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P42679

- MATK_HUMAN

UniProt

P42679 - MATK_HUMAN

Protein

Megakaryocyte-associated tyrosine-protein kinase

Gene

MATK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Could play a significant role in the signal transduction of hematopoietic cells. May regulate tyrosine kinase activity of SRC-family members in brain by specifically phosphorylating their C-terminal regulatory tyrosine residue which acts as a negative regulatory site. It may play an inhibitory role in the control of T-cell proliferation.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei262 – 2621ATPPROSITE-ProRule annotation
    Active sitei352 – 3521Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi241 – 2499ATPPROSITE-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: ProtInc

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. mesoderm development Source: ProtInc
    3. peptidyl-tyrosine phosphorylation Source: GOC
    4. positive regulation of cell proliferation Source: ProtInc
    5. protein phosphorylation Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 2681.
    ReactomeiREACT_115755. Signaling by ERBB2.
    SignaLinkiP42679.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Megakaryocyte-associated tyrosine-protein kinase (EC:2.7.10.2)
    Alternative name(s):
    CSK homologous kinase
    Short name:
    CHK
    Hematopoietic consensus tyrosine-lacking kinase
    Protein kinase HYL
    Tyrosine-protein kinase CTK
    Gene namesi
    Name:MATK
    Synonyms:CTK, HYL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:6906. MATK.

    Subcellular locationi

    Cytoplasm 1 Publication. Membrane 1 Publication
    Note: In platelets, 90% of MATK localizes to the membrane fraction, and translocates to the cytoskeleton upon thrombin stimulation.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30649.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 507507Megakaryocyte-associated tyrosine-protein kinasePRO_0000088073Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei501 – 5011Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP42679.
    PaxDbiP42679.
    PRIDEiP42679.

    PTM databases

    PhosphoSiteiP42679.

    Expressioni

    Tissue specificityi

    Expressed in various myeloid cell lines, detected in brain and lung.

    Gene expression databases

    ArrayExpressiP42679.
    BgeeiP42679.
    CleanExiHS_MATK.
    GenevestigatoriP42679.

    Organism-specific databases

    HPAiHPA004847.

    Interactioni

    Subunit structurei

    Interacts with KIT.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARP102754EBI-751664,EBI-608057
    ERBB2P046262EBI-751664,EBI-641062
    HSP90AB1P082382EBI-751664,EBI-352572
    LRRK2Q5S0072EBI-751664,EBI-5323863

    Protein-protein interaction databases

    BioGridi110315. 12 interactions.
    IntActiP42679. 10 interactions.
    MINTiMINT-1466004.
    STRINGi9606.ENSP00000313859.

    Structurei

    Secondary structure

    1
    507
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi52 – 576
    Beta strandi59 – 613
    Beta strandi74 – 796
    Beta strandi83 – 919
    Turni92 – 943
    Beta strandi97 – 1015
    Helixi102 – 1043
    Beta strandi105 – 1073
    Beta strandi123 – 1264
    Helixi129 – 1357
    Beta strandi144 – 1485
    Beta strandi150 – 1523
    Beta strandi156 – 1627
    Beta strandi165 – 17410
    Beta strandi177 – 18812
    Helixi189 – 19810
    Beta strandi203 – 2053

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JWOX-ray2.50A117-213[»]
    1X6GNMR-A41-108[»]
    3US4X-ray1.50A117-213[»]
    ProteinModelPortaliP42679.
    SMRiP42679. Positions 39-478.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42679.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 11053SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini122 – 21190SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini235 – 482248Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. CSK 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.
    HOGENOMiHOG000233858.
    HOVERGENiHBG008761.
    KOiK08888.
    OMAiYRAKHHA.
    OrthoDBiEOG7SV0V5.
    PhylomeDBiP42679.
    TreeFamiTF351634.

    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.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P42679-1) [UniParc]FASTAAdd to Basket

