UniProtKB - P08631 (HCK_HUMAN)
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- BLAST>sp|P08631|HCK_HUMAN Tyrosine-protein kinase HCK OS=Homo sapiens OX=9606 GN=HCK PE=1 SV=5 MGGRSSCEDPGCPRDEERAPRMGCMKSKFLQVGGNTFSKTETSASPHCPVYVPDPTSTIK PGPNSHNSNTPGIREAGSEDIIVVALYDYEAIHHEDLSFQKGDQMVVLEESGEWWKARSL ATRKEGYIPSNYVARVDSLETEEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGSY SLSVRDYDPRQGDTVKHYKIRTLDNGGFYISPRSTFSTLQELVDHYKKGNDGLCQKLSVP CMSSKPQKPWEKDAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVE AFLAEANVMKTLQHDKLVKLHAVVTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLID FSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAKFP IKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPE NCPEELYNIMMRCWKNRPEERPTFEYIQSVLDDFYTATESQYQQQP
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Tyrosine-protein kinase HCK
HCK
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<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>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Physical and functional association of Src-related protein tyrosine kinases with Fc gamma RII in monocytic THP-1 cells."
Ghazizadeh S., Bolen J.B., Fleit H.B.
J. Biol. Chem. 269:8878-8884(1994) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FCGR2A, CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF FCGR2A. - Ref.11"The Fc gamma RI receptor signals through the activation of hck and MAP kinase."
Durden D.L., Kim H.M., Calore B., Liu Y.
J. Immunol. 154:4039-4047(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN FCGR1A SIGNALING, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION. - Ref.13"Signal transduction of interleukin-6 involves tyrosine phosphorylation of multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck, and Lyn in multiple myeloma cell lines."
Hallek M., Neumann C., Schaffer M., Danhauser-Riedl S., von Bubnoff N., de Vos G., Druker B.J., Yasukawa K., Griffin J.D., Emmerich B.
Exp. Hematol. 25:1367-1377(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION, INTERACTION WITH IL6ST. - Ref.16"The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr."
Warmuth M., Bergmann M., Priess A., Hauslmann K., Emmerich B., Hallek M.
J. Biol. Chem. 272:33260-33270(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION OF BCR, INTERACTION WITH BCR-ABL. - Ref.17"The proto-oncogene p120(Cbl) is a downstream substrate of the Hck protein-tyrosine kinase."
Howlett C.J., Bisson S.A., Resek M.E., Tigley A.W., Robbins S.M.
Biochem. Biophys. Res. Commun. 257:129-138(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CBL PHOSPHORYLATION; CELL PROLIFERATION AND REGULATION OF CELL SHAPE, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-522, INTERACTION WITH CBL. - Ref.18"IL-2 signaling in human monocytes involves the phosphorylation and activation of p59hck."
Bosco M.C., Curiel R.E., Zea A.H., Malabarba M.G., Ortaldo J.R., Espinoza-Delgado I.
J. Immunol. 164:4575-4585(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN IL2 SIGNALING, CATALYTIC ACTIVITY, INDUCTION, ENZYME REGULATION, PHOSPHORYLATION. - Ref.20"Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI."
Barlic J., Andrews J.D., Kelvin A.A., Bosinger S.E., DeVries M.E., Xu L., Dobransky T., Feldman R.D., Ferguson S.S., Kelvin D.J.
Nat. Immunol. 1:227-233(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN IL8-MEDIATED DEGRANULATION, ENZYME REGULATION, INTERACTION WITH ARRB1 AND ARRB2. - Ref.23"The Src family kinase Hck couples BCR/ABL to STAT5 activation in myeloid leukemia cells."
Klejman A., Schreiner S.J., Nieborowska-Skorska M., Slupianek A., Wilson M., Smithgall T.E., Skorski T.
EMBO J. 21:5766-5774(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS EFFECTOR OF THE BCR-ABL FUSION PROTEIN IN PHOSPHORYLATION OF STAT5B, INTERACTION WITH STAT5B AND THE BCR-ABL FUSION PROTEIN, PHOSPHORYLATION. - Ref.24"Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases."
Poghosyan Z., Robbins S.M., Houslay M.D., Webster A., Murphy G., Edwards D.R.
J. Biol. Chem. 277:4999-5007(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ADAM15, FUNCTION IN PHOSPHORYLATION OF ADAM15. - Ref.26"Membrane-anchored Cbl suppresses Hck protein-tyrosine kinase mediated cellular transformation."
Howlett C.J., Robbins S.M.
Oncogene 21:1707-1716(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL PROLIFERATION, UBIQUITINATION, PHOSPHORYLATION AT TYR-51; TYR-411 AND TYR-522, SUBCELLULAR LOCATION, INTERACTION WITH CBL (ISOFORM 2), MUTAGENESIS OF LYS-290 AND TYR-522. - Ref.27"Critical role for hematopoietic cell kinase (Hck)-mediated phosphorylation of Gab1 and Gab2 docking proteins in interleukin 6-induced proliferation and survival of multiple myeloma cells."
Podar K., Mostoslavsky G., Sattler M., Tai Y.T., Hayashi T., Catley L.P., Hideshima T., Mulligan R.C., Chauhan D., Anderson K.C.
J. Biol. Chem. 279:21658-21665(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN IL6 SIGNALING CASCADE AND IN PHOSPHORYLATION OF GAB1 AND GAB2. - Ref.28"Identification of tyrosine residues on ELMO1 that are phosphorylated by the Src-family kinase Hck."
Yokoyama N., deBakker C.D., Zappacosta F., Huddleston M.J., Annan R.S., Ravichandran K.S., Miller W.T.
Biochemistry 44:8841-8849(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION OF ELMO1, INTERACTION WITH ELMO1. - Ref.29"Activation of the lysosome-associated p61Hck isoform triggers the biogenesis of podosomes."
Cougoule C., Carreno S., Castandet J., Labrousse A., Astarie-Dequeker C., Poincloux R., Le Cabec V., Maridonneau-Parini I.
Traffic 6:682-694(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-381. - Ref.31"Regulation of p73 by Hck through kinase-dependent and independent mechanisms."
Paliwal P., Radha V., Swarup G.
BMC Mol. Biol. 8:45-45(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION AND INHIBITION OF TP73 ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH TP73 AND YAP1. - Ref.32"Inhibition of IL-6-dependent growth of myeloma cells by an acidic peptide repressing the gp130-mediated activation of Src family kinases."
Hausherr A., Tavares R., Schaffer M., Obermeier A., Miksch C., Mitina O., Ellwart J., Hallek M., Krause G.
Oncogene 26:4987-4998(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH IL6ST. - Ref.34"The oncogenic activity of the Src family kinase Hck requires the cooperative action of the plasma membrane- and lysosome-associated isoforms."
Poincloux R., Al Saati T., Maridonneau-Parini I., Le Cabec V.
Eur. J. Cancer 45:321-327(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN REORGANIZATION OF ACTIN CYTOSKELETON AND CELL PROLIFERATION, ROLE IN DISEASE. - Ref.37"c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration."
Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G., Berton G.
FEBS Lett. 584:15-21(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN ABL1-MEDIATED CELL MIGRATION, IDENTIFICATION IN A COMPLEX WITH ITGB1 AND WITH ABL1. - Ref.38"Expression of a Src family kinase in chronic myelogenous leukemia cells induces resistance to imatinib in a kinase-dependent manner."
Pene-Dumitrescu T., Smithgall T.E.
