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Q95M30

- HCK_MACFA

UniProt

Q95M30 - HCK_MACFA

Protein

Tyrosine-protein kinase HCK

Gene

HCK

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 3 (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.PROSITE-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-389 is required for optimal activity. Phosphorylation at Tyr-500 inhibits kinase activity By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei268 – 2681ATPPROSITE-ProRule annotation
    Active sitei359 – 3591Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi246 – 2549ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. exocytosis Source: UniProtKB-KW
    2. inflammatory response Source: UniProtKB-KW
    3. innate immune response Source: UniProtKB-KW
    4. peptidyl-tyrosine phosphorylation Source: UniProtKB
    5. phagocytosis Source: UniProtKB-KW
    6. positive regulation of actin cytoskeleton reorganization Source: UniProtKB
    7. positive regulation of cell proliferation Source: UniProtKB
    8. protein autophosphorylation Source: UniProtKB
    9. regulation of cell shape Source: UniProtKB
    10. regulation of phagocytosis Source: UniProtKB
    11. 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. 3121.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase HCK (EC:2.7.10.2)
    Alternative name(s):
    Hematopoietic cell kinase
    Hemopoietic cell kinase
    p56-HCK
    Gene namesi
    Name:HCK
    OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
    Taxonomic identifieri9541 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

    Subcellular locationi

    Cytoplasmic vesiclesecretory vesicle By similarity. Cytoplasmcytosol By similarity. 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: A small fraction 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. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: UniProtKB-SubCell
    4. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    5. focal adhesion Source: UniProtKB-SubCell
    6. Golgi apparatus Source: UniProtKB-SubCell
    7. lysosome Source: UniProtKB
    8. nucleus Source: UniProtKB-SubCell
    9. transport vesicle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 504503Tyrosine-protein kinase HCKPRO_0000088103Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Lipidationi3 – 31S-palmitoyl cysteineBy similarity
    Modified residuei30 – 301PhosphotyrosineBy similarity
    Modified residuei180 – 1801PhosphothreonineBy similarity
    Modified residuei187 – 1871PhosphotyrosineBy similarity
    Modified residuei389 – 3891Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei440 – 4401PhosphoserineBy similarity
    Modified residuei500 – 5001PhosphotyrosineBy similarity

    Post-translational modificationi

    Phosphorylated on several tyrosine residues. Autophosphorylated. Becomes rapidly phosphorylated upon activation of the immunoglobulin receptors FCGR1A and FCGR2A. Phosphorylation at Tyr-389 increases kinase activity. Phosphorylation at Tyr-500 inhibits kinase activity. Kinase activity is not required for phosphorylation at Tyr-500, suggesting that this site may be a target of other kinases By similarity.By similarity
    Ubiquitinated by CBL, leading to its degradation via the proteasome.By similarity
    Palmitoylation requires prior myristoylation. Palmitoylation is required for caveolar localization By similarity.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ95M30.

    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. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with CBL. Interacts with VAV1, WAS and RAPGEF1 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ95M30.
    SMRiQ95M30. Positions 56-504.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini56 – 11661SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini122 – 21998SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini240 – 493254Protein 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

    HOVERGENiHBG008761.

    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]

    Sequencei

    Sequence statusi: Complete.

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

    Q95M30-1 [UniParc]FASTAAdd to Basket

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    MGCMKSKFLQ AGGNTFSKTE TSANPHCPVY VPDPTSTIKP GPNSNNRNTP    50
    GIGEGSEDII VVALYDYEAI HHEDLSFQKG DQMVVLEESG EWWKARSLAT 100
    RKEGYIPSNY VARVDSLETE EWFFKGISRK DAERQLLAPG NMLGSFMIRD 150
    SETTKGSYSL SVRDYDPRQG DTVKHYKIRT LDNGGFYISP RSTFSTLQEL 200
    VDHYKKGSDG LCQKLSVPCV SSKPQKPWEK DAWEIPRESL KLEKKLGAGQ 250
    FGEVWMATYN KHTKVAVKTM KPGSMSVEAF LAEANLMKTL QHDKLVKLHA 300
    VVTKEPIYII TEFMAKGSLL DFLKSDEGSK QPLPKLIDFS AQIAEGMAFI 350
    EQRNYIHRDL RAANILVSAS LVCKIADFGL ARIIEDNEYT AREGAKFPIK 400
    WTAPEAINFG SSTIKSDVWS FGILLMEIVT YGRIPYPGMS NPEVIRALER 450
    GYRMPRPENC PEELYNIMMR CWKNRPEERP TFEYIQSVLD DFYTATESQY 500
    QQQP 504
    Length:504
    Mass (Da):57,096
    Last modified:January 23, 2007 - v3
    Checksum:i53B29322D2DE3423
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ320181 mRNA. Translation: CAC44031.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ320181 mRNA. Translation: CAC44031.1 .

    3D structure databases

    ProteinModelPortali Q95M30.
    SMRi Q95M30. Positions 56-504.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q95M30.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG008761.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 3121.

    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. Picard C.
      Thesis (2001), University of Marseille, France
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiHCK_MACFA
    AccessioniPrimary (citable) accession number: Q95M30
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 98 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3