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UniProtKB/Swiss-Prot entry P08631


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HCK_HUMAN
Primary accession number P08631
Secondary accession numbers Q29RX1 Q2VPE2 Q504R5 Q5T7K1 Q5T7K2 Q96CC0 Q9H5Y5 Q9NUA4 Q9UMJ5
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 5)
Annotations were last modified on    June 16, 2009 (Entry version 134)
Name and origin of the protein
Protein name Tyrosine-protein kinase HCK
Synonyms EC 2.7.10.2
Hemopoietic cell kinase
p59-HCK/p60-HCK
Gene name
Name: HCK
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P60-HCK).
PubMed=3496523 [NCBI, ExPASy, EBI, Israel, Japan]
Quintrell N., Lebo R., Varmus H., Bishop J.M., Pettenati M.J., le Beau M.M., Diaz M.O., Rowley J.D.;
"Identification of a human gene (HCK) that encodes a protein-tyrosine kinase and is expressed in hemopoietic cells.";
Mol. Cell. Biol. 7:2267-2275(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P59-HCK).
PubMed=3453117 [NCBI, ExPASy, EBI, Israel, Japan]
Ziegler S.F., Marth J.D., Lewis D.B., Perlmutter R.M.;
"Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells of hematopoietic origin.";
Mol. Cell. Biol. 7:2276-2285(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P60-HCK).
TISSUE=Ileal mucosa;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P60-HCK).
TISSUE=B-cell, and Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-21 (ISOFORM P60-HCK), AND ALTERNATIVE INITIATION.
TISSUE=Bone marrow;
PubMed=1875927 [NCBI, ExPASy, EBI, Israel, Japan]
Lock P., Ralph S., Stanley E., Boulet I., Ramsay R., Dunn A.R.;
"Two isoforms of murine hck, generated by utilization of alternative translational initiation codons, exhibit different patterns of subcellular localization.";
Mol. Cell. Biol. 11:4363-4370(1991).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 178-526.
TISSUE=Spleen;
DOI=10.1016/0378-1119(92)90407-G; PubMed=1572549 [NCBI, ExPASy, EBI, Israel, Japan]
Hradetzky D., Strebhardt K., Ruesamen-Waigmann H.;
"The genomic locus of the human hemopoietic-specific cell protein tyrosine kinase (PTK)-encoding gene (HCK) confirms conservation of exon-intron structure among human PTKs of the src family.";
Gene 113:275-280(1992).
[8]
INTERACTION WITH HIV-1 NEF.
DOI=10.1074/jbc.272.29.17899; PubMed=9218412 [NCBI, ExPASy, EBI, Israel, Japan]
Briggs S.D., Sharkey M., Stevenson M., Smithgall T.E.;
"SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1.";
J. Biol. Chem. 272:17899-17902(1997).
[9]
INTERACTION WITH HIV-1 VIF.
DOI=10.1074/jbc.M009076200; PubMed=11278465 [NCBI, ExPASy, EBI, Israel, Japan]
Hassaine G., Courcoul M., Bessou G., Barthalay Y., Picard C., Olive D., Collette Y., Vigne R., Decroly E.;
"The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif protein.";
J. Biol. Chem. 276:16885-16893(2001).
[10]
INTERACTION WITH HEV ORF3 PROTEIN.
DOI=10.1074/jbc.M101546200; PubMed=11518702 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK.";
J. Biol. Chem. 276:42389-42400(2001).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-411, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-209, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-411, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[14]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 78-526.
DOI=10.1038/385602a0; PubMed=9024658 [NCBI, ExPASy, EBI, Israel, Japan]
Sicheri F., Moarefi I., Kuriyan J.;
"Crystal structure of the Src family tyrosine kinase Hck.";
Nature 385:602-609(1997).
[15]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 81-137.
DOI=10.1021/bi980989q; PubMed=9778343 [NCBI, ExPASy, EBI, Israel, Japan]
Arold S., O'Brien R., Franken P., Strub M.-P., Hoh F., Dumas C., Ladbury J.E.;
"RT loop flexibility enhances the specificity of Src family SH3 domains for HIV-1 Nef.";
Biochemistry 37:14683-14691(1998).
[16]
STRUCTURE BY NMR OF 78-138.
DOI=10.1006/jmbi.1998.1690; PubMed=9571048 [NCBI, ExPASy, EBI, Israel, Japan]
Horita D.A., Baldisseri D.M., Zhang W., Altieri A.S., Smithgall T.E., Gmeiner W.H., Byrd R.A.;
"Solution structure of the human Hck SH3 domain and identification of its ligand binding site.";
J. Mol. Biol. 278:253-265(1998).
[17]
STRUCTURE BY NMR OF 139-245.
DOI=10.1016/S0014-5793(97)00255-X; PubMed=9109402 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang W., Smithgall T.E., Gmeiner W.H.;
"Sequential assignment and secondary structure determination for the Src homology 2 domain of hematopoietic cellular kinase.";
FEBS Lett. 406:131-135(1997).
[18]
VARIANTS [LARGE SCALE ANALYSIS] THR-44; LEU-105 AND GLY-399.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M16591; AAA52643.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M16592; AAA52644.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK026432; BAB15482.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL353092; CAI19694.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049539; CAI19694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL353092; CAI19695.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049539; CAI19695.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049539; CAI22966.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL353092; CAI22966.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049539; CAI22967.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL353092; CAI22967.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014435; AAH14435.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC094847; AAH94847.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC108930; AAI08931.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC108931; AAI08932.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC113854; AAI13855.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC114463; AAI14464.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X58741; CAA41565.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X58742; CAA41565.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X58743; CAA41565.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00029769; -.
IPI00646510; -.
PIR A27811; TVHUHC.
