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Protein

Tyrosine-protein kinase HCK

Gene

HCK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation8 Publications

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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei290ATP1
Active sitei381Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi268 – 276ATP9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • non-membrane spanning protein tyrosine kinase activity Source: GO_Central
  • phosphotyrosine residue binding Source: CAFA
  • protein tyrosine kinase activity Source: UniProtKB
  • signaling receptor binding Source: GO_Central

GO - Biological processi

Keywordsi

Molecular functionKinase, Transferase, Tyrosine-protein kinase
Biological processExocytosis, Host-virus interaction, Immunity, Inflammatory response, Innate immunity, Phagocytosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-164944 Nef and signal transduction
R-HSA-2029481 FCGR activation
R-HSA-912631 Regulation of signaling by CBL
SignaLinkiP08631
SIGNORiP08631

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

EuPathDBiHostDB:ENSG00000101336.12
HGNCiHGNC:4840 HCK
MIMi142370 gene
neXtProtiNX_P08631

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi3G → C: Slight palmitoylation, cytoplasmic and caveolar localization; in isoform 1;. 2 Publications1
Mutagenesisi3G → S: Abolishes palmitoylation and localization at the cell membrane. 2 Publications1
Mutagenesisi23G → A: Myristoylation and palmitoylation are abolished, leading to entirely cytoplasmic localization; in isoform 2. 1 Publication1
Mutagenesisi24C → S: Palmitoylation is abolished, some cytoplasmic and no calveolar localization; in isoform 2. 1 Publication1
Mutagenesisi290K → E: Loss of kinase activity. 1 Publication1
Mutagenesisi305E → A: Loss of kinase activity. 1 Publication1
Mutagenesisi381D → E: Loss of kinase activity. 1 Publication1
Mutagenesisi411Y → A: Reduced catalytic activity and higher affinity for target peptides. 1 Publication1
Mutagenesisi522Y → F: Constitutively activated kinase, leading to cellular transformation. 2 Publications1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi3055
OpenTargetsiENSG00000101336
PharmGKBiPA29216

Chemistry databases

ChEMBLiCHEMBL3234
DrugBankiDB06616 Bosutinib
DB01962 Phosphonotyrosine
DB04216 Quercetin
GuidetoPHARMACOLOGYi2032

Polymorphism and mutation databases

BioMutaiHCK
DMDMi20141296

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000244332 – 526Tyrosine-protein kinase HCKAdd BLAST525
Isoform 2 (identifier: P08631-2)
Initiator methionineiRemoved

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1
Modified residuei36PhosphothreonineCombined sources1
Modified residuei51Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei202PhosphothreonineCombined sources1
Modified residuei209PhosphotyrosineBy similarity1
Modified residuei411Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei462PhosphoserineCombined sources1
Modified residuei522Phosphotyrosine5 Publications1
Isoform 2 (identifier: P08631-2)
Lipidationi2N-myristoyl glycine1
Lipidationi3S-palmitoyl cysteine1

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

EPDiP08631
MaxQBiP08631
PaxDbiP08631
PeptideAtlasiP08631
PRIDEiP08631
ProteomicsDBi52142
52143 [P08631-2]
52144 [P08631-3]
52145 [P08631-4]

PTM databases

iPTMnetiP08631
PhosphoSitePlusiP08631
SwissPalmiP08631

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

BgeeiENSG00000101336 Expressed in 200 organ(s), highest expression level in blood
ExpressionAtlasiP08631 baseline and differential
GenevisibleiP08631 HS

Organism-specific databases

HPAiCAB005195
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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi109305, 64 interactors
DIPiDIP-1051N
ELMiP08631
IntActiP08631, 104 interactors
MINTiP08631
STRINGi9606.ENSP00000365012

Chemistry databases

BindingDBiP08631

Structurei

Secondary structure

1526
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP08631
SMRiP08631
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08631

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini78 – 138SH3PROSITE-ProRule annotationAdd BLAST61
Domaini144 – 241SH2PROSITE-ProRule annotationAdd BLAST98
Domaini262 – 515Protein kinasePROSITE-ProRule annotationAdd BLAST254

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

eggNOGiKOG0197 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00760000118938
HOGENOMiHOG000233858
HOVERGENiHBG008761
InParanoidiP08631
KOiK08893
PhylomeDBiP08631

Family and domain databases

CDDicd10363 SH2_Src_HCK, 1 hit
Gene3Di3.30.505.10, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00452 SH3DOMAIN
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView 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. AlignAdd to basket

This entry has 4 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P08631-1) [UniParc]FASTAAdd to basket
Also known as: p60-HCK, p61Hck

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.