    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

    MAGRGSLVSW RAFHGCDSAE ELPRVSPRFL RAWHPPPVSA RMPTRRWAPG    50
    TQCITKCEHT RPKPGELAFR KGDVVTILEA CENKSWYRVK HHTSGQEGLL 100
    AAGALREREA LSADPKLSLM PWFHGKISGQ EAVQQLQPPE DGLFLVRESA 150
    RHPGDYVLCV SFGRDVIHYR VLHRDGHLTI DEAVFFCNLM DMVEHYSKDK 200
    GAICTKLVRP KRKHGTKSAE EELARAGWLL NLQHLTLGAQ IGEGEFGAVL 250
    QGEYLGQKVA VKNIKCDVTA QAFLDETAVM TKMQHENLVR LLGVILHQGL 300
    YIVMEHVSKG NLVNFLRTRG RALVNTAQLL QFSLHVAEGM EYLESKKLVH 350
    RDLAARNILV SEDLVAKVSD FGLAKAERKG LDSSRLPVKW TAPEALKHGK 400
    FTSKSDVWSF GVLLWEVFSY GRAPYPKMSL KEVSEAVEKG YRMEPPEGCP 450
    GPVHVLMSSC WEAEPARRPP FRKLAEKLAR ELRSAGAPAS VSGQDADGST 500
    SPRSQEP 507
    Length:507
    Mass (Da):56,469
    Last modified:November 1, 1995 - v1
    Checksum:i85721C6E024575EF
    GO
    Isoform 2 (identifier: P42679-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-24: MAGRGSLVSWRAFHGCDSAEELPR → MQGHFPAERREGRPRRGTRGQQQLL

    Note: No experimental confirmation available.

    Show »
    Length:508
    Mass (Da):56,798
    Checksum:iCEFD5D74DAC082E5
    GO
    Isoform 3 (identifier: P42679-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-41: Missing.

    Show »
    Length:466
    Mass (Da):51,899
    Checksum:iB2C4DFFE995D5FEE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1082ER → DG in AAA16703. (PubMed:8134117)Curated
    Sequence conflicti400 – 4001Missing in AAA16703. (PubMed:8134117)Curated
    Sequence conflicti466 – 50742ARRPP…RSQEP → PAGHPSANWPRSWPGSYAVQ VPQPPSQGRTPTVHLAPKPG ALTPPGGPWPQRTERVESAA WGH in AAA16703. (PubMed:8134117)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti354 – 3541A → T in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
    VAR_041679
    Natural varianti496 – 4961A → T.1 Publication
    Corresponds to variant rs35351680 [ dbSNP | Ensembl ].
    VAR_041680
    Natural varianti503 – 5031R → Q in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041681

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4141Missing in isoform 3. 1 PublicationVSP_044277Add
    BLAST
    Alternative sequencei1 – 2424MAGRG…EELPR → MQGHFPAERREGRPRRGTRG QQQLL in isoform 2. 1 PublicationVSP_043123Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18974 mRNA. Translation: AAA16703.1.
    X77278 mRNA. Translation: CAA54493.1.
    S75164
    , S75145, S75147, S75166, S75168, S75151, S75153, S75155, S75156, S75158, S75159, S75162 Genomic DNA. Translation: AAC60645.1.
    AK055395 mRNA. Translation: BAG51511.1.
    AL137754 mRNA. Translation: CAB70906.2.
    AC005777 Genomic DNA. Translation: AAC62843.1.
    CH471139 Genomic DNA. Translation: EAW69285.1.
    BC000114 mRNA. Translation: AAH00114.1.
    BC003109 mRNA. Translation: AAH03109.1.
    CCDSiCCDS12113.1. [P42679-2]
    CCDS12114.1. [P42679-1]
    CCDS42468.1. [P42679-3]
    PIRiA49865.
    A55625.
    RefSeqiNP_002369.2. NM_002378.3. [P42679-2]
    NP_647611.1. NM_139354.2. [P42679-3]
    NP_647612.1. NM_139355.2. [P42679-1]
    UniGeneiHs.631845.

    Genome annotation databases

    EnsembliENST00000310132; ENSP00000308734; ENSG00000007264. [P42679-1]
    ENST00000395040; ENSP00000378481; ENSG00000007264. [P42679-3]
    ENST00000395045; ENSP00000378485; ENSG00000007264. [P42679-2]
    GeneIDi4145.
    KEGGihsa:4145.
    UCSCiuc002lyt.3. human. [P42679-1]
    uc002lyv.3. human. [P42679-2]

    Polymorphism databases

    DMDMi1169123.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18974 mRNA. Translation: AAA16703.1 .
    X77278 mRNA. Translation: CAA54493.1 .
    S75164
    , S75145 , S75147 , S75166 , S75168 , S75151 , S75153 , S75155 , S75156 , S75158 , S75159 , S75162 Genomic DNA. Translation: AAC60645.1 .
    AK055395 mRNA. Translation: BAG51511.1 .
    AL137754 mRNA. Translation: CAB70906.2 .
    AC005777 Genomic DNA. Translation: AAC62843.1 .
    CH471139 Genomic DNA. Translation: EAW69285.1 .
    BC000114 mRNA. Translation: AAH00114.1 .
    BC003109 mRNA. Translation: AAH03109.1 .
    CCDSi CCDS12113.1. [P42679-2 ]
    CCDS12114.1. [P42679-1 ]
    CCDS42468.1. [P42679-3 ]
    PIRi A49865.
    A55625.
    RefSeqi NP_002369.2. NM_002378.3. [P42679-2 ]
    NP_647611.1. NM_139354.2. [P42679-3 ]
    NP_647612.1. NM_139355.2. [P42679-1 ]
    UniGenei Hs.631845.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JWO X-ray 2.50 A 117-213 [» ]
    1X6G NMR - A 41-108 [» ]
    3US4 X-ray 1.50 A 117-213 [» ]
    ProteinModelPortali P42679.
    SMRi P42679. Positions 39-478.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110315. 12 interactions.
    IntActi P42679. 10 interactions.
    MINTi MINT-1466004.
    STRINGi 9606.ENSP00000313859.

