saga of cystatin C gene mutation causing amyloid angiopathy and brain hemorrhage--clinical genetics in Iceland. |journal=Clin. Genet. |volume=36 |issue= 5 |pages= 368-77 |year= 1990 |pmid= 2689007 |doi= }}
*{{cite journal | author=Mussap M, Plebani M |title=Biochemistry and clinical role of human cystatin C. |journal=Critical reviews in clinical laboratory sciences |volume=41 |issue= 5-6 |pages= 467-550 |year= 2005 |pmid= 15603510 |doi= }}
*{{cite journal | author=Palsdottir A, Snorradottir AO, Thorsteinsson L |title=Hereditary cystatin C amyloid angiopathy: genetic, clinical, and pathological aspects. |journal=Brain Pathol. |volume=16 |issue= 1 |pages= 55-9 |year= 2006 |pmid= 16612982 |doi= }}
*{{cite journal | author=Levy E, Jaskolski M, Grubb A |title=The role of cystatin C in cerebral amyloid angiopathy and stroke: cell biology and animal models. |journal=Brain Pathol. |volume=16 |issue= 1 |pages= 60-70 |year= 2006 |pmid= 16612983 |doi= }}
*{{cite journal | author=Bökenkamp A, Herget-Rosenthal S, Bökenkamp R |title=Cystatin C, kidney function and cardiovascular disease. |journal=Pediatr. Nephrol. |volume=21 |issue= 9 |pages= 1223-30 |year= 2006 |pmid= 16838182 |doi= 10.1007/s00467-006-0192-5 }}
*{{cite journal | author=Abrahamson M, Jonsdottir S, Olafsson I, ''et al.'' |title=Hereditary cystatin C amyloid angiopathy: identification of the disease-causing mutation and specific diagnosis by polymerase chain reaction based analysis. |journal=Hum. Genet. |volume=89 |issue= 4 |pages= 377-80 |year= 1992 |pmid= 1352269 |doi= }}
*{{cite journal | author=Lindahl P, Abrahamson M, Björk I |title=Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin. |journal=Biochem. J. |volume=281 ( Pt 1) |issue= |pages= 49-55 |year= 1992 |pmid= 1731767 |doi= }}
*{{cite journal | author=Abrahamson M, Mason RW, Hansson H, ''et al.'' |title=Human cystatin C. role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase. |journal=Biochem. J. |volume=273 ( Pt 3) |issue= |pages= 621-6 |year= 1991 |pmid= 1996959 |doi= }}
*{{cite journal | author=Lenarcic B, Krasovec M, Ritonja A, ''et al.'' |title=Inactivation of human cystatin C and kininogen by human cathepsin D. |journal=FEBS Lett. |volume=280 |issue= 2 |pages= 211-5 |year= 1991 |pmid= 2013314 |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=Abrahamson M, Olafsson I, Palsdottir A, ''et al.'' |title=Structure and expression of the human cystatin C gene. |journal=Biochem. J. |volume=268 |issue= 2 |pages= 287-94 |year= 1990 |pmid= 2363674 |doi= }}
*{{cite journal | author=Levy E, Lopez-Otin C, Ghiso J, ''et al.'' |title=Stroke in Icelandic patients with hereditary amyloid angiopathy is related to a mutation in the cystatin C gene, an inhibitor of cysteine proteases. |journal=J. Exp. Med. |volume=169 |issue= 5 |pages= 1771-8 |year= 1989 |pmid= 2541223 |doi= }}
*{{cite journal | author=Abrahamson M, Islam MQ, Szpirer J, ''et al.'' |title=The human cystatin C gene (CST3), mutated in hereditary cystatin C amyloid angiopathy, is located on chromosome 20. |journal=Hum. Genet. |volume=82 |issue= 3 |pages= 223-6 |year= 1989 |pmid= 2567273 |doi= }}
*{{cite journal | author=Saitoh E, Sabatini LM, Eddy RL, ''et al.'' |title=The human cystatin C gene (CST3) is a member of the cystatin gene family which is localized on chromosome 20. |journal=Biochem. Biophys. Res. Commun. |volume=162 |issue= 3 |pages= 1324-31 |year= 1989 |pmid= 2764935 |doi= }}
*{{cite journal | author=Palsdottir A, Abrahamson M, Thorsteinsson L, ''et al.'' |title=Mutation in cystatin C gene causes hereditary brain haemorrhage. |journal=Lancet |volume=2 |issue= 8611 |pages= 603-4 |year= 1988 |pmid= 2900981 |doi= }}
*{{cite journal | author=Abrahamson M, Grubb A, Olafsson I, Lundwall A |title=Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C. |journal=FEBS Lett. |volume=216 |issue= 2 |pages= 229-33 |year= 1987 |pmid= 3495457 |doi= }}
*{{cite journal | author=Ghiso J, Jensson O, Frangione B |title=Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of gamma-trace basic protein (cystatin C). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 9 |pages= 2974-8 |year= 1986 |pmid= 3517880 |doi= }}
*{{cite journal | author=Grubb A, Löfberg H |title=Human gamma-trace, a basic microprotein: amino acid sequence and presence in the adenohypophysis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=79 |issue= 9 |pages= 3024-7 |year= 1982 |pmid= 6283552 |doi= }}
*{{cite journal | author=Brzin J, Popovic T, Turk V, ''et al.'' |title=Human cystatin, a new protein inhibitor of cysteine proteinases. |journal=Biochem. Biophys. Res. Commun. |volume=118 |issue= 1 |pages= 103-9 |year= 1984 |pmid= 6365094 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYP11B2... {November 14, 2007 2:19:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:20:17 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 = Cytochrome P450, family 11, subfamily B, polypeptide 2
| HGNCid = 2592
| Symbol = CYP11B2
| AltSymbols =; CPN2; CYP11B; ALDOS; CYP11BL; P-450C18; P450C18; P450aldo
| OMIM = 124080
| ECnumber =
| Homologene = 73878
| MGIid = 88583
| GeneAtlas_image1 = PBB_GE_CYP11B2_214630_at_tn.png
| Function = {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0004507 |text = steroid 11-beta-monooxygenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0047783 |text = corticosterone 18-monooxygenase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006700 |text = C21-steroid hormone biosynthetic process}} {{GNF_GO|id=GO:0006704 |text = glucocorticoid biosynthetic process}} {{GNF_GO|id=GO:0008202 |text = steroid metabolic process}} {{GNF_GO|id=GO:0008217 |text = blood pressure regulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1585
| Hs_Ensembl = ENSG00000179142
| Hs_RefseqProtein = NP_000489
| Hs_RefseqmRNA = NM_000498
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 143988983
| Hs_GenLoc_end = 143996261
| Hs_Uniprot = P19099
| Mm_EntrezGene = 110115
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_001033229
| Mm_RefseqProtein = NP_001028401
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Cytochrome P450, family 11, subfamily B, polypeptide 2''', also known as '''CYP11B2''', is a human [[gene]].
<!-- 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 cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the mitochondrial inner membrane. The enzyme has steroid 18-hydroxylase activity to synthesize aldosterone and 18-oxocortisol as well as steroid 11 beta-hydroxylase activity. Mutations in this gene cause corticosterone methyl oxidase deficiency.<ref>{{cite web | title = Entrez Gene: CYP11B2 cytochrome P450, family 11, subfamily B, polypeptide 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1585| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Helmberg A |title=Twin genes and endocrine disease: CYP21 and CYP11B genes. |journal=Acta Endocrinol. |volume=129 |issue= 2 |pages= 97-108 |year= 1993 |pmid= 8372604 |doi= }}
*{{cite journal | author=Slight SH, Joseph J, Ganjam VK, Weber KT |title=Extra-adrenal mineralocorticoids and cardiovascular tissue. |journal=J. Mol. Cell. Cardiol. |volume=31 |issue= 6 |pages= 1175-84 |year= 1999 |pmid= 10371693 |doi= 10.1006/jmcc.1999.0963 }}
*{{cite journal | author=Stowasser M, Gunasekera TG, Gordon RD |title=Familial varieties of primary aldosteronism. |journal=Clin. Exp. Pharmacol. Physiol. |volume=28 |issue= 12 |pages= 1087-90 |year= 2002 |pmid= 11903322 |doi= }}
*{{cite journal | author=Padmanabhan N, Padmanabhan S, Connell JM |title=Genetic basis of cardiovascular disease--the renin-angiotensin-aldosterone system as a paradigm. |journal=Journal of the renin-angiotensin-aldosterone system : JRAAS |volume=1 |issue= 4 |pages= 316-24 |year= 2002 |pmid= 11967817 |doi= 10.3317/jraas.2000.060 }}
*{{cite journal | author=Lifton RP, Dluhy RG, Powers M, ''et al.'' |title=Hereditary hypertension caused by chimaeric gene duplications and ectopic expression of aldosterone synthase. |journal=Nat. Genet. |volume=2 |issue= 1 |pages= 66-74 |year= 1993 |pmid= 1303253 |doi= 10.1038/ng0992-66 }}
*{{cite journal | author=Mitsuuchi Y, Kawamoto T, Naiki Y, ''et al.'' |title=Congenitally defective aldosterone biosynthesis in humans: the involvement of point mutations of the P-450C18 gene (CYP11B2) in CMO II deficient patients. |journal=Biochem. Biophys. Res. Commun. |volume=182 |issue= 2 |pages= 974-9 |year= 1992 |pmid= 1346492 |doi= }}
*{{cite journal | author=Pascoe L, Curnow KM, Slutsker L, ''et al.'' |title=Glucocorticoid-suppressible hyperaldosteronism results from hybrid genes created by unequal crossovers between CYP11B1 and CYP11B2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 17 |pages= 8327-31 |year= 1992 |pmid= 1518866 |doi= }}
*{{cite journal | author=Pascoe L, Curnow KM, Slutsker L, ''et al.'' |title=Mutations in the human CYP11B2 (aldosterone synthase) gene causing corticosterone methyloxidase II deficiency. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 11 |pages= 4996-5000 |year= 1992 |pmid= 1594605 |doi= }}
*{{cite journal | author=Kawamoto T, Mitsuuchi Y, Toda K, ''et al.'' |title=Role of steroid 11 beta-hydroxylase and steroid 18-hydroxylase in the biosynthesis of glucocorticoids and mineralocorticoids in humans. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 4 |pages= 1458-62 |year= 1992 |pmid= 1741400 |doi= }}
*{{cite journal | author=Curnow KM, Tusie-Luna MT, Pascoe L, ''et al.'' |title=The product of the CYP11B2 gene is required for aldosterone biosynthesis in the human adrenal cortex. |journal=Mol. Endocrinol. |volume=5 |issue= 10 |pages= 1513-22 |year= 1992 |pmid= 1775135 |doi= }}
*{{cite journal | author=Kawainoto T, Mitsuuchi Y, Ohnishi T, ''et al.'' |title=Cloning and expression of a cDNA for human cytochrome P-450aldo as related to primary aldosteronism. |journal=Biochem. Biophys. Res. Commun. |volume=173 |issue= 1 |pages= 309-16 |year= 1991 |pmid= 2256920 |doi= }}
*{{cite journal | author=Mornet E, Dupont J, Vitek A, White PC |title=Characterization of two genes encoding human steroid 11 beta-hydroxylase (P-450(11) beta). |journal=J. Biol. Chem. |volume=264 |issue= 35 |pages= 20961-7 |year= 1990 |pmid= 2592361 |doi= }}
*{{cite journal | author=Martsev SP, Chashchin VL, Akhrem AA |title=[Reconstruction and study of a multi-enzyme system by 11 beta-hydroxylase steroids] |journal=Biokhimiia |volume=50 |issue= 2 |pages= 243-57 |year= 1985 |pmid= 3872685 |doi= }}
*{{cite journal | author=Shizuta Y, Kawamoto T, Mitsuuchi Y, ''et al.'' |title=Inborn errors of aldosterone biosynthesis in humans. |journal=Steroids |volume=60 |issue= 1 |pages= 15-21 |year= 1995 |pmid= 7792802 |doi= }}
*{{cite journal | author=Mitsuuchi Y, Kawamoto T, Miyahara K, ''et al.'' |title=Congenitally defective aldosterone biosynthesis in humans: inactivation of the P-450C18 gene (CYP11B2) due to nucleotide deletion in CMO I deficient patients. |journal=Biochem. Biophys. Res. Commun. |volume=190 |issue= 3 |pages= 864-9 |year= 1993 |pmid= 8439335 |doi= }}
*{{cite journal | author=Fardella CE, Rodriguez H, Montero J, ''et al.'' |title=Genetic variation in P450c11AS in Chilean patients with low renin hypertension. |journal=J. Clin. Endocrinol. Metab. |volume=81 |issue= 12 |pages= 4347-51 |year= 1997 |pmid= 8954040 |doi= }}
*{{cite journal | author=Nomoto S, Massa G, Mitani F, ''et al.'' |title=CMO I deficiency caused by a point mutation in exon 8 of the human CYP11B2 gene encoding steroid 18-hydroxylase (P450C18). |journal=Biochem. Biophys. Res. Commun. |volume=234 |issue= 2 |pages= 382-5 |year= 1997 |pmid= 9177280 |doi= }}
*{{cite journal | author=Peter M, Fawaz L, Drop SL, ''et al.'' |title=Hereditary defect in biosynthesis of aldosterone: aldosterone synthase deficiency 1964-1997. |journal=J. Clin. Endocrinol. Metab. |volume=82 |issue= 11 |pages= 3525-8 |year= 1997 |pmid= 9360501 |doi= }}
*{{cite journal | author=Taymans SE, Pack S, Pak E, ''et al.'' |title=Human CYP11B2 (aldosterone synthase) maps to chromosome 8q24.3. |journal=J. Clin. Endocrinol. Metab. |volume=83 |issue= 3 |pages= 1033-6 |year= 1998 |pmid= 9506770 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DEFB4... {November 14, 2007 2:20:17 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:20:56 PM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_DEFB4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1e4q.
