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Tyrosine-protein kinase HCK (EC 2.7.10.2) (B-cell/myeloid kinase) (BMK) (Hematopoietic cell kinase) (Hemopoietic cell kinase) (p56-HCK/p59-HCK)

 HCK_MOUSE               Reviewed;         524 AA.
P08103; Q0VH03; Q3UD17;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
12-SEP-2018, entry version 195.
RecName: Full=Tyrosine-protein kinase HCK;
EC=2.7.10.2;
AltName: Full=B-cell/myeloid kinase;
Short=BMK;
AltName: Full=Hematopoietic cell kinase;
AltName: Full=Hemopoietic cell kinase;
AltName: Full=p56-HCK/p59-HCK;
Name=Hck;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=ICR; TISSUE=Macrophage;
PubMed=3684607; DOI=10.1093/nar/15.22.9600;
Klemsz M.J., McKercher S.R., Maki R.A.;
"Nucleotide sequence of the mouse hck gene.";
Nucleic Acids Res. 15:9600-9600(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Macrophage;
PubMed=3317404; DOI=10.1073/pnas.84.23.8325;
Holtzman D.A., Cook W.D., Dunn A.R.;
"Isolation and sequence of a cDNA corresponding to a src-related gene
expressed in murine hemopoietic cells.";
Proc. Natl. Acad. Sci. U.S.A. 84:8325-8329(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow macrophage, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary gland;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-21 (ISOFORM 1), SUBCELLULAR LOCATION,
IDENTIFICATION OF ISOFORM 2, AND ALTERNATIVE INITIATION.
PubMed=1875927; DOI=10.1128/MCB.11.9.4363;
Lock P., Ralph S., Stanley E., Boulet I., Ramsay R., Dunn A.R.;
"Two isoforms of murine hck, generated by utilization of alternative
translational initiation codons, exhibit different patterns of
subcellular localization.";
Mol. Cell. Biol. 11:4363-4370(1991).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=8125254; DOI=10.1101/gad.8.4.387;
Lowell C.A., Soriano P., Varmus H.E.;
"Functional overlap in the src gene family: inactivation of hck and
fgr impairs natural immunity.";
Genes Dev. 8:387-398(1994).
[7]
DISRUPTION PHENOTYPE.
PubMed=8666673; DOI=10.1083/jcb.133.4.895;
Lowell C.A., Fumagalli L., Berton G.;
"Deficiency of Src family kinases p59/61hck and p58c-fgr results in
defective adhesion-dependent neutrophil functions.";
J. Cell Biol. 133:895-910(1996).
[8]
FUNCTION, AND INTERACTION WITH VAV1.
PubMed=9400828;
English B.K., Orlicek S.L., Mei Z., Meals E.A.;
"Bacterial LPS and IFN-gamma trigger the tyrosine phosphorylation of
vav in macrophages: evidence for involvement of the hck tyrosine
kinase.";
J. Leukoc. Biol. 62:859-864(1997).
[9]
FUNCTION.
PubMed=10547366;
Suen P.W., Ilic D., Caveggion E., Berton G., Damsky C.H., Lowell C.A.;
"Impaired integrin-mediated signal transduction, altered cytoskeletal
structure and reduced motility in Hck/Fgr deficient macrophages.";
J. Cell Sci. 112:4067-4078(1999).
[10]
FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
PubMed=9916742;
Mocsai A., Ligeti E., Lowell C.A., Berton G.;
"Adhesion-dependent degranulation of neutrophils requires the Src
family kinases Fgr and Hck.";
J. Immunol. 162:1120-1126(1999).
[11]
FUNCTION IN PHOSPHORYLATION OF CBL, SUBCELLULAR LOCATION, AND
INTERACTION WITH CBL.
PubMed=10799548; DOI=10.1074/jbc.275.19.14615;
Scholz G., Cartledge K., Dunn A.R.;
"Hck enhances the adherence of lipopolysaccharide-stimulated
macrophages via Cbl and phosphatidylinositol 3-kinase.";
J. Biol. Chem. 275:14615-14623(2000).
[12]
PHOSPHORYLATION AT TYR-50 AND TYR-409, MUTAGENESIS OF TYR-409, AND
ACTIVITY REGULATION.
PubMed=10934191; DOI=10.1074/jbc.M002022200;
Johnson T.M., Williamson N.A., Scholz G., Jaworowski A.,
Wettenhall R.E., Dunn A.R., Cheng H.C.;
"Modulation of the catalytic activity of the Src family tyrosine
kinase Hck by autophosphorylation at a novel site in the unique
domain.";
J. Biol. Chem. 275:33353-33364(2000).
[13]
FUNCTION IN PHOSPHORYLATION OF WAS, AND INTERACTION WITH WAS.
PubMed=12235133; DOI=10.1074/jbc.M203346200;
Cory G.O., Garg R., Cramer R., Ridley A.J.;
"Phosphorylation of tyrosine 291 enhances the ability of WASp to
stimulate actin polymerization and filopodium formation. Wiskott-
Aldrich Syndrome protein.";
J. Biol. Chem. 277:45115-45121(2002).
[14]
INTERACTION WITH RAPGEF1, AND FUNCTION IN REGULATION OF APOPTOSIS.
