Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P08103 (HCK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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):
B-cell/myeloid kinase
Short name=BMK
Hematopoietic cell kinase
Hemopoietic cell kinase
p56-HCK/p59-HCK
Gene names
Name:Hck
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length524 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 By similarity. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.10

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. Inhibited by PP1. Ref.10 Ref.12

Subunit structure

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. Ref.8 Ref.11 Ref.13 Ref.14 Ref.15 Ref.22

Subcellular location

Cytoplasmic vesiclesecretory vesicle By similarity. Cytoplasmcytosol By similarity.

Isoform 1: Membrane; Lipid-anchor. Membranecaveola By similarity. Lysosome By similarity. Cell projectionpodosome membrane; Lipid-anchor By similarity. Cytoplasmcytosol By similarity. Note: Associated with specialized secretory lysosomes called azurophil granules. A fraction of this isoform isfound in the cytoplasm, some of this fraction is myristoylated By similarity. Ref.5 Ref.11

Isoform 2: Cell membrane; Lipid-anchor. Membranecaveola; Lipid-anchor By similarity. Cell junctionfocal adhesion By similarity. Cytoplasmcytoskeleton By similarity. Golgi apparatus By similarity. Cytoplasmic vesicle By similarity. Lysosome By similarity. Nucleus By similarity. 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 By similarity. Ref.5 Ref.11

Tissue specificity

Expressed predominantly in cells of the myeloid and B-lymphoid lineages.

Post-translational modification

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. Ref.12

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

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

Disruption phenotype

No visible phenotype, but macrophages have impaired phagocytosis. Mice lacking both HCK and FGR are extremely sensitive to infections by L.monocytogenes. Ref.6 Ref.7

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 AAA37305.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

The sequence BAE29054.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

The sequence BAE29445.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

The sequence BAE29787.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

The sequence BAE33532.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

The sequence BAE38133.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

The sequence CAA68544.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

Ontologies

Keywords
   Biological processExocytosis
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
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMLipoprotein
Myristate
Palmitate
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to Gram-positive bacterium

Inferred from genetic interaction Ref.6. Source: MGI

exocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

phagocytosis

Inferred from mutant phenotype Ref.6. Source: MGI

positive regulation of actin cytoskeleton reorganization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell shape

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of phagocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of podosome assembly

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

caveola

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell projection

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

extrinsic component of cytoplasmic side of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

focal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosome

Inferred from sequence or structural similarity. 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 tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

WASP427683EBI-6248894,EBI-346375From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P08103-1)

Also known as: p59-HCK;

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: P08103-2)

Also known as: p56-HCK;

The sequence of this isoform differs from the canonical sequence as follows:
     2-21: Missing.
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).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 524523Tyrosine-protein kinase HCK
PRO_0000024435

Regions

Domain76 – 13661SH3
Domain142 – 23998SH2
Domain260 – 513254Protein kinase
Nucleotide binding266 – 2749ATP By similarity

Sites

Active site3791Proton acceptor By similarity
Binding site2881ATP By similarity

Amino acid modifications

Modified residue501Phosphotyrosine; by autocatalysis Ref.12
Modified residue2001Phosphothreonine By similarity
Modified residue2071Phosphotyrosine Ref.20
Modified residue4091Phosphotyrosine; by autocatalysis Ref.12
Modified residue4601Phosphoserine By similarity
Modified residue5201Phosphotyrosine Ref.20
Lipidation21N-myristoyl glycine By similarity

Natural variations

Alternative sequence2 – 2120Missing in isoform 2.
VSP_018859

Experimental info

Mutagenesis4091Y → F: Reduced autophosphorylation. Ref.12

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (p59-HCK) [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: DF72FD69B38C9706

FASTA52459,129
        10         20         30         40         50         60 
MGGRSSCEDP GCPRSEGRAP RMGCVKSRFL RDGSKASKTE PSANQKGPVY VPDPTSSSKL 

        70         80         90        100        110        120 
GPNNSNSMPP GFVEGSEDTI VVALYDYEAI HREDLSFQKG DQMVVLEEAG EWWKARSLAT 