| PDB = {{PDB2|1e4q}}, {{PDB2|1fd3}}, {{PDB2|1fd4}}, {{PDB2|1fqq}}
| Name = Defensin, beta 4
| HGNCid = 2767
| Symbol = DEFB4
| AltSymbols =; DEFB-2; DEFB102; DEFB2; HBD-2; SAP1
| OMIM = 602215
| ECnumber =
| Homologene = 87854
| MGIid =
| Function =
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1673
| Hs_Ensembl =
| Hs_RefseqProtein = NP_004933
| Hs_RefseqmRNA = NM_004942
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Defensin, beta 4''', also known as '''DEFB4''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 4, an antibiotic peptide which is locally regulated by inflammation.<ref>{{cite web | title = Entrez Gene: DEFB4 defensin, beta 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1673| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Weinberg A, Krisanaprakornkit S, Dale BA |title=Epithelial antimicrobial peptides: review and significance for oral applications. |journal=Crit. Rev. Oral Biol. Med. |volume=9 |issue= 4 |pages= 399-414 |year= 1999 |pmid= 9825219 |doi= }}
*{{cite journal | author=Schröder JM, Harder J |title=Human beta-defensin-2. |journal=Int. J. Biochem. Cell Biol. |volume=31 |issue= 6 |pages= 645-51 |year= 1999 |pmid= 10404637 |doi= }}
*{{cite journal | author=Harder J, Bartels J, Christophers E, Schröder JM |title=A peptide antibiotic from human skin. |journal=Nature |volume=387 |issue= 6636 |pages= 861 |year= 1997 |pmid= 9202117 |doi= 10.1038/43088 }}
*{{cite journal | author=Bals R, Wang X, Wu Z, ''et al.'' |title=Human beta-defensin 2 is a salt-sensitive peptide antibiotic expressed in human lung. |journal=J. Clin. Invest. |volume=102 |issue= 5 |pages= 874-80 |year= 1998 |pmid= 9727055 |doi= }}
*{{cite journal | author=Liu L, Wang L, Jia HP, ''et al.'' |title=Structure and mapping of the human beta-defensin HBD-2 gene and its expression at sites of inflammation. |journal=Gene |volume=222 |issue= 2 |pages= 237-44 |year= 1999 |pmid= 9831658 |doi= }}
*{{cite journal | author=Mathews M, Jia HP, Guthmiller JM, ''et al.'' |title=Production of beta-defensin antimicrobial peptides by the oral mucosa and salivary glands. |journal=Infect. Immun. |volume=67 |issue= 6 |pages= 2740-5 |year= 1999 |pmid= 10338476 |doi= }}
*{{cite journal | author=Jia HP, Mills JN, Barahmand-Pour F, ''et al.'' |title=Molecular cloning and characterization of rat genes encoding homologues of human beta-defensins. |journal=Infect. Immun. |volume=67 |issue= 9 |pages= 4827-33 |year= 1999 |pmid= 10456937 |doi= }}
*{{cite journal | author=Yang D, Chertov O, Bykovskaia SN, ''et al.'' |title=Beta-defensins: linking innate and adaptive immunity through dendritic and T cell CCR6. |journal=Science |volume=286 |issue= 5439 |pages= 525-8 |year= 1999 |pmid= 10521347 |doi= }}
*{{cite journal | author=Diamond G, Kaiser V, Rhodes J, ''et al.'' |title=Transcriptional regulation of beta-defensin gene expression in tracheal epithelial cells. |journal=Infect. Immun. |volume=68 |issue= 1 |pages= 113-9 |year= 2000 |pmid= 10603376 |doi= }}
*{{cite journal | author=Harder J, Meyer-Hoffert U, Teran LM, ''et al.'' |title=Mucoid Pseudomonas aeruginosa, TNF-alpha, and IL-1beta, but not IL-6, induce human beta-defensin-2 in respiratory epithelia. |journal=Am. J. Respir. Cell Mol. Biol. |volume=22 |issue= 6 |pages= 714-21 |year= 2000 |pmid= 10837369 |doi= }}
*{{cite journal | author=Hoover DM, Rajashankar KR, Blumenthal R, ''et al.'' |title=The structure of human beta-defensin-2 shows evidence of higher order oligomerization. |journal=J. Biol. Chem. |volume=275 |issue= 42 |pages= 32911-8 |year= 2000 |pmid= 10906336 |doi= 10.1074/jbc.M006098200 }}
*{{cite journal | author=Meyer JE, Harder J, Görögh T, ''et al.'' |title=[hBD-2 gene expression in nasal mucosa] |journal=Laryngorhinootologie |volume=79 |issue= 7 |pages= 400-3 |year= 2000 |pmid= 11005092 |doi= }}
*{{cite journal | author=Ali RS, Falconer A, Ikram M, ''et al.'' |title=Expression of the peptide antibiotics human beta defensin-1 and human beta defensin-2 in normal human skin. |journal=J. Invest. Dermatol. |volume=117 |issue= 1 |pages= 106-11 |year= 2001 |pmid= 11442756 |doi= 10.1046/j.0022-202x.2001.01401.x }}
*{{cite journal | author=Carothers DG, Graham SM, Jia HP, ''et al.'' |title=Production of beta-defensin antimicrobial peptides by maxillary sinus mucosa. |journal=American journal of rhinology |volume=15 |issue= 3 |pages= 175-9 |year= 2001 |pmid= 11453504 |doi= }}
*{{cite journal | author=Biragyn A, Surenhu M, Yang D, ''et al.'' |title=Mediators of innate immunity that target immature, but not mature, dendritic cells induce antitumor immunity when genetically fused with nonimmunogenic tumor antigens. |journal=J. Immunol. |volume=167 |issue= 11 |pages= 6644-53 |year= 2002 |pmid= 11714836 |doi= }}
*{{cite journal | author=Bauer F, Schweimer K, Klüver E, ''et al.'' |title=Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity. |journal=Protein Sci. |volume=10 |issue= 12 |pages= 2470-9 |year= 2002 |pmid= 11714914 |doi= }}
*{{cite journal | author=Takahashi A, Wada A, Ogushi K, ''et al.'' |title=Production of beta-defensin-2 by human colonic epithelial cells induced by Salmonella enteritidis flagella filament structural protein. |journal=FEBS Lett. |volume=508 |issue= 3 |pages= 484-8 |year= 2001 |pmid= 11728477 |doi= }}
*{{cite journal | author=Schibli DJ, Hunter HN, Aseyev V, ''et al.'' |title=The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus. |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8279-89 |year= 2002 |pmid= 11741980 |doi= 10.1074/jbc.M108830200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FCGR2A... {November 14, 2007 2:20:56 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:21:48 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FCGR2A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fcg.
| PDB = {{PDB2|1fcg}}, {{PDB2|1h9v}}, {{PDB2|2fcb}}
| Name = Fc fragment of IgG, low affinity IIa, receptor (CD32)
| HGNCid = 3616
| Symbol = FCGR2A
| AltSymbols =; CD32; CD32A; CDw32; FCG2; FCGR2; FCGR2A1; FcGR; IGFR2; MGC23887; MGC30032
| OMIM = 146790
| ECnumber =
| Homologene = 47936
| MGIid = 95500
| GeneAtlas_image1 = PBB_GE_FCGR2A_203561_at_tn.png
| GeneAtlas_image2 = PBB_GE_FCGR2A_210992_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_FCGR2A_211395_x_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:0019864 |text = IgG binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2212
| Hs_Ensembl = ENSG00000143226
| Hs_RefseqProtein = XP_001129584
| Hs_RefseqmRNA = XM_001129584
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 159741844
| Hs_GenLoc_end = 159755982
| Hs_Uniprot = P12318
| Mm_EntrezGene = 14131
| Mm_Ensembl = ENSMUSG00000059498
| Mm_RefseqmRNA = NM_010188
| Mm_RefseqProtein = NP_034318
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 172887850
| Mm_GenLoc_end = 172896037
| Mm_Uniprot = Q5D5I8
}}
}}
'''Fc fragment of IgG, low affinity IIa, receptor (CD32)''', also known as '''FCGR2A''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=McKenzie SE |title=Humanized mouse models of FcR clearance in immune platelet disorders. |journal=Blood Rev. |volume=16 |issue= 1 |pages= 3-5 |year= 2002 |pmid= 11913983 |doi= 10.1054/blre.2001.0170 }}
*{{cite journal | author=Ernst LK, van de Winkel JG, Chiu IM, Anderson CL |title=Three genes for the human high affinity Fc receptor for IgG (Fc gamma RI) encode four distinct transcription products. |journal=J. Biol. Chem. |volume=267 |issue= 22 |pages= 15692-700 |year= 1992 |pmid= 1379234 |doi= }}
*{{cite journal | author=Qiu WQ, de Bruin D, Brownstein BH, ''et al.'' |title=Organization of the human and mouse low-affinity Fc gamma R genes: duplication and recombination. |journal=Science |volume=248 |issue= 4956 |pages= 732-5 |year= 1990 |pmid= 2139735 |doi= }}
*{{cite journal | author=Seki T |title=Identification of multiple isoforms of the low-affinity human IgG Fc receptor. |journal=Immunogenetics |volume=30 |issue= 1 |pages= 5-12 |year= 1989 |pmid= 2526077 |doi= }}
*{{cite journal | author=Hessian PA, Highton J, Palmer DG |title=Quantification of macrophage cell surface molecules in rheumatoid arthritis. |journal=Clin. Exp. Immunol. |volume=77 |issue= 1 |pages= 47-51 |year= 1989 |pmid= 2527651 |doi= }}
*{{cite journal | author=Brooks DG, Qiu WQ, Luster AD, Ravetch JV |title=Structure and expression of human IgG FcRII(CD32). Functional heterogeneity is encoded by the alternatively spliced products of multiple genes. |journal=J. Exp. Med. |volume=170 |issue= 4 |pages= 1369-85 |year= 1989 |pmid= 2529342 |doi= }}
*{{cite journal | author=Lanier LL, Cwirla S, Yu G, ''et al.'' |title=Membrane anchoring of a human IgG Fc receptor (CD16) determined by a single amino acid. |journal=Science |volume=246 |issue= 4937 |pages= 1611-3 |year= 1990 |pmid= 2531919 |doi= }}
*{{cite journal | author=Stuart SG, Trounstine ML, Vaux DJ, ''et al.'' |title=Isolation and expression of cDNA clones encoding a human receptor for IgG (Fc gamma RII). |journal=J. Exp. Med. |volume=166 |issue= 6 |pages= 1668-84 |year= 1987 |pmid= 2824655 |doi= }}
*{{cite journal | author=Hibbs ML, Bonadonna L, Scott BM, ''et al.'' |title=Molecular cloning of a human immunoglobulin G Fc receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 7 |pages= 2240-4 |year= 1988 |pmid= 2965389 |doi= }}
*{{cite journal | author=Huizinga TW, van der Schoot CE, Jost C, ''et al.'' |title=The PI-linked receptor FcRIII is released on stimulation of neutrophils. |journal=Nature |volume=333 |issue= 6174 |pages= 667-9 |year= 1988 |pmid= 2967437 |doi= 10.1038/333667a0 }}
*{{cite journal | author=Sammartino L, Webber LM, Hogarth PM, ''et al.'' |title=Assignment of the gene coding for human FcRII (CD32) to bands q23q24 on chromosome 1. |journal=Immunogenetics |volume=28 |issue= 5 |pages= 380-1 |year= 1988 |pmid= 2971615 |doi= }}
*{{cite journal | author=Stengelin S, Stamenkovic I, Seed B |title=Isolation of cDNAs for two distinct human Fc receptors by ligand affinity cloning. |journal=EMBO J. |volume=7 |issue= 4 |pages= 1053-9 |year= 1988 |pmid= 3402431 |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=Chacko GW, Brandt JT, Coggeshall KM, Anderson CL |title=Phosphoinositide 3-kinase and p72syk noncovalently associate with the low affinity Fc gamma receptor on human platelets through an immunoreceptor tyrosine-based activation motif. Reconstitution with synthetic phosphopeptides. |journal=J. Biol. Chem. |volume=271 |issue= 18 |pages= 10775-81 |year= 1996 |pmid= 8631888 |doi= }}
*{{cite journal | author=Salmon JE, Millard S, Schachter LA, ''et al.'' |title=Fc gamma RIIA alleles are heritable risk factors for lupus nephritis in African Americans. |journal=J. Clin. Invest. |volume=97 |issue= 5 |pages= 1348-54 |year= 1996 |pmid= 8636449 |doi= }}
*{{cite journal | author=Bewarder N, Weinrich V, Budde P, ''et al.'' |title=In vivo and in vitro specificity of protein tyrosine kinases for immunoglobulin G receptor (FcgammaRII) phosphorylation. |journal=Mol. Cell. Biol. |volume=16 |issue= 9 |pages= 4735-43 |year= 1996 |pmid= 8756631 |doi= }}
*{{cite journal | author=Sármay G, Koncz G, Gergely J |title=Human type II Fcgamma receptors inhibit B cell activation by interacting with the p21(ras)-dependent pathway. |journal=J. Biol. Chem. |volume=271 |issue= 48 |pages= 30499-504 |year= 1997 |pmid= 8940017 |doi= }}
*{{cite journal | author=Ibarrola I, Vossebeld PJ, Homburg CH, ''et al.'' |title=Influence of tyrosine phosphorylation on protein interaction with FcgammaRIIa. |journal=Biochim. Biophys. Acta |volume=1357 |issue= 3 |pages= 348-58 |year= 1997 |pmid= 9268059 |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=De SK, Venkateshan CN, Seth P, ''et al.'' |title=Adenovirus-mediated human immunodeficiency virus-1 Nef expression in human monocytes/macrophages and effect of Nef on downmodulation of Fcgamma receptors and expression of monokines. |journal=Blood |volume=91 |issue= 6 |pages= 2108-17 |year= 1998 |pmid= 9490697 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GATA1... {November 14, 2007 2:21:48 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:22:26 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GATA1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gnf.
