TEC_HUMAN
ID TEC_HUMAN Reviewed; 631 AA.
AC P42680; B7ZKZ6; Q3MIS5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Tyrosine-protein kinase Tec;
DE EC=2.7.10.2;
GN Name=TEC; Synonyms=PSCTK4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=7934162;
RA Sato K., Mano H., Ariyama T., Inazawa J., Yazaki Y., Hirai H.;
RT "Molecular cloning and analysis of the human Tec protein-tyrosine kinase.";
RL Leukemia 8:1663-1672(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 203-206, AND PHOSPHORYLATION AT TYR-206.
RX PubMed=12573241; DOI=10.1016/s1570-9639(02)00524-1;
RA Nore B.F., Mattsson P.T., Antonsson P., Backesjo C.-M., Westlund A.,
RA Lennartsson J., Hansson H., Low P., Ronnstrand L., Smith C.I.E.;
RT "Identification of phosphorylation sites within the SH3 domains of Tec
RT family tyrosine kinases.";
RL Biochim. Biophys. Acta 1645:123-132(2003).
RN [5]
RP PHOSPHORYLATION, INTERACTION WITH KIT, AND ACTIVITY REGULATION.
RX PubMed=7526158; DOI=10.1128/mcb.14.12.8432-8437.1994;
RA Tang B., Mano H., Yi T., Ihle J.N.;
RT "Tec kinase associates with c-kit and is tyrosine phosphorylated and
RT activated following stem cell factor binding.";
RL Mol. Cell. Biol. 14:8432-8437(1994).
RN [6]
RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=9299487; DOI=10.1006/bbrc.1997.7269;
RA Laffargue M., Monnereau L., Tuech J., Ragab A., Ragab-Thomas J.,
RA Payrastre B., Raynal P., Chap H.;
RT "Integrin-dependent tyrosine phosphorylation and cytoskeletal translocation
RT of Tec in thrombin-activated platelets.";
RL Biochem. Biophys. Res. Commun. 238:247-251(1997).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=9341160; DOI=10.1074/jbc.272.43.27178;
RA Ohya K., Kajigaya S., Yamashita Y., Miyazato A., Hatake K., Miura Y.,
RA Ikeda U., Shimada K., Ozawa K., Mano H.;
RT "SOCS-1/JAB/SSI-1 can bind to and suppress Tec protein-tyrosine kinase.";
RL J. Biol. Chem. 272:27178-27182(1997).
RN [8]
RP INTERACTION WITH GRB10, AND FUNCTION IN PHOSPHORYLATION OF GRB10.
RX PubMed=9753425; DOI=10.1046/j.1365-2443.1998.00201.x;
RA Mano H., Ohya K., Miyazato A., Yamashita Y., Ogawa W., Inazawa J.,
RA Ikeda U., Shimada K., Hatake K., Kasuga M., Ozawa K., Kajigaya S.;
RT "Grb10/GrbIR as an in vivo substrate of Tec tyrosine kinase.";
RL Genes Cells 3:431-441(1998).
RN [9]
RP PHOSPHORYLATION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=9652744; DOI=10.1038/sj.onc.1201799;
RA Hamazaki Y., Kojima H., Mano H., Nagata Y., Todokoro K., Abe T.,
RA Nagasawa T.;
RT "Tec is involved in G protein-coupled receptor- and integrin-mediated
RT signalings in human blood platelets.";
RL Oncogene 16:2773-2779(1998).
RN [10]
RP FUNCTION IN PHOSPHORYLATION OF STAP1, AND ACTIVITY REGULATION.
RX PubMed=10518561; DOI=10.1073/pnas.96.21.11976;
RA Ohya K., Kajigaya S., Kitanaka A., Yoshida K., Miyazato A., Yamashita Y.,
RA Yamanaka T., Ikeda U., Shimada K., Ozawa K., Mano H.;
RT "Molecular cloning of a docking protein, BRDG1, that acts downstream of the
RT Tec tyrosine kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11976-11981(1999).
RN [11]
RP INTERACTION WITH INPP5D AND INPPL1.
RX PubMed=15492005; DOI=10.1074/jbc.m408141200;
RA Tomlinson M.G., Heath V.L., Turck C.W., Watson S.P., Weiss A.;
RT "SHIP family inositol phosphatases interact with and negatively regulate
RT the Tec tyrosine kinase.";
RL J. Biol. Chem. 279:55089-55096(2004).