    Chemistry

    BindingDBi P42679.
    ChEMBLi CHEMBL4175.
    GuidetoPHARMACOLOGYi 2101.

    PTM databases

    PhosphoSitei P42679.

    Polymorphism databases

    DMDMi 1169123.

    Proteomic databases

    MaxQBi P42679.
    PaxDbi P42679.
    PRIDEi P42679.

    Protocols and materials databases

    DNASUi 4145.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310132 ; ENSP00000308734 ; ENSG00000007264 . [P42679-1 ]
    ENST00000395040 ; ENSP00000378481 ; ENSG00000007264 . [P42679-3 ]
    ENST00000395045 ; ENSP00000378485 ; ENSG00000007264 . [P42679-2 ]
    GeneIDi 4145.
    KEGGi hsa:4145.
    UCSCi uc002lyt.3. human. [P42679-1 ]
    uc002lyv.3. human. [P42679-2 ]

    Organism-specific databases

    CTDi 4145.
    GeneCardsi GC19M003777.
    HGNCi HGNC:6906. MATK.
    HPAi HPA004847.
    MIMi 600038. gene.
    neXtProti NX_P42679.
    PharmGKBi PA30649.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233858.
    HOVERGENi HBG008761.
    KOi K08888.
    OMAi YRAKHHA.
    OrthoDBi EOG7SV0V5.
    PhylomeDBi P42679.
    TreeFami TF351634.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_115755. Signaling by ERBB2.
    SignaLinki P42679.

    Miscellaneous databases

    EvolutionaryTracei P42679.
    GeneWikii Megakaryocyte-associated_tyrosine_kinase.
    GenomeRNAii 4145.
    NextBioi 16280.
    PROi P42679.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42679.
    Bgeei P42679.
    CleanExi HS_MATK.
    Genevestigatori P42679.

    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.
    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. "Molecular cloning of a novel non-receptor tyrosine kinase, HYL (hematopoietic consensus tyrosine-lacking kinase)."
      Sakano S., Iwama A., Inazawa J., Ariyama T., Ohno M., Suda T.
      Oncogene 9:1155-1161(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Identification and characterization of a novel tyrosine kinase from megakaryocytes."
      Bennett B.D., Cowley S., Jiang S., London R., Deng B., Grabarek J., Groopman J.E., Goeddel D.V., Avraham H.
      J. Biol. Chem. 269:1068-1074(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Megakaryocyte.
    3. "Structural and functional studies of the intracellular tyrosine kinase MATK gene and its translated product."
      Avraham S., Jiang S., Ota S., Fu Y., Deng B., Dowler L.L., White R.A., Avraham H.
      J. Biol. Chem. 270:1833-1842(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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.
      , 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] (ISOFORM 2).
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Testis.
    6. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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).
      Tissue: Eye.
    9. "Characterization of mouse non-receptor tyrosine kinase gene, HYL."
      Hamaguchi I., Iwama A., Yamaguchi N., Sakano S., Matsuda Y., Suda T.
      Oncogene 9:3371-3374(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    10. "Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets."
      Hirao A., Hamaguchi I., Suda T., Yamaguchi N.
      EMBO J. 16:2342-2351(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Platelet.
    11. "Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes."
      Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.
      J. Biol. Chem. 272:5915-5920(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KIT.
    12. "Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor."
      Roskoski R. Jr.
      Biochem. Biophys. Res. Commun. 337:1-13(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN KIT SIGNALING.
    13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Solution structures of the SH3 domain of human megakaryocyte-associated tyrosine-protein kinase."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 39-108.
    19. "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.
      , 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-354; THR-496 AND GLN-503.

    Entry informationi

    Entry nameiMATK_HUMAN
    AccessioniPrimary (citable) accession number: P42679
    Secondary accession number(s): B3KNZ9, Q9NST8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 159 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3