J. Biol. Chem. 285:21446-21457(2010) [PubMed] [Europe PMC] [Abstract]Cited for: ROLE IN DISEASE, FUNCTION IN PHOSPHORYLATION OF THE BCR-ABL FUSION PROTEIN. - Ref.40"Protein tyrosine kinases in neutrophil activation and recruitment."
Zarbock A., Ley K.
Arch. Biochem. Biophys. 510:112-119(2011) [PubMed] [Europe PMC] [Abstract]Cited for: ROLE IN NEUTROPHIL FUNCTION, SIGNALING.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
8 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Physical and functional association of Src-related protein tyrosine kinases with Fc gamma RII in monocytic THP-1 cells."
Ghazizadeh S., Bolen J.B., Fleit H.B.
J. Biol. Chem. 269:8878-8884(1994) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FCGR2A, CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF FCGR2A. - Ref.10"Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn."
Wang A.V., Scholl P.R., Geha R.S.
J. Exp. Med. 180:1165-1170(1994) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FCGR1A, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, PHOSPHORYLATION. - Ref.11"The Fc gamma RI receptor signals through the activation of hck and MAP kinase."
Durden D.L., Kim H.M., Calore B., Liu Y.
J. Immunol. 154:4039-4047(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN FCGR1A SIGNALING, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION. - Ref.14"Hck is activated by opsonized zymosan and A23187 in distinct subcellular fractions of human granulocytes."
Welch H., Maridonneau-Parini I.
J. Biol. Chem. 272:102-109(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. - Ref.17"The proto-oncogene p120(Cbl) is a downstream substrate of the Hck protein-tyrosine kinase."
Howlett C.J., Bisson S.A., Resek M.E., Tigley A.W., Robbins S.M.
Biochem. Biophys. Res. Commun. 257:129-138(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CBL PHOSPHORYLATION; CELL PROLIFERATION AND REGULATION OF CELL SHAPE, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-522, INTERACTION WITH CBL. - Ref.18"IL-2 signaling in human monocytes involves the phosphorylation and activation of p59hck."
Bosco M.C., Curiel R.E., Zea A.H., Malabarba M.G., Ortaldo J.R., Espinoza-Delgado I.
J. Immunol. 164:4575-4585(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN IL2 SIGNALING, CATALYTIC ACTIVITY, INDUCTION, ENZYME REGULATION, PHOSPHORYLATION. - Ref.29"Activation of the lysosome-associated p61Hck isoform triggers the biogenesis of podosomes."
Cougoule C., Carreno S., Castandet J., Labrousse A., Astarie-Dequeker C., Poincloux R., Le Cabec V., Maridonneau-Parini I.
Traffic 6:682-694(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-381. - Ref.52"Crystal structure of the Src family kinase Hck SH3-SH2 linker regulatory region supports an SH3-dominant activation mechanism."
Alvarado J.J., Betts L., Moroco J.A., Smithgall T.E., Yeh J.I.
J. Biol. Chem. 285:35455-35461(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 72-256, ENZYME REGULATION, CATALYTIC ACTIVITY.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"The Fc gamma RI receptor signals through the activation of hck and MAP kinase."
Durden D.L., Kim H.M., Calore B., Liu Y.
J. Immunol. 154:4039-4047(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN FCGR1A SIGNALING, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION. - Ref.13"Signal transduction of interleukin-6 involves tyrosine phosphorylation of multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck, and Lyn in multiple myeloma cell lines."
Hallek M., Neumann C., Schaffer M., Danhauser-Riedl S., von Bubnoff N., de Vos G., Druker B.J., Yasukawa K., Griffin J.D., Emmerich B.
Exp. Hematol. 25:1367-1377(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION, INTERACTION WITH IL6ST. - Ref.15"SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1."
Briggs S.D., Sharkey M., Stevenson M., Smithgall T.E.
J. Biol. Chem. 272:17899-17902(1997) [PubMed] [Europe PMC] [Abstract]Cited for: ENZYME REGULATION, INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION). - Ref.18"IL-2 signaling in human monocytes involves the phosphorylation and activation of p59hck."
Bosco M.C., Curiel R.E., Zea A.H., Malabarba M.G., Ortaldo J.R., Espinoza-Delgado I.
J. Immunol. 164:4575-4585(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN IL2 SIGNALING, CATALYTIC ACTIVITY, INDUCTION, ENZYME REGULATION, PHOSPHORYLATION. - Ref.19"Reciprocal regulation of Hck activity by phosphorylation of Tyr(527) and Tyr(416). Effect of introducing a high affinity intramolecular SH2 ligand."
Porter M., Schindler T., Kuriyan J., Miller W.T.
J. Biol. Chem. 275:2721-2726(2000) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT TYR-411 AND TYR-522, IDENTIFICATION BY MASS SPECTROMETRY, ENZYME REGULATION, MUTAGENESIS OF GLU-305 AND TYR-411. - Ref.20"Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI."
Barlic J., Andrews J.D., Kelvin A.A., Bosinger S.E., DeVries M.E., Xu L., Dobransky T., Feldman R.D., Ferguson S.S., Kelvin D.J.
Nat. Immunol. 1:227-233(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN IL8-MEDIATED DEGRANULATION, ENZYME REGULATION, INTERACTION WITH ARRB1 AND ARRB2. - Ref.30"HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src through direct SH3 domain interaction."
Trible R.P., Emert-Sedlak L., Smithgall T.E.
J. Biol. Chem. 281:27029-27038(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION), ENZYME REGULATION. - Ref.49"Discovery of A-770041, a src-family selective orally active lck inhibitor that prevents organ allograft rejection."
Burchat A., Borhani D.W., Calderwood D.J., Hirst G.C., Li B., Stachlewitz R.F.
Bioorg. Med. Chem. Lett. 16:118-122(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 81-522 IN COMPLEXES WITH INHIBITORS A-420983; A-641359 AND A-770041, ENZYME REGULATION, PHOSPHORYLATION AT TYR-522. - Ref.52"Crystal structure of the Src family kinase Hck SH3-SH2 linker regulatory region supports an SH3-dominant activation mechanism."
Alvarado J.J., Betts L., Moroco J.A., Smithgall T.E., Yeh J.I.
J. Biol. Chem. 285:35455-35461(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 72-256, ENZYME REGULATION, CATALYTIC ACTIVITY.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 290 | ATP | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 381 | Proton acceptor | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 268 – 276 | ATP | 9 |
<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
- ATP binding Source: UniProtKB-KW
- non-membrane spanning protein tyrosine kinase activity Source: GO_Central
- phosphotyrosine residue binding Source: CAFA <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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein tyrosine kinase activity Source: UniProtKB <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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- signaling receptor binding Source: GO_Central
<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 - Biological processi
- cell adhesion Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- cell differentiation Source: GO_Central
- cytokine-mediated signaling pathway Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
- inflammatory response Source: UniProtKB-KW
- innate immune response-activating signal transduction Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- integrin-mediated signaling pathway Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- interferon-gamma-mediated signaling pathway Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- leukocyte degranulation Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- leukocyte migration involved in immune response Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- lipopolysaccharide-mediated signaling pathway Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- mesoderm development Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- negative regulation of apoptotic process Source: UniProtKB <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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- peptidyl-tyrosine autophosphorylation Source: GO_Central
- peptidyl-tyrosine phosphorylation Source: UniProtKB <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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of actin cytoskeleton reorganization 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-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of actin filament polymerization Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- positive regulation of cell proliferation Source: UniProtKB <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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- protein autophosphorylation Source: UniProtKB <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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- protein phosphorylation Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- regulation of cell shape Source: UniProtKB <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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of defense response to virus by virus Source: Reactome
- regulation of DNA binding transcription factor activity Source: UniProtKB <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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of inflammatory response Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- regulation of phagocytosis Source: UniProtKB <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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of podosome assembly 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-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- respiratory burst after phagocytosis Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
<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
| Molecular function | Kinase, Transferase, Tyrosine-protein kinase |
| Biological process | Exocytosis, Host-virus interaction, Immunity, Inflammatory response, Innate immunity, Phagocytosis |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.10.2 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-164944 Nef and signal transduction R-HSA-2029481 FCGR activation R-HSA-912631 Regulation of signaling by CBL |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P08631 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P08631 |
<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
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Tyrosine-protein kinase HCK (EC:2.7.10.2)Alternative name(s): Hematopoietic cell kinase Hemopoietic cell kinase p59-HCK/p60-HCK p59Hck p61Hck |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:HCK |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000101336.12 |
Human Gene Nomenclature Database More...HGNCi | HGNC:4840 HCK |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 142370 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P08631 |
<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
Cytosol
Lysosome
Plasma membrane
Other locations
Note: Associated with specialized secretory lysosomes called azurophil granules. At least half of this isoform is found in the cytoplasm, some of this fraction is myristoylated.
