Breast cancer anti-estrogen resistance protein 1

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• protein domain specific binding Source: RGD <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Differential regulation of cell migration, actin stress fiber organization, and cell transformation by functional domains of Crk-associated substrate."
    Huang J., Hamasaki H., Nakamoto T., Honda H., Hirai H., Saito M., Takato T., Sakai R.
    J. Biol. Chem. 277:27265-27272(2002) [PubMed] [Europe PMC] [Abstract]
• protein kinase binding Source: RGDInferred from sequence orthologyⁱ
  • "Cell adhesion regulates the interaction between the docking protein p130(Cas) and the 14-3-3 proteins."
    Garcia-Guzman M., Dolfi F., Russello M., Vuori K.
    J. Biol. Chem. 274:5762-5768(1999) [PubMed] [Europe PMC] [Abstract]
  • Ref.1

    "A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner."
    Sakai R., Iwamatsu A., Hirano N., Ogawa S., Tanaka T., Mano H., Yazaki Y., Hirai H.
    EMBO J. 13:3748-3756(1994) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  • "Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinases."
    Vuori K., Hirai H., Aizawa S., Ruoslahti E.
    Mol. Cell. Biol. 16:2606-2613(1996) [PubMed] [Europe PMC] [Abstract]
  • "Involvement of p130(Cas) and p105(HEF1), a novel Cas-like docking protein, in a cytoskeleton-dependent signaling pathway initiated by ligation of integrin or antigen receptor on human B cells."
    Manie S.N., Beck A.R.P., Astier A., Law S.F., Canty T., Hirai H., Druker B.J., Avraham H., Haghayeghi N., Sattler M., Salgia R., Griffin J.D., Golemis E.A., Freedman A.S.
    J. Biol. Chem. 272:4230-4236(1997) [PubMed] [Europe PMC] [Abstract]
  • "CAS/Crk coupling serves as a "molecular switch" for induction of cell migration."
    Klemke R.L., Leng J., Molander R., Brooks P.C., Vuori K., Cheresh D.A.
    J. Cell Biol. 140:961-972(1998) [PubMed] [Europe PMC] [Abstract]
• SH3 domain binding Source: UniProtKB-KW