| PDB = {{PDB2|1gnf}}, {{PDB2|1y0j}}
| Name = GATA binding protein 1 (globin transcription factor 1)
| HGNCid = 4170
| Symbol = GATA1
| AltSymbols =; ERYF1; GF1; NFE1
| OMIM = 305371
| ECnumber =
| Homologene = 1549
| MGIid = 95661
| GeneAtlas_image1 = PBB_GE_GATA1_210446_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2623
| Hs_Ensembl = ENSG00000102145
| Hs_RefseqProtein = NP_002040
| Hs_RefseqmRNA = NM_002049
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 48529906
| Hs_GenLoc_end = 48537660
| Hs_Uniprot = P15976
| Mm_EntrezGene = 14460
| Mm_Ensembl = ENSMUSG00000031162
| Mm_RefseqmRNA = NM_008089
| Mm_RefseqProtein = NP_032115
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 7116225
| Mm_GenLoc_end = 7124835
| Mm_Uniprot = Q3UIH9
}}
}}
'''GATA binding protein 1 (globin transcription factor 1)''', also known as '''GATA1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein which belongs to the GATA family of transcription factors. The protein plays an important role in erythroid development by regulating the switch of fetal hemoglobin to adult hemoglobin. Mutations in this gene have been associated with X-linked dyserythropoietic anemia and thrombocytopenia.<ref>{{cite web | title = Entrez Gene: GATA1 GATA binding protein 1 (globin transcription factor 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2623| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ohneda K, Yamamoto M |title=Roles of hematopoietic transcription factors GATA-1 and GATA-2 in the development of red blood cell lineage. |journal=Acta Haematol. |volume=108 |issue= 4 |pages= 237-45 |year= 2003 |pmid= 12432220 |doi= }}
*{{cite journal | author=Gurbuxani S, Vyas P, Crispino JD |title=Recent insights into the mechanisms of myeloid leukemogenesis in Down syndrome. |journal=Blood |volume=103 |issue= 2 |pages= 399-406 |year= 2004 |pmid= 14512321 |doi= 10.1182/blood-2003-05-1556 }}
*{{cite journal | author=Muntean AG, Ge Y, Taub JW, Crispino JD |title=Transcription factor GATA-1 and Down syndrome leukemogenesis. |journal=Leuk. Lymphoma |volume=47 |issue= 6 |pages= 986-97 |year= 2007 |pmid= 16840187 |doi= 10.1080/10428190500485810 }}
*{{cite journal | author=Caiulo A, Nicolis S, Bianchi P, ''et al.'' |title=Mapping the gene encoding the human erythroid transcriptional factor NFE1-GF1 to Xp11.23. |journal=Hum. Genet. |volume=86 |issue= 4 |pages= 388-90 |year= 1991 |pmid= 1999341 |doi= }}
*{{cite journal | author=Trainor CD, Evans T, Felsenfeld G, Boguski MS |title=Structure and evolution of a human erythroid transcription factor. |journal=Nature |volume=343 |issue= 6253 |pages= 92-6 |year= 1990 |pmid= 2104960 |doi= 10.1038/343092a0 }}
*{{cite journal | author=Zon LI, Tsai SF, Burgess S, ''et al.'' |title=The major human erythroid DNA-binding protein (GF-1): primary sequence and localization of the gene to the X chromosome. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 2 |pages= 668-72 |year= 1990 |pmid= 2300555 |doi= }}
*{{cite journal | author=Martin DI, Tsai SF, Orkin SH |title=Increased gamma-globin expression in a nondeletion HPFH mediated by an erythroid-specific DNA-binding factor. |journal=Nature |volume=338 |issue= 6214 |pages= 435-8 |year= 1989 |pmid= 2467208 |doi= 10.1038/338435a0 }}
*{{cite journal | author=Osada H, Grutz G, Axelson H, ''et al.'' |title=Association of erythroid transcription factors: complexes involving the LIM protein RBTN2 and the zinc-finger protein GATA1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 21 |pages= 9585-9 |year= 1995 |pmid= 7568177 |doi= }}
*{{cite journal | author=Mouthon MA, Bernard O, Mitjavila MT, ''et al.'' |title=Expression of tal-1 and GATA-binding proteins during human hematopoiesis. |journal=Blood |volume=81 |issue= 3 |pages= 647-55 |year= 1993 |pmid= 7678994 |doi= }}
*{{cite journal | author=Zon LI, Yamaguchi Y, Yee K, ''et al.'' |title=Expression of mRNA for the GATA-binding proteins in human eosinophils and basophils: potential role in gene transcription. |journal=Blood |volume=81 |issue= 12 |pages= 3234-41 |year= 1993 |pmid= 8507862 |doi= }}
*{{cite journal | author=Tsang AP, Visvader JE, Turner CA, ''et al.'' |title=FOG, a multitype zinc finger protein, acts as a cofactor for transcription factor GATA-1 in erythroid and megakaryocytic differentiation. |journal=Cell |volume=90 |issue= 1 |pages= 109-19 |year= 1997 |pmid= 9230307 |doi= }}
*{{cite journal | author=Rekhtman N, Radparvar F, Evans T, Skoultchi AI |title=Direct interaction of hematopoietic transcription factors PU.1 and GATA-1: functional antagonism in erythroid cells. |journal=Genes Dev. |volume=13 |issue= 11 |pages= 1398-411 |year= 1999 |pmid= 10364157 |doi= }}
*{{cite journal | author=Holmes M, Turner J, Fox A, ''et al.'' |title=hFOG-2, a novel zinc finger protein, binds the co-repressor mCtBP2 and modulates GATA-mediated activation. |journal=J. Biol. Chem. |volume=274 |issue= 33 |pages= 23491-8 |year= 1999 |pmid= 10438528 |doi= }}
*{{cite journal | author=Nichols KE, Crispino JD, Poncz M, ''et al.'' |title=Familial dyserythropoietic anaemia and thrombocytopenia due to an inherited mutation in GATA1. |journal=Nat. Genet. |volume=24 |issue= 3 |pages= 266-70 |year= 2000 |pmid= 10700180 |doi= 10.1038/73480 }}
*{{cite journal | author=Freson K, Devriendt K, Matthijs G, ''et al.'' |title=Platelet characteristics in patients with X-linked macrothrombocytopenia because of a novel GATA1 mutation. |journal=Blood |volume=98 |issue= 1 |pages= 85-92 |year= 2001 |pmid= 11418466 |doi= }}
*{{cite journal | author=Mehaffey MG, Newton AL, Gandhi MJ, ''et al.'' |title=X-linked thrombocytopenia caused by a novel mutation of GATA-1. |journal=Blood |volume=98 |issue= 9 |pages= 2681-8 |year= 2001 |pmid= 11675338 |doi= }}
*{{cite journal | author=Crawford SE, Qi C, Misra P, ''et al.'' |title=Defects of the heart, eye, and megakaryocytes in peroxisome proliferator activator receptor-binding protein (PBP) null embryos implicate GATA family of transcription factors. |journal=J. Biol. Chem. |volume=277 |issue= 5 |pages= 3585-92 |year= 2002 |pmid= 11724781 |doi= 10.1074/jbc.M107995200 }}
*{{cite journal | author=Freson K, Matthijs G, Thys C, ''et al.'' |title=Different substitutions at residue D218 of the X-linked transcription factor GATA1 lead to altered clinical severity of macrothrombocytopenia and anemia and are associated with variable skewed X inactivation. |journal=Hum. Mol. Genet. |volume=11 |issue= 2 |pages= 147-52 |year= 2002 |pmid= 11809723 |doi= }}
*{{cite journal | author=Molete JM, Petrykowska H, Sigg M, ''et al.'' |title=Functional and binding studies of HS3.2 of the beta-globin locus control region. |journal=Gene |volume=283 |issue= 1-2 |pages= 185-97 |year= 2002 |pmid= 11867225 |doi= }}
*{{cite journal | author=Hirasawa R, Shimizu R, Takahashi S, ''et al.'' |title=Essential and instructive roles of GATA factors in eosinophil development. |journal=J. Exp. Med. |volume=195 |issue= 11 |pages= 1379-86 |year= 2002 |pmid= 12045236 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GNAI1... {November 14, 2007 2:22:26 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:22:57 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GNAI1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1agr.
| PDB = {{PDB2|1agr}}, {{PDB2|1as0}}, {{PDB2|1as2}}, {{PDB2|1as3}}, {{PDB2|1bh2}}, {{PDB2|1bof}}, {{PDB2|1cip}}, {{PDB2|1gdd}}, {{PDB2|1gfi}}, {{PDB2|1gg2}}, {{PDB2|1gia}}, {{PDB2|1gil}}, {{PDB2|1git}}, {{PDB2|1gp2}}, {{PDB2|1kjy}}, {{PDB2|1svk}}, {{PDB2|1svs}}, {{PDB2|1y3a}}, {{PDB2|2g83}}, {{PDB2|2gtp}}, {{PDB2|2hlb}}, {{PDB2|2ihb}}, {{PDB2|2ik8}}, {{PDB2|2ode}}
| Name = Guanine nucleotide binding protein (G protein), alpha inhibiting activity polypeptide 1
| HGNCid = 4384
| Symbol = GNAI1
| AltSymbols =; Gi
| OMIM = 139310
| ECnumber =
| Homologene = 74417
| MGIid = 95771
| GeneAtlas_image1 = PBB_GE_GNAI1_209576_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005834 |text = heterotrimeric G-protein complex}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2770
| Hs_Ensembl = ENSG00000127955
| Hs_RefseqProtein = NP_002060
| Hs_RefseqmRNA = NM_002069
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 79602076
| Hs_GenLoc_end = 79686655
| Hs_Uniprot = P63096
| Mm_EntrezGene = 14677
| Mm_Ensembl = ENSMUSG00000057614
| Mm_RefseqmRNA = NM_010305
| Mm_RefseqProtein = NP_034435
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 17776959
| Mm_GenLoc_end = 17872237
| Mm_Uniprot =
}}
}}
'''Guanine nucleotide binding protein (G protein), alpha inhibiting activity polypeptide 1''', also known as '''GNAI1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sidhu A, Niznik HB |title=Coupling of dopamine receptor subtypes to multiple and diverse G proteins. |journal=Int. J. Dev. Neurosci. |volume=18 |issue= 7 |pages= 669-77 |year= 2000 |pmid= 10978845 |doi= }}
*{{cite journal | author=Brown EJ, Frazier WA |title=Integrin-associated protein (CD47) and its ligands. |journal=Trends Cell Biol. |volume=11 |issue= 3 |pages= 130-5 |year= 2001 |pmid= 11306274 |doi= }}
*{{cite journal | author=Raymond JR, Mukhin YV, Gelasco A, ''et al.'' |title=Multiplicity of mechanisms of serotonin receptor signal transduction. |journal=Pharmacol. Ther. |volume=92 |issue= 2-3 |pages= 179-212 |year= 2002 |pmid= 11916537 |doi= }}
*{{cite journal | author=Jiang M, Pandey S, Tran VT, Fong HK |title=Guanine nucleotide-binding regulatory proteins in retinal pigment epithelial cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 9 |pages= 3907-11 |year= 1991 |pmid= 1902575 |doi= }}
*{{cite journal | author=Gennity JM, Siess W |title=Thrombin inhibits the pertussis-toxin-dependent ADP-ribosylation of a novel soluble Gi-protein in human platelets. |journal=Biochem. J. |volume=279 ( Pt 3) |issue= |pages= 643-50 |year= 1991 |pmid= 1953657 |doi= }}
*{{cite journal | author=Itoh H, Toyama R, Kozasa T, ''et al.'' |title=Presence of three distinct molecular species of Gi protein alpha subunit. Structure of rat cDNAs and human genomic DNAs. |journal=J. Biol. Chem. |volume=263 |issue= 14 |pages= 6656-64 |year= 1988 |pmid= 2834384 |doi= }}
*{{cite journal | author=Bray P, Carter A, Guo V, ''et al.'' |title=Human cDNA clones for an alpha subunit of Gi signal-transduction protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 15 |pages= 5115-9 |year= 1987 |pmid= 3110783 |doi= }}
*{{cite journal | author=Bloch DB, Bloch KD, Iannuzzi M, ''et al.'' |title=The gene for the alpha i1 subunit of human guanine nucleotide binding protein maps near the cystic fibrosis locus. |journal=Am. J. Hum. Genet. |volume=42 |issue= 6 |pages= 884-8 |year= 1988 |pmid= 3130752 |doi= }}
*{{cite journal | author=Nagata K, Katada T, Tohkin M, ''et al.'' |title=GTP-binding proteins in human platelet membranes serving as the specific substrate of islet-activating protein, pertussis toxin. |journal=FEBS Lett. |volume=237 |issue= 1-2 |pages= 113-7 |year= 1988 |pmid= 3139448 |doi= }}
*{{cite journal | author=Kagimoto S, Yamada Y, Kubota A, ''et al.'' |title=Human somatostatin receptor, SSTR2, is coupled to adenylyl cyclase in the presence of Gi alpha 1 protein. |journal=Biochem. Biophys. Res. Commun. |volume=202 |issue= 2 |pages= 1188-95 |year= 1994 |pmid= 7914078 |doi= 10.1006/bbrc.1994.2054 }}
*{{cite journal | author=Nitta K, Uchida K, Kawashima A, ''et al.'' |title=Identification of GTP-binding proteins in human glomeruli. |journal=Nippon Jinzo Gakkai shi |volume=36 |issue= 1 |pages= 9-12 |year= 1994 |pmid= 8107314 |doi= }}
*{{cite journal | author=Law SF, Zaina S, Sweet R, ''et al.'' |title=Gi alpha 1 selectively couples somatostatin receptor subtype 3 to adenylyl cyclase: identification of the functional domains of this alpha subunit necessary for mediating the inhibition by somatostatin of cAMP formation. |journal=Mol. Pharmacol. |volume=45 |issue= 4 |pages= 587-90 |year= 1994 |pmid= 8183236 |doi= }}
*{{cite journal | author=Europe-Finner GN, Phaneuf S, Watson SP, López Bernal A |title=Identification and expression of G-proteins in human myometrium: up-regulation of G alpha s in pregnancy. |journal=Endocrinology |volume=132 |issue= 6 |pages= 2484-90 |year= 1993 |pmid= 8504751 |doi= }}
*{{cite journal | author=Laugwitz KL, Allgeier A, Offermanns S, ''et al.'' |title=The human thyrotropin receptor: a heptahelical receptor capable of stimulating members of all four G protein families. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 1 |pages= 116-20 |year= 1996 |pmid= 8552586 |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=Lee MJ, Evans M, Hla T |title=The inducible G protein-coupled receptor edg-1 signals via the G(i)/mitogen-activated protein kinase pathway. |journal=J. Biol. Chem. |volume=271 |issue= 19 |pages= 11272-9 |year= 1996 |pmid= 8626678 |doi= }}
*{{cite journal | author=De Vries L, Elenko E, Hubler L, ''et al.'' |title=GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 26 |pages= 15203-8 |year= 1997 |pmid= 8986788 |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= }}
*{{cite journal | author=Popov S, Yu K, Kozasa T, Wilkie TM |title=The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 14 |pages= 7216-20 |year= 1997 |pmid= 9207071 |doi= }}
*{{cite journal | author=Shuey DJ, Betty M, Jones PG, ''et al.'' |title=RGS7 attenuates signal transduction through the G(alpha q) family of heterotrimeric G proteins in mammalian cells. |journal=J. Neurochem. |volume=70 |issue= 5 |pages= 1964-72 |year= 1998 |pmid= 9572280 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GNAI2... {November 14, 2007 2:22:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:23:30 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- 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 = Guanine nucleotide binding protein (G protein), alpha inhibiting activity polypeptide 2
| HGNCid = 4385
| Symbol = GNAI2
