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P42680

- TEC_HUMAN

UniProt

P42680 - TEC_HUMAN

Protein

Tyrosine-protein kinase Tec

Gene

TEC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (11 Sep 2007)
      Previous versions | rss
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    Functioni

    Non-receptor tyrosine kinase that contributes to signaling from many receptors and participates as a signal transducer in multiple downstream pathways, including regulation of the actin cytoskeleton. Plays a redundant role to ITK in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. Required for TCR-dependent IL2 gene induction. Phosphorylates DOK1, one CD28-specific substrate, and contributes to CD28-signaling. Mediates signals that negatively regulate IL2RA expression induced by TCR cross-linking. Plays a redundant role to BTK in BCR-signaling for B-cell development and activation, especially by phosphorylating STAP1, a BCR-signaling protein. Required in mast cells for efficient cytokine production. Involved in both growth and differentiation mechanisms of myeloid cells through activation by the granulocyte colony-stimulating factor CSF3, a critical cytokine to promoting the growth, differentiation, and functional activation of myeloid cells. Participates in platelet signaling downstream of integrin activation. Cooperates with JAK2 through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. GRB10, a negative modifier of the FOS activation pathway, is another substrate of TEC. TEC is involved in G protein-coupled receptor- and integrin-mediated signalings in blood platelets. Plays a role in hepatocyte proliferation and liver regeneration and is involved in HGF-induced ERK signaling pathway. TEC regulates also FGF2 unconventional secretion (endoplasmic reticulum (ER)/Golgi-independent mechanism) under various physiological conditions through phosphorylation of FGF2 'Tyr-215'. May also be involved in the regulation of osteoclast differentiation.4 Publications

    Catalytic activityi

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

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Enzyme regulationi

    Activated by tyrosine phosphorylation by a wide range of cytokine stimulations. When T-cells or B-cells receptors are activated, a series of phosphorylation leads to the recruitment of TEC to the cell membrane, where it is phosphorylated at Tyr-519. Also activated in response to SCF. Integrin engagement induces tyrosine phosphorylation of TEC in platelets. STAP1 participates in a positive feedback loop by increasing the activity of TEC. SOCS1 is an inhibitor of TEC kinase activity.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi121 – 1211ZincBy similarity
    Metal bindingi132 – 1321ZincBy similarity
    Metal bindingi133 – 1331ZincBy similarity
    Metal bindingi143 – 1431ZincBy similarity
    Binding sitei398 – 3981ATPPROSITE-ProRule annotation
    Active sitei489 – 4891Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri113 – 14937Btk-typePROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi376 – 3849ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. B cell receptor signaling pathway Source: UniProtKB
    2. Fc-epsilon receptor signaling pathway Source: Reactome
    3. innate immune response Source: Reactome
    4. integrin-mediated signaling pathway Source: UniProtKB
    5. intracellular signal transduction Source: ProtInc
    6. peptidyl-tyrosine phosphorylation Source: GOC
    7. protein phosphorylation Source: ProtInc
    8. regulation of platelet activation Source: UniProtKB
    9. tissue regeneration Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Keywords - Ligandi

    ATP-binding, Lipid-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 2681.
    ReactomeiREACT_111040. Signaling by SCF-KIT.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    SignaLinkiP42680.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Tec (EC:2.7.10.2)
    Gene namesi
    Name:TEC
    Synonyms:PSCTK4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:11719. TEC.

    Subcellular locationi

    Cytoplasm. Cell membrane; Peripheral membrane protein. Cytoplasmcytoskeleton
    Note: Following B-cell or T-cell receptors activation by antigen, translocates to the plasma membrane through its PH domain. Thrombin and integrin engagement induces translocation of TEC to the cytoskeleton during platelet activation. In cardiac myocytes, assumes a diffuse intracellular localization under basal conditions but is recruited to striated structures upon various stimuli, including ATP By similarity.By similarity

    GO - Cellular componenti

    1. cytoskeleton Source: UniProtKB
    2. cytosol Source: Reactome
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36436.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 631631Tyrosine-protein kinase TecPRO_0000088170Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei206 – 2061Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei228 – 2281Phosphotyrosine1 Publication
    Modified residuei519 – 5191Phosphotyrosine; by autocatalysis, LYN and JAK21 Publication

    Post-translational modificationi

    Following B-cell or T-cell receptors engagement, translocates to the plasma membrane where it gets phosphorylated at Tyr-519. Undergoes also tyrosine phosphorylation during platelet activation.6 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP42680.
    PaxDbiP42680.
    PRIDEiP42680.

