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P08631 (HCK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 194. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase HCK

EC=2.7.10.2
Alternative name(s):
Hematopoietic cell kinase
Hemopoietic cell kinase
p59-HCK/p60-HCK
p59Hck
p61Hck
Gene names
Name:HCK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.9 Ref.11 Ref.13 Ref.16 Ref.17 Ref.18 Ref.20 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.31 Ref.32 Ref.34 Ref.37 Ref.38 Ref.40

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.9 Ref.10 Ref.11 Ref.14 Ref.17 Ref.18 Ref.29 Ref.49

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-411 is required for optimal activity. Phosphorylation at Tyr-522 inhibits kinase activity. Inhibited by PP1 and A-770041. Ref.11 Ref.13 Ref.15 Ref.18 Ref.19 Ref.20 Ref.30 Ref.46 Ref.49

Subunit structure

Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with VAV1, WAS and RAPGEF1 By similarity. Interacts (via SH3 domain) with HIV-1 Nef and Vif. This interaction stimulates its tyrosine-kinase activity. Interacts (via SH3 domain) with HEV ORF3 protein. Interacts with ARRB1 and ARRB2. Interacts with ADAM15. Interacts with FASLG. Interacts with CBL. 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. Ref.9 Ref.10 Ref.13 Ref.15 Ref.16 Ref.17 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.28 Ref.30 Ref.31 Ref.32 Ref.33 Ref.35 Ref.37 Ref.50 Ref.51

Subcellular location

Isoform 1: Lysosome. Membrane; Lipid-anchor. Cell projectionpodosome membrane; Lipid-anchor. Cytoplasmcytosol. Note: Associated with specialized secretory lysosomes called azurophil granules. At least half of this isoform isfound in the cytoplasm, some of this fraction is myristoylated. Ref.12 Ref.14 Ref.25 Ref.26 Ref.29 Ref.31

Isoform 2: Cell membrane; Lipid-anchor. Membranecaveola; Lipid-anchor. Cell junctionfocal adhesion. Cytoplasmcytoskeleton. Golgi apparatus. Cytoplasmic vesicle. Lysosome. Nucleus. Note: 20% of this isoform isassociated with caveolae. Localization at the cell membrane and at caveolae requires palmitoylation at Cys-3. Colocalizes with the actin cytoskeleton at focal adhesions. Ref.12 Ref.14 Ref.25 Ref.26 Ref.29 Ref.31

Cytoplasmic vesiclesecretory vesicle. Cytoplasmcytosol Ref.12 Ref.14 Ref.25 Ref.26 Ref.29 Ref.31.

Tissue specificity

Detected in monocytes and neutrophils (at protein level). Expressed predominantly in cells of the myeloid and B-lymphoid lineages. Highly expressed in granulocytes. Detected in tonsil. Ref.2 Ref.10 Ref.14

Induction

Up-regulated during myeloid cell differentiation. The highest levels are detected in fully differentiated phagocytes. Up-regulated by IL2. Ref.11 Ref.13 Ref.14 Ref.15 Ref.18 Ref.19 Ref.20 Ref.30 Ref.46 Ref.49

Domain

The SH3 domain mediates binding to HIV-1 Nef.

Post-translational modification

Phosphorylated on several tyrosine residues. Autophosphorylated. Becomes rapidly phosphorylated upon activation of the immunoglobulin receptors FCGR1A and FCGR2A. Phosphorylation by the BCR-ABL fusion protein mediates activation of HCK. Phosphorylation at Tyr-411 increases kinase activity. Phosphorylation at Tyr-522 inhibits kinase activity. Kinase activity is not required for phosphorylation at Tyr-522, suggesting that this site is a target of other kinases. Ref.10 Ref.11 Ref.13 Ref.17 Ref.18 Ref.19 Ref.23 Ref.26 Ref.42 Ref.45 Ref.46

Ubiquitinated by CBL, leading to its degradation via the proteasome. Ref.26

Isoform 2 palmitoylation at position 2 requires prior myristoylation. Palmitoylation at position 3 is required for caveolar localization of isoform 2. Ref.12

Involvement in disease

Aberrant activation of HCK by HIV-1 protein Nef enhances HIV-1 replication and contributes to HIV-1 pathogenicity. Ref.34 Ref.38

Aberrant activation of HCK, e.g. by the BCR-ABL fusion protein, promotes cancer cell proliferation. Ref.34 Ref.38

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Sequence caution

The sequence AAA52643.1 differs from that shown. Reason: Frameshift at position 20.