Nucleus
- Nucleus 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"p59Hck isoform induces F-actin reorganization to form protrusions of the plasma membrane in a Cdc42- and Rac-dependent manner."
Carreno S., Caron E., Cougoule C., Emorine L.J., Maridonneau-Parini I.
J. Biol. Chem. 277:21007-21016(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN REORGANIZATION OF THE ACTIN CYTOSKELETON; FORMATION OF CELL PROTRUSIONS AND PHAGOCYTOSIS (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), MUTAGENESIS OF GLY-3.
- Nucleus 1 Publication
Cytoskeleton
- cytoskeleton 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"p59Hck isoform induces F-actin reorganization to form protrusions of the plasma membrane in a Cdc42- and Rac-dependent manner."
Carreno S., Caron E., Cougoule C., Emorine L.J., Maridonneau-Parini I.
J. Biol. Chem. 277:21007-21016(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN REORGANIZATION OF THE ACTIN CYTOSKELETON; FORMATION OF CELL PROTRUSIONS AND PHAGOCYTOSIS (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), MUTAGENESIS OF GLY-3.
- cytoskeleton 1 Publication
Lysosome
- Lysosome 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"p59Hck isoform induces F-actin reorganization to form protrusions of the plasma membrane in a Cdc42- and Rac-dependent manner."
Carreno S., Caron E., Cougoule C., Emorine L.J., Maridonneau-Parini I.
J. Biol. Chem. 277:21007-21016(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN REORGANIZATION OF THE ACTIN CYTOSKELETON; FORMATION OF CELL PROTRUSIONS AND PHAGOCYTOSIS (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), MUTAGENESIS OF GLY-3.
- Lysosome 1 Publication
Plasma membrane
- Cell membrane 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"p59Hck isoform induces F-actin reorganization to form protrusions of the plasma membrane in a Cdc42- and Rac-dependent manner."
Carreno S., Caron E., Cougoule C., Emorine L.J., Maridonneau-Parini I.
J. Biol. Chem. 277:21007-21016(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN REORGANIZATION OF THE ACTIN CYTOSKELETON; FORMATION OF CELL PROTRUSIONS AND PHAGOCYTOSIS (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), MUTAGENESIS OF GLY-3.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"p59Hck isoform induces F-actin reorganization to form protrusions of the plasma membrane in a Cdc42- and Rac-dependent manner."
Carreno S., Caron E., Cougoule C., Emorine L.J., Maridonneau-Parini I.
J. Biol. Chem. 277:21007-21016(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN REORGANIZATION OF THE ACTIN CYTOSKELETON; FORMATION OF CELL PROTRUSIONS AND PHAGOCYTOSIS (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), MUTAGENESIS OF GLY-3.
- Cell membrane 1 Publication
Golgi apparatus
- Golgi apparatus 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"p59Hck isoform induces F-actin reorganization to form protrusions of the plasma membrane in a Cdc42- and Rac-dependent manner."
Carreno S., Caron E., Cougoule C., Emorine L.J., Maridonneau-Parini I.
J. Biol. Chem. 277:21007-21016(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN REORGANIZATION OF THE ACTIN CYTOSKELETON; FORMATION OF CELL PROTRUSIONS AND PHAGOCYTOSIS (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), MUTAGENESIS OF GLY-3.
- Golgi apparatus 1 Publication
Other locations
- caveola 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"p59Hck isoform induces F-actin reorganization to form protrusions of the plasma membrane in a Cdc42- and Rac-dependent manner."
Carreno S., Caron E., Cougoule C., Emorine L.J., Maridonneau-Parini I.
J. Biol. Chem. 277:21007-21016(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN REORGANIZATION OF THE ACTIN CYTOSKELETON; FORMATION OF CELL PROTRUSIONS AND PHAGOCYTOSIS (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), MUTAGENESIS OF GLY-3.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"p59Hck isoform induces F-actin reorganization to form protrusions of the plasma membrane in a Cdc42- and Rac-dependent manner."
Carreno S., Caron E., Cougoule C., Emorine L.J., Maridonneau-Parini I.
J. Biol. Chem. 277:21007-21016(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN REORGANIZATION OF THE ACTIN CYTOSKELETON; FORMATION OF CELL PROTRUSIONS AND PHAGOCYTOSIS (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), MUTAGENESIS OF GLY-3.
- focal adhesion 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"p59Hck isoform induces F-actin reorganization to form protrusions of the plasma membrane in a Cdc42- and Rac-dependent manner."
Carreno S., Caron E., Cougoule C., Emorine L.J., Maridonneau-Parini I.
J. Biol. Chem. 277:21007-21016(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN REORGANIZATION OF THE ACTIN CYTOSKELETON; FORMATION OF CELL PROTRUSIONS AND PHAGOCYTOSIS (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), MUTAGENESIS OF GLY-3.
- Cytoplasmic vesicle 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"p59Hck isoform induces F-actin reorganization to form protrusions of the plasma membrane in a Cdc42- and Rac-dependent manner."
Carreno S., Caron E., Cougoule C., Emorine L.J., Maridonneau-Parini I.
J. Biol. Chem. 277:21007-21016(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN REORGANIZATION OF THE ACTIN CYTOSKELETON; FORMATION OF CELL PROTRUSIONS AND PHAGOCYTOSIS (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), MUTAGENESIS OF GLY-3.
