HCK

Functionⁱ

Non-receptor tyrosine-protein kinase found in hematopoietic cells that transmits signals from cell surface receptors and plays an important role in the regulation of innate immune responses, including neutrophil, monocyte, macrophage and mast cell functions, phagocytosis, cell survival and proliferation, cell adhesion and migration. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as FCGR1A and FCGR2A, but also CSF3R, PLAUR, the receptors for IFNG, IL2, IL6 and IL8, and integrins, such as ITGB1 and ITGB2. During the phagocytic process, mediates mobilization of secretory lysosomes, degranulation, and activation of NADPH oxidase to bring about the respiratory burst. Plays a role in the release of inflammatory molecules. Promotes reorganization of the actin cytoskeleton and actin polymerization, formation of podosomes and cell protrusions. Inhibits TP73-mediated transcription activation and TP73-mediated apoptosis. Phosphorylates CBL in response to activation of immunoglobulin gamma Fc region receptors. Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, GAB2, RAPGEF1, STAT5B, TP73, VAV1 and WAS.19 Publications

Catalytic activityⁱ

ATP
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See the description of this molecule in ChEBI.
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L-tyrosyl-[protein]
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Search chemical reactions in Rhea for this molecule.
=
ADP
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H⁺
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
O-phospho-L-tyrosyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10028
8 Publications
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, ACTIVITY 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, ACTIVITY 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, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
EC:
2.7.10.2
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10028
8 Publications
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, ACTIVITY 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, ACTIVITY 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, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
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ATP
+
L-tyrosyl-[protein]
L-tyrosine residue
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=
ADP
+
H⁺
+
O-phospho-L-tyrosyl-[protein]
L-tyrosine-phosphate residue
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Activity regulationⁱ

Subject to autoinhibition, mediated by intramolecular interactions involving the SH2 and SH3 domains. Kinase activity is also regulated by phosphorylation at regulatory tyrosine residues. Phosphorylation at Tyr-411 is required for optimal activity. Phosphorylation at Tyr-522 inhibits kinase activity. Inhibited by PP1 and A-770041.9 Publications

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	290	ATP		1
Active siteⁱ	381	Proton acceptor		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	268 – 276	ATP		9

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

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

BRENDAⁱ	2.7.10.2 2681
Reactomeⁱ	R-HSA-164944 Nef and signal transduction R-HSA-2029481 FCGR activation R-HSA-912631 Regulation of signaling by CBL R-HSA-9607240 FLT3 Signaling
SignaLinkⁱ	P08631
SIGNORⁱ	P08631

Names & Taxonomyⁱ

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
Gene namesⁱ	Name:HCK
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
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
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 20

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:4840 HCK
MIMⁱ	142370 gene
neXtProtⁱ	NX_P08631

Keywords - Cellular componentⁱ

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Golgi apparatus, Lysosome, Membrane, Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Aberrant activation of HCK by HIV-1 protein Nef enhances HIV-1 replication and contributes to HIV-1 pathogenicity.

Aberrant activation of HCK, e.g. by the BCR-ABL fusion protein, promotes cancer cell proliferation.

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	3	G → C: Slight palmitoylation, cytoplasmic and caveolar localization; in isoform 1;. 2 Publications	1
Mutagenesisⁱ	3	G → S: Abolishes palmitoylation and localization at the cell membrane. 2 Publications	1
Mutagenesisⁱ	23	G → A: Myristoylation and palmitoylation are abolished, leading to entirely cytoplasmic localization; in isoform 2. 1 Publication	1
Mutagenesisⁱ	24	C → S: Palmitoylation is abolished, some cytoplasmic and no calveolar localization; in isoform 2. 1 Publication	1
Mutagenesisⁱ	290	K → E: Loss of kinase activity. 1 Publication	1
Mutagenesisⁱ	305	E → A: Loss of kinase activity. 1 Publication	1
Mutagenesisⁱ	381	D → E: Loss of kinase activity. 1 Publication	1
Mutagenesisⁱ	411	Y → A: Reduced catalytic activity and higher affinity for target peptides. 1 Publication	1
Mutagenesisⁱ	522	Y → F: Constitutively activated kinase, leading to cellular transformation. 2 Publications	1

