Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00907
Entry Name
UniProt Accession
Theoretical PI
6.27
Molecular Weight
59599.84
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Tyrosine-protein kinase HCK
Protein Synonyms/Alias
2.7.10.2; Hematopoietic cell kinase; Hemopoietic cell kinase; p59-HCK/p60-HCK; p59Hck; p61Hck;
Gene Name
HCK
Gene Synonyms/Alias
Created Date
01-AUG-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGGRSSCED
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Robbins SM, Quintrell NA, Bishop JM. Myristoylation and differentialpalmitoylation of the HCK protein-tyrosine kinases govern their attachment tomembranes and association with caveolae. Mol Cell Biol. 1995 Jul;15(7):3507-15.[PMID:7791757]
Functional Description
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.
Sequence Annotation
Domain: 78 138 SH3.
Domain: 144 241 SH2.
Domain: 262 515 Protein kinase.
Nucleotide-binding: 268 276 ATP.
Active site: 381 381 Proton acceptor.
Binding site: 290 290 ATP.
Modified residue: 51 51 Phosphotyrosine; by autocatalysis.
Modified residue: 202 202 Phosphothreonine.
Modified residue: 209 209 Phosphotyrosine.
Modified residue: 411 411 Phosphotyrosine; by autocatalysis.
Modified residue: 462 462 Phosphoserine.
Modified residue: 522 522 Phosphotyrosine.
Protein Length
526 AA.
Protein Sequence
(Canonical)
MGGRSSCEDP GCPRDEERAP RMGCMKSKFL QVGGNTFSKT ETSASPHCPV YVPDPTSTIK  60
PGPNSHNSNT PGIREAGSED IIVVALYDYE AIHHEDLSFQ KGDQMVVLEE SGEWWKARSL  120
ATRKEGYIPS NYVARVDSLE TEEWFFKGIS RKDAERQLLA PGNMLGSFMI RDSETTKGSY  180
SLSVRDYDPR QGDTVKHYKI RTLDNGGFYI SPRSTFSTLQ ELVDHYKKGN DGLCQKLSVP  240
CMSSKPQKPW EKDAWEIPRE SLKLEKKLGA GQFGEVWMAT YNKHTKVAVK TMKPGSMSVE  300
AFLAEANVMK TLQHDKLVKL HAVVTKEPIY IITEFMAKGS LLDFLKSDEG SKQPLPKLID  360
FSAQIAEGMA FIEQRNYIHR DLRAANILVS ASLVCKIADF GLARVIEDNE YTAREGAKFP  420
IKWTAPEAIN FGSFTIKSDV WSFGILLMEI VTYGRIPYPG MSNPEVIRAL ERGYRMPRPE  480
NCPEELYNIM MRCWKNRPEE RPTFEYIQSV LDDFYTATES QYQQQP                 526
FASTA
(Canonical)
>LipidDB-9606-00907|P08631
MGGRSSCEDPGCPRDEERAPRMGCMKSKFLQVGGNTFSKTETSASPHCPVYVPDPTSTIK
PGPNSHNSNTPGIREAGSEDIIVVALYDYEAIHHEDLSFQKGDQMVVLEESGEWWKARSL
ATRKEGYIPSNYVARVDSLETEEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGSY
SLSVRDYDPRQGDTVKHYKIRTLDNGGFYISPRSTFSTLQELVDHYKKGNDGLCQKLSVP
CMSSKPQKPWEKDAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVE
AFLAEANVMKTLQHDKLVKLHAVVTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLID
FSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAKFP
IKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPE
NCPEELYNIMMRCWKNRPEERPTFEYIQSVLDDFYTATESQYQQQP
Gene Ontology
GO:0005901; C:caveola; IDA:UniProtKB
GO:0042995; C:cell projection; IEA:UniProtKB-KW
GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW
GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW
GO:0005829; C:cytosol; TAS:Reactome
GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IMP:UniProtKB
GO:0005925; C:focal adhesion; IMP:UniProtKB
GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW
GO:0005764; C:lysosome; IDA:UniProtKB
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC
GO:0004713; F:protein tyrosine kinase activity; IMP:UniProtKB
GO:0007155; P:cell adhesion; TAS:UniProtKB
GO:0019221; P:cytokine-mediated signaling pathway; TAS:UniProtKB
GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome
GO:0006954; P:inflammatory response; IEA:UniProtKB-KW
GO:0045087; P:innate immune response; TAS:Reactome
GO:0002758; P:innate immune response-activating signal transduction; TAS:UniProtKB
GO:0007229; P:integrin-mediated signaling pathway; TAS:UniProtKB
GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:UniProtKB
GO:0043299; P:leukocyte degranulation; TAS:UniProtKB
GO:0002522; P:leukocyte migration involved in immune response; TAS:UniProtKB
GO:0031663; P:lipopolysaccharide-mediated signaling pathway; TAS:UniProtKB
GO:0007498; P:mesoderm development; TAS:ProtInc
GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB
GO:0018108; P:peptidyl-tyrosine phosphorylation; IMP:UniProtKB
GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IDA:UniProtKB
GO:0030838; P:positive regulation of actin filament polymerization; TAS:UniProtKB
GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB
GO:0046777; P:protein autophosphorylation; IMP:UniProtKB
GO:0006468; P:protein phosphorylation; TAS:ProtInc
GO:0008360; P:regulation of cell shape; IMP:UniProtKB
GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome
GO:0050727; P:regulation of inflammatory response; TAS:UniProtKB
GO:0050764; P:regulation of phagocytosis; IMP:UniProtKB
GO:0071801; P:regulation of podosome assembly; IDA:UniProtKB
GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; IMP:UniProtKB
GO:0045728; P:respiratory burst after phagocytosis; TAS:UniProtKB
GO:0016032; P:viral process; TAS:Reactome
Interpro
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR017441; Protein_kinase_ATP_BS
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom
InterPro; IPR000980; SH2
InterPro; IPR001452; SH3_domain
InterPro; IPR008266; Tyr_kinase_AS
InterPro; IPR020635; Tyr_kinase_cat_dom
Pfam
Pfam; PF07714; Pkinase_Tyr;
Pfam; PF00017; SH2;
Pfam; PF00018; SH3_1;
SMART
SMART; SM00252; SH2;
SMART; SM00326; SH3;
SMART; SM00219; TyrKc;
PROSITE
PROSITE; PS00107; PROTEIN_KINASE_ATP;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00109; PROTEIN_KINASE_TYR;
PROSITE; PS50001; SH2;
PROSITE; PS50002; SH3;
PRINTS
PRINTS; PR00401; SH2DOMAIN;
PRINTS; PR00452; SH3DOMAIN;
PRINTS; PR00109; TYRKINASE;