The sequence BAF82585.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processExocytosis
Host-virus interaction
Immunity
Inflammatory response
Innate immunity
Phagocytosis
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Golgi apparatus
Lysosome
Membrane
Nucleus
   Coding sequence diversityAlternative initiation
Alternative splicing
Polymorphism
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMLipoprotein
Myristate
Palmitate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

cell adhesion

Traceable author statement Ref.39. Source: UniProtKB

cytokine-mediated signaling pathway

Traceable author statement Ref.39. Source: UniProtKB

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Traceable author statement. Source: Reactome

innate immune response-activating signal transduction

Traceable author statement Ref.39. Source: UniProtKB

integrin-mediated signaling pathway

Traceable author statement Ref.39. Source: UniProtKB

interferon-gamma-mediated signaling pathway

Traceable author statement Ref.39. Source: UniProtKB

leukocyte degranulation

Traceable author statement Ref.39. Source: UniProtKB

leukocyte migration involved in immune response

Traceable author statement Ref.39. Source: UniProtKB

lipopolysaccharide-mediated signaling pathway

Traceable author statement Ref.39. Source: UniProtKB

mesoderm development

Traceable author statement Ref.2. Source: ProtInc

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.31. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype Ref.17. Source: UniProtKB

positive regulation of actin cytoskeleton reorganization

Inferred from direct assay Ref.29. Source: UniProtKB

positive regulation of actin filament polymerization

Traceable author statement Ref.39. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype Ref.17. Source: UniProtKB

protein autophosphorylation

Inferred from mutant phenotype Ref.17. Source: UniProtKB

protein phosphorylation

Traceable author statement Ref.1. Source: ProtInc

regulation of cell shape

Inferred from mutant phenotype Ref.17Ref.25. Source: UniProtKB

regulation of defense response to virus by virus

Traceable author statement. Source: Reactome

regulation of inflammatory response

Traceable author statement Ref.39. Source: UniProtKB

regulation of phagocytosis

Inferred from mutant phenotype Ref.25. Source: UniProtKB

regulation of podosome assembly

Inferred from direct assay Ref.29. Source: UniProtKB

regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype Ref.31. Source: UniProtKB

respiratory burst after phagocytosis

Traceable author statement Ref.39. Source: UniProtKB

viral process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

caveola

Inferred from direct assay Ref.12. Source: UniProtKB

cell projection

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

extrinsic component of cytoplasmic side of plasma membrane

Inferred from mutant phenotype Ref.25. Source: UniProtKB

focal adhesion

Inferred from mutant phenotype Ref.25. Source: UniProtKB

lysosome

Inferred from direct assay Ref.29. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

transport vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction PubMed 12029088PubMed 7859737. Source: UniProtKB

protein tyrosine kinase activity

Inferred from mutant phenotype Ref.17. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform 1 (identifier: P08631-1)

Also known as: p60-HCK; p61Hck;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Initiates from a CTG codon.
Isoform 2 (identifier: P08631-2)

Also known as: p59-HCK; p59Hck;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
Note: Initiator Met-1 is removed. Contains a N-myristoyl glycine at position 2. S-palmitoylated at Cys-3.
Isoform 3 (identifier: P08631-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
     76-76: Missing.
Isoform 4 (identifier: P08631-4)

The sequence of this isoform differs from the canonical sequence as follows:
     76-76: Missing.
Note: Initiates from a CTG codon.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 526525Tyrosine-protein kinase HCK
PRO_0000024433

Regions

Domain78 – 13861SH3
Domain144 – 24198SH2
Domain262 – 515254Protein kinase
Nucleotide binding268 – 2769ATP

