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 02-SEP-2026, entry version 223. 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. CC TEC also regulates 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=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:61978, 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 CC TEC 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: Part of a complex composed of EEIG1, TNFRSF11A/RANK, PLCG2, CC GAB2, TEC and BTK; complex formation increases in the presence of CC TNFSF11/RANKL (By similarity). Interacts with INPP5D/SHIP1 and CC INPPL1/SHIP2. Interacts with CD28, FASLG, FGF2, GRB10, LYN and KIT. CC Interacts with VAV1 and JAK2 (By similarity). Interacts with STAC2; CC this interaction affects association with PLCG2 and subsequent PLCG2 CC phosphorylation (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:P24604}. 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_003215.3. DR PDB; 2LUL; NMR; -; A=1-154. DR AlphaFoldDB; P42680; -. DR BMRB; P42680; -. DR SMR; P42680; -. DR BioGRID; 112865; 62. DR FunCoup; P42680; 655. DR IntAct; P42680; 47. DR MINT; P42680; -. DR NDEx; IQUERY-CP-TEC; 7 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000370912; -. DR BindingDB; P42680; -. DR ChEMBL; CHEMBL4246; -. DR DrugBank; DB06616; Bosutinib. DR DrugBank; DB12010; Fostamatinib. DR DrugBank; DB14924; Ritlecitinib. DR DrugBank; DB15035; Zanubrutinib. DR DrugCentral; P42680; -. DR GuidetoPHARMACOLOGY; 2238; -. DR iPTMnet; P42680; -. DR PhosphoSitePlus; P42680; -. DR BioMuta; TEC; -. DR DMDM; 158518392; -. DR CPTAC; CPTAC-3135; -. DR CPTAC; CPTAC-3136; -. DR CPTAC; CPTAC-3137; -. DR jPOST; P42680; -. DR MassIVE; P42680; -. DR PaxDb; 9606-ENSP00000370912; -. DR PeptideAtlas; P42680; -. DR ProteomicsDB; 55526; -. DR Pumba; P42680; -. DR ABCD; P42680; 3 sequenced antibodies. DR Antibodypedia; 715; 355 antibodies from 36 providers. DR DNASU; 7006; -. DR Ensembl; ENST00000381501.8; ENSP00000370912.3; ENSG00000135605.14. DR Ensembl; ENST00000955076.1; ENSP00000625135.1; ENSG00000135605.14. DR Ensembl; ENST00000955077.1; ENSP00000625136.1; ENSG00000135605.14. DR Ensembl; ENST00000955078.1; ENSP00000625137.1; ENSG00000135605.14. 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 AGR; HGNC:11719; -. DR ClinPGx; PA36436; -. 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 OpenTargets; ENSG00000135605; -. DR VEuPathDB; HostDB:ENSG00000135605; -. DR eggNOG; KOG0197; Eukaryota. DR GeneTree; ENSGT00940000155951; -. DR HOGENOM; CLU_000288_7_2_1; -. DR InParanoid; P42680; -. DR OMA; NVTGHAH; -. DR OrthoDB; 4062651at2759; -. DR PAN-GO; P42680; 5 GO annotations based on evolutionary models. DR PhylomeDB; P42680; -. 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 Agora; ENSG00000135605; -. DR BioGRID-ORCS; 7006; 19 hits in 1180 CRISPR screens. DR ChiTaRS; TEC; human. DR EvolutionaryTrace; P42680; -. 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 primordial germ cell in gonad and 97 other cell types or tissues. DR ExpressionAtlas; P42680; baseline and differential. 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:InterPro. 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: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; IEA:Ensembl. DR CDD; cd01238; PH_Btk; 1. DR CDD; cd05114; PTKc_Tec_Rlk; 1. DR CDD; cd10396; SH2_Tec_Itk; 1. DR CDD; cd11905; SH3_Tec; 1. DR FunFam; 1.10.510.10:FF:000052; Tyrosine-protein kinase; 1. DR FunFam; 2.30.29.30:FF:000210; Tyrosine-protein kinase; 1. DR FunFam; 2.30.30.40:FF:000151; Tyrosine-protein kinase; 1. DR FunFam; 3.30.200.20:FF:000053; Tyrosine-protein kinase; 1. DR FunFam; 3.30.505.10:FF:000041; Tyrosine-protein kinase; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR050198; Non-receptor_tyrosine_kinases. 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 PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1. 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; SSF50729; PH domain-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR SUPFAM; SSF50044; SH3-domain; 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. DR PDBsum; 2LUL; -. 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 Proteomics identification; Reference proteome; SH2 domain; SH3 domain; KW Transferase; 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 //