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Tyrosine-protein kinase HCK (EC 2.7.10.2) (Hematopoietic cell kinase) (Hemopoietic cell kinase) (p56-HCK) (p56Hck) (p59Hck)

 HCK_RAT                 Reviewed;         524 AA.
P50545; Q64647; Q6AYV7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
23-MAY-2018, entry version 170.
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;
AltName: Full=p56Hck;
AltName: Full=p59Hck;
Name=Hck;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Megakaryocyte;
PubMed=1764064; DOI=10.1016/0006-291X(91)92057-Q;
Okano Y., Sugimoto Y., Fukuoka M., Matsui A., Nagata K., Nozawa Y.;
"Identification of rat cDNA encoding hck tyrosine kinase from
megakaryocytes.";
Biochem. Biophys. Res. Commun. 181:1137-1144(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
STRAIN=Wistar; TISSUE=Spleen;
Vijaya Gouri B.S., Rema V., Kamatkar S., Swarup G.;
"Nucleotide sequence of a cDNA coding for rat hck tyrosine kinase and
characterization of its gene product.";
J. Biosci. 19:117-129(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=Brown Norway; TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[4]
INTERACTION WITH RAPGEF1, AND FUNCTION IN PHOSPHORYLATION OF RAPGEF1.
PubMed=14551197; DOI=10.1074/jbc.M310656200;
Shivakrupa R., Radha V., Sudhakar C., Swarup G.;
"Physical and functional interaction between Hck tyrosine kinase and
guanine nucleotide exchange factor C3G results in apoptosis, which is
independent of C3G catalytic domain.";
J. Biol. Chem. 278:52188-52194(2003).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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,
ECO:0000269|PubMed:14551197}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME 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-409 is required for
optimal activity. Phosphorylation at Tyr-520 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}.
-!- SUBCELLULAR LOCATION: Isoform 1: Membrane; Lipid-anchor. Membrane,
caveola {ECO:0000250}. Lysosome {ECO:0000250}. Cell projection,
podosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
Cytoplasm, cytosol {ECO:0000250}. Note=Associated with specialized
secretory lysosomes called azurophil granules. A fraction of this
isoform is found in the cytoplasm, some of this fraction is
myristoylated (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: 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 of this isoform 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=1; Synonyms=p59-HCK;
IsoId=P50545-1; Sequence=Displayed;
Name=2; Synonyms=p56-HCK;
IsoId=P50545-2; Sequence=VSP_022248;
Note=Initiator Met-1 is removed. Contains a N-myristoyl glycine
at position 2 (By similarity). Contains a S-palmitoyl cysteine
at position 3 (By similarity). {ECO:0000250|UniProtKB:P08631};
-!- TISSUE SPECIFICITY: Expressed strongly in spleen and at very low
levels in thymus. {ECO:0000269|Ref.2}.
-!- PTM: Phosphorylated on several tyrosine residues.
Autophosphorylated. Becomes rapidly phosphorylated upon activation
of the immunoglobulin receptors FCGR1A and FCGR2A. Phosphorylation
at Tyr-409 increases kinase activity. Phosphorylation at Tyr-520
inhibits kinase activity. Kinase activity is not required for
phosphorylation at Tyr-520, 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: Isoform 2 palmitoylation at position 2 requires prior
myristoylation. Palmitoylation at position 3 is required for
caveolar localization of isoform 2.
{ECO:0000250|UniProtKB:P08631}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAA41312.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAB20754.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA44218.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M83666; AAA41312.1; ALT_INIT; mRNA.
EMBL; S74141; AAB20754.1; ALT_INIT; mRNA.
EMBL; X62345; CAA44218.1; ALT_INIT; mRNA.
EMBL; BC078890; AAH78890.2; -; mRNA.
PIR; JQ1321; JQ1321.
RefSeq; NP_037317.2; NM_013185.3. [P50545-1]
UniGene; Rn.10945; -.
ProteinModelPortal; P50545; -.
SMR; P50545; -.
STRING; 10116.ENSRNOP00000012432; -.
iPTMnet; P50545; -.
PhosphoSitePlus; P50545; -.
PaxDb; P50545; -.
PRIDE; P50545; -.
Ensembl; ENSRNOT00000012432; ENSRNOP00000012432; ENSRNOG00000009331. [P50545-2]
GeneID; 25734; -.
KEGG; rno:25734; -.
UCSC; RGD:2785; rat. [P50545-1]
CTD; 3055; -.
RGD; 2785; Hck.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; P50545; -.
KO; K08893; -.
OMA; RPEHCPE; -.
PhylomeDB; P50545; -.
BRENDA; 2.7.10.2; 5301.
Reactome; R-RNO-2029481; FCGR activation.
Reactome; R-RNO-912631; Regulation of signaling by CBL.
PRO; PR:P50545; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000009331; -.
GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
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:0005654; C:nucleoplasm; IEA:Ensembl.
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; IBA:GO_Central.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
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:0042127; P:regulation of cell proliferation; IBA:GO_Central.
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.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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.
1: Evidence at protein level;
Alternative initiation; ATP-binding; Cell junction; Cell membrane;
Cell projection; Complete proteome; 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; Reference proteome;
SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P08631}.
CHAIN 2 524 Tyrosine-protein kinase HCK.
/FTId=PRO_0000088104.
DOMAIN 76 136 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 142 239 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 260 513 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 266 274 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 379 379 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 288 288 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 50 50 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P08631}.
MOD_RES 200 200 Phosphothreonine.
{ECO:0000250|UniProtKB:P08631}.
MOD_RES 207 207 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08103}.
MOD_RES 409 409 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P08631}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000250|UniProtKB:P08631}.
MOD_RES 520 520 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08631}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
VAR_SEQ 1 21 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1764064,
ECO:0000303|Ref.2}.
/FTId=VSP_022248.
CONFLICT 72 72 V -> F (in Ref. 1; AAA41312/AAB20754).
{ECO:0000305}.
CONFLICT 226 226 K -> R (in Ref. 2; CAA44218).
{ECO:0000305}.
CONFLICT 327 327 I -> T (in Ref. 2; CAA44218).
{ECO:0000305}.
SEQUENCE 524 AA; 59154 MW; BBD928C9E717BF4B CRC64;
MGGRSSCEDP GCPRGEGRVP RMGCVKSRFL REGSKASKIE PNANQKGPVY VPDPTSPKKL
GPNSINSLPP GVVEGSEDTI VVALYDYEAI HREDLSFQKG DQMVVLEESG EWWKARSLAT
KKEGYIPSNY VARVNSLETE EWFFKGISRK DAERHLLAPG NMLGSFMIRD SETTKGSYSL
SVRDFDPQHG DTVKHYKIRT LDSGGFYISP RSTFSSLQEL VVHYKKGKDG LCQKLSVPCV
SPKPQKPWEK DAWEIPRESL QMEKKLGAGQ FGEVWMATYN KHTKVAVKTM KPGSMSVEAF
LAEANLMKTL QHDKLVKLHA VVSQEPIFIV TEFMAKGSLL DFLKSEEGSK QPLPKLIDFS
AQISEGMAFI EQRNYIHRDL RAANILVSAS LVCKIADFGL ARIIEDNEYT AREGAKFPIK
WTAPEAINFG SFTIKSDVWS FGILLMEIVT YGRIPYPGMS NPEVIRALEH GYRMPRPDNC
PEELYSIMIR CWKNRPEERP TFEYIQSVLD DFYTATESQY QQQP


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