RN [12]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-206 AND TYR-228, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-519, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP FUNCTION.
RX PubMed=19883687; DOI=10.1016/j.imlet.2009.10.009;
RA Susaki K., Kitanaka A., Dobashi H., Kubota Y., Kittaka K., Kameda T.,
RA Yamaoka G., Mano H., Mihara K., Ishida T.;
RT "Tec protein tyrosine kinase inhibits CD25 expression in human T-
RT lymphocyte.";
RL Immunol. Lett. 127:135-142(2010).
RN [16]
RP FUNCTION IN PHOSPHORYLATION OF FGF2, AND INTERACTION WITH FGF2.
RX PubMed=20230531; DOI=10.1111/j.1600-0854.2010.01059.x;
RA Ebert A.D., Laussmann M., Wegehingel S., Kaderali L., Erfle H.,
RA Reichert J., Lechner J., Beer H.D., Pepperkok R., Nickel W.;
RT "Tec-kinase-mediated phosphorylation of fibroblast growth factor 2 is
RT essential for unconventional secretion.";
RL Traffic 11:813-826(2010).
RN [17]
RP VARIANTS [LARGE SCALE ANALYSIS] GLN-44 AND LYS-563.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Non-receptor tyrosine kinase that contributes to signaling
CC from many receptors and participates as a signal transducer in multiple
CC downstream pathways, including regulation of the actin cytoskeleton.
CC Plays a redundant role to ITK in regulation of the adaptive immune
CC response. Regulates the development, function and differentiation of
CC conventional T-cells and nonconventional NKT-cells. Required for TCR-
CC dependent IL2 gene induction. Phosphorylates DOK1, one CD28-specific
CC substrate, and contributes to CD28-signaling. Mediates signals that
CC negatively regulate IL2RA expression induced by TCR cross-linking.
CC Plays a redundant role to BTK in BCR-signaling for B-cell development
CC and activation, especially by phosphorylating STAP1, a BCR-signaling
CC protein. Required in mast cells for efficient cytokine production.
CC Involved in both growth and differentiation mechanisms of myeloid cells
CC through activation by the granulocyte colony-stimulating factor CSF3, a
CC critical cytokine to promoting the growth, differentiation, and
CC functional activation of myeloid cells. Participates in platelet
CC signaling downstream of integrin activation. Cooperates with JAK2
CC through reciprocal phosphorylation to mediate cytokine-driven
CC activation of FOS transcription. GRB10, a negative modifier of the FOS
CC activation pathway, is another substrate of TEC. TEC is involved in G
CC protein-coupled receptor- and integrin-mediated signalings in blood
CC platelets. Plays a role in hepatocyte proliferation and liver
CC regeneration and is involved in HGF-induced ERK signaling pathway. TEC
CC regulates also FGF2 unconventional secretion (endoplasmic reticulum
CC (ER)/Golgi-independent mechanism) under various physiological
CC conditions through phosphorylation of FGF2 'Tyr-215'. May also be
CC involved in the regulation of osteoclast differentiation.
CC {ECO:0000269|PubMed:10518561, ECO:0000269|PubMed:19883687,
CC ECO:0000269|PubMed:20230531, ECO:0000269|PubMed:9753425}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by tyrosine phosphorylation by a wide
CC range of cytokine stimulations. When T-cells or B-cells receptors are
CC activated, a series of phosphorylation leads to the recruitment of TEC
CC to the cell membrane, where it is phosphorylated at Tyr-519. Also
CC activated in response to SCF. Integrin engagement induces tyrosine
CC phosphorylation of TEC in platelets. STAP1 participates in a positive
CC feedback loop by increasing the activity of TEC. SOCS1 is an inhibitor
CC of TEC kinase activity. {ECO:0000269|PubMed:10518561,
CC ECO:0000269|PubMed:7526158, ECO:0000269|PubMed:9341160,
CC ECO:0000269|PubMed:9652744}.