| AltSymbols =; GIP; GNAI2B; H_LUCA15.1; H_LUCA16.1
| OMIM = 139360
| ECnumber =
| Homologene = 55539
| MGIid = 95772
| GeneAtlas_image1 = PBB_GE_GNAI2_201040_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}} {{GNF_GO|id=GO:0019001 |text = guanyl nucleotide binding}}
| Component =
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007193 |text = G-protein signaling, adenylate cyclase inhibiting pathway}} {{GNF_GO|id=GO:0007194 |text = negative regulation of adenylate cyclase activity}} {{GNF_GO|id=GO:0007213 |text = acetylcholine receptor signaling, muscarinic pathway}} {{GNF_GO|id=GO:0007584 |text = response to nutrient}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2771
| Hs_Ensembl = ENSG00000114353
| Hs_RefseqProtein = NP_002061
| Hs_RefseqmRNA = NM_002070
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 50239173
| Hs_GenLoc_end = 50271775
| Hs_Uniprot = P04899
| Mm_EntrezGene = 14678
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_980919
| Mm_RefseqProtein = XP_986013
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Guanine nucleotide binding protein (G protein), alpha inhibiting activity polypeptide 2''', also known as '''GNAI2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sidhu A, Niznik HB |title=Coupling of dopamine receptor subtypes to multiple and diverse G proteins. |journal=Int. J. Dev. Neurosci. |volume=18 |issue= 7 |pages= 669-77 |year= 2000 |pmid= 10978845 |doi= }}
*{{cite journal | author=Offermanns S, Schultz G, Rosenthal W |title=Evidence for opioid receptor-mediated activation of the G-proteins, Go and Gi2, in membranes of neuroblastoma x glioma (NG108-15) hybrid cells. |journal=J. Biol. Chem. |volume=266 |issue= 6 |pages= 3365-8 |year= 1991 |pmid= 1671672 |doi= }}
*{{cite journal | author=Cormont M, Le Marchand-Brustel Y, Van Obberghen E, ''et al.'' |title=Identification of G protein alpha-subunits in RINm5F cells and their selective interaction with galanin receptor. |journal=Diabetes |volume=40 |issue= 9 |pages= 1170-6 |year= 1991 |pmid= 1718802 |doi= }}
*{{cite journal | author=Magovcevic I, Ang SL, Seidman JG, ''et al.'' |title=Regional localization of the human G protein alpha i2 (GNAI2) gene: assignment to 3p21 and a related sequence (GNAI2L) to 12p12-p13. |journal=Genomics |volume=12 |issue= 1 |pages= 125-9 |year= 1992 |pmid= 1733849 |doi= }}
*{{cite journal | author=Bushfield M, Murphy GJ, Lavan BE, ''et al.'' |title=Hormonal regulation of Gi2 alpha-subunit phosphorylation in intact hepatocytes. |journal=Biochem. J. |volume=268 |issue= 2 |pages= 449-57 |year= 1990 |pmid= 2114093 |doi= }}
*{{cite journal | author=Lyons J, Landis CA, Harsh G, ''et al.'' |title=Two G protein oncogenes in human endocrine tumors. |journal=Science |volume=249 |issue= 4969 |pages= 655-9 |year= 1990 |pmid= 2116665 |doi= }}
*{{cite journal | author=Osawa S, Dhanasekaran N, Woon CW, Johnson GL |title=G alpha i-G alpha s chimeras define the function of alpha chain domains in control of G protein activation and beta gamma subunit complex interactions. |journal=Cell |volume=63 |issue= 4 |pages= 697-706 |year= 1990 |pmid= 2121366 |doi= }}
*{{cite journal | author=McClue SJ, Milligan G |title=The alpha 2B adrenergic receptor of undifferentiated neuroblastoma x glioma hybrid NG108-15 cells, interacts directly with the guanine nucleotide binding protein, Gi2. |journal=FEBS Lett. |volume=269 |issue= 2 |pages= 430-4 |year= 1990 |pmid= 2169434 |doi= }}
*{{cite journal | author=Rudolph U, Koesling D, Hinsch KD, ''et al.'' |title=G-protein alpha-subunits in cytosolic and membranous fractions of human neutrophils. |journal=Mol. Cell. Endocrinol. |volume=63 |issue= 1-2 |pages= 143-53 |year= 1989 |pmid= 2502457 |doi= }}
*{{cite journal | author=Lang JC, Costa T |title=Distribution of the alpha-subunit of the guanine nucleotide-binding protein Gi2 and its comparison to G alpha o. |journal=J. Recept. Res. |volume=9 |issue= 4-5 |pages= 313-29 |year= 1990 |pmid= 2512386 |doi= }}
*{{cite journal | author=Itoh H, Toyama R, Kozasa T, ''et al.'' |title=Presence of three distinct molecular species of Gi protein alpha subunit. Structure of rat cDNAs and human genomic DNAs. |journal=J. Biol. Chem. |volume=263 |issue= 14 |pages= 6656-64 |year= 1988 |pmid= 2834384 |doi= }}
*{{cite journal | author=Weinstein LS, Spiegel AM, Carter AD |title=Cloning and characterization of the human gene for the alpha-subunit of Gi2, a GTP-binding signal transduction protein. |journal=FEBS Lett. |volume=232 |issue= 2 |pages= 333-40 |year= 1988 |pmid= 2837412 |doi= }}
*{{cite journal | author=Didsbury JR, Ho YS, Snyderman R |title=Human Gi protein alpha-subunit: deduction of amino acid structure from a cloned cDNA. |journal=FEBS Lett. |volume=211 |issue= 2 |pages= 160-4 |year= 1987 |pmid= 3100330 |doi= }}
*{{cite journal | author=Beals CR, Wilson CB, Perlmutter RM |title=A small multigene family encodes Gi signal-transduction proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 22 |pages= 7886-90 |year= 1987 |pmid= 3120178 |doi= }}
*{{cite journal | author=Williamson EA, Ince PG, Harrison D, ''et al.'' |title=G-protein mutations in human pituitary adrenocorticotrophic hormone-secreting adenomas. |journal=Eur. J. Clin. Invest. |volume=25 |issue= 2 |pages= 128-31 |year= 1995 |pmid= 7737262 |doi= }}
*{{cite journal | author=Takigawa M, Sakurai T, Kasuya Y, ''et al.'' |title=Molecular identification of guanine-nucleotide-binding regulatory proteins which couple to endothelin receptors. |journal=Eur. J. Biochem. |volume=228 |issue= 1 |pages= 102-8 |year= 1995 |pmid= 7882989 |doi= }}
*{{cite journal | author=Grassie MA, Milligan G |title=Analysis of the relative interactions between the alpha 2C10 adrenoceptor and the guanine-nucleotide-binding proteins G(o)1 alpha and Gi 2 alpha following co-expression of these polypeptides in rat 1 fibroblasts. |journal=Biochem. J. |volume=306 ( Pt 2) |issue= |pages= 525-30 |year= 1995 |pmid= 7887906 |doi= }}
*{{cite journal | author=Migeon JC, Thomas SL, Nathanson NM |title=Regulation of cAMP-mediated gene transcription by wild type and mutated G-protein alpha subunits. Inhibition of adenylyl cyclase activity by muscarinic receptor-activated and constitutively activated G(o) alpha. |journal=J. Biol. Chem. |volume=269 |issue= 46 |pages= 29146-52 |year= 1994 |pmid= 7961880 |doi= }}
*{{cite journal | author=Wennogle LP, Conder L, Winter C, ''et al.'' |title=Stabilization of C5a receptor--G-protein interactions through ligand binding. |journal=J. Cell. Biochem. |volume=55 |issue= 3 |pages= 380-8 |year= 1994 |pmid= 7962171 |doi= 10.1002/jcb.240550316 }}
*{{cite journal | author=Valet P, Senard JM, Devedjian JC, ''et al.'' |title=Characterization and distribution of alpha 2-adrenergic receptors in the human intestinal mucosa. |journal=J. Clin. Invest. |volume=91 |issue= 5 |pages= 2049-57 |year= 1993 |pmid= 8098045 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IAPP... {November 14, 2007 2:23:30 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:24:00 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
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_IAPP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2g48.
| PDB = {{PDB2|2g48}}
| Name = Islet amyloid polypeptide
| HGNCid = 5329
| Symbol = IAPP
| AltSymbols =; IAP; DAP; AMYLIN
| OMIM = 147940
| ECnumber =
| Homologene = 36024
| MGIid = 96382
| GeneAtlas_image1 = PBB_GE_IAPP_207062_at_tn.png
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3375
| Hs_Ensembl = ENSG00000121351
| Hs_RefseqProtein = NP_000406
| Hs_RefseqmRNA = NM_000415
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 21417085
| Hs_GenLoc_end = 21423683
| Hs_Uniprot = P10997
| Mm_EntrezGene = 15874
| Mm_Ensembl = ENSMUSG00000041681
| Mm_RefseqmRNA = NM_010491
| Mm_RefseqProtein = NP_034621
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 142255650
| Mm_GenLoc_end = 142261039
| Mm_Uniprot = P12968
}}
}}
'''Islet amyloid polypeptide''', also known as '''IAPP''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Islet, or insulinoma, amyloid polypeptide (IAPP, or amylin) is commonly found in pancreatic islets of patients suffering diabetes mellitus type II, or harboring an insulinoma. While the assosciation of amylin with the development of type II diabetes has been known for some time, a direct causative role for amylin has been harder to establish. Recent results suggest that amylin, like the related beta-amyloid (Abeta) assosciated with Alzheimer's disease, can induce apoptotic cell-death in particular cultured cells, an effect that may be relevant to the development of type II diabetes.<ref>{{cite web | title = Entrez Gene: IAPP islet amyloid polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3375| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pittner RA, Albrandt K, Beaumont K, ''et al.'' |title=Molecular physiology of amylin. |journal=J. Cell. Biochem. |volume=55 Suppl |issue= |pages= 19-28 |year= 1994 |pmid= 7929615 |doi= }}
*{{cite journal | author=Hayden MR |title=Islet amyloid, metabolic syndrome, and the natural progressive history of type 2 diabetes mellitus. |journal=JOP |volume=3 |issue= 5 |pages= 126-38 |year= 2002 |pmid= 12221327 |doi= }}
*{{cite journal | author=Westermark P, Andersson A, Westermark GT |title=Is aggregated IAPP a cause of beta-cell failure in transplanted human pancreatic islets? |journal=Curr. Diab. Rep. |volume=5 |issue= 3 |pages= 184-8 |year= 2005 |pmid= 15929864 |doi= }}
*{{cite journal | author=Höppener JW, Oosterwijk C, Visser-Vernooy HJ, ''et al.'' |title=Characterization of the human islet amyloid polypeptide/amylin gene transcripts: identification of a new polyadenylation site. |journal=Biochem. Biophys. Res. Commun. |volume=189 |issue= 3 |pages= 1569-77 |year= 1993 |pmid= 1282806 |doi= }}
*{{cite journal | author=Hubbard JA, Martin SR, Chaplin LC, ''et al.'' |title=Solution structures of calcitonin-gene-related-peptide analogues of calcitonin-gene-related peptide and amylin. |journal=Biochem. J. |volume=275 ( Pt 3) |issue= |pages= 785-8 |year= 1991 |pmid= 2039456 |doi= }}
*{{cite journal | author=Butler PC, Chou J, Carter WB, ''et al.'' |title=Effects of meal ingestion on plasma amylin concentration in NIDDM and nondiabetic humans. |journal=Diabetes |volume=39 |issue= 6 |pages= 752-6 |year= 1990 |pmid= 2189768 |doi= }}
*{{cite journal | author=van Mansfeld AD, Mosselman S, Höppener JW, ''et al.'' |title=Islet amyloid polypeptide: structure and upstream sequences of the IAPP gene in rat and man. |journal=Biochim. Biophys. Acta |volume=1087 |issue= 2 |pages= 235-40 |year= 1990 |pmid= 2223885 |doi= }}
*{{cite journal | author=Christmanson L, Rorsman F, Stenman G, ''et al.'' |title=The human islet amyloid polypeptide (IAPP) gene. Organization, chromosomal localization and functional identification of a promoter region. |journal=FEBS Lett. |volume=267 |issue= 1 |pages= 160-6 |year= 1990 |pmid= 2365085 |doi= }}
*{{cite journal | author=Clark A, Edwards CA, Ostle LR, ''et al.'' |title=Localisation of islet amyloid peptide in lipofuscin bodies and secretory granules of human B-cells and in islets of type-2 diabetic subjects. |journal=Cell Tissue Res. |volume=257 |issue= 1 |pages= 179-85 |year= 1989 |pmid= 2546670 |doi= }}
*{{cite journal | author=Nishi M, Sanke T, Seino S, ''et al.'' |title=Human islet amyloid polypeptide gene: complete nucleotide sequence, chromosomal localization, and evolutionary history. |journal=Mol. Endocrinol. |volume=3 |issue= 11 |pages= 1775-81 |year= 1990 |pmid= 2608057 |doi= }}
*{{cite journal | author=Mosselman S, Höppener JW, Lips CJ, Jansz HS |title=The complete islet amyloid polypeptide precursor is encoded by two exons. |journal=FEBS Lett. |volume=247 |issue= 1 |pages= 154-8 |year= 1989 |pmid= 2651160 |doi= }}
*{{cite journal | author=Roberts AN, Leighton B, Todd JA, ''et al.'' |title=Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 24 |pages= 9662-6 |year= 1990 |pmid= 2690069 |doi= }}
*{{cite journal | author=Westermark P, Wernstedt C, Wilander E, ''et al.'' |title=Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 11 |pages= 3881-5 |year= 1987 |pmid= 3035556 |doi= }}
*{{cite journal | author=Sanke T, Bell GI, Sample C, ''et al.'' |title=An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing. |journal=J. Biol. Chem. |volume=263 |issue= 33 |pages= 17243-6 |year= 1988 |pmid= 3053705 |doi= }}
*{{cite journal | author=Mosselman S, Höppener JW, Zandberg J, ''et al.'' |title=Islet amyloid polypeptide: identification and chromosomal localization of the human gene. |journal=FEBS Lett. |volume=239 |issue= 2 |pages= 227-32 |year= 1988 |pmid= 3181427 |doi= }}
*{{cite journal | author=Cooper GJ, Willis AC, Clark A, ''et al.'' |title=Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 23 |pages= 8628-32 |year= 1988 |pmid= 3317417 |doi= }}
*{{cite journal | author=Westermark P, Wernstedt C, Wilander E, Sletten K |title=A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas. |journal=Biochem. Biophys. Res. Commun. |volume=140 |issue= 3 |pages= 827-31 |year= 1986 |pmid= 3535798 |doi= }}
*{{cite journal | author=Lorenzo A, Razzaboni B, Weir GC, Yankner BA |title=Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus. |journal=Nature |volume=368 |issue= 6473 |pages= 756-60 |year= 1994 |pmid= 8152488 |doi= 10.1038/368756a0 }}
*{{cite journal | author=Höppener JW, Verbeek JS, de Koning EJ, ''et al.'' |title=Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia. |journal=Diabetologia |volume=36 |issue= 12 |pages= 1258-65 |year= 1994 |pmid= 8307253 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on INHBA... {November 14, 2007 2:24:00 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:24:59 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_INHBA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1nys.