    PTM databases

    PhosphoSiteiP42680.

    Expressioni

    Tissue specificityi

    Expressed in a wide range of cells, including hematopoietic cell lines like myeloid, B-, and T-cell lineages.

    Gene expression databases

    ArrayExpressiP42680.
    BgeeiP42680.
    CleanExiHS_TEC.
    GenevestigatoriP42680.

    Organism-specific databases

    HPAiHPA005733.

    Interactioni

    Subunit structurei

    Interacts with INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with CD28, FASLG, FGF2, GRB10, LYN and KIT. Interacts with VAV1 and JAK2 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GAB1Q134802EBI-1383480,EBI-517684
    METP085812EBI-1383480,EBI-1039152

    Protein-protein interaction databases

    BioGridi112865. 23 interactions.
    IntActiP42680. 16 interactions.
    MINTiMINT-1498364.
    STRINGi9606.ENSP00000370912.

    Structurei

    Secondary structure

    1
    631
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 1412
    Beta strandi19 – 213
    Beta strandi26 – 4116
    Beta strandi45 – 473
    Beta strandi53 – 553
    Helixi56 – 583
    Beta strandi61 – 644
    Beta strandi69 – 713
    Beta strandi74 – 763
    Beta strandi78 – 836
    Beta strandi88 – 925
    Helixi96 – 11015
    Beta strandi118 – 1203
    Beta strandi132 – 1343
    Beta strandi143 – 1453

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LULNMR-A1-154[»]
    ProteinModelPortaliP42680.
    SMRiP42680. Positions 1-154, 182-624.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 111108PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini179 – 23961SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini247 – 34599SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini370 – 623254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The PH domain mediates the binding to inositol polyphosphate and phosphoinositides, leading to its targeting to the plasma membrane. It is extended in the BTK kinase family by a region designated the TH (Tec homology) domain, which consists of about 80 residues preceding the SH3 domain.
    The SH3 domain is essential for its targeting to activated CD28 costimulatory molecule.By similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. TEC subfamily.PROSITE-ProRule annotation
    Contains 1 Btk-type zinc finger.PROSITE-ProRule annotation
    Contains 1 PH domain.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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri113 – 14937Btk-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    SH2 domain, SH3 domain, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233859.
    HOVERGENiHBG008761.
    InParanoidiP42680.
    KOiK07364.
    OMAiCTQQKPI.
    OrthoDBiEOG7KM5SC.
    PhylomeDBiP42680.
    TreeFamiTF351634.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    3.30.505.10. 1 hit.
    InterProiIPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_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.
    IPR001562. Znf_Btk_motif.
    [Graphical view]
    PfamiPF00779. BTK. 1 hit.
    PF00169. PH. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00402. TECBTKDOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00107. BTK. 1 hit.
    SM00233. PH. 1 hit.
    SM00252. 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.
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    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.
    PS51113. ZF_BTK. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P42680-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNFNTILEEI LIKRSQQKKK TSPLNYKERL FVLTKSMLTY YEGRAEKKYR    50
    KGFIDVSKIK CVEIVKNDDG VIPCQNKYPF QVVHDANTLY IFAPSPQSRD 100
    LWVKKLKEEI KNNNNIMIKY HPKFWTDGSY QCCRQTEKLA PGCEKYNLFE 150
    SSIRKALPPA PETKKRRPPP PIPLEEEDNS EEIVVAMYDF QAAEGHDLRL 200
    ERGQEYLILE KNDVHWWRAR DKYGNEGYIP SNYVTGKKSN NLDQYEWYCR 250
    NMNRSKAEQL LRSEDKEGGF MVRDSSQPGL YTVSLYTKFG GEGSSGFRHY 300
    HIKETTTSPK KYYLAEKHAF GSIPEIIEYH KHNAAGLVTR LRYPVSVKGK 350
    NAPTTAGFSY EKWEINPSEL TFMRELGSGL FGVVRLGKWR AQYKVAIKAI 400
    REGAMCEEDF IEEAKVMMKL THPKLVQLYG VCTQQKPIYI VTEFMERGCL 450
    LNFLRQRQGH FSRDVLLSMC QDVCEGMEYL ERNSFIHRDL AARNCLVSEA 500
    GVVKVSDFGM ARYVLDDQYT SSSGAKFPVK WCPPEVFNYS RFSSKSDVWS 550
    FGVLMWEVFT EGRMPFEKYT NYEVVTMVTR GHRLYQPKLA SNYVYEVMLR 600
    CWQEKPEGRP SFEDLLRTID ELVECEETFG R 631
    Length:631
    Mass (Da):73,581
    Last modified:September 11, 2007 - v2
    Checksum:iF55DECBF9916E1F9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti514 – 5141V → F in BAA06171. (PubMed:7934162)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti44 – 441R → Q.1 Publication
    Corresponds to variant rs35374286 [ dbSNP | Ensembl ].
    VAR_041850
    Natural varianti563 – 5631R → K in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041851