GO - Biological processⁱ

• actin cytoskeleton organization Source: RGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Differential regulation of cell migration, actin stress fiber organization, and cell transformation by functional domains of Crk-associated substrate."
    Huang J., Hamasaki H., Nakamoto T., Honda H., Hirai H., Saito M., Takato T., Sakai R.
    J. Biol. Chem. 277:27265-27272(2002) [PubMed] [Europe PMC] [Abstract]
• actin filament organization Source: UniProtKB
• actin filament reorganization Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• antigen receptor-mediated signaling pathway Source: UniProtKB
• B cell receptor signaling pathway Source: UniProtKB
• cell adhesion Source: UniProtKB-KW
• cell chemotaxis Source: RGDInferred from sequence orthologyⁱ
  • "Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cells."
    Evans I.M., Yamaji M., Britton G., Pellet-Many C., Lockie C., Zachary I.C., Frankel P.
    Mol. Cell. Biol. 31:1174-1185(2011) [PubMed] [Europe PMC] [Abstract]
• cell migration Source: RGDInferred from mutant phenotypeⁱ
  • "Differential regulation of cell migration, actin stress fiber organization, and cell transformation by functional domains of Crk-associated substrate."
    Huang J., Hamasaki H., Nakamoto T., Honda H., Hirai H., Saito M., Takato T., Sakai R.
    J. Biol. Chem. 277:27265-27272(2002) [PubMed] [Europe PMC] [Abstract]
• cellular response to endothelin Source: RGDInferred from physical interactionⁱ
  • "Selective involvement of p130Cas/Crk/Pyk2/c-Src in endothelin-1-induced JNK activation."
    Kodama H., Fukuda K., Takahashi E., Tahara S., Tomita Y., Ieda M., Kimura K., Owada K.M., Vuori K., Ogawa S.
    Hypertension 41:1372-1379(2003) [PubMed] [Europe PMC] [Abstract]
• cellular response to hepatocyte growth factor stimulus Source: RGDInferred from sequence orthologyⁱ
  • "Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cells."
    Evans I.M., Yamaji M., Britton G., Pellet-Many C., Lockie C., Zachary I.C., Frankel P.
    Mol. Cell. Biol. 31:1174-1185(2011) [PubMed] [Europe PMC] [Abstract]
• cellular response to nitric oxide Source: RGDInferred from physical interactionⁱ
  • "Nitric oxide-induced inhibition of aortic smooth muscle cell motility: role of PTP-PEST and adaptor proteins p130cas and Crk."
    Lin Y., Ceacareanu A.C., Hassid A.
    Am. J. Physiol. Heart Circ. Physiol. 285:H710-21(2003) [PubMed] [Europe PMC] [Abstract]
• endothelin receptor signaling pathway Source: UniProtKB
• epidermal growth factor receptor signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Epidermal growth factor modulates tyrosine phosphorylation of p130Cas. Involvement of phosphatidylinositol 3'-kinase and actin cytoskeleton."
    Ojaniemi M., Vuori K.
    J. Biol. Chem. 272:25993-25998(1997) [PubMed] [Europe PMC] [Abstract]
• G protein-coupled receptor signaling pathway Source: UniProtKB
• hepatocyte growth factor receptor signaling pathway Source: RGDInferred from sequence orthologyⁱ
  • "Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cells."
    Evans I.M., Yamaji M., Britton G., Pellet-Many C., Lockie C., Zachary I.C., Frankel P.
    Mol. Cell. Biol. 31:1174-1185(2011) [PubMed] [Europe PMC] [Abstract]
• insulin receptor signaling pathway Source: UniProtKBInferred from direct assayⁱ
  • "Crk protein binds to PDGF receptor and insulin receptor substrate-1 with different modulating effects on PDGF- and insulin-dependent signaling pathways."
    Sorokin A., Reed E., Nnkemere N., Dulin N.O., Schlessinger J.
    Oncogene 16:2425-2434(1998) [PubMed] [Europe PMC] [Abstract]
• integrin-mediated signaling pathway Source: UniProtKB
• negative regulation of substrate adhesion-dependent cell spreading Source: RGDInferred from mutant phenotypeⁱ
  • "p130cas but not paxillin is essential for Caco-2 intestinal epithelial cell spreading and migration on collagen IV."
    Sanders M.A., Basson M.D.
    J. Biol. Chem. 280:23516-23522(2005) [PubMed] [Europe PMC] [Abstract]
• neurotrophin TRK receptor signaling pathway Source: UniProtKBInferred from direct assayⁱ
  • "Nerve growth factor stimulates the tyrosine phosphorylation of endogenous Crk-II and augments its association with p130Cas in PC-12 cells."
    Ribon V., Saltiel A.R.
    J. Biol. Chem. 271:7375-7380(1996) [PubMed] [Europe PMC] [Abstract]
• platelet-derived growth factor receptor signaling pathway Source: UniProtKB
• positive regulation of cell migration Source: UniProtKB
• positive regulation of endothelial cell migration Source: RGDInferred from sequence orthologyⁱ
  • "Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cells."
    Evans I.M., Yamaji M., Britton G., Pellet-Many C., Lockie C., Zachary I.C., Frankel P.
    Mol. Cell. Biol. 31:1174-1185(2011) [PubMed] [Europe PMC] [Abstract]
• transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• vascular endothelial growth factor receptor signaling pathway Source: RGDInferred from sequence orthologyⁱ
  • "Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cells."
    Evans I.M., Yamaji M., Britton G., Pellet-Many C., Lockie C., Zachary I.C., Frankel P.
    Mol. Cell. Biol. 31:1174-1185(2011) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• protein domain specific binding Source: RGDInferred from physical interactionⁱ
  • "Differential regulation of cell migration, actin stress fiber organization, and cell transformation by functional domains of Crk-associated substrate."
    Huang J., Hamasaki H., Nakamoto T., Honda H., Hirai H., Saito M., Takato T., Sakai R.
    J. Biol. Chem. 277:27265-27272(2002) [PubMed] [Europe PMC] [Abstract]
• protein kinase binding Source: RGDInferred from sequence orthologyⁱ
  • "Cell adhesion regulates the interaction between the docking protein p130(Cas) and the 14-3-3 proteins."
    Garcia-Guzman M., Dolfi F., Russello M., Vuori K.
    J. Biol. Chem. 274:5762-5768(1999) [PubMed] [Europe PMC] [Abstract]
  • Ref.1