« 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]FASTAAdd to basket
Also known as: p59-HCK, p59Hck

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

Show »
Length:505
Mass (Da):57,312
Checksum:i4F1EC1E8F3EDF9CA
GO
Isoform 3 (identifier: P08631-3) [UniParc]FASTAAdd to basket

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

Show »
Length:504
Mass (Da):57,241
Checksum:iC07FF5B8D3C1B862
GO
Isoform 4 (identifier: P08631-4) [UniParc]FASTAAdd to basket

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

Note: Initiates from a CTG codon.
Show »
Length:525
Mass (Da):59,529
Checksum:i803967415A2F57FC
GO

Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0Y3C5H0Y3C5_HUMAN
Tyrosine-protein kinase
HCK
525Annotation score:
J3KPD6J3KPD6_HUMAN
Tyrosine-protein kinase
HCK
526Annotation score:
F6SF04F6SF04_HUMAN
Tyrosine-protein kinase
HCK
526Annotation score:
H7BXG4H7BXG4_HUMAN
Tyrosine-protein kinase HCK
HCK
41Annotation score:
H7C5P9H7C5P9_HUMAN
Tyrosine-protein kinase HCK
HCK
61Annotation score:

Sequence cautioni

The sequence AAA52643 differs from that shown. Reason: Frameshift at position 20.Curated
The sequence BAF82585 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti24C → S in AAA52643 (PubMed:3496523).Curated1
Sequence conflicti69N → D in BAF82585 (PubMed:14702039).Curated1
Sequence conflicti144W → R in BAB15482 (PubMed:14702039).Curated1
Sequence conflicti168F → Y in BAF82585 (PubMed:14702039).Curated1
Sequence conflicti378I → T in AAI13855 (PubMed:15489334).Curated1
Sequence conflicti488N → S in BAF82585 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04170744A → T1 PublicationCorresponds to variant dbSNP:rs56029200Ensembl.1
Natural variantiVAR_041708105M → L2 PublicationsCorresponds to variant dbSNP:rs55722810Ensembl.1
Natural variantiVAR_041709399D → G in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_033836502P → Q. Corresponds to variant dbSNP:rs17093828Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0188581 – 21Missing in isoform 2 and isoform 3. 3 PublicationsAdd BLAST21
Alternative sequenceiVSP_04192676Missing in isoform 3 and isoform 4. 2 Publications1

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
CCDSiCCDS33460.1 [P08631-1]
CCDS54453.1 [P08631-4]
CCDS54455.1 [P08631-2]
CCDS54456.1 [P08631-3]
PIRiA27811 TVHUHC
A41263
RefSeqiNP_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]
UniGeneiHs.655210

Genome annotation databases

EnsembliENST00000518730; 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]
GeneIDi3055
KEGGihsa:3055
UCSCiuc002wxi.4 human [P08631-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Similar proteinsi

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
CCDSiCCDS33460.1 [P08631-1]
CCDS54453.1 [P08631-4]
CCDS54455.1 [P08631-2]
CCDS54456.1 [P08631-3]
PIRiA27811 TVHUHC
A41263
RefSeqiNP_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]
UniGeneiHs.655210

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AD5X-ray2.60A/B79-526[»]
1BU1X-ray2.60A/B/C/D/E/F81-137[»]
1QCFX-ray2.00A81-526[»]
2C0IX-ray2.30A/B81-526[»]
2C0OX-ray2.85A/B81-526[»]
2C0TX-ray2.15A/B81-526[»]
2HCKX-ray3.00A/B79-526[»]
2HK5X-ray2.00A247-514[»]
2OI3NMR-A61-141[»]
2OJ2NMR-A61-141[»]
3HCKNMR-A140-245[»]
3NHNX-ray2.61A72-256[»]
3RBBX-ray2.35B/D79-138[»]
3REAX-ray2.00B/D79-138[»]
3REBX-ray3.45B/D79-138[»]
3VRYX-ray2.48A/B81-526[»]
3VRZX-ray2.22A/B81-526[»]
3VS0X-ray2.93A/B81-526[»]
3VS1X-ray2.46A/B81-526[»]
3VS2X-ray2.61A/B81-526[»]
3VS3X-ray2.17A/B81-526[»]
3VS4X-ray2.75A/B81-526[»]
3VS5X-ray2.85A/B81-526[»]
3VS6X-ray2.37A/B81-526[»]
3VS7X-ray3.00A/B81-526[»]
4HCKNMR-A72-143[»]
4LUDX-ray2.85A/B81-526[»]
4LUEX-ray3.04A/B81-526[»]
4ORZX-ray2.00A77-138[»]
4U5WX-ray1.86B/D72-242[»]
5H09X-ray1.95A81-526[»]
5H0BX-ray1.65A81-526[»]
5H0EX-ray2.10A81-526[»]
5H0GX-ray1.80A81-526[»]
5H0HX-ray1.72A81-526[»]
5HCKNMR-A72-143[»]
5NUHX-ray2.78C/D79-138[»]
5ZJ6X-ray1.70A/B242-521[»]
ProteinModelPortaliP08631
SMRiP08631
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109305, 64 interactors
DIPiDIP-1051N
ELMiP08631
IntActiP08631, 104 interactors
MINTiP08631
STRINGi9606.ENSP00000365012

Chemistry databases

BindingDBiP08631
ChEMBLiCHEMBL3234
DrugBankiDB06616 Bosutinib
DB01962 Phosphonotyrosine
DB04216 Quercetin
GuidetoPHARMACOLOGYi2032

PTM databases

iPTMnetiP08631
PhosphoSitePlusiP08631
SwissPalmiP08631

Polymorphism and mutation databases

BioMutaiHCK
DMDMi20141296

Proteomic databases

EPDiP08631
MaxQBiP08631
PaxDbiP08631
PeptideAtlasiP08631
PRIDEiP08631
ProteomicsDBi52142
52143 [P08631-2]
52144 [P08631-3]
52145 [P08631-4]

Protocols and materials databases

DNASUi3055
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000518730; 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]
GeneIDi3055
KEGGihsa:3055
UCSCiuc002wxi.4 human [P08631-1]

Organism-specific databases

CTDi3055
DisGeNETi3055
EuPathDBiHostDB:ENSG00000101336.12
GeneCardsiHCK
HGNCiHGNC:4840 HCK
HPAiCAB005195
HPA063768
MIMi142370 gene
neXtProtiNX_P08631
OpenTargetsiENSG00000101336
PharmGKBiPA29216
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0197 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00760000118938
HOGENOMiHOG000233858
HOVERGENiHBG008761
InParanoidiP08631
KOiK08893
PhylomeDBiP08631

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-164944 Nef and signal transduction
R-HSA-2029481 FCGR activation
R-HSA-912631 Regulation of signaling by CBL
SignaLinkiP08631
SIGNORiP08631

Miscellaneous databases

ChiTaRSiHCK human
EvolutionaryTraceiP08631
GeneWikiiHCK
GenomeRNAii3055
PROiPR:P08631
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101336 Expressed in 200 organ(s), highest expression level in blood
ExpressionAtlasiP08631 baseline and differential
GenevisibleiP08631 HS

Family and domain databases

CDDicd10363 SH2_Src_HCK, 1 hit
Gene3Di3.30.505.10, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00452 SH3DOMAIN
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView 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
ProtoNetiSearch...

Entry informationi

Entry nameiHCK_HUMAN
AccessioniPrimary (citable) accession number: P08631
Secondary accession number(s): A8K1I1
, B4DQB6, E1P5M2, Q29RX1, Q2VPE2, Q504R5, Q5T7K1, Q5T7K2, Q96CC0, Q9H5Y5, Q9NUA4, Q9UMJ5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: September 12, 2018
This is version 238 of the entry and version 5 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

  1. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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