INFO: Beginning work on BCR... {November 1, 2007 3:05:47 PM PDT}
UPLOAD: Added new Image to wiki: {November 1, 2007 3:06:11 PM PDT}
AMBIGUITY: Did not locate an acceptable page to update. {November 1, 2007 3:06:34 PM PDT}
<!-- 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_BCR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1k1f.
| PDB = {{PDB2|1k1f}}
| Name = Breakpoint cluster region
| HGNCid = 1014
| Symbol = BCR
| AltSymbols =; ALL; BCR/FGFR1; BCR1; CML; D22S11; D22S662; FGFR1/BCR; FLJ16453; PHL
| OMIM = 151410
| ECnumber =
| Homologene = 3192
| MGIid = 88141
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005085 |text = guanyl-nucleotide exchange factor activity}} {{GNF_GO|id=GO:0005089 |text = Rho guanyl-nucleotide exchange factor activity}} {{GNF_GO|id=GO:0005096 |text = GTPase activator activity}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0035023 |text = regulation of Rho protein signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 613
| Hs_Ensembl =
| Hs_RefseqProtein = NP_004318
| Hs_RefseqmRNA = NM_004327
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 110279
| Mm_Ensembl = ENSMUSG00000009681
| Mm_RefseqmRNA = XM_898043
| Mm_RefseqProtein = XP_903136
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 74505374
| Mm_GenLoc_end = 74626498
| Mm_Uniprot =
}}
}}
'''Breakpoint cluster region''', also known as '''BCR''', 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 = A reciprocal translocation between chromosomes 22 and 9 produces the Philadelphia chromosome, which is often found in patients with chronic myelogenous leukemia. The chromosome 22 breakpoint for this translocation is located within the BCR gene. The translocation produces a fusion protein which is encoded by sequence from both BCR and ABL, the gene at the chromosome 9 breakpoint. Although the BCR-ABL fusion protein has been extensively studied, the function of the normal BCR gene product is not clear. The protein has serine/threonine kinase activity and is a GTPase-activating protein for p21rac. Two transcript variants encoding different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: BCR breakpoint cluster region| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=613| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wang L, Seale J, Woodcock BE, Clark RE |title=e19a2-positive chronic myeloid leukaemia with BCR exon e16-deleted transcripts. |journal=Leukemia |volume=16 |issue= 8 |pages= 1562-3 |year= 2002 |pmid= 12145699 |doi= 10.1038/sj.leu.2402600 }}
}}
{{refend}}
{{protein-stub}}
INFO: Beginning work on COL1A2... {November 1, 2007 3:07:35 PM PDT}
AMBIGUITY: Did not locate an acceptable page to update. {November 1, 2007 3:08:40 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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| 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 = Collagen, type I, alpha 2
| HGNCid = 2198
| Symbol = COL1A2
| AltSymbols =; OI4
| OMIM = 120160
| ECnumber =
| Homologene = 69
| MGIid = 88468
| GeneAtlas_image1 = PBB_GE_COL1A2_202403_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_COL1A2_202404_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008147 |text = structural constituent of bone}}
| Component = {{GNF_GO|id=GO:0005581 |text = collagen}} {{GNF_GO|id=GO:0005584 |text = collagen type I}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1278
| Hs_Ensembl = ENSG00000164692
| Hs_RefseqProtein = NP_000080
| Hs_RefseqmRNA = NM_000089
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 93861809
| Hs_GenLoc_end = 93898480
| Hs_Uniprot = P08123
| Mm_EntrezGene = 12843
| Mm_Ensembl = ENSMUSG00000029661
| Mm_RefseqmRNA = NM_007743
| Mm_RefseqProtein = NP_031769
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 4455840
| Mm_GenLoc_end = 4490729
| Mm_Uniprot = Q3TP88
}}
}}
'''Collagen, type I, alpha 2''', also known as '''COL1A2''', 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 one of the chains for type I collagen, the fibrillar collagen found in most connective tissues. Mutations in this gene are associated with osteogenesis imperfecta, Ehlers-Danlos syndrome, idiopathic osteoporosis, and atypical Marfan syndrome. Symptoms associated with mutations in this gene, however, tend to be less severe than mutations in the gene for alpha-1 type I collagen since alpha-2 is less abundant. Multiple messages for this gene result from multiple polyadenylation signals, a feature shared by most of the other collagen genes.<ref>{{cite web | title = Entrez Gene: COL1A2 collagen, type I, alpha 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1278| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Byers PH, Wallis GA, Willing MC |title=Osteogenesis imperfecta: translation of mutation to phenotype. |journal=J. Med. Genet. |volume=28 |issue= 7 |pages= 433-42 |year= 1991 |pmid= 1895312 |doi= }}
*{{cite journal | author=Kuivaniemi H, Tromp G, Prockop DJ |title=Mutations in collagen genes: causes of rare and some common diseases in humans. |journal=FASEB J. |volume=5 |issue= 7 |pages= 2052-60 |year= 1991 |pmid= 2010058 |doi= }}
*{{cite journal | author=Kuivaniemi H, Tromp G, Prockop DJ |title=Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels. |journal=Hum. Mutat. |volume=9 |issue= 4 |pages= 300-15 |year= 1997 |pmid= 9101290 |doi= 10.1002/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.0.CO;2-9 }}
*{{cite journal | author=Rossert J, Terraz C, Dupont S |title=Regulation of type I collagen genes expression. |journal=Nephrol. Dial. Transplant. |volume=15 Suppl 6 |issue= |pages= 66-8 |year= 2001 |pmid= 11143996 |doi= }}
}}
{{refend}}
{{protein-stub}}
AMBIGUITY: Did not locate an acceptable page to update. {November 1, 2007 3:14:19 PM PDT}
<!-- 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_F7_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bf9.