Keywords - Diseaseⁱ

Proto-oncogene

Organism-specific databases

DisGeNET More...DisGeNETⁱ	3055
Open Targets More...OpenTargetsⁱ	ENSG00000101336
PharmGKBⁱ	PA29216

Miscellaneous databases

Pharosⁱ	P08631

Pharosⁱ

P08631

Chemistry databases

ChEMBLⁱ	CHEMBL3234
Drug and drug target database More...DrugBankⁱ	DB01809 1-Ter-Butyl-3-P-Tolyl-1h-Pyrazolo[3,4-D]Pyrimidin-4-Ylamine DB06616 Bosutinib DB12010 Fostamatinib DB01962 Phosphonotyrosine DB04216 Quercetin
DrugCentral More...DrugCentralⁱ	P08631
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2032

Polymorphism and mutation databases

BioMutaⁱ	HCK
DMDMⁱ	20141296

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Initiator methionineⁱ		Removed
ChainⁱPRO_0000024433	2 – 526	Tyrosine-protein kinase HCKAdd BLAST	525
Isoform 2 (identifier: P08631-2)
Initiator methionineⁱ		Removed

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Lipidationⁱ	2	N-myristoyl glycine1 Publication	1
Modified residueⁱ	36	PhosphothreonineCombined sources	1
Modified residueⁱ	51	Phosphotyrosine; by autocatalysis1 Publication	1
Modified residueⁱ	202	PhosphothreonineCombined sources	1
Modified residueⁱ	209	PhosphotyrosineBy similarity	1
Modified residueⁱ	411	Phosphotyrosine; by autocatalysis2 Publications	1
Modified residueⁱ	462	PhosphoserineCombined sources	1
Modified residueⁱ	522	Phosphotyrosine5 Publications	1
Isoform 2 (identifier: P08631-2)
Lipidationⁱ	2	N-myristoyl glycine	1
Lipidationⁱ	3	S-palmitoyl cysteine	1

Post-translational modificationⁱ

Phosphorylated on several tyrosine residues. Autophosphorylated. Becomes rapidly phosphorylated upon activation of the immunoglobulin receptors FCGR1A and FCGR2A. Phosphorylation by the BCR-ABL fusion protein mediates activation of HCK. Phosphorylation at Tyr-411 increases kinase activity. Phosphorylation at Tyr-522 inhibits kinase activity. Kinase activity is not required for phosphorylation at Tyr-522, suggesting that this site is a target of other kinases.9 Publications

Ubiquitinated by CBL, leading to its degradation via the proteasome.1 Publication

Isoform 2 palmitoylation at position 2 requires prior myristoylation. Palmitoylation at position 3 is required for caveolar localization of isoform 2.1 Publication

Keywords - PTMⁱ

Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOSTⁱ	P08631
MassIVEⁱ	P08631
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P08631
PaxDbⁱ	P08631
PeptideAtlas More...PeptideAtlasⁱ	P08631
PRIDEⁱ	P08631
ProteomicsDBⁱ	52142 [P08631-1] 52143 [P08631-2] 52144 [P08631-3] 52145 [P08631-4]

PTM databases

iPTMnetⁱ	P08631
PhosphoSitePlusⁱ	P08631
SwissPalmⁱ	P08631

Expressionⁱ

Tissue specificityⁱ

Detected in monocytes and neutrophils (at protein level). Expressed predominantly in cells of the myeloid and B-lymphoid lineages. Highly expressed in granulocytes. Detected in tonsil.3 Publications

Inductionⁱ

Up-regulated during myeloid cell differentiation. The highest levels are detected in fully differentiated phagocytes. Up-regulated by IL2.2 Publications

Gene expression databases

Bgeeⁱ	ENSG00000101336 Expressed in 200 organ(s), highest expression level in blood
ExpressionAtlasⁱ	P08631 baseline and differential
Genevisibleⁱ	P08631 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB005195 HPA063768

HPAⁱ

CAB005195
HPA063768

Interactionⁱ

Subunit structureⁱ

Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated).

Interacts with VAV1, WAS and RAPGEF1 (By similarity). This interaction stimulates its tyrosine-kinase activity.

Interacts with ARRB1 and ARRB2.

Interacts with ADAM15.

Interacts with FASLG.

Interacts with CBL.

Interacts with FCGR1A; the interaction may be indirect.

Interacts with IL6ST.

Interacts (via SH3 domain) with ELMO1.

Interacts (via SH3 domain) with TP73.

Interacts with YAP1.

Interacts with ABL1 and ITGB1, and thereby recruits ABL1 to activated ITGB1.

Interacts (via SH3 domain) with WDCP.

By similarity19 Publications

(Microbial infection) Interacts (via SH3 domain) with HEV ORF3 protein.

1 Publication

(Microbial infection) Interacts (via SH3 domain) with HIV-1 Nef and Vif.

5 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
	O92972	2	EBI-346340,EBI-710506	From Hepatitis C virus genotype 1b (strain HC-J4).
	P27958	5	EBI-346340,EBI-706378	From Hepatitis C virus genotype 1a (isolate H).
ADAM15	Q13444	3	EBI-346340,EBI-77818
ALOX5	P09917	2	EBI-346340,EBI-79934
ASAP1	Q9ULH1	2	EBI-346340,EBI-346622
CBL	P22681	2	EBI-9834454,EBI-518228
EGFR	P00533	2	EBI-346340,EBI-297353
ELMO1	Q92556	4	EBI-346340,EBI-346417
ERBB3	P21860	2	EBI-346340,EBI-720706
FLT1	P17948	2	EBI-346340,EBI-1026718
FRS3	O43559	2	EBI-9834454,EBI-725515
GOPC	Q9HD26	3	EBI-346340,EBI-349832
KHDRBS1	Q07666	4	EBI-346340,EBI-1364
KIT	P10721	2	EBI-346340,EBI-1379503
KRT40	Q6A162	3	EBI-346340,EBI-10171697
KRTAP10-9	P60411	3	EBI-346340,EBI-10172052
MTUS2	Q5JR59	3	EBI-346340,EBI-742948
nef	P03406	2	EBI-346340,EBI-15672419	From Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI).
nef	Q90VU7	2	EBI-346340,EBI-7460704	From Human immunodeficiency virus 1.
NOTCH2NLA	Q7Z3S9	3	EBI-346340,EBI-945833
OLIG1	Q8TAK6	2	EBI-9834454,EBI-3867416
PAK2	Q13177	2	EBI-346340,EBI-1045887
PDCD6IP	Q8WUM4	4	EBI-346340,EBI-310624
PIK3CB	P42338	2	EBI-346340,EBI-2609540
PIK3R3	Q92569	4	EBI-9834454,EBI-79893
PLCG1	P19174	2	EBI-346340,EBI-79387
PTK2	Q05397	2	EBI-9834454,EBI-702142
SOS1	Q07889	4	EBI-346340,EBI-297487
vif	P12504	3	EBI-346340,EBI-779991	From Human immunodeficiency virus type 1 group M subtype B (isolate NY5).
WAS	P42768	9	EBI-346340,EBI-346375
WIPF1	O43516	3	EBI-346340,EBI-346356

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	109305, 70 interactors
Database of interacting proteins More...DIPⁱ	DIP-1051N
ELMⁱ	P08631
IntActⁱ	P08631, 103 interactors
Molecular INTeraction database More...MINTⁱ	P08631
STRINGⁱ	9606.ENSP00000444986