       130        140        150        160        170        180 
KKEGYIPSNY VARVNSLETE EWFFKGISRK DAERHLLAPG NMLGSFMIRD SETTKGSYSL 

       190        200        210        220        230        240 
SVRDFDPQHG DTVKHYKIRT LDSGGFYISP RSTFSSLQEL VLHYKKGKDG LCQKLSVPCV 

       250        260        270        280        290        300 
SPKPQKPWEK DAWEIPRESL QMEKKLGAGQ FGEVWMATYN KHTKVAVKTM KPGSMSVEAF 

       310        320        330        340        350        360 
LAEANLMKSL QHDKLVKLHA VVSQEPIFIV TEFMAKGSLL DFLKSEEGSK QPLPKLIDFS 

       370        380        390        400        410        420 
AQISEGMAFI EQRNYIHRDL RAANILVSAS LVCKIADFGL ARIIEDNEYT AREGAKFPIK 

       430        440        450        460        470        480 
WTAPEAINFG SFTIKSDVWS FGILLMEIVT YGRIPYPGMS NPEVIRALEH GYRMPRPDNC 

       490        500        510        520 
PEELYNIMIR CWKNRPEERP TFEYIQSVLD DFYTATESQY QQQP 

« Hide

Isoform 2 (p56-HCK) [UniParc].

Checksum: CC4D04E0ABA7DF55
Show »

