HCK

For the ice hockey team, see HC Keski-Uusimaa.

HCK

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1AD5, 1BU1, 1QCF, 2C0I, 2C0O, 2C0T, 2HCK, 2HK5, 2OI3, 2OJ2, 3HCK, 3NHN, 3RBB, 3REA, 3REB, 3VRY, 3VRZ, 3VS0, 3VS1, 3VS2, 3VS3, 3VS4, 3VS5, 3VS6, 3VS7, 4HCK, 4LUD, 4LUE, 4ORZ, 4U5W, 5HCK

Identifiers

Aliases

HCK, JTK9, p59Hck, p61Hck, HCK proto-oncogene, Src family tyrosine kinase

External IDs

MGI: 96052 HomoloGene: 20489 GeneCards: HCK

Gene ontology
Molecular function	• transferase activity • nucleotide binding • protein kinase activity • non-membrane spanning protein tyrosine kinase activity • kinase activity • protein binding • receptor binding • ATP binding • protein tyrosine kinase activity
Cellular component	• cytoplasm • cytosol • Golgi apparatus • cell projection • membrane • focal adhesion • extrinsic component of cytoplasmic side of plasma membrane • plasma membrane • transport vesicle • cytoplasmic, membrane-bounded vesicle • cell junction • actin filament • caveola • lysosome • cytoskeleton • cytoplasmic vesicle • nucleus
Biological process	• cell differentiation • leukocyte migration involved in immune response • positive regulation of actin filament polymerization • Fc-gamma receptor signaling pathway involved in phagocytosis • phosphorylation • transmembrane receptor protein tyrosine kinase signaling pathway • cytokine-mediated signaling pathway • interferon-gamma-mediated signaling pathway • immune system process • leukocyte degranulation • negative regulation of apoptotic process • regulation of defense response to virus by virus • protein phosphorylation • cell adhesion • respiratory burst after phagocytosis • regulation of sequence-specific DNA binding transcription factor activity • positive regulation of cell proliferation • regulation of inflammatory response • regulation of cell shape • regulation of podosome assembly • peptidyl-tyrosine autophosphorylation • phagocytosis • integrin-mediated signaling pathway • protein autophosphorylation • peptidyl-tyrosine phosphorylation • regulation of phagocytosis • mesoderm development • inflammatory response • innate immune response-activating signal transduction • positive regulation of actin cytoskeleton reorganization • lipopolysaccharide-mediated signaling pathway • exocytosis • viral process • innate immune response
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


3055


15162

Ensembl


ENSG00000101336


ENSMUSG00000003283

UniProt


P08631


P08103

RefSeq (mRNA)

NM_002110 NM_001172129 NM_001172130 NM_001172131 NM_001172132
NM_001172133


NM_001172117 NM_010407

RefSeq (protein)


NP_001165600.1 NP_001165601.1 NP_001165602.1 NP_001165604.1 NP_002101.2


NP_001165588.1 NP_034537.2

Location (UCSC)

Chr 20: 32.05 – 32.1 Mb

Chr 2: 153.11 – 153.15 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Tyrosine-protein kinase HCK is an enzyme that in humans is encoded by the HCK gene.^[3]

Function

The protein encoded by this gene is a protein-tyrosine kinase that is predominantly expressed in hemopoietic cell types, and belongs to the Src family of tyrosine kinases. The encoded protein may help couple the Fc receptor to the activation of the respiratory burst. In addition, it may play a role in neutrophil migration and in the degranulation of neutrophils. Alternate translation initiation site usage, including a non-AUG (CUG) codon, results in the production of two different isoforms, that have different subcellular localization.^[4]

Interactions

HCK has been shown to interact with:

ADAM15^[5]
BCR gene,^[6]^[7]
Cbl gene,^[8]^[9]
ELMO1,^[10]
Granulocyte colony-stimulating factor receptor,^[11]
RAPGEF1,^[12]
RAS p21 protein activator 1,^[13] and
RASA3.^[13]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Quintrell N, Lebo R, Varmus H, Bishop JM, Pettenati MJ, Le Beau MM, Diaz MO, Rowley JD (August 1987). "Identification of a human gene (HCK) that encodes a protein-tyrosine kinase and is expressed in hemopoietic cells". Mol Cell Biol. 7 (6): 2267–75. PMC 365351. PMID 3496523.
↑ "Entrez Gene: HCK hemopoietic cell kinase".
↑ Poghosyan Z, Robbins SM, Houslay MD, Webster A, Murphy G, Edwards DR (Feb 2002). "Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases". The Journal of Biological Chemistry. 277 (7): 4999–5007. doi:10.1074/jbc.M107430200. PMID 11741929.
↑ Stanglmaier M, Warmuth M, Kleinlein I, Reis S, Hallek M (Feb 2003). "The interaction of the Bcr-Abl tyrosine kinase with the Src kinase Hck is mediated by multiple binding domains". Leukemia. 17 (2): 283–9. doi:10.1038/sj.leu.2402778. PMID 12592324.
↑ Lionberger JM, Wilson MB, Smithgall TE (Jun 2000). "Transformation of myeloid leukemia cells to cytokine independence by Bcr-Abl is suppressed by kinase-defective Hck". The Journal of Biological Chemistry. 275 (24): 18581–5. doi:10.1074/jbc.C000126200. PMID 10849448.
↑ Howlett CJ, Robbins SM (Mar 2002). "Membrane-anchored Cbl suppresses Hck protein-tyrosine kinase mediated cellular transformation". Oncogene. 21 (11): 1707–16. doi:10.1038/sj.onc.1205228. PMID 11896602.
↑ Howlett CJ, Bisson SA, Resek ME, Tigley AW, Robbins SM (Apr 1999). "The proto-oncogene p120(Cbl) is a downstream substrate of the Hck protein-tyrosine kinase". Biochemical and Biophysical Research Communications. 257 (1): 129–38. doi:10.1006/bbrc.1999.0427. PMID 10092522.
↑ Scott MP, Zappacosta F, Kim EY, Annan RS, Miller WT (Aug 2002). "Identification of novel SH3 domain ligands for the Src family kinase Hck. Wiskott-Aldrich syndrome protein (WASP), WASP-interacting protein (WIP), and ELMO1". The Journal of Biological Chemistry. 277 (31): 28238–46. doi:10.1074/jbc.M202783200. PMID 12029088.
↑ Ward AC, Monkhouse JL, Csar XF, Touw IP, Bello PA (Oct 1998). "The Src-like tyrosine kinase Hck is activated by granulocyte colony-stimulating factor (G-CSF) and docks to the activated G-CSF receptor". Biochemical and Biophysical Research Communications. 251 (1): 117–23. doi:10.1006/bbrc.1998.9441. PMID 9790917.
↑ Shivakrupa R, Radha V, Sudhakar C, Swarup G (Dec 2003). "Physical and functional interaction between Hck tyrosine kinase and guanine nucleotide exchange factor C3G results in apoptosis, which is independent of C3G catalytic domain". The Journal of Biological Chemistry. 278 (52): 52188–94. doi:10.1074/jbc.M310656200. PMID 14551197.
1 2 Briggs SD, Bryant SS, Jove R, Sanderson SD, Smithgall TE (Jun 1995). "The Ras GTPase-activating protein (GAP) is an SH3 domain-binding protein and substrate for the Src-related tyrosine kinase, Hck". The Journal of Biological Chemistry. 270 (24): 14718–24. doi:10.1074/jbc.270.24.14718. PMID 7782336.

Geyer M, Fackler OT, Peterlin BM (2001). "Structure--function relationships in HIV-1 Nef.". EMBO Rep. 2 (7): 580–5. doi:10.1093/embo-reports/kve141. PMC 1083955. PMID 11463741.
Lake JA, Carr J, Feng F, Mundy L, Burrell C, Li P (2003). "The role of Vif during HIV-1 infection: interaction with novel host cellular factors.". J. Clin. Virol. 26 (2): 143–52. doi:10.1016/S1386-6532(02)00113-0. PMID 12600646.
Greenway AL, Holloway G, McPhee DA, Ellis P, Cornall A, Lidman M (2004). "HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication.". J. Biosci. 28 (3): 323–35. doi:10.1007/BF02970151. PMID 12734410.
Tolstrup M, Ostergaard L, Laursen AL, Pedersen SF, Duch M (2004). "HIV/SIV escape from immune surveillance: focus on Nef.". Curr. HIV Res. 2 (2): 141–51. doi:10.2174/1570162043484924. PMID 15078178.
Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection.". Curr. HIV Res. 3 (1): 87–94. doi:10.2174/1570162052773013. PMID 15638726.
Stove V, Verhasselt B (2006). "Modelling thymic HIV-1 Nef effects.". Curr. HIV Res. 4 (1): 57–64. doi:10.2174/157016206775197583. PMID 16454711.
Lichtenberg U, Quintrell N, Bishop JM (1992). "Human protein-tyrosine kinase gene HCK: expression and structural analysis of the promoter region.". Oncogene. 7 (5): 849–58. PMID 1373873.
Hradetzky D, Strebhardt K, Rübsamen-Waigmann H (1992). "The genomic locus of the human hemopoietic-specific cell protein tyrosine kinase (PTK)-encoding gene (HCK) confirms conservation of exon-intron structure among human PTKs of the src family.". Gene. 113 (2): 275–80. doi:10.1016/0378-1119(92)90407-G. PMID 1572549.
Kim JW, Sim SS, Kim UH, Nishibe S, Wahl MI, Carpenter G, Rhee SG (1990). "Tyrosine residues in bovine phospholipase C-gamma phosphorylated by the epidermal growth factor receptor in vitro.". J. Biol. Chem. 265 (7): 3940–3. PMID 1689310.
Holtrich U, Bräuninger A, Strebhardt K, Rübsamen-Waigmann H (1992). "Two additional protein-tyrosine kinases expressed in human lung: fourth member of the fibroblast growth factor receptor family and an intracellular protein-tyrosine kinase.". Proc. Natl. Acad. Sci. U.S.A. 88 (23): 10411–5. doi:10.1073/pnas.88.23.10411. PMC 52938. PMID 1720539.
Lock P, Ralph S, Stanley E, Boulet I, Ramsay R, Dunn AR (1991). "Two isoforms of murine hck, generated by utilization of alternative translational initiation codons, exhibit different patterns of subcellular localization.". Mol. Cell. Biol. 11 (9): 4363–70. PMC 361298. PMID 1875927.
Ziegler SF, Marth JD, Lewis DB, Perlmutter RM (1987). "Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells of hematopoietic origin.". Mol. Cell. Biol. 7 (6): 2276–85. PMC 365352. PMID 3453117.
Lee CH, Leung B, Lemmon MA, Zheng J, Cowburn D, Kuriyan J, Saksela K (1995). "A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein.". EMBO J. 14 (20): 5006–15. PMC 394604. PMID 7588629.
Liao F, Shin HS, Rhee SG (1993). "In vitro tyrosine phosphorylation of PLC-gamma 1 and PLC-gamma 2 by src-family protein tyrosine kinases.". Biochem. Biophys. Res. Commun. 191 (3): 1028–33. doi:10.1006/bbrc.1993.1320. PMID 7682059.
Briggs SD, Bryant SS, Jove R, Sanderson SD, Smithgall TE (1995). "The Ras GTPase-activating protein (GAP) is an SH3 domain-binding protein and substrate for the Src-related tyrosine kinase, Hck.". J. Biol. Chem. 270 (24): 14718–24. doi:10.1074/jbc.270.24.14718. PMID 7782336.
Robbins SM, Quintrell NA, Bishop JM (1995). "Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae.". Mol. Cell. Biol. 15 (7): 3507–15. PMC 230587. PMID 7791757.
Saksela K, Cheng G, Baltimore D (1995). "Proline-rich (PxxP) motifs in HIV-1 Nef bind to SH3 domains of a subset of Src kinases and are required for the enhanced growth of Nef+ viruses but not for down-regulation of CD4.". EMBO J. 14 (3): 484–91. PMC 398106. PMID 7859737.
Cheng G, Ye ZS, Baltimore D (1994). "Binding of Bruton's tyrosine kinase to Fyn, Lyn, or Hck through a Src homology 3 domain-mediated interaction.". Proc. Natl. Acad. Sci. U.S.A. 91 (17): 8152–5. doi:10.1073/pnas.91.17.8152. PMC 44563. PMID 8058772.
Wang AV, Scholl PR, Geha RS (1994). "Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn.". J. Exp. Med. 180 (3): 1165–70. doi:10.1084/jem.180.3.1165. PMC 2191633. PMID 8064233.

PDB gallery

1ad5: SRC FAMILY KINASE HCK-AMP-PNP COMPLEX

1bu1: SRC FAMILY KINASE HCK SH3 DOMAIN

1qcf: CRYSTAL STRUCTURE OF HCK IN COMPLEX WITH A SRC FAMILY-SELECTIVE TYROSINE KINASE INHIBITOR

2c0i: SRC FAMILY KINASE HCK WITH BOUND INHIBITOR A-420983

2c0o: SRC FAMILY KINASE HCK WITH BOUND INHIBITOR A-770041

2c0t: SRC FAMILY KINASE HCK WITH BOUND INHIBITOR A-641359

2hck: SRC FAMILY KINASE HCK-QUERCETIN COMPLEX

2hk5: Hck Kinase in Complex with Lck targetted Inhibitor PG-1009247

2oi3: NMR Structure Analysis of the Hematopoetic Cell Kinase SH3 Domain complexed with an artificial high affinity ligand (PD1)

2oj2: NMR Structure Analysis of the Hematopoetic Cell Kinase SH3 Domain complexed with an artificial high affinity ligand (PD1)

3hck: NMR ensemble of the uncomplexed human HCK SH2 domain, 20 structures

4hck: HUMAN HCK SH3 DOMAIN, NMR, 25 STRUCTURES

5hck: HUMAN HCK SH3 DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE

Protein kinases: tyrosine kinases (EC 2.7.10)

Receptor tyrosine kinases (EC 2.7.10.1)

Growth factor receptors

EGF receptor family	EGFR ERBB2 ERBB3 ERBB4

Insulin receptor family	IGF1R INSR INSRR

PDGF receptor family	CSF1R FLT3 KIT PDGFR (PDGFRA PDGFRB)

FGF receptor family	FGFR1 FGFR2 FGFR3 FGFR4

VEGF receptors family	VEGFR1 VEGFR2 VEGFR3

HGF receptor family	MET RON

Trk receptor family	NTRK1 NTRK2 NTRK3

EPH receptor family

LTK receptor family

TIE receptor family

ROR receptor family

ROR1
ROR2

DDR receptor family

DDR1
DDR2

PTK7 receptor family

PTK7

RYK receptor family

MuSK receptor family

MUSK

ROS receptor family

ROS1

AATYK receptor family

AATYK
AATYK2

AXL receptor family

RET receptor family

uncategorised

STYK1

Non-receptor tyrosine kinases (EC 2.7.10.2)

ABL family	ABL1 ARG

ACK family	ACK1 TNK1

CSK family	CSK MATK

FAK family	FAK PYK2

FES family	FES FER

FRK family	FRK BRK SRMS

JAK family	JAK1 JAK2 JAK3 TYK2

SRC-A family	SRC FGR FYN YES1

SRC-B family	BLK HCK LCK LYN

TEC family	TEC BMX BTK ITK TXK

SYK family	SYK ZAP70

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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HCK

Function

Interactions

References

Further reading