| PDB = {{PDB2|1nys}}, {{PDB2|1nyu}}, {{PDB2|1s4y}}, {{PDB2|2arp}}, {{PDB2|2arv}}, {{PDB2|2b0u}}, {{PDB2|2p6a}}
| Name = Inhibin, beta A (activin A, activin AB alpha polypeptide)
| HGNCid = 6066
| Symbol = INHBA
| AltSymbols =; EDF; FRP
| OMIM = 147290
| ECnumber =
| Homologene = 1653
| MGIid = 96570
| GeneAtlas_image1 = PBB_GE_INHBA_210511_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_INHBA_204926_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005160 |text = transforming growth factor beta receptor binding}} {{GNF_GO|id=GO:0005179 |text = hormone activity}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0017106 |text = activin inhibitor activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}} {{GNF_GO|id=GO:0048184 |text = follistatin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0043509 |text = activin A complex}} {{GNF_GO|id=GO:0043512 |text = inhibin A complex}}
| Process = {{GNF_GO|id=GO:0000082 |text = G1/S transition of mitotic cell cycle}} {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0001541 |text = ovarian follicle development}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{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:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007498 |text = mesoderm development}} {{GNF_GO|id=GO:0009605 |text = response to external stimulus}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030218 |text = erythrocyte differentiation}} {{GNF_GO|id=GO:0030308 |text = negative regulation of cell growth}} {{GNF_GO|id=GO:0040007 |text = growth}} {{GNF_GO|id=GO:0042326 |text = negative regulation of phosphorylation}} {{GNF_GO|id=GO:0042541 |text = hemoglobin biosynthetic process}} {{GNF_GO|id=GO:0045077 |text = negative regulation of interferon-gamma biosynthetic process}} {{GNF_GO|id=GO:0045578 |text = negative regulation of B cell differentiation}} {{GNF_GO|id=GO:0045648 |text = positive regulation of erythrocyte differentiation}} {{GNF_GO|id=GO:0045650 |text = negative regulation of macrophage differentiation}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0046881 |text = positive regulation of follicle-stimulating hormone secretion}} {{GNF_GO|id=GO:0046882 |text = negative regulation of follicle-stimulating hormone secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3624
| Hs_Ensembl = ENSG00000122641
| Hs_RefseqProtein = NP_002183
| Hs_RefseqmRNA = NM_002192
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 41695126
| Hs_GenLoc_end = 41709231
| Hs_Uniprot = P08476
| Mm_EntrezGene = 16323
| Mm_Ensembl = ENSMUSG00000041324
| Mm_RefseqmRNA = NM_008380
| Mm_RefseqProtein = NP_032406
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 15805370
| Mm_GenLoc_end = 15818147
| Mm_Uniprot = Q3UXL8
}}
}}
'''Inhibin, beta A (activin A, activin AB alpha polypeptide)''', also known as '''INHBA''', is a human [[gene]].
<!-- 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 inhibin beta A subunit joins the alpha subunit to form a pituitary FSH secretion inhibitor. Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumor-suppressor activity. In addition, serum levels of inhibin have been shown to reflect the size of granulosa-cell tumors and can therefore be used as a marker for primary as well as recurrent disease. Because expression in gonadal and various extragonadal tissues may vary severalfold in a tissue-specific fashion, it is proposed that inhibin may be both a growth/differentiation factor and a hormone. Furthermore, the beta A subunit forms a homodimer, activin A, and also joins with a beta B subunit to form a heterodimer, activin AB, both of which stimulate FSH secretion. Finally, it has been shown that the beta A subunit mRNA is identical to the erythroid differentiation factor subunit mRNA and that only one gene for this mRNA exists in the human genome.<ref>{{cite web | title = Entrez Gene: INHBA inhibin, beta A (activin A, activin AB alpha polypeptide)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3624| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Munz B, Hübner G, Tretter Y, ''et al.'' |title=A novel role of activin in inflammation and repair. |journal=J. Endocrinol. |volume=161 |issue= 2 |pages= 187-93 |year= 1999 |pmid= 10320815 |doi= }}
*{{cite journal | author=Welt C, Sidis Y, Keutmann H, Schneyer A |title=Activins, inhibins, and follistatins: from endocrinology to signaling. A paradigm for the new millennium. |journal=Exp. Biol. Med. (Maywood) |volume=227 |issue= 9 |pages= 724-52 |year= 2002 |pmid= 12324653 |doi= }}
*{{cite journal | author=Shav-Tal Y, Zipori D |title=The role of activin a in regulation of hemopoiesis. |journal=Stem Cells |volume=20 |issue= 6 |pages= 493-500 |year= 2003 |pmid= 12456957 |doi= }}
*{{cite journal | author=Reis FM, Luisi S, Carneiro MM, ''et al.'' |title=Activin, inhibin and the human breast. |journal=Mol. Cell. Endocrinol. |volume=225 |issue= 1-2 |pages= 77-82 |year= 2005 |pmid= 15451571 |doi= 10.1016/j.mce.2004.02.016 }}
*{{cite journal | author=Shao L, Frigon NL, Young AL, ''et al.'' |title=Effect of activin A on globin gene expression in purified human erythroid progenitors. |journal=Blood |volume=79 |issue= 3 |pages= 773-81 |year= 1992 |pmid= 1310063 |doi= }}
*{{cite journal | author=Mathews LS, Vale WW |title=Expression cloning of an activin receptor, a predicted transmembrane serine kinase. |journal=Cell |volume=65 |issue= 6 |pages= 973-82 |year= 1991 |pmid= 1646080 |doi= }}
*{{cite journal | author=Tanimoto K, Handa S, Ueno N, ''et al.'' |title=Structure and sequence analysis of the human activin beta A subunit gene. |journal=DNA Seq. |volume=2 |issue= 2 |pages= 103-10 |year= 1992 |pmid= 1777673 |doi= }}
*{{cite journal | author=Mason AJ, Berkemeier LM, Schmelzer CH, Schwall RH |title=Activin B: precursor sequences, genomic structure and in vitro activities. |journal=Mol. Endocrinol. |volume=3 |issue= 9 |pages= 1352-8 |year= 1990 |pmid= 2575216 |doi= }}
*{{cite journal | author=Barton DE, Yang-Feng TL, Mason AJ, ''et al.'' |title=Mapping of genes for inhibin subunits alpha, beta A, and beta B on human and mouse chromosomes and studies of jsd mice. |journal=Genomics |volume=5 |issue= 1 |pages= 91-9 |year= 1989 |pmid= 2767687 |doi= }}
*{{cite journal | author=Murata M, Eto Y, Shibai H, ''et al.'' |title=Erythroid differentiation factor is encoded by the same mRNA as that of the inhibin beta A chain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 8 |pages= 2434-8 |year= 1988 |pmid= 3267209 |doi= }}
*{{cite journal | author=Burger HG, Igarashi M |title=Inhibin: definition and nomenclature, including related substances. |journal=Endocrinology |volume=122 |issue= 4 |pages= 1701-2 |year= 1988 |pmid= 3345731 |doi= }}
*{{cite journal | author=Mason AJ, Niall HD, Seeburg PH |title=Structure of two human ovarian inhibins. |journal=Biochem. Biophys. Res. Commun. |volume=135 |issue= 3 |pages= 957-64 |year= 1986 |pmid= 3754442 |doi= }}
*{{cite journal | author=Stewart AG, Milborrow HM, Ring JM, ''et al.'' |title=Human inhibin genes. Genomic characterisation and sequencing. |journal=FEBS Lett. |volume=206 |issue= 2 |pages= 329-34 |year= 1986 |pmid= 3758355 |doi= }}
*{{cite journal | author=Sumitomo S, Inouye S, Liu XJ, ''et al.'' |title=The heparin binding site of follistatin is involved in its interaction with activin. |journal=Biochem. Biophys. Res. Commun. |volume=208 |issue= 1 |pages= 1-9 |year= 1995 |pmid= 7887917 |doi= 10.1006/bbrc.1995.1297 }}
*{{cite journal | author=Xu J, McKeehan K, Matsuzaki K, McKeehan WL |title=Inhibin antagonizes inhibition of liver cell growth by activin by a dominant-negative mechanism. |journal=J. Biol. Chem. |volume=270 |issue= 11 |pages= 6308-13 |year= 1995 |pmid= 7890768 |doi= }}
*{{cite journal | author=Mason AJ |title=Functional analysis of the cysteine residues of activin A. |journal=Mol. Endocrinol. |volume=8 |issue= 3 |pages= 325-32 |year= 1994 |pmid= 8015550 |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=Nishihara T, Okahashi N, Ueda N |title=Activin A induces apoptotic cell death. |journal=Biochem. Biophys. Res. Commun. |volume=197 |issue= 2 |pages= 985-91 |year= 1994 |pmid= 8267637 |doi= 10.1006/bbrc.1993.2576 }}
*{{cite journal | author=ten Dijke P, Ichijo H, Franzén P, ''et al.'' |title=Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity. |journal=Oncogene |volume=8 |issue= 10 |pages= 2879-87 |year= 1993 |pmid= 8397373 |doi= }}
*{{cite journal | author=Tanimoto K, Yoshida E, Mita S, ''et al.'' |title=Human activin betaA gene. Identification of novel 5' exon, functional promoter, and enhancers. |journal=J. Biol. Chem. |volume=271 |issue= 51 |pages= 32760-9 |year= 1997 |pmid= 8955111 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IRF3... {November 14, 2007 2:24:59 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:25:27 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_IRF3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1j2f.