FASTA50457,073

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the mouse hck gene."
Klemsz M.J., McKercher S.R., Maki R.A.
Nucleic Acids Res. 15:9600-9600(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: ICR.
Tissue: Macrophage.
[2]"Isolation and sequence of a cDNA corresponding to a src-related gene expressed in murine hemopoietic cells."
Holtzman D.A., Cook W.D., Dunn A.R.
Proc. Natl. Acad. Sci. U.S.A. 84:8325-8329(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Macrophage.
[3]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J and NOD.
Tissue: Bone marrow macrophage and Spleen.
[4]"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] (ISOFORM 1).
Strain: FVB/N.
Tissue: Mammary gland.
[5]"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), SUBCELLULAR LOCATION, IDENTIFICATION OF ISOFORM 2, ALTERNATIVE INITIATION.
[6]"Functional overlap in the src gene family: inactivation of hck and fgr impairs natural immunity."
Lowell C.A., Soriano P., Varmus H.E.
Genes Dev. 8:387-398(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[7]"Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions."
Lowell C.A., Fumagalli L., Berton G.
J. Cell Biol. 133:895-910(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[8]"Bacterial LPS and IFN-gamma trigger the tyrosine phosphorylation of vav in macrophages: evidence for involvement of the hck tyrosine kinase."
English B.K., Orlicek S.L., Mei Z., Meals E.A.
J. Leukoc. Biol. 62:859-864(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VAV1.
[9]"Impaired integrin-mediated signal transduction, altered cytoskeletal structure and reduced motility in Hck/Fgr deficient macrophages."
Suen P.W., Ilic D., Caveggion E., Berton G., Damsky C.H., Lowell C.A.
J. Cell Sci. 112:4067-4078(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Adhesion-dependent degranulation of neutrophils requires the Src family kinases Fgr and Hck."
Mocsai A., Ligeti E., Lowell C.A., Berton G.
J. Immunol. 162:1120-1126(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
[11]"Hck enhances the adherence of lipopolysaccharide-stimulated macrophages via Cbl and phosphatidylinositol 3-kinase."
Scholz G., Cartledge K., Dunn A.R.
J. Biol. Chem. 275:14615-14623(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF CBL, SUBCELLULAR LOCATION, INTERACTION WITH CBL.
[12]"Modulation of the catalytic activity of the Src family tyrosine kinase Hck by autophosphorylation at a novel site in the unique domain."
Johnson T.M., Williamson N.A., Scholz G., Jaworowski A., Wettenhall R.E., Dunn A.R., Cheng H.C.
J. Biol. Chem. 275:33353-33364(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-50 AND TYR-409, MUTAGENESIS OF TYR-409, ENZYME REGULATION.
[13]"Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein."
Cory G.O., Garg R., Cramer R., Ridley A.J.
J. Biol. Chem. 277:45115-45121(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF WAS, INTERACTION WITH WAS.
[14]"Physical and functional interaction between Hck tyrosine kinase and guanine nucleotide exchange factor C3G results in apoptosis, which is independent of C3G catalytic domain."
Shivakrupa R., Radha V., Sudhakar C., Swarup G.
J. Biol. Chem. 278:52188-52194(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAPGEF1, FUNCTION IN REGULATION OF APOPTOSIS.
[15]"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."
Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S., Ronnstrand L.
Blood 108:1542-1550(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLT3.
[16]"CpG DNA enhances macrophage cell spreading by promoting the Src-family kinase-mediated phosphorylation of paxillin."
Achuthan A., Elsegood C., Masendycz P., Hamilton J.A., Scholz G.M.
Cell. Signal. 18:2252-2261(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"The Src family kinase Hck regulates mast cell activation by suppressing an inhibitory Src family kinase Lyn."
Hong H., Kitaura J., Xiao W., Horejsi V., Ra C., Lowell C.A., Kawakami Y., Kawakami T.
Blood 110:2511-2519(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"Regulation of myeloproliferation and M2 macrophage programming in mice by Lyn/Hck, SHIP, and Stat5."
Xiao W., Hong H., Kawakami Y., Lowell C.A., Kawakami T.
J. Clin. Invest. 118:924-934(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"Myeloid Src kinases regulate phagocytosis and oxidative burst in pneumococcal meningitis by activating NADPH oxidase."
Paul R., Obermaier B., Van Ziffle J., Angele B., Pfister H.W., Lowell C.A., Koedel U.
J. Leukoc. Biol. 84:1141-1150(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-207 AND TYR-520, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Three-dimensional migration of macrophages requires Hck for podosome organization and extracellular matrix proteolysis."
Cougoule C., Le Cabec V., Poincloux R., Al Saati T., Mege J.L., Tabouret G., Lowell C.A., Laviolette-Malirat N., Maridonneau-Parini I.
Blood 115:1444-1452(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"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 MYELOID CELL MIGRATION, INTERACTION WITH ABL1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00487 mRNA. Translation: CAA68544.1. Sequence problems.
J03023 mRNA. Translation: AAA37305.1. Sequence problems.
AK149736 mRNA. Translation: BAE29054.1. Sequence problems.
AK150290 mRNA. Translation: BAE29445.1. Sequence problems.
AK150709 mRNA. Translation: BAE29787.1. Sequence problems.
AK155975 mRNA. Translation: BAE33532.1. Sequence problems.
AK165315 mRNA. Translation: BAE38133.1. Sequence problems.
BC010478 mRNA. Translation: AAH10478.2.
PIRTVMSHC. A27282.
RefSeqNP_001165588.1. NM_001172117.1.
NP_034537.2. NM_010407.4.
UniGeneMm.715.

3D structure databases

ProteinModelPortalP08103.
SMRP08103. Positions 80-524.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200249. 4 interactions.
IntActP08103. 5 interactions.
MINTMINT-4097288.

PTM databases

PhosphoSiteP08103.

Proteomic databases

PaxDbP08103.
PRIDEP08103.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000109799; ENSMUSP00000105423; ENSMUSG00000003283.
GeneID15162.
KEGGmmu:15162.
UCSCuc008nhc.2. mouse. [P08103-1]

Organism-specific databases

CTD3055.
MGIMGI:96052. Hck.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00620000087866.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidP08103.
KOK08893.
PhylomeDBP08103.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.

Gene expression databases

ArrayExpressP08103.
BgeeP08103.
CleanExMM_HCK.
GenevestigatorP08103.

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

NextBio287656.
PROP08103.
SOURCESearch...

Entry information

Entry nameHCK_MOUSE
AccessionPrimary (citable) accession number: P08103
Secondary accession number(s): Q0VH03, Q3UD17
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 158 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot