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P08103

- HCK_MOUSE

UniProt

P08103 - HCK_MOUSE

Protein

Tyrosine-protein kinase HCK

Gene

Hck

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 PublicationPROSITE-ProRule annotation

    Enzyme regulationi

    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 PP1.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei288 – 2881ATPPROSITE-ProRule annotation
    Active sitei379 – 3791Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi266 – 2749ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    3. protein binding Source: IntAct
    4. protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. defense response to Gram-positive bacterium Source: MGI
    2. exocytosis Source: UniProtKB-KW
    3. inflammatory response Source: UniProtKB-KW
    4. innate immune response Source: UniProtKB-KW
    5. peptidyl-tyrosine phosphorylation Source: UniProtKB
    6. phagocytosis Source: MGI
    7. positive regulation of actin cytoskeleton reorganization Source: UniProtKB
    8. positive regulation of cell proliferation Source: UniProtKB
    9. protein autophosphorylation Source: UniProtKB
    10. regulation of cell shape Source: UniProtKB
    11. regulation of phagocytosis Source: UniProtKB
    12. regulation of podosome assembly Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Exocytosis, Immunity, Inflammatory response, Innate immunity, Phagocytosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 3474.
    ReactomeiREACT_196487. FCGR activation.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Hck
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:96052. Hck.

    Subcellular locationi

    Cytoplasmic vesiclesecretory vesicle By similarity. Cytoplasmcytosol By similarity
    Isoform 1 : Membrane; Lipid-anchor. Membranecaveola By similarity. Lysosome By similarity. Cell projectionpodosome membrane By similarity; Lipid-anchor By similarity. Cytoplasmcytosol By similarity
    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.By similarity
    Isoform 2 : Cell membrane; Lipid-anchor. Membranecaveola By similarity; 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 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.By similarity

    GO - Cellular componenti

    1. caveola Source: UniProtKB-SubCell
    2. cell projection Source: UniProtKB-KW
    3. cytoskeleton Source: UniProtKB-SubCell
    4. cytosol Source: UniProtKB-SubCell
    5. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    6. focal adhesion Source: UniProtKB-SubCell
    7. Golgi apparatus Source: UniProtKB-SubCell
    8. lysosome Source: UniProtKB
    9. nucleus Source: UniProtKB-SubCell
    10. transport vesicle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Golgi apparatus, Lysosome, Membrane, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype, but macrophages have impaired phagocytosis. Mice lacking both HCK and FGR are extremely sensitive to infections by L.monocytogenes.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi409 – 4091Y → F: Reduced autophosphorylation. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 524523Tyrosine-protein kinase HCKPRO_0000024435Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Modified residuei50 – 501Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei200 – 2001PhosphothreonineBy similarity
    Modified residuei207 – 2071Phosphotyrosine1 Publication
    Modified residuei409 – 4091Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei460 – 4601PhosphoserineBy similarity
    Modified residuei520 – 5201Phosphotyrosine1 Publication

    Post-translational modificationi

    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.2 Publications
    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.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP08103.
    PRIDEiP08103.

    PTM databases

    PhosphoSiteiP08103.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP08103.
    BgeeiP08103.
    CleanExiMM_HCK.
    GenevestigatoriP08103.

    Interactioni

    Subunit structurei

    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.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    WASP427683EBI-6248894,EBI-346375From a different organism.

    Protein-protein interaction databases

    BioGridi200249. 4 interactions.
    IntActiP08103. 5 interactions.
    MINTiMINT-4097288.