Note: 20% of this isoform is associated with caveolae. Localization at the cell membrane and at caveolae requires palmitoylation at Cys-3. Colocalizes with the actin cytoskeleton at focal adhesions.- caveola 1 Publication
Cytosol
Other locations
Cytoskeleton
- cytoskeleton Source: UniProtKB-SubCell
Cytosol
- cytosol Source: Reactome
Golgi apparatus
- Golgi apparatus Source: UniProtKB-SubCell
Lysosome
- lysosome 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-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Nucleus
- nucleoplasm Source: HPA
Plasma Membrane
- caveola 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-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB <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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- plasma membrane Source: HPA
Other locations
- cell projection Source: UniProtKB-KW
- focal adhesion Source: UniProtKB <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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- transport vesicle Source: UniProtKB-SubCell
<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>Keywords - Cellular componenti
Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Golgi apparatus, Lysosome, Membrane, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 3 | G → C: Slight palmitoylation, cytoplasmic and caveolar localization; in isoform 1;. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 3 | G → S: Abolishes palmitoylation and localization at the cell membrane. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 23 | G → A: Myristoylation and palmitoylation are abolished, leading to entirely cytoplasmic localization; in isoform 2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 24 | C → S: Palmitoylation is abolished, some cytoplasmic and no calveolar localization; in isoform 2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 290 | K → E: Loss of kinase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 305 | E → A: Loss of kinase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 381 | D → E: Loss of kinase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 411 | Y → A: Reduced catalytic activity and higher affinity for target peptides. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 522 | Y → F: Constitutively activated kinase, leading to cellular transformation. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<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>Keywords - Diseasei
Proto-oncogeneOrganism-specific databases
DisGeNET More...DisGeNETi | 3055 |
Open Targets More...OpenTargetsi | ENSG00000101336 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA29216 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3234 |
Drug and drug target database More...DrugBanki | DB06616 Bosutinib DB01962 Phosphonotyrosine DB04216 Quercetin |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2032 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | HCK |
Domain mapping of disease mutations (DMDM) More...DMDMi | 20141296 |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed | ||||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000024433 | 2 – 526 | Tyrosine-protein kinase HCKAdd BLAST | 525 | ||
| Isoform 2 (identifier: P08631-2) | |||||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed | ||||
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 2 | N-myristoyl glycine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 36 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 51 | Phosphotyrosine; by autocatalysis1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 202 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 209 | PhosphotyrosineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 411 | Phosphotyrosine; by autocatalysis2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 462 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 522 | Phosphotyrosine5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| Isoform 2 (identifier: P08631-2) | |||||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 2 | N-myristoyl glycine | 1 | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 3 | S-palmitoyl cysteine | 1 | ||
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn."
Wang A.V., Scholl P.R., Geha R.S.
J. Exp. Med. 180:1165-1170(1994) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FCGR1A, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, PHOSPHORYLATION. - Ref.13"Signal transduction of interleukin-6 involves tyrosine phosphorylation of multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck, and Lyn in multiple myeloma cell lines."
Hallek M., Neumann C., Schaffer M., Danhauser-Riedl S., von Bubnoff N., de Vos G., Druker B.J., Yasukawa K., Griffin J.D., Emmerich B.
Exp. Hematol. 25:1367-1377(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION, INTERACTION WITH IL6ST. - Ref.18"IL-2 signaling in human monocytes involves the phosphorylation and activation of p59hck."
Bosco M.C., Curiel R.E., Zea A.H., Malabarba M.G., Ortaldo J.R., Espinoza-Delgado I.
J. Immunol. 164:4575-4585(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN IL2 SIGNALING, CATALYTIC ACTIVITY, INDUCTION, ENZYME REGULATION, PHOSPHORYLATION. - Ref.19"Reciprocal regulation of Hck activity by phosphorylation of Tyr(527) and Tyr(416). Effect of introducing a high affinity intramolecular SH2 ligand."
Porter M., Schindler T., Kuriyan J., Miller W.T.
J. Biol. Chem. 275:2721-2726(2000) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT TYR-411 AND TYR-522, IDENTIFICATION BY MASS SPECTROMETRY, ENZYME REGULATION, MUTAGENESIS OF GLU-305 AND TYR-411. - Ref.23"The Src family kinase Hck couples BCR/ABL to STAT5 activation in myeloid leukemia cells."
Klejman A., Schreiner S.J., Nieborowska-Skorska M., Slupianek A., Wilson M., Smithgall T.E., Skorski T.
EMBO J. 21:5766-5774(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS EFFECTOR OF THE BCR-ABL FUSION PROTEIN IN PHOSPHORYLATION OF STAT5B, INTERACTION WITH STAT5B AND THE BCR-ABL FUSION PROTEIN, PHOSPHORYLATION. - Ref.26"Membrane-anchored Cbl suppresses Hck protein-tyrosine kinase mediated cellular transformation."
Howlett C.J., Robbins S.M.
Oncogene 21:1707-1716(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL PROLIFERATION, UBIQUITINATION, PHOSPHORYLATION AT TYR-51; TYR-411 AND TYR-522, SUBCELLULAR LOCATION, INTERACTION WITH CBL (ISOFORM 2), MUTAGENESIS OF LYS-290 AND TYR-522. - Ref.45"Crystal structure of the Src family tyrosine kinase Hck."
Sicheri F., Moarefi I., Kuriyan J.
Nature 385:602-609(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 78-526 IN COMPLEX WITH CALCIUM, PHOSPHORYLATION AT TYR-522. - Ref.48"Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor."
Schindler T., Sicheri F., Pico A., Gazit A., Levitzki A., Kuriyan J.
Mol. Cell 3:639-648(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 81-522 IN COMPLEX WITH THE PYRAZOLO PYRIMIDINE-TYPE INHIBITOR PP1, PHOSPHORYLATION AT TYR-522. - Ref.49"Discovery of A-770041, a src-family selective orally active lck inhibitor that prevents organ allograft rejection."
Burchat A., Borhani D.W., Calderwood D.J., Hirst G.C., Li B., Stachlewitz R.F.
Bioorg. Med. Chem. Lett. 16:118-122(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 81-522 IN COMPLEXES WITH INHIBITORS A-420983; A-641359 AND A-770041, ENZYME REGULATION, PHOSPHORYLATION AT TYR-522.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.26"Membrane-anchored Cbl suppresses Hck protein-tyrosine kinase mediated cellular transformation."
Howlett C.J., Robbins S.M.
Oncogene 21:1707-1716(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL PROLIFERATION, UBIQUITINATION, PHOSPHORYLATION AT TYR-51; TYR-411 AND TYR-522, SUBCELLULAR LOCATION, INTERACTION WITH CBL (ISOFORM 2), MUTAGENESIS OF LYS-290 AND TYR-522.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae."
Robbins S.M., Quintrell N.A., Bishop J.M.
Mol. Cell. Biol. 15:3507-3515(1995) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, ALTERNATIVE INITIATION, MYRISTOYLATION AT GLY-2, MYRISTOYLATION AT GLY-2 (ISOFORM 2), PALMITOYLATION AT CYS-3 (ISOFORM 2), MUTAGENESIS OF GLY-3; GLY-23 AND CYS-24.
<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>Keywords - PTMi
Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P08631 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P08631 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P08631 |
PeptideAtlas More...PeptideAtlasi | P08631 |
PRoteomics IDEntifications database More...PRIDEi | P08631 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 52142 52143 [P08631-2] 52144 [P08631-3] 52145 [P08631-4] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P08631 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P08631 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P08631 |
<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>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells of hematopoietic origin."
Ziegler S.F., Marth J.D., Lewis D.B., Perlmutter R.M.
Mol. Cell. Biol. 7:2276-2285(1987) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY. - Ref.10"Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn."
Wang A.V., Scholl P.R., Geha R.S.
J. Exp. Med. 180:1165-1170(1994) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FCGR1A, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, PHOSPHORYLATION. - Ref.14"Hck is activated by opsonized zymosan and A23187 in distinct subcellular fractions of human granulocytes."
Welch H., Maridonneau-Parini I.
J. Biol. Chem. 272:102-109(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Hck is activated by opsonized zymosan and A23187 in distinct subcellular fractions of human granulocytes."
Welch H., Maridonneau-Parini I.
J. Biol. Chem. 272:102-109(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. - Ref.18"IL-2 signaling in human monocytes involves the phosphorylation and activation of p59hck."