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).
[15]
INTERACTION WITH FLT3.
PubMed=16684964; DOI=10.1182/blood-2005-07-008896;
Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S.,
Ronnstrand L.;
"Identification of Y589 and Y599 in the juxtamembrane domain of Flt3
as ligand-induced autophosphorylation sites involved in binding of Src
family kinases and the protein tyrosine phosphatase SHP2.";
Blood 108:1542-1550(2006).
[16]
FUNCTION.
PubMed=16809022; DOI=10.1016/j.cellsig.2006.05.007;
Achuthan A., Elsegood C., Masendycz P., Hamilton J.A., Scholz G.M.;
"CpG DNA enhances macrophage cell spreading by promoting the Src-
family kinase-mediated phosphorylation of paxillin.";
Cell. Signal. 18:2252-2261(2006).
[17]
FUNCTION.
PubMed=17513616; DOI=10.1182/blood-2007-01-066092;
Hong H., Kitaura J., Xiao W., Horejsi V., Ra C., Lowell C.A.,
Kawakami Y., Kawakami T.;
"The Src family kinase Hck regulates mast cell activation by
suppressing an inhibitory Src family kinase Lyn.";
Blood 110:2511-2519(2007).
[18]
FUNCTION.
PubMed=18246197; DOI=10.1172/JCI34013;
Xiao W., Hong H., Kawakami Y., Lowell C.A., Kawakami T.;
"Regulation of myeloproliferation and M2 macrophage programming in
mice by Lyn/Hck, SHIP, and Stat5.";
J. Clin. Invest. 118:924-934(2008).
[19]
FUNCTION.
PubMed=18625913; DOI=10.1189/jlb.0208118;
Paul R., Obermaier B., Van Ziffle J., Angele B., Pfister H.W.,
Lowell C.A., Koedel U.;
"Myeloid Src kinases regulate phagocytosis and oxidative burst in
pneumococcal meningitis by activating NADPH oxidase.";
J. Leukoc. Biol. 84:1141-1150(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-207 AND TYR-520, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[21]
FUNCTION.
PubMed=19897576; DOI=10.1182/blood-2009-04-218735;
Cougoule C., Le Cabec V., Poincloux R., Al Saati T., Mege J.L.,
Tabouret G., Lowell C.A., Laviolette-Malirat N.,
Maridonneau-Parini I.;
"Three-dimensional migration of macrophages requires Hck for podosome
organization and extracellular matrix proteolysis.";
Blood 115:1444-1452(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[23]
FUNCTION IN MYELOID CELL MIGRATION, AND INTERACTION WITH ABL1.
PubMed=19903482; DOI=10.1016/j.febslet.2009.11.009;
Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G.,
Berton G.;
"c-Abl and Src-family kinases cross-talk in regulation of myeloid cell
migration.";
FEBS Lett. 584:15-21(2010).
-!- 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:10547366, ECO:0000269|PubMed:10799548,
ECO:0000269|PubMed:12235133, ECO:0000269|PubMed:14551197,
ECO:0000269|PubMed:16809022, ECO:0000269|PubMed:17513616,
ECO:0000269|PubMed:18246197, ECO:0000269|PubMed:18625913,
ECO:0000269|PubMed:19897576, ECO:0000269|PubMed:19903482,
ECO:0000269|PubMed:8125254, ECO:0000269|PubMed:9400828,
ECO:0000269|PubMed:9916742}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:9916742}.
-!- 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-409 is required for
optimal activity. Phosphorylation at Tyr-520 inhibits kinase
activity. Inhibited by PP1. {ECO:0000269|PubMed:10934191,
ECO:0000269|PubMed:9916742}.
-!- 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 (By similarity). Interacts (via SH2 domain) with
FLT3 (tyrosine phosphorylated). Interacts with CBL. Interacts with
VAV1, WAS and RAPGEF1. Interacts (via SH3 domain) with WDCP (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P08631,
ECO:0000269|PubMed:10799548, ECO:0000269|PubMed:12235133,
ECO:0000269|PubMed:14551197, ECO:0000269|PubMed:16684964,
ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:9400828}.
-!- INTERACTION:
P42768:WAS (xeno); NbExp=3; IntAct=EBI-6248894, EBI-346375;
-!- 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=20% 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=P08103-1; Sequence=Displayed;
Note=Initiates from a CTG codon.;
Name=2; Synonyms=p56-HCK;
IsoId=P08103-2; Sequence=VSP_018859;
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 predominantly in cells of the
myeloid and B-lymphoid lineages.
-!- 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. {ECO:0000269|PubMed:10934191}.
-!- PTM: Ubiquitinated by CBL, leading to its degradation via the
proteasome.
-!- 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}.
-!- DISRUPTION PHENOTYPE: No visible phenotype, but macrophages have
impaired phagocytosis. Mice lacking both HCK and FGR are extremely
sensitive to infections by L.monocytogenes.
{ECO:0000269|PubMed:8125254, ECO:0000269|PubMed:8666673}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAA37305.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=BAE29054.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=BAE29445.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=BAE29787.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=BAE33532.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=BAE38133.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=CAA68544.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
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EMBL; Y00487; CAA68544.1; ALT_SEQ; mRNA.
EMBL; J03023; AAA37305.1; ALT_SEQ; mRNA.
EMBL; AK149736; BAE29054.1; ALT_SEQ; mRNA.
EMBL; AK150290; BAE29445.1; ALT_SEQ; mRNA.
EMBL; AK150709; BAE29787.1; ALT_SEQ; mRNA.
EMBL; AK155975; BAE33532.1; ALT_SEQ; mRNA.
EMBL; AK165315; BAE38133.1; ALT_SEQ; mRNA.
EMBL; BC010478; AAH10478.2; -; mRNA.
CCDS; CCDS38284.1; -. [P08103-1]
CCDS; CCDS50756.1; -. [P08103-2]
PIR; A27282; TVMSHC.
RefSeq; NP_001165588.1; NM_001172117.1. [P08103-2]
RefSeq; NP_034537.2; NM_010407.4. [P08103-1]
UniGene; Mm.715; -.
ProteinModelPortal; P08103; -.
SMR; P08103; -.
BioGrid; 200249; 5.
IntAct; P08103; 5.
MINT; P08103; -.
STRING; 10090.ENSMUSP00000003370; -.
iPTMnet; P08103; -.
PhosphoSitePlus; P08103; -.
SwissPalm; P08103; -.
MaxQB; P08103; -.
PaxDb; P08103; -.
PeptideAtlas; P08103; -.
PRIDE; P08103; -.
Ensembl; ENSMUST00000109799; ENSMUSP00000105423; ENSMUSG00000003283. [P08103-2]
Ensembl; ENSMUST00000189688; ENSMUSP00000141030; ENSMUSG00000003283. [P08103-2]
Ensembl; ENSMUST00000191431; ENSMUSP00000139988; ENSMUSG00000003283. [P08103-1]
GeneID; 15162; -.
KEGG; mmu:15162; -.
UCSC; uc008nhc.3; mouse. [P08103-1]
CTD; 3055; -.
MGI; MGI:96052; Hck.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; P08103; -.
KO; K08893; -.
PhylomeDB; P08103; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-2029481; FCGR activation.
Reactome; R-MMU-912631; Regulation of signaling by CBL.
PRO; PR:P08103; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000003283; Expressed in 144 organ(s), highest expression level in spleen.
CleanEx; MM_HCK; -.
ExpressionAtlas; P08103; baseline and differential.
Genevisible; P08103; MM.
GO; GO:0005901; C:caveola; ISO:MGI.
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; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
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:0001784; F:phosphotyrosine residue binding; ISO:MGI.
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:0050830; P:defense response to Gram-positive bacterium; IGI:MGI.
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:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0006909; P:phagocytosis; IMP:MGI.
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:0051090; P:regulation of DNA-binding transcription factor activity; ISO:MGI.
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_0000024435.
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:0000269|PubMed:10934191}.
MOD_RES 200 200 Phosphothreonine.
{ECO:0000250|UniProtKB:P08631}.
MOD_RES 207 207 Phosphotyrosine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 409 409 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10934191}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000250|UniProtKB:P08631}.
MOD_RES 520 520 Phosphotyrosine.
{ECO:0000244|PubMed:19144319}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
VAR_SEQ 1 21 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_018859.
MUTAGEN 409 409 Y->F: Reduced autophosphorylation.
{ECO:0000269|PubMed:10934191}.
SEQUENCE 524 AA; 59129 MW; DF72FD69B38C9706 CRC64;
MGGRSSCEDP GCPRSEGRAP RMGCVKSRFL RDGSKASKTE PSANQKGPVY VPDPTSSSKL
GPNNSNSMPP GFVEGSEDTI VVALYDYEAI HREDLSFQKG DQMVVLEEAG EWWKARSLAT
KKEGYIPSNY VARVNSLETE EWFFKGISRK DAERHLLAPG NMLGSFMIRD SETTKGSYSL
SVRDFDPQHG DTVKHYKIRT LDSGGFYISP RSTFSSLQEL VLHYKKGKDG LCQKLSVPCV
SPKPQKPWEK DAWEIPRESL QMEKKLGAGQ FGEVWMATYN KHTKVAVKTM KPGSMSVEAF
LAEANLMKSL QHDKLVKLHA VVSQEPIFIV TEFMAKGSLL DFLKSEEGSK QPLPKLIDFS
AQISEGMAFI EQRNYIHRDL RAANILVSAS LVCKIADFGL ARIIEDNEYT AREGAKFPIK
WTAPEAINFG SFTIKSDVWS FGILLMEIVT YGRIPYPGMS NPEVIRALEH GYRMPRPDNC
PEELYNIMIR CWKNRPEERP TFEYIQSVLD DFYTATESQY QQQP


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