CC -!- SUBUNIT: Interacts with INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with
CC CD28, FASLG, FGF2, GRB10, LYN and KIT. Interacts with VAV1 and JAK2 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P42680; P78325: ADAM8; NbExp=2; IntAct=EBI-1383480, EBI-2625954;
CC P42680; Q13480: GAB1; NbExp=2; IntAct=EBI-1383480, EBI-517684;
CC P42680; P08581: MET; NbExp=2; IntAct=EBI-1383480, EBI-1039152;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC protein. Cytoplasm, cytoskeleton. Note=Following B-cell or T-cell
CC receptors activation by antigen, translocates to the plasma membrane
CC through its PH domain. Thrombin and integrin engagement induces
CC translocation of TEC to the cytoskeleton during platelet activation. In
CC cardiac myocytes, assumes a diffuse intracellular localization under
CC basal conditions but is recruited to striated structures upon various
CC stimuli, including ATP (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in a wide range of cells, including
CC hematopoietic cell lines like myeloid, B-, and T-cell lineages.
CC -!- DOMAIN: The PH domain mediates the binding to inositol polyphosphate
CC and phosphoinositides, leading to its targeting to the plasma membrane.
CC It is extended in the BTK kinase family by a region designated the TH
CC (Tec homology) domain, which consists of about 80 residues preceding
CC the SH3 domain.
CC -!- DOMAIN: The SH3 domain is essential for its targeting to activated CD28
CC costimulatory molecule. {ECO:0000250}.
CC -!- PTM: Following B-cell or T-cell receptors engagement, translocates to
CC the plasma membrane where it gets phosphorylated at Tyr-519. Undergoes
CC also tyrosine phosphorylation during platelet activation.
CC {ECO:0000269|PubMed:12573241, ECO:0000269|PubMed:7526158,
CC ECO:0000269|PubMed:9299487, ECO:0000269|PubMed:9652744}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. TEC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: It is uncertain whether Met-1 is the initiator. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D29767; BAA06171.1; -; mRNA.
DR EMBL; CH471069; EAW93055.1; -; Genomic_DNA.
DR EMBL; BC101711; AAI01712.1; -; mRNA.
DR EMBL; BC101713; AAI01714.1; -; mRNA.
DR EMBL; BC143487; AAI43488.1; -; mRNA.
DR CCDS; CCDS3481.1; -.
DR PIR; I38268; I38268.
DR PIR; I56997; I56997.
DR RefSeq; NP_003206.2; NM_003215.2.
DR PDB; 2LUL; NMR; -; A=1-154.
DR PDBsum; 2LUL; -.
DR AlphaFoldDB; P42680; -.
DR BMRB; P42680; -.
DR SMR; P42680; -.
DR BioGRID; 112865; 33.
DR IntAct; P42680; 38.
DR MINT; P42680; -.
DR STRING; 9606.ENSP00000370912; -.
DR BindingDB; P42680; -.
DR ChEMBL; CHEMBL4246; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB15035; Zanubrutinib.
DR DrugCentral; P42680; -.
DR GuidetoPHARMACOLOGY; 2238; -.
DR iPTMnet; P42680; -.
DR PhosphoSitePlus; P42680; -.
DR BioMuta; TEC; -.
DR DMDM; 158518392; -.
DR EPD; P42680; -.
DR jPOST; P42680; -.
DR MassIVE; P42680; -.
DR MaxQB; P42680; -.
DR PaxDb; P42680; -.
DR PeptideAtlas; P42680; -.
DR PRIDE; P42680; -.
DR ProteomicsDB; 55526; -.
DR ABCD; P42680; 3 sequenced antibodies.
DR Antibodypedia; 715; 351 antibodies from 33 providers.
DR DNASU; 7006; -.
DR Ensembl; ENST00000381501.8; ENSP00000370912.3; ENSG00000135605.13.
DR GeneID; 7006; -.
DR KEGG; hsa:7006; -.
DR MANE-Select; ENST00000381501.8; ENSP00000370912.3; NM_003215.3; NP_003206.2.
DR UCSC; uc003gxz.4; human.
DR CTD; 7006; -.
DR DisGeNET; 7006; -.
DR GeneCards; TEC; -.
DR HGNC; HGNC:11719; TEC.
DR HPA; ENSG00000135605; Low tissue specificity.
DR MalaCards; TEC; -.
DR MIM; 600583; gene.
DR neXtProt; NX_P42680; -.
DR OpenTargets; ENSG00000135605; -.
DR PharmGKB; PA36436; -.
DR VEuPathDB; HostDB:ENSG00000135605; -.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000155951; -.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; P42680; -.
DR OMA; PEVIEYH; -.
DR OrthoDB; 1047190at2759; -.