    "A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner."
    Sakai R., Iwamatsu A., Hirano N., Ogawa S., Tanaka T., Mano H., Yazaki Y., Hirai H.
    EMBO J. 13:3748-3756(1994) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  • "Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinases."
    Vuori K., Hirai H., Aizawa S., Ruoslahti E.
    Mol. Cell. Biol. 16:2606-2613(1996) [PubMed] [Europe PMC] [Abstract]
  • "Involvement of p130(Cas) and p105(HEF1), a novel Cas-like docking protein, in a cytoskeleton-dependent signaling pathway initiated by ligation of integrin or antigen receptor on human B cells."
    Manie S.N., Beck A.R.P., Astier A., Law S.F., Canty T., Hirai H., Druker B.J., Avraham H., Haghayeghi N., Sattler M., Salgia R., Griffin J.D., Golemis E.A., Freedman A.S.
    J. Biol. Chem. 272:4230-4236(1997) [PubMed] [Europe PMC] [Abstract]
  • "CAS/Crk coupling serves as a "molecular switch" for induction of cell migration."
    Klemke R.L., Leng J., Molander R., Brooks P.C., Vuori K., Cheresh D.A.
    J. Cell Biol. 140:961-972(1998) [PubMed] [Europe PMC] [Abstract]
• SH3 domain binding Source: UniProtKB-KW

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

Motif

Compositional bias

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MKYLVSVGAG PARRAGGLED VSWGPRVSRR PQSYRAARHV NESLPRSAFR 
        60         70         80         90        100
VPAAHGASVT PSAALGSGLP ETQPEAVCRG TEKPRFAEGC KPAASRDKNV 
       110        120        130        140        150
LAKALYDNVA ESPDELSFRK GDIMTVLERD TQGLDGWWLC SLHGRQGIVP 
       160        170        180        190        200
GNRLKILVGM YDKKPAAPGP GPPATPPQPQ PSLPQGVHTP VPPASQYSPM 
       210        220        230        240        250
LPTAYQPQPD NVYLVPTPSK TQQGLYQAPG PNPQFQSPPA KQTSTFSKQT 
       260        270        280        290        300
PHHSFPSPAT DLYQVPPGPG SPAQDIYQVP PSAGTGHDIY QVPPSLDTRS 
       310        320        330        340        350
WEGTKPPAKV VVPTRVGQGY VYEASQAEQD EYDTPRHLLA PGSQDIYDVP 
       360        370        380        390        400
PVRGLLPNQY GQEVYDTPPM AVKGPNGRDP LLDVYDVPPS VEKGLPPSNH 
       410        420        430        440        450
HSVYDVPPSV SKDVPDGPLL REETYDVPPA FAKPKPFDPT RHPLILAAPP 
       460        470        480        490        500
PDSPPAEDVY DVPPPAPDLY DVPPGLRRPG PGTLYDVPRE RVLPPEVADG 
       510        520        530        540        550
SVIDDGVYAV PPPAEREAPT DGKRLSASST GSTRSSQSAS SLEVVVPGRE 
       560        570        580        590        600
PLELEVAVET LARLQQGVST TVAHLLDLVG SASGPGGWRS TSEPQEPPVQ 
       610        620        630        640        650
DLKAAVAAVH GAVHELLEFA RSAVSSATHT SDRTLHAKLS RQLQKMEDVY 
       660        670        680        690        700
QTLVVHGQVL DSGRGGPGFT LDDLDRLVAC SRAVPEDAKQ LASFLHGNAS 
       710        720        730        740        750
LLFRRTKAPG PGPEGSSSLH LNPTDKASSI QSRPLPSPPK FTSQDSPDGQ 
       760        770        780        790        800
YENSEGGWME DYDYVHLQGK EEFEKTQKEL LEKGNIVRQG KGQLELQQLK 
       810        820        830        840        850
QFERLEQEVS RPIDHDLANW TPAQPLVPGR TGGLGPSDRQ LLLFYLEQCE 
       860        870        880        890        900
ANLTTLTDAV DAFFTAVATN QPPKIFVAHS KFVILSAHKL VFIGDTLSRQ 
       910        920        930        940        950
AKAADVRSKV THYSNLLCDL LRGIVATTKA AALQYPSPSA AQDMVDRVKE 
       960 
LGHSTQQFRR VLGQLAAA                                    