A41263; A41263.
RefSeq NP_002101.2; -.
UniGene Hs.655210
3D structure databases
PDB
1AD5; X-ray; 2.60 A; A/B=79-526.[ExPASy / RCSB / EBI]
1BU1; X-ray; 2.60 A; A/B/C/D/E/F=81-137.[ExPASy / RCSB / EBI]
1QCF; X-ray; 2.00 A; A=81-522.[ExPASy / RCSB / EBI]
2C0I; X-ray; 2.30 A; A/B=81-522.[ExPASy / RCSB / EBI]
2C0O; X-ray; 2.85 A; A/B=81-522.[ExPASy / RCSB / EBI]
2C0T; X-ray; 2.15 A; A/B=81-522.[ExPASy / RCSB / EBI]
2HCK; X-ray; 3.00 A; A/B=79-526.[ExPASy / RCSB / EBI]
2HK5; X-ray; 2.00 A; A=247-513.[ExPASy / RCSB / EBI]
2OI3; NMR; -; A=61-140.[ExPASy / RCSB / EBI]
2OJ2; NMR; -; A=61-140.[ExPASy / RCSB / EBI]
3HCK; NMR; -; A=140-245.[ExPASy / RCSB / EBI]
4HCK; NMR; -; A=72-143.[ExPASy / RCSB / EBI]
5HCK; NMR; -; A=72-143.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AD5; -.
1BU1; -.
1QCF; -.
2C0I; -.
2C0O; -.
2C0T; -.
2HCK; -.
2HK5; -.
2OI3; -.
2OJ2; -.
3HCK; -.
4HCK; -.
5HCK; -.
ModBase P08631.
Protein-protein interaction databases
DIP DIP:1051N; -.
IntAct P08631; 32.
PTM databases
PhosphoSite P08631; -.
Enzyme and pathway databases
BRENDA 2.7.10.2; 247.
Pathway_Interaction_DB alphasynuclein_pathway; Alpha-synuclein signaling.
amb2_neutrophils_pathway; amb2 Integrin signaling.
pi3kcipathway; Class I PI3K signaling events.
epha_fwdpathway; EPHA forward signaling.
ephrinbrevpathway; Ephrin B reverse signaling.
glypican_1pathway; Glypican 1 network.
il6_7pathway; IL6-mediated signaling events.
pdgfrbpathway; PDGFR-beta signaling pathway.
p38alphabetapathway; Regulation of p38-alpha and p38-beta.
ptp1bpathway; Signaling events mediated by PTP1B.
txa2pathway; Thromboxane A2 receptor signaling.
Reactome REACT_6185; HIV Infection.
Organism-specific databases
GeneCards GC20P030103; -.
H-InvDB HIX0015721; -.
HGNC HGNC:4840; HCK.
GenAtlas HCK.
HPA CAB005195; -.
MIM 142370; gene. [NCBI / EBI]
PharmGKB PA29216; -.
Gene expression databases
ArrayExpress P08631; -.
Bgee P08631; -.
GermOnline ENSG00000101336; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004715; Molecular function: non-membrane spanning protein tyrosine kinase activity (inferred from electronic annotation from EC).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0007498; Biological process: mesoderm development (traceable author statement from ProtInc).
GO:0006468; Biological process: protein amino acid phosphorylation (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR000980; SH2.
IPR001452; SH3_domain.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
Graphical view of domain structure.
Gene3D G3DSA:3.30.505.10; SH2; 1.
Pfam PF07714; Pkinase_Tyr; 1.
PF00017; SH2; 1.
PF00018; SH3_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00401; SH2DOMAIN.
PR00109; TYRKINASE.
ProDom PD000001; Prot_kinase; 1.
PD000093; SH2; 1.
PD000066; SH3; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00252; SH2; 1.
SM00326; SH3; 1.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS50001; SH2; 1.
PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P08631; -.
Genome annotation databases
Ensembl ENSG00000101336; Homo sapiens. [Contig view]
GeneID 3055; -.
KEGG hsa:3055; -.
Phylogenomic databases
HOVERGEN P08631; -.
Other
NextBio 12093; -.
SOURCE HCK; Homo sapiens.
ProtoNet P08631.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative initiation; ATP-binding; Cytoplasm; Host-virus interaction; Kinase; Lipoprotein; Membrane; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein; Polymorphism; SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   526  525     Tyrosine-protein kinase HCK. PRO_0000024433
DOMAIN   78   138  61     SH3. 
DOMAIN   144   241  98     SH2. 
DOMAIN   262   515  254     Protein kinase. 
NP_BIND   268   276  9     ATP. 
ACT_SITE   381   381        Proton acceptor. 
BINDING   290   290        ATP. 
MOD_RES   209   209        Phosphotyrosine. 
MOD_RES   411   411        Phosphotyrosine; by autocatalysis (By similarity). 
LIPID   2     2        N-myristoyl glycine (By similarity). 
VAR_SEQ   1    21        Missing (in isoform p59-HCK). VSP_018858
VARIANT   44    44  1     A -> T. VAR_041707 
VARIANT   105   105  1     M -> L. VAR_041708 
VARIANT   399   399  1     D -> G (in an ovarian mucinous carcinoma sample; somatic mutation). VAR_041709 [3D]
VARIANT   502   502  1     P -> Q (in dbSNP:rs17093828 [NCBI]). VAR_033836 [3D]
CONFLICT   24    24        C -> S (in Ref. 1; AAA52643). 
CONFLICT   76    76        Missing (in Ref. 4; CAI19695/CAI22967 and 5; AAI13855). 
CONFLICT   144   144        W -> R (in Ref. 3; BAB15482). 
CONFLICT   378   378        I -> T (in Ref. 5; AAI13855). 
STRAND   82    87  6      
STRAND   104   109  6      
STRAND   114   119  6      
TURN   120   122  3      
STRAND   125   129  5      
HELIX   130   132  3      
STRAND   133   135  3      
HELIX   139   141  3      
HELIX   151   159  9      
STRAND   168   172  5      
STRAND   174   176  3      
STRAND   179   188  10      
TURN   189   191  3      
STRAND   192   202  11      
STRAND   208   214  7      
STRAND   216   218  3      
HELIX   219   226  8      
STRAND   233   235  3      
HELIX   259   261  3      
STRAND   262   269  8      
STRAND   272   281  10      
TURN   282   284  3      
STRAND   285   292  8      
HELIX   299   309  11      
STRAND   320   324  5      
STRAND   326   328  3      
STRAND   330   333  4      
HELIX   341   346  6      
HELIX   348   351  4      
HELIX   355   374  20      
HELIX   384   386  3      
STRAND   387   389  3      
STRAND   395   397  3      
HELIX   402   405  4      
HELIX   409   412  4      
STRAND   416   419  4      
HELIX   421   423  3      
HELIX   426   431  6      
HELIX   436   451  16      
HELIX   463   472  10      
HELIX   484   493  10      
HELIX   498   500  3      
HELIX   504   512  9      
STRAND   514   518  5      
Sequence information
Length: 526 AA [This is the length of the unprocessed precursor] Molecular weight: 59600 Da [This is the MW of the unprocessed precursor] CRC64: 847E877A0A641725 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGGRSSCEDP GCPRDEERAP RMGCMKSKFL QVGGNTFSKT ETSASPHCPV YVPDPTSTIK 

        70         80         90        100        110        120 
PGPNSHNSNT PGIREAGSED IIVVALYDYE AIHHEDLSFQ KGDQMVVLEE SGEWWKARSL 

       130        140        150        160        170        180 
ATRKEGYIPS NYVARVDSLE TEEWFFKGIS RKDAERQLLA PGNMLGSFMI RDSETTKGSY 

       190        200        210        220        230        240 
SLSVRDYDPR QGDTVKHYKI RTLDNGGFYI SPRSTFSTLQ ELVDHYKKGN DGLCQKLSVP 

       250        260        270        280        290        300 
CMSSKPQKPW EKDAWEIPRE SLKLEKKLGA GQFGEVWMAT YNKHTKVAVK TMKPGSMSVE 

       310        320        330        340        350        360 
AFLAEANVMK TLQHDKLVKL HAVVTKEPIY IITEFMAKGS LLDFLKSDEG SKQPLPKLID 

       370        380        390        400        410        420 
FSAQIAEGMA FIEQRNYIHR DLRAANILVS ASLVCKIADF GLARVIEDNE YTAREGAKFP 

       430        440        450        460        470        480 
IKWTAPEAIN FGSFTIKSDV WSFGILLMEI VTYGRIPYPG MSNPEVIRAL ERGYRMPRPE 

       490        500        510        520 
NCPEELYNIM MRCWKNRPEE RPTFEYIQSV LDDFYTATES QYQQQP 

P08631 in FASTA format

View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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