Chemistry databases

BindingDBⁱ

P08631

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	82 – 85	Combined sources	4
Beta strandⁱ	93 – 96	Combined sources	4
Beta strandⁱ	99 – 102	Combined sources	4
Beta strandⁱ	104 – 111	Combined sources	8
Beta strandⁱ	114 – 122	Combined sources	9
Beta strandⁱ	127 – 129	Combined sources	3
Helixⁱ	130 – 132	Combined sources	3
Beta strandⁱ	133 – 135	Combined sources	3
Helixⁱ	136 – 138	Combined sources	3
Helixⁱ	139 – 141	Combined sources	3
Beta strandⁱ	145 – 148	Combined sources	4
Helixⁱ	151 – 159	Combined sources	9
Beta strandⁱ	168 – 172	Combined sources	5
Beta strandⁱ	174 – 176	Combined sources	3
Beta strandⁱ	180 – 188	Combined sources	9
Turnⁱ	189 – 191	Combined sources	3
Beta strandⁱ	192 – 202	Combined sources	11
Beta strandⁱ	204 – 206	Combined sources	3
Beta strandⁱ	208 – 211	Combined sources	4
Beta strandⁱ	215 – 218	Combined sources	4
Helixⁱ	219 – 228	Combined sources	10
Beta strandⁱ	233 – 235	Combined sources	3
Turnⁱ	252 – 255	Combined sources	4
Helixⁱ	259 – 261	Combined sources	3
Beta strandⁱ	262 – 270	Combined sources	9
Beta strandⁱ	272 – 281	Combined sources	10
Turnⁱ	282 – 284	Combined sources	3
Beta strandⁱ	285 – 292	Combined sources	8
Beta strandⁱ	294 – 297	Combined sources	4
Helixⁱ	299 – 309	Combined sources	11
Beta strandⁱ	320 – 324	Combined sources	5
Beta strandⁱ	326 – 328	Combined sources	3
Beta strandⁱ	330 – 333	Combined sources	4
Helixⁱ	341 – 345	Combined sources	5
Helixⁱ	350 – 352	Combined sources	3
Helixⁱ	355 – 374	Combined sources	20
Helixⁱ	384 – 386	Combined sources	3
Beta strandⁱ	387 – 389	Combined sources	3
Beta strandⁱ	395 – 397	Combined sources	3
Helixⁱ	402 – 405	Combined sources	4
Helixⁱ	410 – 413	Combined sources	4
Beta strandⁱ	416 – 419	Combined sources	4
Helixⁱ	421 – 423	Combined sources	3
Helixⁱ	426 – 431	Combined sources	6
Helixⁱ	436 – 451	Combined sources	16
Turnⁱ	452 – 454	Combined sources	3
Beta strandⁱ	457 – 460	Combined sources	4
Helixⁱ	463 – 471	Combined sources	9
Beta strandⁱ	480 – 482	Combined sources	3
Helixⁱ	484 – 493	Combined sources	10
Helixⁱ	498 – 500	Combined sources	3
Helixⁱ	504 – 512	Combined sources	9
Turnⁱ	513 – 518	Combined sources	6
Beta strandⁱ	521 – 523	Combined sources	3

Show more details

3D structure databases

SMRⁱ	P08631
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P08631

EvolutionaryTraceⁱ

P08631

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	78 – 138	SH3PROSITE-ProRule annotationAdd BLAST	61
Domainⁱ	144 – 241	SH2PROSITE-ProRule annotationAdd BLAST	98
Domainⁱ	262 – 515	Protein kinasePROSITE-ProRule annotationAdd BLAST	254

Domainⁱ

The SH3 domain mediates binding to HIV-1 Nef.