        10         20         30         40         50
MKYLNVLAKA LYDNVAESPD ELSFRKGDIM TVLERDTQGL DGWWLCSLHG 
        60         70         80         90        100
RQGIVPGNRL KILVGMYDKK PAAPGPGPPA TPPQPQPSLP QGVHTPVPPA 
       110        120        130        140        150
SQYSPMLPTA YQPQPDNVYL VPTPSKTQQG LYQAPGPNPQ FQSPPAKQTS 
       160        170        180        190        200
TFSKQTPHHS FPSPATDLYQ VPPGPGSPAQ DIYQVPPSAG TGHDIYQVPP 
       210        220        230        240        250
SLDTRSWEGT KPPAKVVVPT RVGQGYVYEA SQAEQDEYDT PRHLLAPGSQ 
       260        270        280        290        300
DIYDVPPVRG LLPNQYGQEV YDTPPMAVKG PNGRDPLLDV YDVPPSVEKG 
       310        320        330        340        350
LPPSNHHSVY DVPPSVSKDV PDGPLLREET YDVPPAFAKP KPFDPTRHPL 
       360        370        380        390        400
ILAAPPPDSP PAEDVYDVPP PAPDLYDVPP GLRRPGPGTL YDVPRERVLP 
       410        420        430        440        450
PEVADGSVID DGVYAVPPPA EREAPTDGKR LSASSTGSTR SSQSASSLEV 
       460        470        480        490        500
VVPGREPLEL EVAVETLARL QQGVSTTVAH LLDLVGSASG PGGWRSTSEP 
       510        520        530        540        550
QEPPVQDLKA AVAAVHGAVH ELLEFARSAV SSATHTSDRT LHAKLSRQLQ 
       560        570        580        590        600
KMEDVYQTLV VHGQVLDSGR GGPGFTLDDL DRLVACSRAV PEDAKQLASF 
       610        620        630        640        650
LHGNASLLFR RTKAPGPGPE GSSSLHLNPT DKASSIQSRP LPSPPKFTSQ 
       660        670        680        690        700
DSPDGQYENS EGGWMEDYDY VHLQGKEEFE KTQKELLEKG NIVRQGKGQL 
       710        720        730        740        750
ELQQLKQFER LEQEVSRPID HDLANWTPAQ PLVPGRTGGL GPSDRQLLLF 
       760        770        780        790        800
YLEQCEANLT TLTDAVDAFF TAVATNQPPK IFVAHSKFVI LSAHKLVFIG 
       810        820        830        840        850
DTLSRQAKAA DVRSKVTHYS NLLCDLLRGI VATTKAAALQ YPSPSAAQDM 
       860        870 
VDRVKELGHS TQQFRRVLGQ LAAA                             

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families