DR PhylomeDB; P42680; -.
DR TreeFam; TF351634; -.
DR BRENDA; 2.7.10.2; 2681.
DR PathwayCommons; P42680; -.
DR Reactome; R-HSA-1433557; Signaling by SCF-KIT.
DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-HSA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR SignaLink; P42680; -.
DR SIGNOR; P42680; -.
DR BioGRID-ORCS; 7006; 14 hits in 1100 CRISPR screens.
DR ChiTaRS; TEC; human.
DR GeneWiki; TEC_(gene); -.
DR GenomeRNAi; 7006; -.
DR Pharos; P42680; Tchem.
DR PRO; PR:P42680; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P42680; protein.
DR Bgee; ENSG00000135605; Expressed in lower esophagus mucosa and 95 other tissues.
DR ExpressionAtlas; P42680; baseline and differential.
DR Genevisible; P42680; HS.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; NAS:BHF-UCL.
DR GO; GO:0043621; F:protein self-association; IPI:BHF-UCL.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IBA:GO_Central.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0010543; P:regulation of platelet activation; IDA:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0042246; P:tissue regeneration; IBA:GO_Central.
DR CDD; cd11905; SH3_Tec; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035572; Tec_SH3.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR001562; Znf_Btk_motif.
DR Pfam; PF00779; BTK; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00402; TECBTKDOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00107; BTK; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51113; ZF_BTK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; ATP-binding; Cell membrane; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Immunity; Kinase; Lipid-binding;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; SH2 domain; SH3 domain; Transferase;
KW Tyrosine-protein kinase; Zinc; Zinc-finger.
FT CHAIN 1..631
FT /note="Tyrosine-protein kinase Tec"
FT /id="PRO_0000088170"
FT DOMAIN 4..111
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 179..239
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 247..345
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 370..623
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 113..149
FT /note="Btk-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT REGION 157..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 489
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 376..384
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 206
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12573241,
FT ECO:0007744|PubMed:19369195"
FT MOD_RES 228
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 519
FT /note="Phosphotyrosine; by autocatalysis, LYN and JAK2"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VARIANT 44
FT /note="R -> Q (in dbSNP:rs35374286)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041850"
FT VARIANT 563
FT /note="R -> K (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041851"
FT CONFLICT 514
FT /note="V -> F (in Ref. 1; BAA06171)"
FT /evidence="ECO:0000305"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:2LUL"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2LUL"
FT STRAND 26..41
FT /evidence="ECO:0007829|PDB:2LUL"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2LUL"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2LUL"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2LUL"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2LUL"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2LUL"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2LUL"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2LUL"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2LUL"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:2LUL"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2LUL"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2LUL"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:2LUL"
SQ SEQUENCE 631 AA; 73581 MW; F55DECBF9916E1F9 CRC64;
MNFNTILEEI LIKRSQQKKK TSPLNYKERL FVLTKSMLTY YEGRAEKKYR KGFIDVSKIK
CVEIVKNDDG VIPCQNKYPF QVVHDANTLY IFAPSPQSRD LWVKKLKEEI KNNNNIMIKY
HPKFWTDGSY QCCRQTEKLA PGCEKYNLFE SSIRKALPPA PETKKRRPPP PIPLEEEDNS
EEIVVAMYDF QAAEGHDLRL ERGQEYLILE KNDVHWWRAR DKYGNEGYIP SNYVTGKKSN
NLDQYEWYCR NMNRSKAEQL LRSEDKEGGF MVRDSSQPGL YTVSLYTKFG GEGSSGFRHY
HIKETTTSPK KYYLAEKHAF GSIPEIIEYH KHNAAGLVTR LRYPVSVKGK NAPTTAGFSY
EKWEINPSEL TFMRELGSGL FGVVRLGKWR AQYKVAIKAI REGAMCEEDF IEEAKVMMKL
THPKLVQLYG VCTQQKPIYI VTEFMERGCL LNFLRQRQGH FSRDVLLSMC QDVCEGMEYL
ERNSFIHRDL AARNCLVSEA GVVKVSDFGM ARYVLDDQYT SSSGAKFPVK WCPPEVFNYS
RFSSKSDVWS FGVLMWEVFT EGRMPFEKYT NYEVVTMVTR GHRLYQPKLA SNYVYEVMLR
CWQEKPEGRP SFEDLLRTID ELVECEETFG R