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D29767 mRNA. Translation: BAA06171.1.
    CH471069 Genomic DNA. Translation: EAW93055.1.
    BC101711 mRNA. Translation: AAI01712.1.
    BC101713 mRNA. Translation: AAI01714.1.
    BC143487 mRNA. Translation: AAI43488.1.
    CCDSiCCDS3481.1.
    PIRiI38268.
    I56997.
    RefSeqiNP_003206.2. NM_003215.2.
    UniGeneiHs.479670.

    Genome annotation databases

    EnsembliENST00000381501; ENSP00000370912; ENSG00000135605.
    GeneIDi7006.
    KEGGihsa:7006.
    UCSCiuc003gxz.3. human.

    Polymorphism databases

    DMDMi158518392.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D29767 mRNA. Translation: BAA06171.1 .
    CH471069 Genomic DNA. Translation: EAW93055.1 .
    BC101711 mRNA. Translation: AAI01712.1 .
    BC101713 mRNA. Translation: AAI01714.1 .
    BC143487 mRNA. Translation: AAI43488.1 .
    CCDSi CCDS3481.1.
    PIRi I38268.
    I56997.
    RefSeqi NP_003206.2. NM_003215.2.
    UniGenei Hs.479670.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LUL NMR - A 1-154 [» ]
    ProteinModelPortali P42680.
    SMRi P42680. Positions 1-154, 182-624.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112865. 23 interactions.
    IntActi P42680. 16 interactions.
    MINTi MINT-1498364.
    STRINGi 9606.ENSP00000370912.

    Chemistry

    BindingDBi P42680.
    ChEMBLi CHEMBL4246.
    GuidetoPHARMACOLOGYi 2238.

    PTM databases

    PhosphoSitei P42680.

    Polymorphism databases

    DMDMi 158518392.

    Proteomic databases

    MaxQBi P42680.
    PaxDbi P42680.
    PRIDEi P42680.

    Protocols and materials databases

    DNASUi 7006.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381501 ; ENSP00000370912 ; ENSG00000135605 .
    GeneIDi 7006.
    KEGGi hsa:7006.
    UCSCi uc003gxz.3. human.

    Organism-specific databases

    CTDi 7006.
    GeneCardsi GC04M048137.
    HGNCi HGNC:11719. TEC.
    HPAi HPA005733.
    MIMi 600583. gene.
    neXtProti NX_P42680.
    PharmGKBi PA36436.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233859.
    HOVERGENi HBG008761.
    InParanoidi P42680.
    KOi K07364.
    OMAi CTQQKPI.
    OrthoDBi EOG7KM5SC.
    PhylomeDBi P42680.
    TreeFami TF351634.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_111040. Signaling by SCF-KIT.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    SignaLinki P42680.

    Miscellaneous databases

    GeneWikii TEC_(gene).
    GenomeRNAii 7006.
    NextBioi 27366.
    PROi P42680.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42680.
    Bgeei P42680.
    CleanExi HS_TEC.
    Genevestigatori P42680.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    3.30.505.10. 1 hit.
    InterProi IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_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.
    IPR001562. Znf_Btk_motif.
    [Graphical view ]
    Pfami PF00779. BTK. 1 hit.
    PF00169. PH. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00402. TECBTKDOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00107. BTK. 1 hit.
    SM00233. PH. 1 hit.
    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 PS50003. PH_DOMAIN. 1 hit.
    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.
    PS51113. ZF_BTK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and analysis of the human Tec protein-tyrosine kinase."
      Sato K., Mano H., Ariyama T., Inazawa J., Yazaki Y., Hirai H.
      Leukemia 8:1663-1672(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Blood.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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].
      Tissue: Liver.
    4. "Identification of phosphorylation sites within the SH3 domains of Tec family tyrosine kinases."
      Nore B.F., Mattsson P.T., Antonsson P., Backesjo C.-M., Westlund A., Lennartsson J., Hansson H., Low P., Ronnstrand L., Smith C.I.E.
      Biochim. Biophys. Acta 1645:123-132(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 203-206, PHOSPHORYLATION AT TYR-206.
    5. "Tec kinase associates with c-kit and is tyrosine phosphorylated and activated following stem cell factor binding."
      Tang B., Mano H., Yi T., Ihle J.N.
      Mol. Cell. Biol. 14:8432-8437(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH KIT, ENZYME REGULATION.
    6. "Integrin-dependent tyrosine phosphorylation and cytoskeletal translocation of Tec in thrombin-activated platelets."
      Laffargue M., Monnereau L., Tuech J., Ragab A., Ragab-Thomas J., Payrastre B., Raynal P., Chap H.
      Biochem. Biophys. Res. Commun. 238:247-251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
    7. Cited for: ENZYME REGULATION.
    8. Cited for: INTERACTION WITH GRB10, FUNCTION IN PHOSPHORYLATION OF GRB10.
    9. "Tec is involved in G protein-coupled receptor- and integrin-mediated signalings in human blood platelets."
      Hamazaki Y., Kojima H., Mano H., Nagata Y., Todokoro K., Abe T., Nagasawa T.
      Oncogene 16:2773-2779(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, ENZYME REGULATION, SUBCELLULAR LOCATION.
    10. "Molecular cloning of a docking protein, BRDG1, that acts downstream of the Tec tyrosine kinase."
      Ohya K., Kajigaya S., Kitanaka A., Yoshida K., Miyazato A., Yamashita Y., Yamanaka T., Ikeda U., Shimada K., Ozawa K., Mano H.
      Proc. Natl. Acad. Sci. U.S.A. 96:11976-11981(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF STAP1, ENZYME REGULATION.
    11. "SHIP family inositol phosphatases interact with and negatively regulate the Tec tyrosine kinase."
      Tomlinson M.G., Heath V.L., Turck C.W., Watson S.P., Weiss A.
      J. Biol. Chem. 279:55089-55096(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D AND INPPL1.
    12. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-206 AND TYR-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-519, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Tec protein tyrosine kinase inhibits CD25 expression in human T-lymphocyte."
      Susaki K., Kitanaka A., Dobashi H., Kubota Y., Kittaka K., Kameda T., Yamaoka G., Mano H., Mihara K., Ishida T.
      Immunol. Lett. 127:135-142(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Tec-kinase-mediated phosphorylation of fibroblast growth factor 2 is essential for unconventional secretion."
      Ebert A.D., Laussmann M., Wegehingel S., Kaderali L., Erfle H., Reichert J., Lechner J., Beer H.D., Pepperkok R., Nickel W.
      Traffic 11:813-826(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF FGF2, INTERACTION WITH FGF2.
    17. "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] GLN-44 AND LYS-563.

    Entry informationi

    Entry nameiTEC_HUMAN
    AccessioniPrimary (citable) accession number: P42680
    Secondary accession number(s): B7ZKZ6, Q3MIS5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 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

    Caution

    It is uncertain whether Met-1 is the initiator.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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