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Tyrosine-protein kinase HCK (EC 2.7.10.2) (Hematopoietic cell kinase) (Hemopoietic cell kinase) (p56-HCK)

 HCK_MACFA               Reviewed;         504 AA.
Q95M30;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 117.
RecName: Full=Tyrosine-protein kinase HCK;
EC=2.7.10.2;
AltName: Full=Hematopoietic cell kinase;
AltName: Full=Hemopoietic cell kinase;
AltName: Full=p56-HCK;
Name=HCK;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Picard C.;
Thesis (2001), University of Marseille, France.
-!- FUNCTION: 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 (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-
tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136,
Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
-!- ACTIVITY REGULATION: 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-389 is required for
optimal activity. Phosphorylation at Tyr-500 inhibits kinase
activity (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with ADAM15. Interacts with FASLG. Interacts
with ARRB1 and ARRB2. 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 SH2 domain) with FLT3 (tyrosine
phosphorylated). Interacts with CBL. Interacts with VAV1, WAS and
RAPGEF1. Interacts (via SH3 domain) with WDCP.
{ECO:0000250|UniProtKB:P08103, ECO:0000250|UniProtKB:P08631}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
{ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cell membrane;
Lipid-anchor. Membrane, caveola {ECO:0000250}; Lipid-anchor
{ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}.
Cytoplasm, cytoskeleton {ECO:0000250}. Golgi apparatus
{ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Lysosome
{ECO:0000250}. Nucleus {ECO:0000250}. Note=A small fraction is
associated with caveolae. Localization at the cell membrane and at
caveolae requires palmitoylation at Cys-3. Colocalizes with the
actin cytoskeleton at focal adhesions (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylated on several tyrosine residues.
Autophosphorylated. Becomes rapidly phosphorylated upon activation
of the immunoglobulin receptors FCGR1A and FCGR2A. Phosphorylation
at Tyr-389 increases kinase activity. Phosphorylation at Tyr-500
inhibits kinase activity. Kinase activity is not required for
phosphorylation at Tyr-500, suggesting that this site may be a
target of other kinases (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated by CBL, leading to its degradation via the
proteasome. {ECO:0000250}.
-!- PTM: Palmitoylation requires prior myristoylation. Palmitoylation
is required for caveolar localization (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; AJ320181; CAC44031.1; -; mRNA.
RefSeq; NP_001306372.1; NM_001319443.1.
UniGene; Mfa.6652; -.
ProteinModelPortal; Q95M30; -.
SMR; Q95M30; -.
PRIDE; Q95M30; -.
GeneID; 102115729; -.
KEGG; mcf:102115729; -.
CTD; 3055; -.
HOVERGEN; HBG008761; -.
KO; K08893; -.
BRENDA; 2.7.10.2; 1793.
GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
GO; GO:0050764; P:regulation of phagocytosis; ISS:UniProtKB.
GO; GO:0071801; P:regulation of podosome assembly; ISS:UniProtKB.
CDD; cd10363; SH2_Src_HCK; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035851; HCK_SH2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
2: Evidence at transcript level;
ATP-binding; Cell junction; Cell membrane; Cytoplasm;
Cytoplasmic vesicle; Cytoskeleton; Exocytosis; Golgi apparatus;
Immunity; Inflammatory response; Innate immunity; Kinase; Lipoprotein;
Lysosome; Membrane; Myristate; Nucleotide-binding; Nucleus; Palmitate;
Phagocytosis; Phosphoprotein; Proto-oncogene; SH2 domain; SH3 domain;
Transferase; Tyrosine-protein kinase; Ubl conjugation.
INIT_MET 1 1 Removed.
CHAIN 2 504 Tyrosine-protein kinase HCK.
/FTId=PRO_0000088103.
DOMAIN 56 116 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 122 219 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 240 493 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 246 254 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 359 359 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 268 268 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 15 15 Phosphothreonine.
{ECO:0000250|UniProtKB:P08631}.
MOD_RES 30 30 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08631}.
MOD_RES 180 180 Phosphothreonine.
{ECO:0000250|UniProtKB:P08631}.
MOD_RES 187 187 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08103}.
MOD_RES 389 389 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P08631}.
MOD_RES 440 440 Phosphoserine.
{ECO:0000250|UniProtKB:P08631}.
MOD_RES 500 500 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08631}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
LIPID 3 3 S-palmitoyl cysteine. {ECO:0000250}.
SEQUENCE 504 AA; 57096 MW; 53B29322D2DE3423 CRC64;
MGCMKSKFLQ AGGNTFSKTE TSANPHCPVY VPDPTSTIKP GPNSNNRNTP GIGEGSEDII
VVALYDYEAI HHEDLSFQKG DQMVVLEESG EWWKARSLAT RKEGYIPSNY VARVDSLETE
EWFFKGISRK DAERQLLAPG NMLGSFMIRD SETTKGSYSL SVRDYDPRQG DTVKHYKIRT
LDNGGFYISP RSTFSTLQEL VDHYKKGSDG LCQKLSVPCV SSKPQKPWEK DAWEIPRESL
KLEKKLGAGQ FGEVWMATYN KHTKVAVKTM KPGSMSVEAF LAEANLMKTL QHDKLVKLHA
VVTKEPIYII TEFMAKGSLL DFLKSDEGSK QPLPKLIDFS AQIAEGMAFI EQRNYIHRDL
RAANILVSAS LVCKIADFGL ARIIEDNEYT AREGAKFPIK WTAPEAINFG SSTIKSDVWS
FGILLMEIVT YGRIPYPGMS NPEVIRALER GYRMPRPENC PEELYNIMMR CWKNRPEERP
TFEYIQSVLD DFYTATESQY QQQP


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