| PDB = {{PDB2|1j2f}}, {{PDB2|1qwt}}, {{PDB2|1t2k}}, {{PDB2|1zoq}}
| Name = Interferon regulatory factor 3
| HGNCid = 6118
| Symbol = IRF3
| AltSymbols =;
| OMIM = 603734
| ECnumber =
| Homologene = 1208
| MGIid = 1859179
| GeneAtlas_image1 = PBB_GE_IRF3_202621_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0003712 |text = transcription cofactor activity}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0009615 |text = response to virus}} {{GNF_GO|id=GO:0045351 |text = interferon type I biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3661
| Hs_Ensembl = ENSG00000126456
| Hs_RefseqProtein = NP_001562
| Hs_RefseqmRNA = NM_001571
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 54854642
| Hs_GenLoc_end = 54860926
| Hs_Uniprot = Q14653
| Mm_EntrezGene = 54131
| Mm_Ensembl = ENSMUSG00000003184
| Mm_RefseqmRNA = NM_016849
| Mm_RefseqProtein = NP_058545
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 44865702
| Mm_GenLoc_end = 44870890
| Mm_Uniprot = O54726
}}
}}
'''Interferon regulatory factor 3''', also known as '''IRF3''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = IRF3 encodes interferon regulatory factor 3, a member of the interferon regulatory transcription factor (IRF) family. IRF3 is found in an inactive cytoplasmic form that upon serine/threonine phosphorylation forms a complex with CREBBP. This complex translocates to the nucleus and activates the transcription of interferons alpha and beta, as well as other interferon-induced genes.<ref>{{cite web | title = Entrez Gene: IRF3 interferon regulatory factor 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3661| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pitha PM, Au WC, Lowther W, ''et al.'' |title=Role of the interferon regulatory factors (IRFs) in virus-mediated signaling and regulation of cell growth. |journal=Biochimie |volume=80 |issue= 8-9 |pages= 651-8 |year= 1999 |pmid= 9865487 |doi= }}
*{{cite journal | author=Yoneyama M, Suhara W, Fujita T |title=Control of IRF-3 activation by phosphorylation. |journal=J. Interferon Cytokine Res. |volume=22 |issue= 1 |pages= 73-6 |year= 2002 |pmid= 11846977 |doi= 10.1089/107999002753452674 }}
*{{cite journal | author=Au WC, Moore PA, Lowther W, ''et al.'' |title=Identification of a member of the interferon regulatory factor family that binds to the interferon-stimulated response element and activates expression of interferon-induced genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 25 |pages= 11657-61 |year= 1996 |pmid= 8524823 |doi= }}
*{{cite journal | author=Yoneyama M, Suhara W, Fukuhara Y, ''et al.'' |title=Direct triggering of the type I interferon system by virus infection: activation of a transcription factor complex containing IRF-3 and CBP/p300. |journal=EMBO J. |volume=17 |issue= 4 |pages= 1087-95 |year= 1998 |pmid= 9463386 |doi= 10.1093/emboj/17.4.1087 }}
*{{cite journal | author=Weaver BK, Kumar KP, Reich NC |title=Interferon regulatory factor 3 and CREB-binding protein/p300 are subunits of double-stranded RNA-activated transcription factor DRAF1. |journal=Mol. Cell. Biol. |volume=18 |issue= 3 |pages= 1359-68 |year= 1998 |pmid= 9488451 |doi= }}
*{{cite journal | author=Lin R, Heylbroeck C, Pitha PM, Hiscott J |title=Virus-dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential, and proteasome-mediated degradation. |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 2986-96 |year= 1998 |pmid= 9566918 |doi= }}
*{{cite journal | author=Ronco LV, Karpova AY, Vidal M, Howley PM |title=Human papillomavirus 16 E6 oncoprotein binds to interferon regulatory factor-3 and inhibits its transcriptional activity. |journal=Genes Dev. |volume=12 |issue= 13 |pages= 2061-72 |year= 1998 |pmid= 9649509 |doi= }}
*{{cite journal | author=Bellingham J, Gregory-Evans K, Gregory-Evans CY |title=Mapping of human interferon regulatory factor 3 (IRF3) to chromosome 19q13.3-13.4 by an intragenic polymorphic marker. |journal=Ann. Hum. Genet. |volume=62 |issue= Pt 3 |pages= 231-4 |year= 1999 |pmid= 9803267 |doi= 10.1046/j.1469-1809.1998.6230231.x }}
*{{cite journal | author=Lowther WJ, Moore PA, Carter KC, Pitha PM |title=Cloning and functional analysis of the human IRF-3 promoter. |journal=DNA Cell Biol. |volume=18 |issue= 9 |pages= 685-92 |year= 1999 |pmid= 10492399 |doi= 10.1089/104454999314962 }}
*{{cite journal | author=Kim T, Kim TY, Song YH, ''et al.'' |title=Activation of interferon regulatory factor 3 in response to DNA-damaging agents. |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 30686-9 |year= 1999 |pmid= 10521456 |doi= }}
*{{cite journal | author=Kumar KP, McBride KM, Weaver BK, ''et al.'' |title=Regulated nuclear-cytoplasmic localization of interferon regulatory factor 3, a subunit of double-stranded RNA-activated factor 1. |journal=Mol. Cell. Biol. |volume=20 |issue= 11 |pages= 4159-68 |year= 2000 |pmid= 10805757 |doi= }}
*{{cite journal | author=Suhara W, Yoneyama M, Iwamura T, ''et al.'' |title=Analyses of virus-induced homomeric and heteromeric protein associations between IRF-3 and coactivator CBP/p300. |journal=J. Biochem. |volume=128 |issue= 2 |pages= 301-7 |year= 2000 |pmid= 10920266 |doi= }}
*{{cite journal | author=Servant MJ, ten Oever B, LePage C, ''et al.'' |title=Identification of distinct signaling pathways leading to the phosphorylation of interferon regulatory factor 3. |journal=J. Biol. Chem. |volume=276 |issue= 1 |pages= 355-63 |year= 2001 |pmid= 11035028 |doi= 10.1074/jbc.M007790200 }}
*{{cite journal | author=Smith EJ, Marié I, Prakash A, ''et al.'' |title=IRF3 and IRF7 phosphorylation in virus-infected cells does not require double-stranded RNA-dependent protein kinase R or Ikappa B kinase but is blocked by Vaccinia virus E3L protein. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 8951-7 |year= 2001 |pmid= 11124948 |doi= 10.1074/jbc.M008717200 }}
*{{cite journal | author=Au WC, Yeow WS, Pitha PM |title=Analysis of functional domains of interferon regulatory factor 7 and its association with IRF-3. |journal=Virology |volume=280 |issue= 2 |pages= 273-82 |year= 2001 |pmid= 11162841 |doi= 10.1006/viro.2000.0782 }}
*{{cite journal | author=Barnes BJ, Moore PA, Pitha PM |title=Virus-specific activation of a novel interferon regulatory factor, IRF-5, results in the induction of distinct interferon alpha genes. |journal=J. Biol. Chem. |volume=276 |issue= 26 |pages= 23382-90 |year= 2001 |pmid= 11303025 |doi= 10.1074/jbc.M101216200 }}
*{{cite journal | author=Mach CM, Hargrove BW, Kunkel GR |title=The Small RNA gene activator protein, SphI postoctamer homology-binding factor/selenocysteine tRNA gene transcription activating factor, stimulates transcription of the human interferon regulatory factor-3 gene. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 4853-8 |year= 2002 |pmid= 11724783 |doi= 10.1074/jbc.M108308200 }}
*{{cite journal | author=Morin P, Bragança J, Bandu MT, ''et al.'' |title=Preferential binding sites for interferon regulatory factors 3 and 7 involved in interferon-A gene transcription. |journal=J. Mol. Biol. |volume=316 |issue= 5 |pages= 1009-22 |year= 2002 |pmid= 11884139 |doi= 10.1006/jmbi.2001.5401 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MAP2K2... {November 14, 2007 2:27:10 PM PST}
- SEARCH REDIRECT: Control Box Found: MAP2K2 {November 14, 2007 2:27:48 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 2:27:49 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 2:27:49 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 2:27:49 PM PST}
- UPDATED: Updated protein page: MAP2K2 {November 14, 2007 2:27:58 PM PST}
- INFO: Beginning work on MAP3K7... {November 14, 2007 2:27:58 PM PST}
- SEARCH REDIRECT: Control Box Found: MAP3K7 {November 14, 2007 2:29:05 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 2:29:07 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 2:29:07 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 2:29:07 PM PST}
- UPDATED: Updated protein page: MAP3K7 {November 14, 2007 2:29:13 PM PST}
- INFO: Beginning work on NGFR... {November 14, 2007 2:25:28 PM PST}
- SEARCH REDIRECT: Control Box Found: NGFR {November 14, 2007 2:25:57 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 2:25:58 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 2:25:58 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 2:25:58 PM PST}
- UPDATED: Updated protein page: NGFR {November 14, 2007 2:26:05 PM PST}
- INFO: Beginning work on PIN1... {November 14, 2007 2:26:05 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:26:39 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PIN1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1f8a.
| PDB = {{PDB2|1f8a}}, {{PDB2|1i6c}}, {{PDB2|1i8g}}, {{PDB2|1i8h}}, {{PDB2|1nmv}}, {{PDB2|1nmw}}, {{PDB2|1pin}}, {{PDB2|1zcn}}, {{PDB2|2f21}}, {{PDB2|2iti}}, {{PDB2|2itk}}
| Name = Protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1
| HGNCid = 8988
| Symbol = PIN1
| AltSymbols =; DOD; UBL5
| OMIM = 601052
| ECnumber =
| Homologene = 4531
| MGIid = 1346036
| GeneAtlas_image1 = PBB_GE_PIN1_202927_at_tn.png
| Function = {{GNF_GO|id=GO:0003755 |text = peptidyl-prolyl cis-trans isomerase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016853 |text = isomerase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007088 |text = regulation of mitosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5300
| Hs_Ensembl = ENSG00000127445
| Hs_RefseqProtein = NP_006212
| Hs_RefseqmRNA = NM_006221
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 9806999
| Hs_GenLoc_end = 9821359
| Hs_Uniprot = Q13526
| Mm_EntrezGene = 23988
| Mm_Ensembl = ENSMUSG00000032171
| Mm_RefseqmRNA = NM_023371
| Mm_RefseqProtein = NP_075860
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 20402532
| Mm_GenLoc_end = 20416986
| Mm_Uniprot = Q3UTI7
}}
}}
'''Protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1''', also known as '''PIN1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lu KP, Liou YC, Zhou XZ |title=Pinning down proline-directed phosphorylation signaling. |journal=Trends Cell Biol. |volume=12 |issue= 4 |pages= 164-72 |year= 2002 |pmid= 11978535 |doi= }}
*{{cite journal | author=Wulf G, Finn G, Suizu F, Lu KP |title=Phosphorylation-specific prolyl isomerization: is there an underlying theme? |journal=Nat. Cell Biol. |volume=7 |issue= 5 |pages= 435-41 |year= 2005 |pmid= 15867923 |doi= 10.1038/ncb0505-435 }}
*{{cite journal | author=Etzkorn FA |title=Pin1 flips Alzheimer's switch. |journal=ACS Chem. Biol. |volume=1 |issue= 4 |pages= 214-6 |year= 2007 |pmid= 17163675 |doi= 10.1021/cb600171g }}
*{{cite journal | author=Balastik M, Lim J, Pastorino L, Lu KP |title=Pin1 in Alzheimer's disease: multiple substrates, one regulatory mechanism? |journal=Biochim. Biophys. Acta |volume=1772 |issue= 4 |pages= 422-9 |year= 2007 |pmid= 17317113 |doi= 10.1016/j.bbadis.2007.01.006 }}
*{{cite journal | author=Maleszka R, Hanes SD, Hackett RL, ''et al.'' |title=The Drosophila melanogaster dodo (dod) gene, conserved in humans, is functionally interchangeable with the ESS1 cell division gene of Saccharomyces cerevisiae. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 1 |pages= 447-51 |year= 1996 |pmid= 8552658 |doi= }}
*{{cite journal | author=Lu KP, Hanes SD, Hunter T |title=A human peptidyl-prolyl isomerase essential for regulation of mitosis. |journal=Nature |volume=380 |issue= 6574 |pages= 544-7 |year= 1996 |pmid= 8606777 |doi= 10.1038/380544a0 }}
*{{cite journal | author=Ranganathan R, Lu KP, Hunter T, Noel JP |title=Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. |journal=Cell |volume=89 |issue= 6 |pages= 875-86 |year= 1997 |pmid= 9200606 |doi= }}
*{{cite journal | author=Campbell HD, Webb GC, Fountain S, Young IG |title=The human PIN1 peptidyl-prolyl cis/trans isomerase gene maps to human chromosome 19p13 and the closely related PIN1L gene to 1p31. |journal=Genomics |volume=44 |issue= 2 |pages= 157-62 |year= 1997 |pmid= 9299231 |doi= 10.1006/geno.1997.4854 }}
*{{cite journal | author=Crenshaw DG, Yang J, Means AR, Kornbluth S |title=The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1. |journal=EMBO J. |volume=17 |issue= 5 |pages= 1315-27 |year= 1998 |pmid= 9482729 |doi= 10.1093/emboj/17.5.1315 }}
*{{cite journal | author=Shen M, Stukenberg PT, Kirschner MW, Lu KP |title=The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. |journal=Genes Dev. |volume=12 |issue= 5 |pages= 706-20 |year= 1998 |pmid= 9499405 |doi= }}
*{{cite journal | author=Lu PJ, Zhou XZ, Shen M, Lu KP |title=Function of WW domains as phosphoserine- or phosphothreonine-binding modules. |journal=Science |volume=283 |issue= 5406 |pages= 1325-8 |year= 1999 |pmid= 10037602 |doi= }}
*{{cite journal | author=Lu PJ, Wulf G, Zhou XZ, ''et al.'' |title=The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. |journal=Nature |volume=399 |issue= 6738 |pages= 784-8 |year= 1999 |pmid= 10391244 |doi= 10.1038/21650 }}
*{{cite journal | author=Albert A, Lavoie S, Vincent M |title=A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pin1. |journal=J. Cell. Sci. |volume=112 ( Pt 15) |issue= |pages= 2493-500 |year= 1999 |pmid= 10393805 |doi= }}
*{{cite journal | author=Wells NJ, Watanabe N, Tokusumi T, ''et al.'' |title=The C-terminal domain of the Cdc2 inhibitory kinase Myt1 interacts with Cdc2 complexes and is required for inhibition of G(2)/M progression. |journal=J. Cell. Sci. |volume=112 ( Pt 19) |issue= |pages= 3361-71 |year= 1999 |pmid= 10504341 |doi= }}
*{{cite journal | author=Gerez L, Mohrmann K, van Raak M, ''et al.'' |title=Accumulation of rab4GTP in the cytoplasm and association with the peptidyl-prolyl isomerase pin1 during mitosis. |journal=Mol. Biol. Cell |volume=11 |issue= 7 |pages= 2201-11 |year= 2000 |pmid= 10888662 |doi= }}
*{{cite journal | author=Verdecia MA, Bowman ME, Lu KP, ''et al.'' |title=Structural basis for phosphoserine-proline recognition by group IV WW domains. |journal=Nat. Struct. Biol. |volume=7 |issue= 8 |pages= 639-43 |year= 2000 |pmid= 10932246 |doi= 10.1038/77929 }}
*{{cite journal | author=Rippmann JF, Hobbie S, Daiber C, ''et al.'' |title=Phosphorylation-dependent proline isomerization catalyzed by Pin1 is essential for tumor cell survival and entry into mitosis. |journal=Cell Growth Differ. |volume=11 |issue= 7 |pages= 409-16 |year= 2000 |pmid= 10939594 |doi= }}
*{{cite journal | author=Liu W, Youn HD, Zhou XZ, ''et al.'' |title=Binding and regulation of the transcription factor NFAT by the peptidyl prolyl cis-trans isomerase Pin1. |journal=FEBS Lett. |volume=496 |issue= 2-3 |pages= 105-8 |year= 2001 |pmid= 11356192 |doi= }}
*{{cite journal | author=Wulf GM, Ryo A, Wulf GG, ''et al.'' |title=Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1. |journal=EMBO J. |volume=20 |issue= 13 |pages= 3459-72 |year= 2001 |pmid= 11432833 |doi= 10.1093/emboj/20.13.3459 }}
*{{cite journal | author=Kamimoto T, Zama T, Aoki R, ''et al.'' |title=Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1. |journal=J. Biol. Chem. |volume=276 |issue= 40 |pages= 37520-8 |year= 2001 |pmid= 11470801 |doi= 10.1074/jbc.M106207200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PLP1... {November 14, 2007 2:26:39 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:27:10 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- 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 = Proteolipid protein 1 (Pelizaeus-Merzbacher disease, spastic paraplegia 2, uncomplicated)
| HGNCid = 9086
| Symbol = PLP1
| AltSymbols =; MMPL; PLP; PLP/DM20; PMD; SPG2
| OMIM = 300401
| ECnumber =
| Homologene = 448
| MGIid = 97623
| GeneAtlas_image1 = PBB_GE_PLP1_210198_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0008366 |text = axon ensheathment}} {{GNF_GO|id=GO:0042759 |text = long-chain fatty acid biosynthetic process}} {{GNF_GO|id=GO:0048469 |text = cell maturation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5354
| Hs_Ensembl = ENSG00000123560
| Hs_RefseqProtein = NP_000524
| Hs_RefseqmRNA = NM_000533
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 102918410
| Hs_GenLoc_end = 102934201
| Hs_Uniprot = P60201
| Mm_EntrezGene = 18823
| Mm_Ensembl = ENSMUSG00000031425
| Mm_RefseqmRNA = NM_011123
| Mm_RefseqProtein = NP_035253
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 132169200
| Mm_GenLoc_end = 132184124
| Mm_Uniprot = Q3UYM8
}}
}}
'''Proteolipid protein 1 (Pelizaeus-Merzbacher disease, spastic paraplegia 2, uncomplicated)''', also known as '''PLP1''', is a human [[gene]].