Sites

Active site3811Proton acceptor
Binding site2901ATP

Amino acid modifications

Modified residue511Phosphotyrosine; by autocatalysis Ref.26
Modified residue2021Phosphothreonine Ref.36
Modified residue2091Phosphotyrosine By similarity
Modified residue4111Phosphotyrosine; by autocatalysis Ref.19 Ref.26
Modified residue4621Phosphoserine Ref.36
Modified residue5221Phosphotyrosine Ref.19 Ref.26 Ref.42 Ref.45 Ref.46
Lipidation21N-myristoyl glycine Ref.12

Natural variations

Alternative sequence1 – 2121Missing in isoform 2 and isoform 3.
VSP_018858
Alternative sequence761Missing in isoform 3 and isoform 4.
VSP_041926
Natural variant441A → T. Ref.52
Corresponds to variant rs56029200 [ dbSNP | Ensembl ].
VAR_041707
Natural variant1051M → L. Ref.3 Ref.52
Corresponds to variant rs55722810 [ dbSNP | Ensembl ].
VAR_041708
Natural variant3991D → G in an ovarian mucinous carcinoma sample; somatic mutation. Ref.52
VAR_041709
Natural variant5021P → Q.
Corresponds to variant rs17093828 [ dbSNP | Ensembl ].
VAR_033836

Experimental info

Mutagenesis31G → C: Slight palmitoylation, cytoplasmic and caveolar localization; in isoform 1;. Ref.12 Ref.25
Mutagenesis31G → S: Abolishes palmitoylation and localization at the cell membrane. Ref.12 Ref.25
Mutagenesis231G → A: Myristoylation and palmitoylation are abolished, leading to entirely cytoplasmic localization; in isoform 2. Ref.12
Mutagenesis241C → S: Palmitoylation is abolished, some cytoplasmic and no calveolar localization; in isoform 2. Ref.12
Mutagenesis2901K → E: Loss of kinase activity. Ref.26
Mutagenesis3051E → A: Loss of kinase activity. Ref.19
Mutagenesis3811D → E: Loss of kinase activity. Ref.29
Mutagenesis4111Y → A: Reduced catalytic activity and higher affinity for target peptides. Ref.19
Mutagenesis5221Y → F: Constitutively activated kinase, leading to cellular transformation. Ref.17 Ref.26
Sequence conflict241C → S in AAA52643. Ref.1
Sequence conflict691N → D in BAF82585. Ref.3
Sequence conflict1441W → R in BAB15482. Ref.3
Sequence conflict1681F → Y in BAF82585. Ref.3
Sequence conflict3781I → T in AAI13855. Ref.6
Sequence conflict4881N → S in BAF82585. Ref.3

Secondary structure

................................................................................................ 526
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (p60-HCK) (p61Hck) [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 847E877A0A641725

FASTA52659,600
        10         20         30         40         50         60 
MGGRSSCEDP GCPRDEERAP RMGCMKSKFL QVGGNTFSKT ETSASPHCPV YVPDPTSTIK 

        70         80         90        100        110        120 
PGPNSHNSNT PGIREAGSED IIVVALYDYE AIHHEDLSFQ KGDQMVVLEE SGEWWKARSL 

       130        140        150        160        170        180 
ATRKEGYIPS NYVARVDSLE TEEWFFKGIS RKDAERQLLA PGNMLGSFMI RDSETTKGSY 

       190        200        210        220        230        240 
SLSVRDYDPR QGDTVKHYKI RTLDNGGFYI SPRSTFSTLQ ELVDHYKKGN DGLCQKLSVP 

       250        260        270        280        290        300 
CMSSKPQKPW EKDAWEIPRE SLKLEKKLGA GQFGEVWMAT YNKHTKVAVK TMKPGSMSVE 

       310        320        330        340        350        360 
AFLAEANVMK TLQHDKLVKL HAVVTKEPIY IITEFMAKGS LLDFLKSDEG SKQPLPKLID 

       370        380        390        400        410        420 
FSAQIAEGMA FIEQRNYIHR DLRAANILVS ASLVCKIADF GLARVIEDNE YTAREGAKFP 

       430        440        450        460        470        480 
IKWTAPEAIN FGSFTIKSDV WSFGILLMEI VTYGRIPYPG MSNPEVIRAL ERGYRMPRPE 

       490        500        510        520 
NCPEELYNIM MRCWKNRPEE RPTFEYIQSV LDDFYTATES QYQQQP 

« Hide

Isoform 2 (p59-HCK) (p59Hck) [UniParc].

Checksum: 4F1EC1E8F3EDF9CA
Show »

FASTA50557,312
Isoform 3 [UniParc].

Checksum: C07FF5B8D3C1B862
Show »

FASTA50457,241
Isoform 4 [UniParc].

Checksum: 803967415A2F57FC
Show »

FASTA52559,529

References

« Hide 'large scale' references
[1]"Identification of a human gene (HCK) that encodes a protein-tyrosine kinase and is expressed in hemopoietic cells."
Quintrell N., Lebo R., Varmus H., Bishop J.M., Pettenati M.J., le Beau M.M., Diaz M.O., Rowley J.D.
Mol. Cell. Biol. 7:2267-2275(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells of hematopoietic origin."
Ziegler S.F., Marth J.D., Lewis D.B., Perlmutter R.M.
Mol. Cell. Biol. 7:2276-2285(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), VARIANT LEU-105.
Tissue: Corpus callosum and Ileal mucosa.
[4]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: B-cell and Lymph.
[7]"Two isoforms of murine hck, generated by utilization of alternative translational initiation codons, exhibit different patterns of subcellular localization."
Lock P., Ralph S., Stanley E., Boulet I., Ramsay R., Dunn A.R.
Mol. Cell. Biol. 11:4363-4370(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-21 (ISOFORM 1), ALTERNATIVE INITIATION.
Tissue: Bone marrow.
[8]"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."
Hradetzky D., Strebhardt K., Ruesamen-Waigmann H.
Gene 113:275-280(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 178-526.
Tissue: Spleen.
[9]"Physical and functional association of Src-related protein tyrosine kinases with Fc gamma RII in monocytic THP-1 cells."
Ghazizadeh S., Bolen J.B., Fleit H.B.
J. Biol. Chem. 269:8878-8884(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCGR2A, CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF FCGR2A.
[10]"Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn."
Wang A.V., Scholl P.R., Geha R.S.
J. Exp. Med. 180:1165-1170(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCGR1A, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, PHOSPHORYLATION.
[11]"The Fc gamma RI receptor signals through the activation of hck and MAP kinase."
Durden D.L., Kim H.M., Calore B., Liu Y.
J. Immunol. 154:4039-4047(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN FCGR1A SIGNALING, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION.
[12]"Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae."
Robbins S.M., Quintrell N.A., Bishop J.M.
Mol. Cell. Biol. 15:3507-3515(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, ALTERNATIVE INITIATION, MYRISTOYLATION AT GLY-2, PALMITOYLATION, MUTAGENESIS OF GLY-3; GLY-23 AND CYS-24.
[13]"Signal transduction of interleukin-6 involves tyrosine phosphorylation of multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck, and Lyn in multiple myeloma cell lines."
Hallek M., Neumann C., Schaffer M., Danhauser-Riedl S., von Bubnoff N., de Vos G., Druker B.J., Yasukawa K., Griffin J.D., Emmerich B.
Exp. Hematol. 25:1367-1377(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION, INTERACTION WITH IL6ST.
[14]"Hck is activated by opsonized zymosan and A23187 in distinct subcellular fractions of human granulocytes."
Welch H., Maridonneau-Parini I.
J. Biol. Chem. 272:102-109(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[15]"SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1."
Briggs S.D., Sharkey M., Stevenson M., Smithgall T.E.
J. Biol. Chem. 272:17899-17902(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, INTERACTION WITH HIV-1 NEF.
[16]"The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr."
Warmuth M., Bergmann M., Priess A., Hauslmann K., Emmerich B., Hallek M.
J. Biol. Chem. 272:33260-33270(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF BCR, INTERACTION WITH BCR-ABL.
[17]"The proto-oncogene p120(Cbl) is a downstream substrate of the Hck protein-tyrosine kinase."
Howlett C.J., Bisson S.A., Resek M.E., Tigley A.W., Robbins S.M.
Biochem. Biophys. Res. Commun. 257:129-138(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CBL PHOSPHORYLATION; CELL PROLIFERATION AND REGULATION OF CELL SHAPE, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-522, INTERACTION WITH CBL.
[18]"IL-2 signaling in human monocytes involves the phosphorylation and activation of p59hck."
Bosco M.C., Curiel R.E., Zea A.H., Malabarba M.G., Ortaldo J.R., Espinoza-Delgado I.