| PDB = {{PDB2|1bf9}}, {{PDB2|1cvw}}, {{PDB2|1dan}}, {{PDB2|1dva}}, {{PDB2|1f7e}}, {{PDB2|1f7m}}, {{PDB2|1fak}}, {{PDB2|1ff7}}, {{PDB2|1ffm}}, {{PDB2|1j9c}}, {{PDB2|1jbu}}, {{PDB2|1kli}}, {{PDB2|1klj}}, {{PDB2|1o5d}}, {{PDB2|1qfk}}, {{PDB2|1w0y}}, {{PDB2|1w2k}}, {{PDB2|1w7x}}, {{PDB2|1w8b}}, {{PDB2|1wqv}}, {{PDB2|1wss}}, {{PDB2|1wtg}}, {{PDB2|1wun}}, {{PDB2|1wv7}}, {{PDB2|1ygc}}, {{PDB2|1z6j}}, {{PDB2|2a2q}}, {{PDB2|2aei}}, {{PDB2|2aer}}, {{PDB2|2b7d}}, {{PDB2|2b8o}}, {{PDB2|2bz6}}, {{PDB2|2c4f}}, {{PDB2|2f9b}}, {{PDB2|2fir}}, {{PDB2|2flb}}, {{PDB2|2flr}}, {{PDB2|2puq}}
| Name = Coagulation factor VII (serum prothrombin conversion accelerator)
| HGNCid = 3544
| Symbol = F7
| AltSymbols =;
| OMIM = 227500
| ECnumber =
| Homologene = 7710
| MGIid = 109325
| GeneAtlas_image1 = PBB_GE_F7_207300_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003802 |text = coagulation factor VIIa activity}} {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2155
| Hs_Ensembl = ENSG00000057593
| Hs_RefseqProtein = NP_000122
| Hs_RefseqmRNA = NM_000131
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 112808106
| Hs_GenLoc_end = 112822996
| Hs_Uniprot = P08709
| Mm_EntrezGene = 14068
| Mm_Ensembl = ENSMUSG00000031443
| Mm_RefseqmRNA = NM_010172
| Mm_RefseqProtein = NP_034302
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 13026011
| Mm_GenLoc_end = 13035782
| Mm_Uniprot = Q542C2
}}
}}
'''Coagulation factor VII (serum prothrombin conversion accelerator)''', also known as '''F7''', 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 coagulation factor VII which is a vitamin K-dependent factor essential for hemostasis. This factor circulates in the blood in a zymogen form, and is converted to an active form by either factor IXa, factor Xa, factor XIIa, or thrombin by minor proteolysis. Upon activation of the factor VII, a heavy chain containing a catalytic domain and a light chain containing 2 EGF-like domains are generated, and two chains are held together by a disulfide bond. In the presence of factor III and calcium ions, the activated factor then further activates the coagulation cascade by converting factor IX to factor IXa and/or factor X to factor Xa. Alternative splicing of this gene results in 2 transcripts. Defects in this gene can cause coagulopathy.<ref>{{cite web | title = Entrez Gene: F7 coagulation factor VII (serum prothrombin conversion accelerator)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2155| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Versteeg HH, Peppelenbosch MP, Spek CA |title=The pleiotropic effects of tissue factor: a possible role for factor VIIa-induced intracellular signalling? |journal=Thromb. Haemost. |volume=86 |issue= 6 |pages= 1353-9 |year= 2002 |pmid= 11776298 |doi= }}
*{{cite journal | author=Golino P |title=The inhibitors of the tissue factor:factor VII pathway. |journal=Thromb. Res. |volume=106 |issue= 3 |pages= V257-65 |year= 2003 |pmid= 12356487 |doi= }}
}}
{{refend}}
{{protein-stub}}
AMBIGUITY: Did not locate an acceptable page to update. {November 1, 2007 3:15:12 PM PDT}
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{{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_F9_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cfh.