<!-- 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 transmembrane proteolipid protein that is the predominant myelin protein present in the central nervous system. The encoded protein functions in myelination. This protein may play a role in the compaction, stabilization, and maintenance of myelin sheaths, as well as in oligodendrocyte development and axonal survival. Mutations associated with this gene cause X-linked Pelizaeus-Merzbacher disease and spastic paraplegia type 2. Two transcript variants encoding distinct isoforms have been identified for this gene.<ref>{{cite web | title = Entrez Gene: PLP1 proteolipid protein 1 (Pelizaeus-Merzbacher disease, spastic paraplegia 2, uncomplicated)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5354| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Woodward K, Malcolm S |title=Proteolipid protein gene: Pelizaeus-Merzbacher disease in humans and neurodegeneration in mice. |journal=Trends Genet. |volume=15 |issue= 4 |pages= 125-8 |year= 1999 |pmid= 10203813 |doi= }}
*{{cite journal | author=Garbern J, Cambi F, Shy M, Kamholz J |title=The molecular pathogenesis of Pelizaeus-Merzbacher disease. |journal=Arch. Neurol. |volume=56 |issue= 10 |pages= 1210-4 |year= 1999 |pmid= 10520936 |doi= }}
*{{cite journal | author=Yool DA, Edgar JM, Montague P, Malcolm S |title=The proteolipid protein gene and myelin disorders in man and animal models. |journal=Hum. Mol. Genet. |volume=9 |issue= 6 |pages= 987-92 |year= 2000 |pmid= 10767322 |doi= }}
*{{cite journal | author=Hudson LD |title=Pelizaeus-Merzbacher disease and spastic paraplegia type 2: two faces of myelin loss from mutations in the same gene. |journal=J. Child Neurol. |volume=18 |issue= 9 |pages= 616-24 |year= 2003 |pmid= 14572140 |doi= }}
*{{cite journal | author=Inoue K |title=PLP1-related inherited dysmyelinating disorders: Pelizaeus-Merzbacher disease and spastic paraplegia type 2. |journal=Neurogenetics |volume=6 |issue= 1 |pages= 1-16 |year= 2005 |pmid= 15627202 |doi= 10.1007/s10048-004-0207-y }}
*{{cite journal | author=Doll R, Natowicz MR, Schiffmann R, Smith FI |title=Molecular diagnostics for myelin proteolipid protein gene mutations in Pelizaeus-Merzbacher disease. |journal=Am. J. Hum. Genet. |volume=51 |issue= 1 |pages= 161-9 |year= 1992 |pmid= 1376966 |doi= }}
*{{cite journal | author=Strautnieks S, Rutland P, Winter RM, ''et al.'' |title=Pelizaeus-Merzbacher disease: detection of mutations Thr181----Pro and Leu223----Pro in the proteolipid protein gene, and prenatal diagnosis. |journal=Am. J. Hum. Genet. |volume=51 |issue= 4 |pages= 871-8 |year= 1992 |pmid= 1384324 |doi= }}
*{{cite journal | author=Pratt VM, Trofatter JA, Schinzel A, ''et al.'' |title=A new mutation in the proteolipid protein (PLP) gene in a German family with Pelizaeus-Merzbacher disease. |journal=Am. J. Med. Genet. |volume=38 |issue= 1 |pages= 136-9 |year= 1991 |pmid= 1707231 |doi= 10.1002/ajmg.1320380129 }}
*{{cite journal | author=Weimbs T, Dick T, Stoffel W, Boltshauser E |title=A point mutation at the X-chromosomal proteolipid protein locus in Pelizaeus-Merzbacher disease leads to disruption of myelinogenesis. |journal=Biol. Chem. Hoppe-Seyler |volume=371 |issue= 12 |pages= 1175-83 |year= 1991 |pmid= 1708672 |doi= }}
*{{cite journal | author=Popot JL, Pham Dinh D, Dautigny A |title=Major Myelin proteolipid: the 4-alpha-helix topology. |journal=J. Membr. Biol. |volume=120 |issue= 3 |pages= 233-46 |year= 1991 |pmid= 1711121 |doi= }}
*{{cite journal | author=Pham-Dinh D, Popot JL, Boespflug-Tanguy O, ''et al.'' |title=Pelizaeus-Merzbacher disease: a valine to phenylalanine point mutation in a putative extracellular loop of myelin proteolipid. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 17 |pages= 7562-6 |year= 1991 |pmid= 1715570 |doi= }}
*{{cite journal | author=Simons R, Alon N, Riordan JR |title=Human myelin DM-20 proteolipid protein deletion defined by cDNA sequence. |journal=Biochem. Biophys. Res. Commun. |volume=146 |issue= 2 |pages= 666-71 |year= 1987 |pmid= 2441695 |doi= }}
*{{cite journal | author=Kronquist KE, Crandall BF, Macklin WB, Campagnoni AT |title=Expression of myelin proteins in the developing human spinal cord: cloning and sequencing of human proteolipid protein cDNA. |journal=J. Neurosci. Res. |volume=18 |issue= 3 |pages= 395-401 |year= 1988 |pmid= 2449536 |doi= 10.1002/jnr.490180303 }}
*{{cite journal | author=Edwards AM, Ross NW, Ulmer JB, Braun PE |title=Interaction of myelin basic protein and proteolipid protein. |journal=J. Neurosci. Res. |volume=22 |issue= 1 |pages= 97-102 |year= 1989 |pmid= 2467009 |doi= 10.1002/jnr.490220113 }}
*{{cite journal | author=Hudson LD, Puckett C, Berndt J, ''et al.'' |title=Mutation of the proteolipid protein gene PLP in a human X chromosome-linked myelin disorder. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 20 |pages= 8128-31 |year= 1989 |pmid= 2479017 |doi= }}
*{{cite journal | author=Trofatter JA, Dlouhy SR, DeMyer W, ''et al.'' |title=Pelizaeus-Merzbacher disease: tight linkage to proteolipid protein gene exon variant. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 23 |pages= 9427-30 |year= 1990 |pmid= 2480601 |doi= }}
*{{cite journal | author=Gencic S, Abuelo D, Ambler M, Hudson LD |title=Pelizaeus-Merzbacher disease: an X-linked neurologic disorder of myelin metabolism with a novel mutation in the gene encoding proteolipid protein. |journal=Am. J. Hum. Genet. |volume=45 |issue= 3 |pages= 435-42 |year= 1989 |pmid= 2773936 |doi= }}
*{{cite journal | author=Mattei MG, Alliel PM, Dautigny A, ''et al.'' |title=The gene encoding for the major brain proteolipid (PLP) maps on the q-22 band of the human X chromosome. |journal=Hum. Genet. |volume=72 |issue= 4 |pages= 352-3 |year= 1986 |pmid= 3457761 |doi= }}
*{{cite journal | author=Diehl HJ, Schaich M, Budzinski RM, Stoffel W |title=Individual exons encode the integral membrane domains of human myelin proteolipid protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 24 |pages= 9807-11 |year= 1987 |pmid= 3467339 |doi= }}
*{{cite journal | author=Kahan I, Moscarello MA |title=The intramembranous domains of lipophilin in phosphatidylcholine vesicles are similar to those in the myelin membrane. |journal=Biochim. Biophys. Acta |volume=862 |issue= 1 |pages= 223-6 |year= 1986 |pmid= 3768366 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SCARB1... {November 14, 2007 2:18:26 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:19:11 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- 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 = Scavenger receptor class B, member 1
| HGNCid = 1664
| Symbol = SCARB1
| AltSymbols =; CD36L1; CLA-1; CLA1; MGC138242; SR-BI; SRB1
| OMIM = 601040
| ECnumber =
| Homologene = 21132
| MGIid = 893578
| GeneAtlas_image1 = PBB_GE_SCARB1_201819_at_tn.png
| GeneAtlas_image2 = PBB_GE_SCARB1_215834_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0000299 |text = integral to membrane of membrane fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016599 |text = caveolar membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0008203 |text = cholesterol metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 949
| Hs_Ensembl = ENSG00000073060
| Hs_RefseqProtein = NP_005496
| Hs_RefseqmRNA = NM_005505
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 123828139
| Hs_GenLoc_end = 123914346
| Hs_Uniprot = Q8WTV0
| Mm_EntrezGene = 20778
| Mm_Ensembl = ENSMUSG00000037936
| Mm_RefseqmRNA = NM_016741
| Mm_RefseqProtein = NP_058021
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 125570084
| Mm_GenLoc_end = 125629861
| Mm_Uniprot = Q3TZ42
}}
}}
'''Scavenger receptor class B, member 1''', also known as '''SCARB1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Williams DL, Temel RE, Connelly MA |title=Roles of scavenger receptor BI and APO A-I in selective uptake of HDL cholesterol by adrenal cells. |journal=Endocr. Res. |volume=26 |issue= 4 |pages= 639-51 |year= 2001 |pmid= 11196441 |doi= }}
*{{cite journal | author=Krause BR, Auerbach BJ |title=Reverse cholesterol transport and future pharmacological approaches to the treatment of atherosclerosis. |journal=Current opinion in investigational drugs (London, England : 2000) |volume=2 |issue= 3 |pages= 375-81 |year= 2001 |pmid= 11575708 |doi= }}
*{{cite journal | author=Connelly MA, Williams DL |title=Scavenger receptor BI: a scavenger receptor with a mission to transport high density lipoprotein lipids. |journal=Curr. Opin. Lipidol. |volume=15 |issue= 3 |pages= 287-95 |year= 2005 |pmid= 15166784 |doi= }}
*{{cite journal | author=Phillips RW |title=The new era in restorative dental materials. |journal=Oper Dent |volume=1 |issue= 1 |pages= 29-35 |year= 1978 |pmid= 1076467 |doi= }}
*{{cite journal | author=Skre H, Berg K |title=Cerebellar ataxia and total albinism: a kindred suggesting pleitotropism or linkage. |journal=Clin. Genet. |volume=5 |issue= 3 |pages= 196-204 |year= 1974 |pmid= 4838888 |doi= }}
*{{cite journal | author=Calvo D, Dopazo J, Vega MA |title=The CD36, CLA-1 (CD36L1), and LIMPII (CD36L2) gene family: cellular distribution, chromosomal location, and genetic evolution. |journal=Genomics |volume=25 |issue= 1 |pages= 100-6 |year= 1995 |pmid= 7539776 |doi= }}
*{{cite journal | author=Calvo D, Vega MA |title=Identification, primary structure, and distribution of CLA-1, a novel member of the CD36/LIMPII gene family. |journal=J. Biol. Chem. |volume=268 |issue= 25 |pages= 18929-35 |year= 1993 |pmid= 7689561 |doi= }}
*{{cite journal | author=Murao K, Terpstra V, Green SR, ''et al.'' |title=Characterization of CLA-1, a human homologue of rodent scavenger receptor BI, as a receptor for high density lipoprotein and apoptotic thymocytes. |journal=J. Biol. Chem. |volume=272 |issue= 28 |pages= 17551-7 |year= 1997 |pmid= 9211901 |doi= }}
*{{cite journal | author=Ikemoto M, Arai H, Feng D, ''et al.'' |title=Identification of a PDZ-domain-containing protein that interacts with the scavenger receptor class B type I. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 12 |pages= 6538-43 |year= 2000 |pmid= 10829064 |doi= 10.1073/pnas.100114397 }}
*{{cite journal | author=Husemann J, Silverstein SC |title=Expression of scavenger receptor class B, type I, by astrocytes and vascular smooth muscle cells in normal adult mouse and human brain and in Alzheimer's disease brain. |journal=Am. J. Pathol. |volume=158 |issue= 3 |pages= 825-32 |year= 2001 |pmid= 11238031 |doi= }}
*{{cite journal | author=Li XA, Titlow WB, Jackson BA, ''et al.'' |title=High density lipoprotein binding to scavenger receptor, Class B, type I activates endothelial nitric-oxide synthase in a ceramide-dependent manner. |journal=J. Biol. Chem. |volume=277 |issue= 13 |pages= 11058-63 |year= 2002 |pmid= 11792700 |doi= 10.1074/jbc.M110985200 }}