    Structurei

    3D structure databases

    ProteinModelPortaliP08103.
    SMRiP08103. Positions 80-524.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini76 – 13661SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini142 – 23998SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini260 – 513254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00620000087866.
    HOGENOMiHOG000233858.
    HOVERGENiHBG008761.
    InParanoidiP08103.
    KOiK08893.
    PhylomeDBiP08103.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR011009. 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]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform 1 (identifier: P08103-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGGRSSCEDP GCPRSEGRAP RMGCVKSRFL RDGSKASKTE PSANQKGPVY    50
    VPDPTSSSKL GPNNSNSMPP GFVEGSEDTI VVALYDYEAI HREDLSFQKG 100
    DQMVVLEEAG EWWKARSLAT KKEGYIPSNY VARVNSLETE EWFFKGISRK 150
    DAERHLLAPG NMLGSFMIRD SETTKGSYSL SVRDFDPQHG DTVKHYKIRT 200
    LDSGGFYISP RSTFSSLQEL VLHYKKGKDG LCQKLSVPCV SPKPQKPWEK 250
    DAWEIPRESL QMEKKLGAGQ FGEVWMATYN KHTKVAVKTM KPGSMSVEAF 300
    LAEANLMKSL QHDKLVKLHA VVSQEPIFIV TEFMAKGSLL DFLKSEEGSK 350
    QPLPKLIDFS AQISEGMAFI EQRNYIHRDL RAANILVSAS LVCKIADFGL 400
    ARIIEDNEYT AREGAKFPIK WTAPEAINFG SFTIKSDVWS FGILLMEIVT 450
    YGRIPYPGMS NPEVIRALEH GYRMPRPDNC PEELYNIMIR CWKNRPEERP 500
    TFEYIQSVLD DFYTATESQY QQQP 524

    Note: Initiates from a CTG codon.

    Length:524
    Mass (Da):59,129
    Last modified:January 23, 2007 - v4
    Checksum:iDF72FD69B38C9706
    GO
    Isoform 2 (identifier: P08103-2) [UniParc]FASTAAdd to Basket

    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).By similarity

    Show »
    Length:504
    Mass (Da):57,073
    Checksum:iCC4D04E0ABA7DF55
    GO

    Sequence cautioni

    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.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 2120Missing in isoform 2. CuratedVSP_018859Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS38284.1. [P08103-1]
    PIRiA27282. TVMSHC.
    RefSeqiNP_001165588.1. NM_001172117.1.
    NP_034537.2. NM_010407.4. [P08103-1]
    UniGeneiMm.715.

    Genome annotation databases

    EnsembliENSMUST00000109799; ENSMUSP00000105423; ENSMUSG00000003283.
    GeneIDi15162.
    KEGGimmu:15162.
    UCSCiuc008nhc.2. mouse. [P08103-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS38284.1. [P08103-1 ]
    PIRi A27282. TVMSHC.
    RefSeqi NP_001165588.1. NM_001172117.1.
    NP_034537.2. NM_010407.4. [P08103-1 ]
    UniGenei Mm.715.

    3D structure databases

    ProteinModelPortali P08103.
    SMRi P08103. Positions 80-524.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200249. 4 interactions.
    IntActi P08103. 5 interactions.
    MINTi MINT-4097288.

    PTM databases

    PhosphoSitei P08103.

    Proteomic databases

    PaxDbi P08103.
    PRIDEi P08103.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000109799 ; ENSMUSP00000105423 ; ENSMUSG00000003283 .
    GeneIDi 15162.
    KEGGi mmu:15162.
    UCSCi uc008nhc.2. mouse. [P08103-1 ]

    Organism-specific databases

    CTDi 3055.
    MGIi MGI:96052. Hck.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00620000087866.
    HOGENOMi HOG000233858.
    HOVERGENi HBG008761.
    InParanoidi P08103.
    KOi K08893.
    PhylomeDBi P08103.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 3474.
    Reactomei REACT_196487. FCGR activation.

    Miscellaneous databases

    NextBioi 287656.
    PROi P08103.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08103.
    Bgeei P08103.
    CleanExi MM_HCK.
    Genevestigatori P08103.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR011009. 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 ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. 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.
      , 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.

    Entry informationi

    Entry nameiHCK_MOUSE
    AccessioniPrimary (citable) accession number: P08103
    Secondary accession number(s): Q0VH03, Q3UD17
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 163 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3