J. Immunol. 164:4575-4585(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN IL2 SIGNALING, CATALYTIC ACTIVITY, INDUCTION, ENZYME REGULATION, PHOSPHORYLATION.
[19]"Reciprocal regulation of Hck activity by phosphorylation of Tyr(527) and Tyr(416). Effect of introducing a high affinity intramolecular SH2 ligand."
Porter M., Schindler T., Kuriyan J., Miller W.T.
J. Biol. Chem. 275:2721-2726(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-411 AND TYR-522, IDENTIFICATION BY MASS SPECTROMETRY, ENZYME REGULATION, MUTAGENESIS OF GLU-305 AND TYR-411.
[20]"Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI."
Barlic J., Andrews J.D., Kelvin A.A., Bosinger S.E., DeVries M.E., Xu L., Dobransky T., Feldman R.D., Ferguson S.S., Kelvin D.J.
Nat. Immunol. 1:227-233(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN IL8-MEDIATED DEGRANULATION, ENZYME REGULATION, INTERACTION WITH ARRB1 AND ARRB2.
[21]"The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif protein."
Hassaine G., Courcoul M., Bessou G., Barthalay Y., Picard C., Olive D., Collette Y., Vigne R., Decroly E.
J. Biol. Chem. 276:16885-16893(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 VIF.
[22]"The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK."
Korkaya H., Jameel S., Gupta D., Tyagi S., Kumar R., Zafrullah M., Mazumdar M., Lal S.K., Xiaofang L., Sehgal D., Das S.R., Sahal D.
J. Biol. Chem. 276:42389-42400(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HEV ORF3 PROTEIN.
[23]"The Src family kinase Hck couples BCR/ABL to STAT5 activation in myeloid leukemia cells."
Klejman A., Schreiner S.J., Nieborowska-Skorska M., Slupianek A., Wilson M., Smithgall T.E., Skorski T.
EMBO J. 21:5766-5774(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS EFFECTOR OF THE BCR-ABL FUSION PROTEIN IN PHOSPHORYLATION OF STAT5B, INTERACTION WITH STAT5B AND THE BCR-ABL FUSION PROTEIN, PHOSPHORYLATION.
[24]"Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases."
Poghosyan Z., Robbins S.M., Houslay M.D., Webster A., Murphy G., Edwards D.R.
J. Biol. Chem. 277:4999-5007(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADAM15, FUNCTION IN PHOSPHORYLATION OF ADAM15.
[25]"p59Hck isoform induces F-actin reorganization to form protrusions of the plasma membrane in a Cdc42- and Rac-dependent manner."
Carreno S., Caron E., Cougoule C., Emorine L.J., Maridonneau-Parini I.
J. Biol. Chem. 277:21007-21016(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN REORGANIZATION OF THE ACTIN CYTOSKELETON; FORMATION OF CELL PROTRUSIONS AND PHAGOCYTOSIS (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), MUTAGENESIS OF GLY-3.
[26]"Membrane-anchored Cbl suppresses Hck protein-tyrosine kinase mediated cellular transformation."
Howlett C.J., Robbins S.M.
Oncogene 21:1707-1716(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION, UBIQUITINATION, PHOSPHORYLATION AT TYR-51; TYR-411 AND TYR-522, SUBCELLULAR LOCATION, INTERACTION WITH CBL (ISOFORM 2), MUTAGENESIS OF LYS-290 AND TYR-522.
[27]"Critical role for hematopoietic cell kinase (Hck)-mediated phosphorylation of Gab1 and Gab2 docking proteins in interleukin 6-induced proliferation and survival of multiple myeloma cells."
Podar K., Mostoslavsky G., Sattler M., Tai Y.T., Hayashi T., Catley L.P., Hideshima T., Mulligan R.C., Chauhan D., Anderson K.C.
J. Biol. Chem. 279:21658-21665(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN IL6 SIGNALING CASCADE AND IN PHOSPHORYLATION OF GAB1 AND GAB2.
[28]"Identification of tyrosine residues on ELMO1 that are phosphorylated by the Src-family kinase Hck."
Yokoyama N., deBakker C.D., Zappacosta F., Huddleston M.J., Annan R.S., Ravichandran K.S., Miller W.T.
Biochemistry 44:8841-8849(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF ELMO1, INTERACTION WITH ELMO1.
[29]"Activation of the lysosome-associated p61Hck isoform triggers the biogenesis of podosomes."
Cougoule C., Carreno S., Castandet J., Labrousse A., Astarie-Dequeker C., Poincloux R., Le Cabec V., Maridonneau-Parini I.
Traffic 6:682-694(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-381.
[30]"HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src through direct SH3 domain interaction."
Trible R.P., Emert-Sedlak L., Smithgall T.E.