*{{cite journal | author=Duncan KG, Bailey KR, Kane JP, Schwartz DM |title=Human retinal pigment epithelial cells express scavenger receptors BI and BII. |journal=Biochem. Biophys. Res. Commun. |volume=292 |issue= 4 |pages= 1017-22 |year= 2002 |pmid= 11944916 |doi= 10.1006/bbrc.2002.6756 }}
*{{cite journal | author=Kawasaki Y, Nakagawa A, Nagaosa K, ''et al.'' |title=Phosphatidylserine binding of class B scavenger receptor type I, a phagocytosis receptor of testicular sertoli cells. |journal=J. Biol. Chem. |volume=277 |issue= 30 |pages= 27559-66 |year= 2002 |pmid= 12016218 |doi= 10.1074/jbc.M202879200 }}
*{{cite journal | author=Qi C, Chang J, Zhu Y, ''et al.'' |title=Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha. |journal=J. Biol. Chem. |volume=277 |issue= 32 |pages= 28624-30 |year= 2002 |pmid= 12039952 |doi= 10.1074/jbc.M201053200 }}
*{{cite journal | author=Johnson MS, Svensson PA, Borén J, ''et al.'' |title=Expression of scavenger receptor class B type I in gallbladder columnar epithelium. |journal=J. Gastroenterol. Hepatol. |volume=17 |issue= 6 |pages= 713-20 |year= 2002 |pmid= 12100619 |doi= }}
*{{cite journal | author=Silver DL |title=A carboxyl-terminal PDZ-interacting domain of scavenger receptor B, type I is essential for cell surface expression in liver. |journal=J. Biol. Chem. |volume=277 |issue= 37 |pages= 34042-7 |year= 2002 |pmid= 12119305 |doi= 10.1074/jbc.M206584200 }}
*{{cite journal | author=Bultel-Brienne S, Lestavel S, Pilon A, ''et al.'' |title=Lipid free apolipoprotein E binds to the class B Type I scavenger receptor I (SR-BI) and enhances cholesteryl ester uptake from lipoproteins. |journal=J. Biol. Chem. |volume=277 |issue= 39 |pages= 36092-9 |year= 2002 |pmid= 12138091 |doi= 10.1074/jbc.M201943200 }}
*{{cite journal | author=Strauss JG, Zimmermann R, Hrzenjak A, ''et al.'' |title=Endothelial cell-derived lipase mediates uptake and binding of high-density lipoprotein (HDL) particles and the selective uptake of HDL-associated cholesterol esters independent of its enzymic activity. |journal=Biochem. J. |volume=368 |issue= Pt 1 |pages= 69-79 |year= 2002 |pmid= 12164779 |doi= 10.1042/BJ20020306 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TAP1... {November 14, 2007 2:29:13 PM PST}
- SEARCH REDIRECT: Control Box Found: TAP1 {November 14, 2007 2:30:31 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 2:30:32 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 2:30:32 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 2:30:32 PM PST}
- UPDATED: Updated protein page: TAP1 {November 14, 2007 2:30:40 PM PST}
- INFO: Beginning work on TEK... {November 14, 2007 2:30:40 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:31:23 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 = PBB_Protein_TEK_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fvr.
| PDB = {{PDB2|1fvr}}, {{PDB2|2gy5}}, {{PDB2|2gy7}}, {{PDB2|2oo8}}, {{PDB2|2osc}}, {{PDB2|2p4i}}
| Name = TEK tyrosine kinase, endothelial (venous malformations, multiple cutaneous and mucosal)
| HGNCid = 11724
| Symbol = TEK
| AltSymbols =; CD202B; TIE-2; TIE2; VMCM; VMCM1
| OMIM = 600221
| ECnumber =
| Homologene = 397
| MGIid = 98664
| GeneAtlas_image1 = PBB_GE_TEK_206702_at_tn.png
| GeneAtlas_image2 = PBB_GE_TEK_217711_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004714 |text = transmembrane receptor protein tyrosine kinase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7010
| Hs_Ensembl = ENSG00000120156
| Hs_RefseqProtein = NP_000450
| Hs_RefseqmRNA = NM_000459
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 27099236
| Hs_GenLoc_end = 27220173
| Hs_Uniprot = Q02763
| Mm_EntrezGene = 21687
| Mm_Ensembl = ENSMUSG00000006386
| Mm_RefseqmRNA = NM_013690
| Mm_RefseqProtein = NP_038718
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 94231313
| Mm_GenLoc_end = 94366957
| Mm_Uniprot = Q02858
}}
}}
'''TEK tyrosine kinase, endothelial (venous malformations, multiple cutaneous and mucosal)''', also known as '''TEK''', is a human [[gene]].
<!-- 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 TEK receptor tyrosine kinase is expressed almost exclusively in endothelial cells in mice, rats, and humans. This receptor possesses a unique extracellular domain containing 2 immunoglobulin-like loops separated by 3 epidermal growth factor-like repeats that are connected to 3 fibronectin type III-like repeats. The ligand for the receptor is angiopoietin-1. Defects in TEK are associated with inherited venous malformations; the TEK signaling pathway appears to be critical for endothelial cell-smooth muscle cell communication in venous morphogenesis. TEK is closely related to the TIE receptor tyrosine kinase.<ref>{{cite web | title = Entrez Gene: TEK TEK tyrosine kinase, endothelial (venous malformations, multiple cutaneous and mucosal)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7010| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Partanen J, Armstrong E, Mäkelä TP, ''et al.'' |title=A novel endothelial cell surface receptor tyrosine kinase with extracellular epidermal growth factor homology domains. |journal=Mol. Cell. Biol. |volume=12 |issue= 4 |pages= 1698-707 |year= 1992 |pmid= 1312667 |doi= }}
*{{cite journal | author=Huang L, Turck CW, Rao P, Peters KG |title=GRB2 and SH-PTP2: potentially important endothelial signaling molecules downstream of the TEK/TIE2 receptor tyrosine kinase. |journal=Oncogene |volume=11 |issue= 10 |pages= 2097-103 |year= 1995 |pmid= 7478529 |doi= }}
*{{cite journal | author=Deans JP, Kalt L, Ledbetter JA, ''et al.'' |title=Association of 75/80-kDa phosphoproteins and the tyrosine kinases Lyn, Fyn, and Lck with the B cell molecule CD20. Evidence against involvement of the cytoplasmic regions of CD20. |journal=J. Biol. Chem. |volume=270 |issue= 38 |pages= 22632-8 |year= 1995 |pmid= 7545683 |doi= }}
*{{cite journal | author=Gallione CJ, Pasyk KA, Boon LM, ''et al.'' |title=A gene for familial venous malformations maps to chromosome 9p in a second large kindred. |journal=J. Med. Genet. |volume=32 |issue= 3 |pages= 197-9 |year= 1995 |pmid= 7783168 |doi= }}
*{{cite journal | author=Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, ''et al.'' |title=Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening. |journal=Genomics |volume=23 |issue= 1 |pages= 42-50 |year= 1995 |pmid= 7829101 |doi= 10.1006/geno.1994.1457 }}
*{{cite journal | author=Boon LM, Mulliken JB, Vikkula M, ''et al.'' |title=Assignment of a locus for dominantly inherited venous malformations to chromosome 9p. |journal=Hum. Mol. Genet. |volume=3 |issue= 9 |pages= 1583-7 |year= 1995 |pmid= 7833915 |doi= }}
*{{cite journal | author=Dumont DJ, Anderson L, Breitman ML, Duncan AM |title=Assignment of the endothelial-specific protein receptor tyrosine kinase gene (TEK) to human chromosome 9p21. |journal=Genomics |volume=23 |issue= 2 |pages= 512-3 |year= 1995 |pmid= 7835909 |doi= 10.1006/geno.1994.1536 }}
*{{cite journal | author=Ziegler SF, Bird TA, Schneringer JA, ''et al.'' |title=Molecular cloning and characterization of a novel receptor protein tyrosine kinase from human placenta. |journal=Oncogene |volume=8 |issue= 3 |pages= 663-70 |year= 1993 |pmid= 8382358 |doi= }}
*{{cite journal | author=Davis S, Aldrich TH, Jones PF, ''et al.'' |title=Isolation of angiopoietin-1, a ligand for the TIE2 receptor, by secretion-trap expression cloning. |journal=Cell |volume=87 |issue= 7 |pages= 1161-9 |year= 1997 |pmid= 8980223 |doi= }}
*{{cite journal | author=Suri C, Jones PF, Patan S, ''et al.'' |title=Requisite role of angiopoietin-1, a ligand for the TIE2 receptor, during embryonic angiogenesis. |journal=Cell |volume=87 |issue= 7 |pages= 1171-80 |year= 1997 |pmid= 8980224 |doi= }}
*{{cite journal | author=Vikkula M, Boon LM, Carraway KL, ''et al.'' |title=Vascular dysmorphogenesis caused by an activating mutation in the receptor tyrosine kinase TIE2. |journal=Cell |volume=87 |issue= 7 |pages= 1181-90 |year= 1997 |pmid= 8980225 |doi= }}
*{{cite journal | author=Witzenbichler B, Maisonpierre PC, Jones P, ''et al.'' |title=Chemotactic properties of angiopoietin-1 and -2, ligands for the endothelial-specific receptor tyrosine kinase Tie2. |journal=J. Biol. Chem. |volume=273 |issue= 29 |pages= 18514-21 |year= 1998 |pmid= 9660821 |doi= }}
*{{cite journal | author=Asahara T, Chen D, Takahashi T, ''et al.'' |title=Tie2 receptor ligands, angiopoietin-1 and angiopoietin-2, modulate VEGF-induced postnatal neovascularization. |journal=Circ. Res. |volume=83 |issue= 3 |pages= 233-40 |year= 1998 |pmid= 9710115 |doi= }}
*{{cite journal | author=Sato A, Iwama A, Takakura N, ''et al.'' |title=Characterization of TEK receptor tyrosine kinase and its ligands, Angiopoietins, in human hematopoietic progenitor cells. |journal=Int. Immunol. |volume=10 |issue= 8 |pages= 1217-27 |year= 1998 |pmid= 9723709 |doi= }}
*{{cite journal | author=Jones N, Dumont DJ |title=The Tek/Tie2 receptor signals through a novel Dok-related docking protein, Dok-R. |journal=Oncogene |volume=17 |issue= 9 |pages= 1097-108 |year= 1998 |pmid= 9764820 |doi= 10.1038/sj.onc.1202115 }}
*{{cite journal | author=De Sepulveda P, Okkenhaug K, Rose JL, ''et al.'' |title=Socs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferation. |journal=EMBO J. |volume=18 |issue= 4 |pages= 904-15 |year= 1999 |pmid= 10022833 |doi= 10.1093/emboj/18.4.904 }}
*{{cite journal | author=Valenzuela DM, Griffiths JA, Rojas J, ''et al.'' |title=Angiopoietins 3 and 4: diverging gene counterparts in mice and humans. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 5 |pages= 1904-9 |year= 1999 |pmid= 10051567 |doi= }}
*{{cite journal | author=Calvert JT, Riney TJ, Kontos CD, ''et al.'' |title=Allelic and locus heterogeneity in inherited venous malformations. |journal=Hum. Mol. Genet. |volume=8 |issue= 7 |pages= 1279-89 |year= 1999 |pmid= 10369874 |doi= }}
*{{cite journal | author=Jones N, Master Z, Jones J, ''et al.'' |title=Identification of Tek/Tie2 binding partners. Binding to a multifunctional docking site mediates cell survival and migration. |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 30896-905 |year= 1999 |pmid= 10521483 |doi= }}
*{{cite journal | author=Fachinger G, Deutsch U, Risau W |title=Functional interaction of vascular endothelial-protein-tyrosine phosphatase with the angiopoietin receptor Tie-2. |journal=Oncogene |volume=18 |issue= 43 |pages= 5948-53 |year= 1999 |pmid= 10557082 |doi= 10.1038/sj.onc.1202992 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TNNI3... {November 14, 2007 2:31:23 PM PST}
- SEARCH REDIRECT: Control Box Found: TNNI3 {November 14, 2007 2:31:54 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 2:31:55 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 2:31:55 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 2:31:55 PM PST}
- UPDATED: Updated protein page: TNNI3 {November 14, 2007 2:32:01 PM PST}
end log.