Sequence similaritiesⁱ

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation

Keywords - Domainⁱ

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGⁱ	KOG0197 Eukaryota COG0515 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000158738
HOGENOMⁱ	HOG000233858
InParanoidⁱ	P08631
KEGG Orthology (KO) More...KOⁱ	K08893
Database of Orthologous Groups More...OrthoDBⁱ	539311at2759
PhylomeDBⁱ	P08631

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd10363 SH2_Src_HCK, 1 hit
Gene3Dⁱ	3.30.505.10, 1 hit
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
PRINTSⁱ	PR00401 SH2DOMAIN PR00452 SH3DOMAIN PR00109 TYRKINASE
SMARTⁱ	View protein in SMART SM00252 SH2, 1 hit SM00326 SH3, 1 hit SM00219 TyrKc, 1 hit
SUPFAMⁱ	SSF50044 SSF50044, 1 hit SSF55550 SSF55550, 1 hit SSF56112 SSF56112, 1 hit
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

Sequences (4+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsⁱ produced by alternative splicing and alternative initiation. Align Add to basket

This entry has 4 described isoforms and 4 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P08631-1) [UniParc]FASTA Add to basket

Also known as: p60-HCK, p61Hck

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        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

Note: Initiates from a CTG codon.

Length:526

Mass (Da):59,600

Last modified:January 23, 2007 - v5

Checksum:ⁱ847E877A0A641725

GO

Isoform 2 (identifier: P08631-2) [UniParc]FASTA Add to basket

Also known as: p59-HCK, p59Hck

The sequence of this isoform differs from the canonical sequence as follows:
1-21: Missing.

« Hide

        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

Show »

Length:505

Mass (Da):57,312

Checksum:ⁱ4F1EC1E8F3EDF9CA

GO

Isoform 3 (identifier: P08631-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-21: Missing.
76-76: Missing.

« Hide

        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

Show »

Length:504

Mass (Da):57,241

Checksum:ⁱC07FF5B8D3C1B862

GO

Isoform 4 (identifier: P08631-4) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
76-76: Missing.

« Hide

        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

Note: Initiates from a CTG codon.

Show »

Length:525

Mass (Da):59,529

Checksum:ⁱ803967415A2F57FC

GO

Computationally mapped potential isoform sequencesⁱ

There are 4 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H0Y3C5	H0Y3C5_HUMAN	Tyrosine-protein kinase Tyrosine-protein kinase, EC 2.7.10.2	HCK	525	Annotation score:
J3KPD6	J3KPD6_HUMAN	Tyrosine-protein kinase Tyrosine-protein kinase, EC 2.7.10.2	HCK	526	Annotation score:
H7C5P9	H7C5P9_HUMAN	Tyrosine-protein kinase HCK Tyrosine-protein kinase HCK	HCK	61	Annotation score:
H7BXG4	H7BXG4_HUMAN	Tyrosine-protein kinase HCK Tyrosine-protein kinase HCK	HCK	41	Annotation score:

Sequence cautionⁱ

The sequence AAA52643 differs from that shown. Reason: Frameshift.Curated

The sequence BAF82585 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	24	C → S in AAA52643 (PubMed:3496523).Curated	1
Sequence conflictⁱ	69	N → D in BAF82585 (PubMed:14702039).Curated	1
Sequence conflictⁱ	144	W → R in BAB15482 (PubMed:14702039).Curated	1
Sequence conflictⁱ	168	F → Y in BAF82585 (PubMed:14702039).Curated	1
Sequence conflictⁱ	378	I → T in AAI13855 (PubMed:15489334).Curated	1
Sequence conflictⁱ	488	N → S in BAF82585 (PubMed:14702039).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_041707	44	A → T1 PublicationCorresponds to variant dbSNP:rs56029200Ensembl.	1
Natural variantⁱVAR_041708	105	M → L2 PublicationsCorresponds to variant dbSNP:rs55722810Ensembl.	1
Natural variantⁱVAR_041709	399	D → G in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication	1
Natural variantⁱVAR_033836	502	P → Q. Corresponds to variant dbSNP:rs17093828Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_018858	1 – 21	Missing in isoform 2 and isoform 3. 3 PublicationsAdd BLAST		21
Alternative sequenceⁱVSP_041926	76	Missing in isoform 3 and isoform 4. 2 Publications		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links 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]
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]