Bosco M.C., Curiel R.E., Zea A.H., Malabarba M.G., Ortaldo J.R., Espinoza-Delgado I.
J. Immunol. 164:4575-4585(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN IL2 SIGNALING, CATALYTIC ACTIVITY, INDUCTION, ENZYME REGULATION, PHOSPHORYLATION.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000101336 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P08631 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P08631 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB005195 HPA063768 |
<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Physical and functional association of Src-related protein tyrosine kinases with Fc gamma RII in monocytic THP-1 cells."
Ghazizadeh S., Bolen J.B., Fleit H.B.
J. Biol. Chem. 269:8878-8884(1994) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FCGR2A, CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF FCGR2A. - Ref.10"Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn."
Wang A.V., Scholl P.R., Geha R.S.
J. Exp. Med. 180:1165-1170(1994) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FCGR1A, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, PHOSPHORYLATION. - Ref.13"Signal transduction of interleukin-6 involves tyrosine phosphorylation of multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck, and Lyn in multiple myeloma cell lines."
Hallek M., Neumann C., Schaffer M., Danhauser-Riedl S., von Bubnoff N., de Vos G., Druker B.J., Yasukawa K., Griffin J.D., Emmerich B.
Exp. Hematol. 25:1367-1377(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION, INTERACTION WITH IL6ST. - Ref.16"The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr."
Warmuth M., Bergmann M., Priess A., Hauslmann K., Emmerich B., Hallek M.
J. Biol. Chem. 272:33260-33270(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION OF BCR, INTERACTION WITH BCR-ABL. - Ref.17"The proto-oncogene p120(Cbl) is a downstream substrate of the Hck protein-tyrosine kinase."
Howlett C.J., Bisson S.A., Resek M.E., Tigley A.W., Robbins S.M.
Biochem. Biophys. Res. Commun. 257:129-138(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CBL PHOSPHORYLATION; CELL PROLIFERATION AND REGULATION OF CELL SHAPE, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-522, INTERACTION WITH CBL. - Ref.20"Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI."
Barlic J., Andrews J.D., Kelvin A.A., Bosinger S.E., DeVries M.E., Xu L., Dobransky T., Feldman R.D., Ferguson S.S., Kelvin D.J.
Nat. Immunol. 1:227-233(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN IL8-MEDIATED DEGRANULATION, ENZYME REGULATION, INTERACTION WITH ARRB1 AND ARRB2. - Ref.23"The Src family kinase Hck couples BCR/ABL to STAT5 activation in myeloid leukemia cells."
Klejman A., Schreiner S.J., Nieborowska-Skorska M., Slupianek A., Wilson M., Smithgall T.E., Skorski T.
EMBO J. 21:5766-5774(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS EFFECTOR OF THE BCR-ABL FUSION PROTEIN IN PHOSPHORYLATION OF STAT5B, INTERACTION WITH STAT5B AND THE BCR-ABL FUSION PROTEIN, PHOSPHORYLATION. - Ref.24"Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases."
Poghosyan Z., Robbins S.M., Houslay M.D., Webster A., Murphy G., Edwards D.R.
J. Biol. Chem. 277:4999-5007(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ADAM15, FUNCTION IN PHOSPHORYLATION OF ADAM15. - Ref.28"Identification of tyrosine residues on ELMO1 that are phosphorylated by the Src-family kinase Hck."
Yokoyama N., deBakker C.D., Zappacosta F., Huddleston M.J., Annan R.S., Ravichandran K.S., Miller W.T.
Biochemistry 44:8841-8849(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION OF ELMO1, INTERACTION WITH ELMO1. - Ref.31"Regulation of p73 by Hck through kinase-dependent and independent mechanisms."
Paliwal P., Radha V., Swarup G.
BMC Mol. Biol. 8:45-45(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION AND INHIBITION OF TP73 ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH TP73 AND YAP1. - Ref.32"Inhibition of IL-6-dependent growth of myeloma cells by an acidic peptide repressing the gp130-mediated activation of Src family kinases."
Hausherr A., Tavares R., Schaffer M., Obermeier A., Miksch C., Mitina O., Ellwart J., Hallek M., Krause G.
Oncogene 26:4987-4998(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH IL6ST. - Ref.33"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
Voss M., Lettau M., Janssen O.
BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FASLG. - Ref.35"Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins."
Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.
J. Cell. Biochem. 108:877-885(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ADAM15. - Ref.37"c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration."
Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G., Berton G.
FEBS Lett. 584:15-21(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN ABL1-MEDIATED CELL MIGRATION, IDENTIFICATION IN A COMPLEX WITH ITGB1 AND WITH ABL1. - Ref.42"Molecular characterization of WDCP, a novel fusion partner for the anaplastic lymphoma tyrosine kinase ALK."
Yokoyama N., Miller W.T.
Biomed. Rep. 3:9-13(2015) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH WDCP. - Ref.45"Crystal structure of the Src family tyrosine kinase Hck."
Sicheri F., Moarefi I., Kuriyan J.
Nature 385:602-609(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 78-526 IN COMPLEX WITH CALCIUM, PHOSPHORYLATION AT TYR-522. - Ref.48"Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor."
Schindler T., Sicheri F., Pico A., Gazit A., Levitzki A., Kuriyan J.
Mol. Cell 3:639-648(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 81-522 IN COMPLEX WITH THE PYRAZOLO PYRIMIDINE-TYPE INHIBITOR PP1, PHOSPHORYLATION AT TYR-522. - Ref.50"The development of 2-benzimidazole substituted pyrimidine based inhibitors of lymphocyte specific kinase (Lck)."
Sabat M., VanRens J.C., Laufersweiler M.J., Brugel T.A., Maier J., Golebiowski A., De B., Easwaran V., Hsieh L.C., Walter R.L., Mekel M.J., Evdokimov A., Janusz M.J.
Bioorg. Med. Chem. Lett. 16:5973-5977(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 247-513 IN COMPLEX WITH INHIBITOR PG-1009247. - Ref.51"Solution structure of a Hck SH3 domain ligand complex reveals novel interaction modes."
Schmidt H., Hoffmann S., Tran T., Stoldt M., Stangler T., Wiesehan K., Willbold D.
J. Mol. Biol. 365:1517-1532(2007) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 61-140 IN COMPLEX WITH PROLINE-RICH SYNTHETIC PEPTIDE.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.22"The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK."
Korkaya H., Jameel S., Gupta D., Tyagi S., Kumar R., Zafrullah M., Mazumdar M., Lal S.K., Xiaofang L., Sehgal D., Das S.R., Sahal D.
J. Biol. Chem. 276:42389-42400(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HEV ORF3 PROTEIN (MICROBIAL INFECTION).
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.15"SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1."
Briggs S.D., Sharkey M., Stevenson M., Smithgall T.E.
J. Biol. Chem. 272:17899-17902(1997) [PubMed] [Europe PMC] [Abstract]Cited for: ENZYME REGULATION, INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION). - Ref.21"The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif protein."
Hassaine G., Courcoul M., Bessou G., Barthalay Y., Picard C., Olive D., Collette Y., Vigne R., Decroly E.
J. Biol. Chem. 276:16885-16893(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HIV-1 VIF (MICROBIAL INFECTION). - Ref.30"HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src through direct SH3 domain interaction."
Trible R.P., Emert-Sedlak L., Smithgall T.E.
J. Biol. Chem. 281:27029-27038(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION), ENZYME REGULATION. - Ref.53"Molecular design, functional characterization and structural basis of a protein inhibitor against the HIV-1 pathogenicity factor Nef."
Breuer S., Schievink S.I., Schulte A., Blankenfeldt W., Fackler O.T., Geyer M.
PLoS ONE 6:E20033-E20033(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 79-138 IN COMPLEX WITH HIV-1 NEF, INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION). - Ref.54"Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by intermolecular domain assembly."
Horenkamp F.A., Breuer S., Schulte A., Lulf S., Weyand M., Saksela K., Geyer M.
Traffic 12:867-877(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 79-138 IN COMPLEX WITH HIV-1 NEF, INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION).
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%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
<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
- phosphotyrosine residue binding Source: CAFA <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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- signaling receptor binding Source: GO_Central
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 109305, 64 interactors |
Database of interacting proteins More...DIPi | DIP-1051N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P08631 |
Protein interaction database and analysis system More...IntActi | P08631, 108 interactors |
Molecular INTeraction database More...MINTi | P08631 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000365012 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P08631 |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 82 – 85 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 93 – 96 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 99 – 102 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 104 – 111 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 114 – 122 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 127 – 129 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 130 – 132 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 133 – 135 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 136 – 138 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 139 – 141 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 145 – 148 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 151 – 159 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 168 – 172 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 174 – 176 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 180 – 188 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 189 – 191 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 192 – 202 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 204 – 206 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 208 – 211 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 215 – 218 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 219 – 228 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 233 – 235 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 252 – 255 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 259 – 261 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 262 – 270 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 272 – 281 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 282 – 284 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 285 – 292 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 294 – 297 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 299 – 309 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 320 – 324 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 326 – 328 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 330 – 333 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 341 – 345 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 350 – 352 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 355 – 374 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 384 – 386 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 387 – 389 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 395 – 397 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 402 – 405 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 410 – 413 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 416 – 419 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 421 – 423 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 426 – 431 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 436 – 451 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 452 – 454 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 457 – 460 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 463 – 471 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 480 – 482 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 484 – 493 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 498 – 500 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 504 – 512 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 513 – 518 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 521 – 523 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P08631 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P08631 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P08631 |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 78 – 138 | SH3PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 61 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 144 – 241 | SH2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 98 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 262 – 515 | Protein kinasePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 254 |
<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
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
<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>Keywords - Domaini
SH2 domain, SH3 domainPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0197 Eukaryota COG0515 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118938 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000233858 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG008761 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P08631 |
KEGG Orthology (KO) More...KOi | K08893 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P08631 |
Family and domain databases
Conserved Domains Database More...CDDi | cd10363 SH2_Src_HCK, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.505.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR035851 HCK_SH2 IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR001245 Ser-Thr/Tyr_kinase_cat_dom IPR000980 SH2 IPR036860 SH2_dom_sf IPR036028 SH3-like_dom_sf IPR001452 SH3_domain IPR008266 Tyr_kinase_AS IPR020635 Tyr_kinase_cat_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF07714 Pkinase_Tyr, 1 hit PF00017 SH2, 1 hit PF00018 SH3_1, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00401 SH2DOMAIN PR00452 SH3DOMAIN PR00109 TYRKINASE |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00252 SH2, 1 hit SM00326 SH3, 1 hit SM00219 TyrKc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50044 SSF50044, 1 hit SSF55550 SSF55550, 1 hit SSF56112 SSF56112, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00109 PROTEIN_KINASE_TYR, 1 hit PS50001 SH2, 1 hit PS50002 SH3, 1 hit |
<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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MGGRSSCEDP GCPRDEERAP RMGCMKSKFL QVGGNTFSKT ETSASPHCPV
60 70 80 90 100
YVPDPTSTIK PGPNSHNSNT PGIREAGSED IIVVALYDYE AIHHEDLSFQ
110 120 130 140 150
KGDQMVVLEE SGEWWKARSL ATRKEGYIPS NYVARVDSLE TEEWFFKGIS
160 170 180 190 200
RKDAERQLLA PGNMLGSFMI RDSETTKGSY SLSVRDYDPR QGDTVKHYKI
210 220 230 240 250
RTLDNGGFYI SPRSTFSTLQ ELVDHYKKGN DGLCQKLSVP CMSSKPQKPW
260 270 280 290 300
EKDAWEIPRE SLKLEKKLGA GQFGEVWMAT YNKHTKVAVK TMKPGSMSVE
310 320 330 340 350
AFLAEANVMK TLQHDKLVKL HAVVTKEPIY IITEFMAKGS LLDFLKSDEG
360 370 380 390 400
SKQPLPKLID FSAQIAEGMA FIEQRNYIHR DLRAANILVS ASLVCKIADF
410 420 430 440 450
GLARVIEDNE YTAREGAKFP IKWTAPEAIN FGSFTIKSDV WSFGILLMEI
460 470 480 490 500
VTYGRIPYPG MSNPEVIRAL ERGYRMPRPE NCPEELYNIM MRCWKNRPEE
510 520
RPTFEYIQSV LDDFYTATES QYQQQP
The sequence of this isoform differs from the canonical sequence as follows:
1-21: Missing.
10 20 30 40 50
MGCMKSKFLQ VGGNTFSKTE TSASPHCPVY VPDPTSTIKP GPNSHNSNTP
60 70 80 90 100
GIREAGSEDI IVVALYDYEA IHHEDLSFQK GDQMVVLEES GEWWKARSLA
110 120 130 140 150
TRKEGYIPSN YVARVDSLET EEWFFKGISR KDAERQLLAP GNMLGSFMIR
160 170 180 190 200
DSETTKGSYS LSVRDYDPRQ GDTVKHYKIR TLDNGGFYIS PRSTFSTLQE
210 220 230 240 250
LVDHYKKGND GLCQKLSVPC MSSKPQKPWE KDAWEIPRES LKLEKKLGAG
260 270 280 290 300
QFGEVWMATY NKHTKVAVKT MKPGSMSVEA FLAEANVMKT LQHDKLVKLH
310 320 330 340 350
AVVTKEPIYI ITEFMAKGSL LDFLKSDEGS KQPLPKLIDF SAQIAEGMAF
360 370 380 390 400
IEQRNYIHRD LRAANILVSA SLVCKIADFG LARVIEDNEY TAREGAKFPI
410 420 430 440 450
KWTAPEAINF GSFTIKSDVW SFGILLMEIV TYGRIPYPGM SNPEVIRALE
460 470 480 490 500
RGYRMPRPEN CPEELYNIMM RCWKNRPEER PTFEYIQSVL DDFYTATESQ
YQQQP
The sequence of this isoform differs from the canonical sequence as follows:
1-21: Missing.
76-76: Missing.
10 20 30 40 50
MGCMKSKFLQ VGGNTFSKTE TSASPHCPVY VPDPTSTIKP GPNSHNSNTP
60 70 80 90 100
GIREGSEDII VVALYDYEAI HHEDLSFQKG DQMVVLEESG EWWKARSLAT
110 120 130 140 150
RKEGYIPSNY VARVDSLETE EWFFKGISRK DAERQLLAPG NMLGSFMIRD
160 170 180 190 200
SETTKGSYSL SVRDYDPRQG DTVKHYKIRT LDNGGFYISP RSTFSTLQEL
210 220 230 240 250
VDHYKKGNDG LCQKLSVPCM SSKPQKPWEK DAWEIPRESL KLEKKLGAGQ
260 270 280 290 300
FGEVWMATYN KHTKVAVKTM KPGSMSVEAF LAEANVMKTL QHDKLVKLHA
310 320 330 340 350
VVTKEPIYII TEFMAKGSLL DFLKSDEGSK QPLPKLIDFS AQIAEGMAFI
360 370 380 390 400
EQRNYIHRDL RAANILVSAS LVCKIADFGL ARVIEDNEYT AREGAKFPIK
410 420 430 440 450
WTAPEAINFG SFTIKSDVWS FGILLMEIVT YGRIPYPGMS NPEVIRALER
460 470 480 490 500
GYRMPRPENC PEELYNIMMR CWKNRPEERP TFEYIQSVLD DFYTATESQY
QQQP
The sequence of this isoform differs from the canonical sequence as follows:
76-76: Missing.
10 20 30 40 50
MGGRSSCEDP GCPRDEERAP RMGCMKSKFL QVGGNTFSKT ETSASPHCPV
60 70 80 90 100
YVPDPTSTIK PGPNSHNSNT PGIREGSEDI IVVALYDYEA IHHEDLSFQK
110 120 130 140 150
GDQMVVLEES GEWWKARSLA TRKEGYIPSN YVARVDSLET EEWFFKGISR
160 170 180 190 200
KDAERQLLAP GNMLGSFMIR DSETTKGSYS LSVRDYDPRQ GDTVKHYKIR
210 220 230 240 250
TLDNGGFYIS PRSTFSTLQE LVDHYKKGND GLCQKLSVPC MSSKPQKPWE
260 270 280 290 300
KDAWEIPRES LKLEKKLGAG QFGEVWMATY NKHTKVAVKT MKPGSMSVEA
310 320 330 340 350
FLAEANVMKT LQHDKLVKLH AVVTKEPIYI ITEFMAKGSL LDFLKSDEGS
360 370 380 390 400
KQPLPKLIDF SAQIAEGMAF IEQRNYIHRD LRAANILVSA SLVCKIADFG
410 420 430 440 450
LARVIEDNEY TAREGAKFPI KWTAPEAINF GSFTIKSDVW SFGILLMEIV
460 470 480 490 500
TYGRIPYPGM SNPEVIRALE RGYRMPRPEN CPEELYNIMM RCWKNRPEER
510 520
PTFEYIQSVL DDFYTATESQ YQQQP
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 24 | C → S in AAA52643 (PubMed:3496523).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 69 | N → D in BAF82585 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 144 | W → R in BAB15482 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 168 | F → Y in BAF82585 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 378 | I → T in AAI13855 (PubMed:15489334).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 488 | N → S in BAF82585 (PubMed:14702039).Curated | 1 |
Natural variant
Alternative sequence
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M16591 mRNA Translation: AAA52643.1 Frameshift. M16592 mRNA Translation: AAA52644.1 AK026432 mRNA Translation: BAB15482.1 AK289896 mRNA Translation: BAF82585.1 Different initiation. AK298726 mRNA Translation: BAG60878.1 AL353092, AL049539 Genomic DNA Translation: CAI19694.1 AL353092, AL049539 Genomic DNA Translation: CAI19695.1 AL049539, AL353092 Genomic DNA Translation: CAI22966.1 AL049539, AL353092 Genomic DNA Translation: CAI22967.1 CH471077 Genomic DNA Translation: EAW76392.1 CH471077 Genomic DNA Translation: EAW76393.1 BC014435 mRNA Translation: AAH14435.2 BC094847 mRNA Translation: AAH94847.2 BC108930 mRNA Translation: AAI08931.2 BC108931 mRNA Translation: AAI08932.2 BC113854 mRNA Translation: AAI13855.2 BC114463 mRNA Translation: AAI14464.2 X58741, X58742, X58743 Genomic DNA Translation: CAA41565.2 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS33460.1 [P08631-1] CCDS54453.1 [P08631-4] CCDS54455.1 [P08631-2] CCDS54456.1 [P08631-3] |
Protein sequence database of the Protein Information Resource More...PIRi | A27811 TVHUHC A41263 |
NCBI Reference Sequences More...RefSeqi | NP_001165600.1, NM_001172129.1 [P08631-2] NP_001165601.1, NM_001172130.1 [P08631-4] NP_001165602.1, NM_001172131.1 [P08631-3] NP_001165604.1, NM_001172133.1 [P08631-2] NP_002101.2, NM_002110.3 [P08631-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.655210 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000518730; ENSP00000427757; ENSG00000101336 [P08631-3] ENST00000520553; ENSP00000429848; ENSG00000101336 [P08631-2] ENST00000534862; ENSP00000444986; ENSG00000101336 [P08631-1] ENST00000538448; ENSP00000441169; ENSG00000101336 [P08631-2] ENST00000629881; ENSP00000486627; ENSG00000101336 [P08631-2] ENST00000639405; ENSP00000491964; ENSG00000101336 [P08631-4] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 3055 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:3055 |
UCSC genome browser More...UCSCi | uc002wxi.4 human [P08631-1] |
<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>Keywords - Coding sequence diversityi
Alternative initiation, Alternative splicing, Polymorphism<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
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P08631 | Tyrosine-protein kinase | 526 | |||
| P08631-2 | 505 | ||||
| UPI0000111AFB | 72 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P08631 | Tyrosine-protein kinase | 526 | |||
| Tyrosine-protein kinase | 627 | ||||
| Tyrosine-protein kinase | 527 | ||||
| Tyrosine-protein kinase | 526 | ||||
| Tyrosine-protein kinase | 526 | ||||
| +112 | |||||
| P08631-3 | Tyrosine-protein kinase HCK | 524 | |||
| UPI000A30E2A7 | 634 | ||||
| UPI000A3166DD | 634 | ||||
| Tyrosine-protein kinase | 525 | ||||
| Tyrosine-protein kinase | 525 | ||||
| +14 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P08631 | Tyrosine-protein kinase Lyn | ) | 512 | ||
| Tyrosine-protein kinase | 512 | ||||
| Tyrosine-protein kinase | 512 | ||||
| UPI0004ECFE1A | 602 | ||||
| UPI000B4F8825 | 158 | ||||
| +588 | |||||
| P08631-3 | Tyrosine-protein kinase HCK | 524 | |||
| UPI000A3166DD | 634 | ||||
| UPI000A30E2A7 | 634 | ||||
| Tyrosine-protein kinase | 525 | ||||
| Tyrosine-protein kinase | 525 | ||||
| +268 | |||||
<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
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M16591 mRNA Translation: AAA52643.1 Frameshift. M16592 mRNA Translation: AAA52644.1 AK026432 mRNA Translation: BAB15482.1 AK289896 mRNA Translation: BAF82585.1 Different initiation. AK298726 mRNA Translation: BAG60878.1 AL353092, AL049539 Genomic DNA Translation: CAI19694.1 AL353092, AL049539 Genomic DNA Translation: CAI19695.1 AL049539, AL353092 Genomic DNA Translation: CAI22966.1 AL049539, AL353092 Genomic DNA Translation: CAI22967.1 CH471077 Genomic DNA Translation: EAW76392.1 CH471077 Genomic DNA Translation: EAW76393.1 BC014435 mRNA Translation: AAH14435.2 BC094847 mRNA Translation: AAH94847.2 BC108930 mRNA Translation: AAI08931.2 BC108931 mRNA Translation: AAI08932.2 BC113854 mRNA Translation: AAI13855.2 BC114463 mRNA Translation: AAI14464.2 X58741, X58742, X58743 Genomic DNA Translation: CAA41565.2 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS33460.1 [P08631-1] CCDS54453.1 [P08631-4] CCDS54455.1 [P08631-2] CCDS54456.1 [P08631-3] |
Protein sequence database of the Protein Information Resource More...PIRi | A27811 TVHUHC A41263 |
NCBI Reference Sequences More...RefSeqi | NP_001165600.1, NM_001172129.1 [P08631-2] NP_001165601.1, NM_001172130.1 [P08631-4] NP_001165602.1, NM_001172131.1 [P08631-3] NP_001165604.1, NM_001172133.1 [P08631-2] NP_002101.2, NM_002110.3 [P08631-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.655210 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1AD5 | X-ray | 2.60 | A/B | 79-526 | [»] | |
| 1BU1 | X-ray | 2.60 | A/B/C/D/E/F | 81-137 | [»] | |
| 1QCF | X-ray | 2.00 | A | 81-526 | [»] | |
| 2C0I | X-ray | 2.30 | A/B | 81-526 | [»] | |
| 2C0O | X-ray | 2.85 | A/B | 81-526 | [»] | |
| 2C0T | X-ray | 2.15 | A/B | 81-526 | [»] | |
| 2HCK | X-ray | 3.00 | A/B | 79-526 | [»] | |
| 2HK5 | X-ray | 2.00 | A | 247-514 | [»] | |
| 2OI3 | NMR | - | A | 61-141 | [»] | |
| 2OJ2 | NMR | - | A | 61-141 | [»] | |
| 3HCK | NMR | - | A | 140-245 | [»] | |
| 3NHN | X-ray | 2.61 | A | 72-256 | [»] | |
| 3RBB | X-ray | 2.35 | B/D | 79-138 | [»] | |
| 3REA | X-ray | 2.00 | B/D | 79-138 | [»] | |
| 3REB | X-ray | 3.45 | B/D | 79-138 | [»] | |
| 3VRY | X-ray | 2.48 | A/B | 81-526 | [»] | |
| 3VRZ | X-ray | 2.22 | A/B | 81-526 | [»] | |
| 3VS0 | X-ray | 2.93 | A/B | 81-526 | [»] | |
| 3VS1 | X-ray | 2.46 | A/B | 81-526 | [»] | |
| 3VS2 | X-ray | 2.61 | A/B | 81-526 | [»] | |
| 3VS3 | X-ray | 2.17 | A/B | 81-526 | [»] | |
| 3VS4 | X-ray | 2.75 | A/B | 81-526 | [»] | |
| 3VS5 | X-ray | 2.85 | A/B | 81-526 | [»] | |
| 3VS6 | X-ray | 2.37 | A/B | 81-526 | [»] | |
| 3VS7 | X-ray | 3.00 | A/B | 81-526 | [»] | |
| 4HCK | NMR | - | A | 72-143 | [»] | |
| 4LUD | X-ray | 2.85 | A/B | 81-526 | [»] | |
| 4LUE | X-ray | 3.04 | A/B | 81-526 | [»] | |
| 4ORZ | X-ray | 2.00 | A | 77-138 | [»] | |
| 4U5W | X-ray | 1.86 | B/D | 72-242 | [»] | |
| 5H09 | X-ray | 1.95 | A | 81-526 | [»] | |
| 5H0B | X-ray | 1.65 | A | 81-526 | [»] | |
| 5H0E | X-ray | 2.10 | A | 81-526 | [»] | |
| 5H0G | X-ray | 1.80 | A | 81-526 | [»] | |
| 5H0H | X-ray | 1.72 | A | 81-526 | [»] | |
| 5HCK | NMR | - | A | 72-143 | [»] | |
| 5NUH | X-ray | 2.78 | C/D | 79-138 | [»] | |
| 5ZJ6 | X-ray | 1.70 | A/B | 242-521 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P08631 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P08631 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 109305, 64 interactors |
Database of interacting proteins More...DIPi | DIP-1051N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P08631 |
Protein interaction database and analysis system More...IntActi | P08631, 108 interactors |
Molecular INTeraction database More...MINTi | P08631 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000365012 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P08631 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3234 |
Drug and drug target database More...DrugBanki | DB06616 Bosutinib DB01962 Phosphonotyrosine DB04216 Quercetin |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2032 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P08631 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P08631 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P08631 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | HCK |
Domain mapping of disease mutations (DMDM) More...DMDMi | 20141296 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P08631 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P08631 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P08631 |
PeptideAtlas More...PeptideAtlasi | P08631 |
PRoteomics IDEntifications database More...PRIDEi | P08631 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 52142 52143 [P08631-2] 52144 [P08631-3] 52145 [P08631-4] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 3055 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000518730; ENSP00000427757; ENSG00000101336 [P08631-3] ENST00000520553; ENSP00000429848; ENSG00000101336 [P08631-2] ENST00000534862; ENSP00000444986; ENSG00000101336 [P08631-1] ENST00000538448; ENSP00000441169; ENSG00000101336 [P08631-2] ENST00000629881; ENSP00000486627; ENSG00000101336 [P08631-2] ENST00000639405; ENSP00000491964; ENSG00000101336 [P08631-4] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 3055 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:3055 |
UCSC genome browser More...UCSCi | uc002wxi.4 human [P08631-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 3055 |
DisGeNET More...DisGeNETi | 3055 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000101336.12 |
GeneCards: human genes, protein and diseases More...GeneCardsi | HCK |
Human Gene Nomenclature Database More...HGNCi | HGNC:4840 HCK |
Human Protein Atlas More...HPAi | CAB005195 HPA063768 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 142370 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P08631 |
Open Targets More...OpenTargetsi | ENSG00000101336 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA29216 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0197 Eukaryota COG0515 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118938 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000233858 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG008761 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P08631 |
KEGG Orthology (KO) More...KOi | K08893 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P08631 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.10.2 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-164944 Nef and signal transduction R-HSA-2029481 FCGR activation R-HSA-912631 Regulation of signaling by CBL |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P08631 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P08631 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | HCK human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P08631 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | HCK |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 3055 |
Protein Ontology More...PROi | PR:P08631 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000101336 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P08631 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P08631 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd10363 SH2_Src_HCK, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.505.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR035851 HCK_SH2 IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR001245 Ser-Thr/Tyr_kinase_cat_dom IPR000980 SH2 IPR036860 SH2_dom_sf IPR036028 SH3-like_dom_sf IPR001452 SH3_domain IPR008266 Tyr_kinase_AS IPR020635 Tyr_kinase_cat_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF07714 Pkinase_Tyr, 1 hit PF00017 SH2, 1 hit PF00018 SH3_1, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00401 SH2DOMAIN PR00452 SH3DOMAIN PR00109 TYRKINASE |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00252 SH2, 1 hit SM00326 SH3, 1 hit SM00219 TyrKc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50044 SSF50044, 1 hit SSF55550 SSF55550, 1 hit SSF56112 SSF56112, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00109 PROTEIN_KINASE_TYR, 1 hit PS50001 SH2, 1 hit PS50002 SH3, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<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 subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | HCK_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P08631Primary (citable) accession number: P08631 Secondary accession number(s): A8K1I1 , B4DQB6, E1P5M2, Q29RX1, Q2VPE2, Q504R5, Q5T7K1, Q5T7K2, Q96CC0, Q9H5Y5, Q9NUA4, Q9UMJ5 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1988 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | July 18, 2018 | |
| This is version 237 of the entry and version 5 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<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
<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>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 20
Human chromosome 20: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Human and mouse protein kinases
Human and mouse protein kinases: classification and index - SIMILARITY comments
Index of protein domains and families