J. Biol. Chem. 281:27029-27038(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 NEF, ENZYME REGULATION.
[31]"Regulation of p73 by Hck through kinase-dependent and independent mechanisms."
Paliwal P., Radha V., Swarup G.
BMC Mol. Biol. 8:45-45(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION AND INHIBITION OF TP73 ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH TP73 AND YAP1.
[32]"Inhibition of IL-6-dependent growth of myeloma cells by an acidic peptide repressing the gp130-mediated activation of Src family kinases."
Hausherr A., Tavares R., Schaffer M., Obermeier A., Miksch C., Mitina O., Ellwart J., Hallek M., Krause G.
Oncogene 26:4987-4998(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH IL6ST.
[33]"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
Voss M., Lettau M., Janssen O.
BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FASLG.
[34]"The oncogenic activity of the Src family kinase Hck requires the cooperative action of the plasma membrane- and lysosome-associated isoforms."
Poincloux R., Al Saati T., Maridonneau-Parini I., Le Cabec V.
Eur. J. Cancer 45:321-327(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN REORGANIZATION OF ACTIN CYTOSKELETON AND CELL PROLIFERATION, ROLE IN DISEASE.
[35]"Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins."
Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.
J. Cell. Biochem. 108:877-885(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADAM15.
[36]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202 AND SER-462, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration."
Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G., Berton G.
FEBS Lett. 584:15-21(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ABL1-MEDIATED CELL MIGRATION, IDENTIFICATION IN A COMPLEX WITH ITGB1 AND WITH ABL1.
[38]"Expression of a Src family kinase in chronic myelogenous leukemia cells induces resistance to imatinib in a kinase-dependent manner."
Pene-Dumitrescu T., Smithgall T.E.
J. Biol. Chem. 285:21446-21457(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN DISEASE, FUNCTION IN PHOSPHORYLATION OF THE BCR-ABL FUSION PROTEIN.
[39]"Hematopoietic cell kinase (Hck) isoforms and phagocyte duties - from signaling and actin reorganization to migration and phagocytosis."
Guiet R., Poincloux R., Castandet J., Marois L., Labrousse A., Le Cabec V., Maridonneau-Parini I.
Eur. J. Cell Biol. 87:527-542(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN PHAGOCYTOSIS AND SUBSTRATES.
[40]"Protein tyrosine kinases in neutrophil activation and recruitment."
Zarbock A., Ley K.
Arch. Biochem. Biophys. 510:112-119(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN NEUTROPHIL FUNCTION, SIGNALING.
[41]"Sequential assignment and secondary structure determination for the Src homology 2 domain of hematopoietic cellular kinase."
Zhang W., Smithgall T.E., Gmeiner W.H.
FEBS Lett. 406:131-135(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 140-245.
[42]"Crystal structure of the Src family tyrosine kinase Hck."
Sicheri F., Moarefi I., Kuriyan J.
Nature 385:602-609(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 78-526 IN COMPLEX WITH CALCIUM, PHOSPHORYLATION AT TYR-522.
[43]"RT loop flexibility enhances the specificity of Src family SH3 domains for HIV-1 Nef."
Arold S., O'Brien R., Franken P., Strub M.-P., Hoh F., Dumas C., Ladbury J.E.
Biochemistry 37:14683-14691(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 81-137.
[44]"Solution structure of the human Hck SH3 domain and identification of its ligand binding site."
Horita D.A., Baldisseri D.M., Zhang W., Altieri A.S., Smithgall T.E., Gmeiner W.H., Byrd R.A.
J. Mol. Biol. 278:253-265(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 72-143.
[45]"Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor."
Schindler T., Sicheri F., Pico A., Gazit A., Levitzki A., Kuriyan J.
Mol. Cell 3:639-648(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 81-522 IN COMPLEX WITH THE PYRAZOLO PYRIMIDINE-TYPE INHIBITOR PP1, PHOSPHORYLATION AT TYR-522.
[46]"Discovery of A-770041, a src-family selective orally active lck inhibitor that prevents organ allograft rejection."
Burchat A., Borhani D.W., Calderwood D.J., Hirst G.C., Li B., Stachlewitz R.F.