Genome annotation databases

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]
GeneIDⁱ	3055
KEGGⁱ	hsa:3055
UCSC genome browser More...UCSCⁱ	uc002wxi.4 human [P08631-1]

Keywords - Coding sequence diversityⁱ

Alternative initiation, Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P08631	Isoform 2 of Tyrosine-protein kinase HCK		HUMAN		505	UniRef100_P08631
UPI0000111AFB		HUMAN		72
P08631-3	Tyrosine-protein kinase		HUMAN		525	UniRef100_H0Y3C5

Protein	Similar proteins		Species	Score	Length	Source
P08631	Isoform 2 of Tyrosine-protein kinase HCK		HUMAN		505	UniRef90_P08631
Tyrosine-protein kinase		PANPA		526
Tyrosine-protein kinase		GORGO		526
Tyrosine-protein kinase		PONAB		505
Tyrosine-protein kinase		PANTR		505
+12
P08631-3	Isoform 4 of Tyrosine-protein kinase HCK		HUMAN		525	UniRef90_P08631-4
Tyrosine-protein kinase		RHIRO		591
Tyrosine-protein kinase		MACMU		532
Tyrosine-protein kinase		MACFA		532
Tyrosine-protein kinase		MACNE		504
+27

Protein	Similar proteins		Species	Score	Length	Source
P08631	Tyrosine-protein kinase HCK		MOUSE		524	UniRef50_P08631
Tyrosine-protein kinase HCK		RAT		524
Isoform 2 of Tyrosine-protein kinase HCK		HUMAN		505
Tyrosine-protein kinase		GORGO		526
Tyrosine-protein kinase		PANPA		526
+701
P08631-3	Isoform 4 of Tyrosine-protein kinase HCK		HUMAN		525	UniRef50_P08631-4
Tyrosine-protein kinase		RHIRO		591
Tyrosine-protein kinase		MACMU		532
Tyrosine-protein kinase		MACFA		532
Tyrosine-protein kinase		MACNE		504
+70

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links 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
CCDSⁱ	CCDS33460.1 [P08631-1] CCDS54453.1 [P08631-4] CCDS54455.1 [P08631-2] CCDS54456.1 [P08631-3]
PIRⁱ	A27811 TVHUHC A41263
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]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links 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	[»]
SMRⁱ	P08631
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	109305, 70 interactors
DIPⁱ	DIP-1051N
ELMⁱ	P08631
IntActⁱ	P08631, 103 interactors
MINTⁱ	P08631
STRINGⁱ	9606.ENSP00000444986

Chemistry databases

BindingDBⁱ	P08631
ChEMBLⁱ	CHEMBL3234
DrugBankⁱ	DB01809 1-Ter-Butyl-3-P-Tolyl-1h-Pyrazolo[3,4-D]Pyrimidin-4-Ylamine DB06616 Bosutinib DB12010 Fostamatinib DB01962 Phosphonotyrosine DB04216 Quercetin
DrugCentralⁱ	P08631
GuidetoPHARMACOLOGYⁱ	2032

PTM databases

iPTMnetⁱ	P08631
PhosphoSitePlusⁱ	P08631
SwissPalmⁱ	P08631

Polymorphism and mutation databases

BioMutaⁱ	HCK
DMDMⁱ	20141296

Proteomic databases

jPOSTⁱ	P08631
MassIVEⁱ	P08631
MaxQBⁱ	P08631
PaxDbⁱ	P08631
PeptideAtlasⁱ	P08631
PRIDEⁱ	P08631
ProteomicsDBⁱ	52142 [P08631-1] 52143 [P08631-2] 52144 [P08631-3] 52145 [P08631-4]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	3055