| PDB = {{PDB2|1cfh}}, {{PDB2|1cfi}}, {{PDB2|1edm}}, {{PDB2|1ixa}}, {{PDB2|1j34}}, {{PDB2|1j35}}, {{PDB2|1mgx}}, {{PDB2|1nl0}}, {{PDB2|1rfn}}
| Name = Coagulation factor IX (plasma thromboplastic component, Christmas disease, hemophilia B)
| HGNCid = 3551
| Symbol = F9
| AltSymbols =; FIX; GLA domain; HEMB; MGC129641; MGC129642; PTC
| OMIM = 306900
| ECnumber =
| Homologene = 106
| MGIid = 88384
| GeneAtlas_image1 = PBB_GE_F9_207218_at_tn.png
| Function = {{GNF_GO|id=GO:0003803 |text = coagulation factor IXa activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2158
| Hs_Ensembl = ENSG00000101981
| Hs_RefseqProtein = NP_000124
| Hs_RefseqmRNA = NM_000133
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 138440561
| Hs_GenLoc_end = 138473283
| Hs_Uniprot = P00740
| Mm_EntrezGene = 14071
| Mm_Ensembl = ENSMUSG00000031138
| Mm_RefseqmRNA = NM_007979
| Mm_RefseqProtein = NP_032005
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 56346248
| Mm_GenLoc_end = 56377542
| Mm_Uniprot = A0JLY3
}}
}}
'''Coagulation factor IX (plasma thromboplastic component, Christmas disease, hemophilia B)''', also known as '''F9''', 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 vitamin K-dependent coagulation factor IX that circulates in the blood as an inactive zymogen. This factor is converted to an active form by factor XIa, which excises the activation peptide and thus generates a heavy chain and a light chain held together by one or more disulfide bonds. The role of this activated factor IX in the blood coagulation cascade is to activate factor X to its active form through interactions with Ca+2 ions, membrane phospholipids, and factor VIII. Alterations of this gene, including point mutations, insertions and deletions, cause factor IX deficiency, which is a recessive X-linked disorder, also called hemophilia B or Christmas disease.<ref>{{cite web | title = Entrez Gene: F9 coagulation factor IX (plasma thromboplastic component, Christmas disease, hemophilia B)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2158| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Davie EW, Fujikawa K |title=Basic mechanisms in blood coagulation. |journal=Annu. Rev. Biochem. |volume=44 |issue= |pages= 799-829 |year= 1975 |pmid= 237463 |doi= 10.1146/annurev.bi.44.070175.004055 }}
*{{cite journal | author=Sommer SS |title=Assessing the underlying pattern of human germline mutations: lessons from the factor IX gene. |journal=FASEB J. |volume=6 |issue= 10 |pages= 2767-74 |year= 1992 |pmid= 1634040 |doi= }}
*{{cite journal | author=Lenting PJ, van Mourik JA, Mertens K |title=The life cycle of coagulation factor VIII in view of its structure and function. |journal=Blood |volume=92 |issue= 11 |pages= 3983-96 |year= 1999 |pmid= 9834200 |doi= }}
*{{cite journal | author=Lowe GD |title=Factor IX and thrombosis. |journal=Br. J. Haematol. |volume=115 |issue= 3 |pages= 507-13 |year= 2002 |pmid= 11736930 |doi= }}
*{{cite journal | author=O'Connell NM |title=Factor XI deficiency--from molecular genetics to clinical management. |journal=Blood Coagul. Fibrinolysis |volume=14 Suppl 1 |issue= |pages= S59-64 |year= 2004 |pmid= 14567539 |doi= }}
*{{cite journal | author=Du X |title=Signaling and regulation of the platelet glycoprotein Ib-IX-V complex. |journal=Curr. Opin. Hematol. |volume=14 |issue= 3 |pages= 262-9 |year= 2007 |pmid= 17414217 |doi= 10.1097/MOH.0b013e3280dce51a }}
}}
{{refend}}
{{protein-stub}}
AMBIGUITY: Did not locate an acceptable page to update. {November 1, 2007 3:20:46 PM PDT}
<!-- 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_GH1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a22.
| PDB = {{PDB2|1a22}}, {{PDB2|1axi}}, {{PDB2|1bp3}}, {{PDB2|1hgu}}, {{PDB2|1huw}}, {{PDB2|1hwg}}, {{PDB2|1hwh}}, {{PDB2|1kf9}}, {{PDB2|3hhr}}
| Name = Growth hormone 1
| HGNCid = 4261
| Symbol = GH1
| AltSymbols =; GH; GH-N; GHN; hGH-N
| OMIM = 139250
| ECnumber =
| Homologene =
| MGIid =
| GeneAtlas_image1 = PBB_GE_GH1_205840_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_GH1_206885_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_GH1_206886_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2688
| Hs_Ensembl = ENSG00000189162
| Hs_RefseqProtein = NP_000506
| Hs_RefseqmRNA = NM_000515
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 59348294
| Hs_GenLoc_end = 59349886
| Hs_Uniprot = P01241
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Growth hormone 1''', also known as '''GH1''', 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 somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.<ref>{{cite web | title = Entrez Gene: GH1 growth hormone 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2688| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Binder G |title=Isolated growth hormone deficiency and the GH-1 gene: update 2002. |journal=Horm. Res. |volume=58 Suppl 3 |issue= |pages= 2-6 |year= 2003 |pmid= 12435888 |doi= }}
*{{cite journal | author=Waxman DJ, O'Connor C |title=Growth hormone regulation of sex-dependent liver gene expression. |journal=Mol. Endocrinol. |volume=20 |issue= 11 |pages= 2613-29 |year= 2007 |pmid= 16543404 |doi= 10.1210/me.2006-0007 }}
*{{cite journal | author=Cattini PA, Yang X, Jin Y, Detillieux KA |title=Regulation of the human growth hormone gene family: possible role for Pit-1 in early stages of pituitary-specific expression and repression. |journal=Neuroendocrinology |volume=83 |issue= 3-4 |pages= 145-53 |year= 2006 |pmid= 17047377 |doi= 10.1159/000095522 }}
*{{cite journal | author=Wagner K, Hemminki K, Försti A |title=The GH1/IGF-1 axis polymorphisms and their impact on breast cancer development. |journal=Breast Cancer Res. Treat. |volume=104 |issue= 3 |pages= 233-48 |year= 2007 |pmid= 17082888 |doi= 10.1007/s10549-006-9411-9 }}
}}
{{refend}}
{{protein-stub}}
AMBIGUITY: Did not locate an acceptable page to update. {November 1, 2007 3:31:19 PM PDT}
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{{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_PRKCE_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gmi.
| PDB = {{PDB2|1gmi}}
| Name = Protein kinase C, epsilon
| HGNCid = 9401
| Symbol = PRKCE
| AltSymbols =; MGC125656; MGC125657; PKCE; nPKC-epsilon
| OMIM = 176975
| ECnumber =
| Homologene = 48343
| MGIid = 97599
| GeneAtlas_image1 = PBB_GE_PRKCE_206248_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004672 |text = protein kinase activity}} {{GNF_GO|id=GO:0004699 |text = calcium-independent protein kinase C activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019992 |text = diacylglycerol binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0050730 |text = regulation of peptidyl-tyrosine phosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5581
| Hs_Ensembl = ENSG00000171132
| Hs_RefseqProtein = NP_005391
| Hs_RefseqmRNA = NM_005400
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 45732547
| Hs_GenLoc_end = 46268632
| Hs_Uniprot = Q02156
| Mm_EntrezGene = 18754
| Mm_Ensembl = ENSMUSG00000045038
| Mm_RefseqmRNA = XM_989478
| Mm_RefseqProtein = XP_994572
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 86076111
| Mm_GenLoc_end = 86563725
| Mm_Uniprot = P16054
}}
}}
'''Protein kinase C, epsilon''', also known as '''PRKCE''', 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 = Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This kinase has been shown to be involved in many different cellular functions, such as neuron channel activation, apoptosis, cardioprotection from ischemia, heat shock response, as well as insulin exocytosis. Knockout studies in mice suggest that this kinase is important for lipopolysaccharide (LPS)-mediated signaling in activated macrophages and may also play a role in controlling anxiety-like behavior.<ref>{{cite web | title = Entrez Gene: PRKCE protein kinase C, epsilon| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5581| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Slater SJ, Ho C, Stubbs CD |title=The use of fluorescent phorbol esters in studies of protein kinase C-membrane interactions. |journal=Chem. Phys. Lipids |volume=116 |issue= 1-2 |pages= 75-91 |year= 2003 |pmid= 12093536 |doi= }}
*{{cite journal | author=Aksoy E, Goldman M, Willems F |title=Protein kinase C epsilon: a new target to control inflammation and immune-mediated disorders. |journal=Int. J. Biochem. Cell Biol. |volume=36 |issue= 2 |pages= 183-8 |year= 2004 |pmid= 14643884 |doi= }}
*{{cite journal | author=Tolstrup M, Ostergaard L, Laursen AL, ''et al.'' |title=HIV/SIV escape from immune surveillance: focus on Nef. |journal=Curr. HIV Res. |volume=2 |issue= 2 |pages= 141-51 |year= 2004 |pmid= 15078178 |doi= }}
}}
{{refend}}
{{protein-stub}}