Bioorg. Med. Chem. Lett. 16:118-122(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 81-522 IN COMPLEXES WITH INHIBITORS A-420983; A-641359 AND A-770041, ENZYME REGULATION, PHOSPHORYLATION AT TYR-522.
[47]"The development of 2-benzimidazole substituted pyrimidine based inhibitors of lymphocyte specific kinase (Lck)."
Sabat M., VanRens J.C., Laufersweiler M.J., Brugel T.A., Maier J., Golebiowski A., De B., Easwaran V., Hsieh L.C., Walter R.L., Mekel M.J., Evdokimov A., Janusz M.J.
Bioorg. Med. Chem. Lett. 16:5973-5977(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 247-513 IN COMPLEX WITH INHIBITOR PG-1009247.
[48]"Solution structure of a Hck SH3 domain ligand complex reveals novel interaction modes."
Schmidt H., Hoffmann S., Tran T., Stoldt M., Stangler T., Wiesehan K., Willbold D.
J. Mol. Biol. 365:1517-1532(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 61-140 IN COMPLEX WITH PROLINE-RICH SYNTHETIC PEPTIDE.
[49]"Crystal structure of the Src family kinase Hck SH3-SH2 linker regulatory region supports an SH3-dominant activation mechanism."
Alvarado J.J., Betts L., Moroco J.A., Smithgall T.E., Yeh J.I.
J. Biol. Chem. 285:35455-35461(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 72-256, ENZYME REGULATION, CATALYTIC ACTIVITY.
[50]"Molecular design, functional characterization and structural basis of a protein inhibitor against the HIV-1 pathogenicity factor Nef."
Breuer S., Schievink S.I., Schulte A., Blankenfeldt W., Fackler O.T., Geyer M.
PLoS ONE 6:E20033-E20033(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 79-138 IN COMPLEX WITH HIV-1 NEF, INTERACTION WITH HIV-1 NEF.
[51]"Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by intermolecular domain assembly."
Horenkamp F.A., Breuer S., Schulte A., Lulf S., Weyand M., Saksela K., Geyer M.
Traffic 12:867-877(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 79-138 IN COMPLEX WITH HIV-1 NEF, INTERACTION WITH HIV-1 NEF.
[52]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-44; LEU-105 AND GLY-399.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16591 mRNA. Translation: AAA52643.1. Frameshift.
M16592 mRNA. Translation: AAA52644.1.
AK026432 mRNA. Translation: BAB15482.1.
AK289896 mRNA. Translation: BAF82585.1. Different initiation.
AK298726 mRNA. Translation: BAG60878.1.
AL353092, AL049539 Genomic DNA. Translation: CAI19694.1.
AL353092, AL049539 Genomic DNA. Translation: CAI19695.1.
AL049539, AL353092 Genomic DNA. Translation: CAI22966.1.
AL049539, AL353092 Genomic DNA. Translation: CAI22967.1.
CH471077 Genomic DNA. Translation: EAW76392.1.
CH471077 Genomic DNA. Translation: EAW76393.1.
BC014435 mRNA. Translation: AAH14435.2.
BC094847 mRNA. Translation: AAH94847.2.
BC108930 mRNA. Translation: AAI08931.2.
BC108931 mRNA. Translation: AAI08932.2.
BC113854 mRNA. Translation: AAI13855.2.
BC114463 mRNA. Translation: AAI14464.2.
X58741, X58742, X58743 Genomic DNA. Translation: CAA41565.2.
CCDSCCDS33460.1. [P08631-1]
CCDS54453.1. [P08631-4]
CCDS54455.1. [P08631-2]
CCDS54456.1. [P08631-3]
PIRTVHUHC. A27811.
A41263.
RefSeqNP_001165600.1. NM_001172129.1. [P08631-2]
NP_001165601.1. NM_001172130.1. [P08631-4]
NP_001165602.1. NM_001172131.1. [P08631-3]
NP_001165604.1. NM_001172133.1. [P08631-2]
NP_002101.2. NM_002110.3. [P08631-1]
UniGeneHs.655210.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AD5X-ray2.60A/B79-526[»]
1BU1X-ray2.60A/B/C/D/E/F81-137[»]
1QCFX-ray2.00A81-526[»]
2C0IX-ray2.30A/B81-526[»]
2C0OX-ray2.85A/B81-526[»]
2C0TX-ray2.15A/B81-526[»]
2HCKX-ray3.00A/B79-526[»]
2HK5X-ray2.00A247-514[»]
2OI3NMR-A61-141[»]
2OJ2NMR-A61-141[»]
3HCKNMR-A140-245[»]
3NHNX-ray2.61A72-256[»]
3RBBX-ray2.35B/D79-138[»]
3REAX-ray2.00B/D79-138[»]
3REBX-ray3.45B/D79-138[»]
3VRYX-ray2.48A/B81-526[»]
3VRZX-ray2.22A/B81-526[»]
3VS0X-ray2.93A/B81-526[»]
3VS1X-ray2.46A/B81-526[»]
3VS2X-ray2.61A/B81-526[»]
3VS3X-ray2.17A/B81-526[»]
3VS4X-ray2.75A/B81-526[»]
3VS5X-ray2.85A/B81-526[»]
3VS6X-ray2.37A/B81-526[»]
3VS7X-ray3.00A/B81-526[»]
4HCKNMR-A72-143[»]
4LUDX-ray2.85A/B81-526[»]
4LUEX-ray3.04A/B81-526[»]
4ORZX-ray2.00A77-138[»]
5HCKNMR-A72-143[»]
ProteinModelPortalP08631.
SMRP08631. Positions 49-526.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109305. 44 interactions.
DIPDIP-1051N.
IntActP08631. 57 interactions.
MINTMINT-135300.