DNASUⁱ

3055

Genome annotation databases

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]
GeneIDⁱ	3055
KEGGⁱ	hsa:3055
UCSCⁱ	uc002wxi.4 human [P08631-1]

Organism-specific databases

CTDⁱ	3055
DisGeNETⁱ	3055
GeneCardsⁱ	HCK
HGNCⁱ	HGNC:4840 HCK
HPAⁱ	CAB005195 HPA063768
MIMⁱ	142370 gene
neXtProtⁱ	NX_P08631
OpenTargetsⁱ	ENSG00000101336
PharmGKBⁱ	PA29216
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0197 Eukaryota COG0515 LUCA
GeneTreeⁱ	ENSGT00940000158738
HOGENOMⁱ	HOG000233858
InParanoidⁱ	P08631
KOⁱ	K08893
OrthoDBⁱ	539311at2759
PhylomeDBⁱ	P08631

Enzyme and pathway databases

BRENDAⁱ	2.7.10.2 2681
Reactomeⁱ	R-HSA-164944 Nef and signal transduction R-HSA-2029481 FCGR activation R-HSA-912631 Regulation of signaling by CBL R-HSA-9607240 FLT3 Signaling
SignaLinkⁱ	P08631
SIGNORⁱ	P08631

Miscellaneous databases

ChiTaRSⁱ	HCK human
EvolutionaryTraceⁱ	P08631
GeneWikiⁱ	HCK
GenomeRNAiⁱ	3055
Pharosⁱ	P08631
Protein Ontology More...PROⁱ	PR:P08631
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000101336 Expressed in 200 organ(s), highest expression level in blood
ExpressionAtlasⁱ	P08631 baseline and differential
Genevisibleⁱ	P08631 HS

Family and domain databases

CDDⁱ	cd10363 SH2_Src_HCK, 1 hit
Gene3Dⁱ	3.30.505.10, 1 hit
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
Pfamⁱ	View protein in Pfam PF07714 Pkinase_Tyr, 1 hit PF00017 SH2, 1 hit PF00018 SH3_1, 1 hit
PRINTSⁱ	PR00401 SH2DOMAIN PR00452 SH3DOMAIN PR00109 TYRKINASE
SMARTⁱ	View protein in SMART SM00252 SH2, 1 hit SM00326 SH3, 1 hit SM00219 TyrKc, 1 hit
SUPFAMⁱ	SSF50044 SSF50044, 1 hit SSF55550 SSF55550, 1 hit SSF56112 SSF56112, 1 hit
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
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	HCK_HUMAN
Accessionⁱ	P08631Primary (citable) accession number: P08631 Secondary accession number(s): A8K1I1 Q9UMJ5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
	Last sequence update:	January 23, 2007
	Last modified:	October 16, 2019
	This is version 248 of the entry and version 5 of the sequence. See complete history.
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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human and mouse protein kinases
Human and mouse protein kinases: classification and index
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
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

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UniProtKB - P08631 (HCK_HUMAN)

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Tyrosine-protein kinase HCK

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<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>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. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Regions

<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

GO - Biological processi

Enzyme and pathway databases

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

Organism-specific databases

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

Plasma membrane

Lysosome

Cytosol

Other locations

Plasma membrane

Lysosome

Nucleus

Cytoskeleton

Golgi apparatus

Other locations

Cytosol

Other locations

Cytoskeleton

Cytosol

Golgi apparatus

Lysosome

Nucleus

Plasma Membrane

Other locations

Keywords - Cellular componenti

<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

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

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

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

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

Gene expression databases

Organism-specific databases

<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

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

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

Secondary structure

3D structure databases

Miscellaneous databases

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

Domains and Repeats

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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This 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

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