Chemistry

BindingDBP08631.
ChEMBLCHEMBL3234.
GuidetoPHARMACOLOGY2032.

PTM databases

PhosphoSiteP08631.

Polymorphism databases

DMDM20141296.

Proteomic databases

MaxQBP08631.
PaxDbP08631.
PRIDEP08631.

Protocols and materials databases

DNASU3055.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000518730; ENSP00000427757; ENSG00000101336. [P08631-3]
ENST00000520553; ENSP00000429848; ENSG00000101336. [P08631-2]
ENST00000538448; ENSP00000441169; ENSG00000101336. [P08631-2]
GeneID3055.
KEGGhsa:3055.
UCSCuc002wxh.3. human. [P08631-1]
uc002wxi.3. human. [P08631-3]

Organism-specific databases

CTD3055.
GeneCardsGC20P030648.
HGNCHGNC:4840. HCK.
HPACAB005195.
MIM142370. gene.
neXtProtNX_P08631.
PharmGKBPA29216.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidP08631.
KOK08893.
OrthoDBEOG7GTT2V.
PhylomeDBP08631.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP08631.

Gene expression databases

ArrayExpressP08631.
BgeeP08631.
GenevestigatorP08631.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHCK. human.
EvolutionaryTraceP08631.
GeneWikiHCK.
GenomeRNAi3055.
NextBio12093.
PROP08631.
SOURCESearch...

Entry information

Entry nameHCK_HUMAN
AccessionPrimary (citable) accession number: P08631
Secondary accession number(s): A8K1I1 expand/collapse secondary AC list , B4DQB6, E1P5M2, Q29RX1, Q2VPE2, Q504R5, Q5T7K1, Q5T7K2, Q96CC0, Q9H5Y5, Q9NUA4, Q9UMJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 194 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM