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Tyrosine-protein kinase ITK/TSK (EC 2.7.10.2) (Interleukin-2-inducible T-cell kinase) (IL-2-inducible T-cell kinase) (Kinase EMT) (T-cell-specific kinase) (Tyrosine-protein kinase Lyk)

 ITK_HUMAN               Reviewed;         620 AA.
Q08881; B2R752; Q32ML7;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
18-JUL-2018, entry version 198.
RecName: Full=Tyrosine-protein kinase ITK/TSK;
EC=2.7.10.2;
AltName: Full=Interleukin-2-inducible T-cell kinase;
Short=IL-2-inducible T-cell kinase;
AltName: Full=Kinase EMT;
AltName: Full=T-cell-specific kinase;
AltName: Full=Tyrosine-protein kinase Lyk;
Name=ITK; Synonyms=EMT, LYK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
PubMed=8504851; DOI=10.1016/0014-5793(93)81520-A;
Tanaka N., Asao H., Ohtani K., Nakamura M., Sugamura K.;
"A novel human tyrosine kinase gene inducible in T cells by
interleukin 2.";
FEBS Lett. 324:1-5(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thymus;
PubMed=8364206;
Gibson S., Leung B., Squire J.A., Hill M., Arima N., Goss P., Hogg D.,
Mills G.B.;
"Identification, cloning, and characterization of a novel human T-
cell-specific tyrosine kinase located at the hematopoietin complex on
chromosome 5q.";
Blood 82:1561-1572(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 171-192, AND PHOSPHORYLATION AT TYR-180.
PubMed=12573241; DOI=10.1016/S1570-9639(02)00524-1;
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.;
"Identification of phosphorylation sites within the SH3 domains of Tec
family tyrosine kinases.";
Biochim. Biophys. Acta 1645:123-132(2003).
[7]
PHOSPHORYLATION BY LCK.
PubMed=9312162; DOI=10.1074/jbc.272.40.25401;
Heyeck S.D., Wilcox H.M., Bunnell S.C., Berg L.J.;
"Lck phosphorylates the activation loop tyrosine of the Itk kinase
domain and activates Itk kinase activity.";
J. Biol. Chem. 272:25401-25408(1997).
[8]
INDUCTION.
PubMed=9701039; DOI=10.1093/intimm/10.7.1009;
King P.D., Sadra A., Teng J.M., Bell G.M., Dupont B.;
"CD2-mediated activation of the Tec-family tyrosine kinase ITK is
controlled by proline-rich stretch-4 of the CD2 cytoplasmic tail.";
Int. Immunol. 10:1009-1016(1998).
[9]
DOMAIN.
PubMed=10795735; DOI=10.1016/S1074-7613(00)80189-2;
Yang W.C., Collette Y., Nunes J.A., Olive D.;
"Tec kinases: a family with multiple roles in immunity.";
Immunity 12:373-382(2000).
[10]
FUNCTION IN PHOSPHORYLATION OF LAT.
PubMed=12186560; DOI=10.1021/bi025554o;
Perez-Villar J.J., Whitney G.S., Sitnick M.T., Dunn R.J.,
Venkatesan S., O'Day K., Schieven G.L., Lin T.A., Kanner S.B.;
"Phosphorylation of the linker for activation of T-cells by Itk
promotes recruitment of Vav.";
Biochemistry 41:10732-10740(2002).
[11]
FUNCTION.
PubMed=12682224; DOI=10.4049/jimmunol.170.8.3971;
Grasis J.A., Browne C.D., Tsoukas C.D.;
"Inducible T cell tyrosine kinase regulates actin-dependent
cytoskeletal events induced by the T cell antigen receptor.";
J. Immunol. 170:3971-3976(2003).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[13]
INTERACTION WITH PPIA/CYPA, AND MUTAGENESIS OF PRO-288.
PubMed=15308100; DOI=10.1016/j.immuni.2004.07.005;
Colgan J., Asmal M., Neagu M., Yu B., Schneidkraut J., Lee Y.,
Sokolskaja E., Andreotti A., Luban J.;
"Cyclophilin A regulates TCR signal strength in CD4+ T cells via a
proline-directed conformational switch in Itk.";
Immunity 21:189-201(2004).
[14]
INTERACTION WITH VAV1.
PubMed=15661896; DOI=10.4049/jimmunol.174.3.1385;
Dombroski D., Houghtling R.A., Labno C.M., Precht P., Takesono A.,
Caplen N.J., Billadeau D.D., Wange R.L., Burkhardt J.K.,
Schwartzberg P.L.;
"Kinase-independent functions for Itk in TCR-induced regulation of Vav
and the actin cytoskeleton.";
J. Immunol. 174:1385-1392(2005).
[15]
SUBCELLULAR LOCATION.
PubMed=17060314; DOI=10.1074/jbc.M609180200;
Qi Q., Sahu N., August A.;
"Tec kinase Itk forms membrane clusters specifically in the vicinity
of recruiting receptors.";
J. Biol. Chem. 281:38529-38534(2006).
[16]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[17]
AUTOPHOSPHORYLATION.
PubMed=19523959; DOI=10.1016/j.jmb.2009.06.023;
Joseph R.E., Severin A., Min L., Fulton D.B., Andreotti A.H.;
"SH2-dependent autophosphorylation within the Tec family kinase Itk.";
J. Mol. Biol. 391:164-177(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-512 AND SER-565, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
UBIQUITINATION.
PubMed=20596523; DOI=10.1371/journal.pone.0011332;
Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B.,
Spruck C.;
"Development and validation of a method for profiling post-
translational modification activities using protein microarrays.";
PLoS ONE 5:E11332-E11332(2010).
[20]
FUNCTION IN PHOSPHORYLATION OF LCP2.
PubMed=21725281; DOI=10.1038/emboj.2011.213;
Sela M., Bogin Y., Beach D., Oellerich T., Lehne J.,
Smith-Garvin J.E., Okumura M., Starosvetsky E., Kosoff R., Libman E.,
Koretzky G., Kambayashi T., Urlaub H., Wienands J., Chernoff J.,
Yablonski D.;
"Sequential phosphorylation of SLP-76 at tyrosine 173 is required for
activation of T and mast cells.";
EMBO J. 30:3160-3172(2011).
[21]
STRUCTURE BY NMR OF 113-239.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the BTK motif and the SH3 domain of tyrosine-
protein kinase ITK from human.";
Submitted (OCT-2007) to the PDB data bank.
[22]
VARIANTS [LARGE SCALE ANALYSIS] LYS-19; LEU-23; GLN-451; TRP-581 AND
ILE-587.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[23]
VARIANT LPFS1 TRP-335, AND CHARACTERIZATION OF VARIANT LPSA1 TRP-335.
PubMed=19425169; DOI=10.1172/JCI37901;
Huck K., Feyen O., Niehues T., Rueschendorf F., Huebner N.,
Laws H.-J., Telieps T., Knapp S., Wacker H.-H., Meindl A., Jumaa H.,
Borkhardt A.;
"Girls homozygous for an IL-2-inducible T cell kinase mutation that
leads to protein deficiency develop fatal EBV-associated
lymphoproliferation.";
J. Clin. Invest. 119:1350-1358(2009).
-!- FUNCTION: Tyrosine kinase that plays an essential role in
regulation of the adaptive immune response. Regulates the
development, function and differentiation of conventional T-cells
and nonconventional NKT-cells. When antigen presenting cells (APC)
activate T-cell receptor (TCR), a series of phosphorylation lead
to the recruitment of ITK to the cell membrane, in the vicinity of
the stimulated TCR receptor, where it is phosphorylated by LCK.
Phosphorylation leads to ITK autophosphorylation and full
activation. Once activated, phosphorylates PLCG1, leading to the
activation of this lipase and subsequent cleavage of its
substrates. In turn, the endoplasmic reticulum releases calcium in
the cytoplasm and the nuclear activator of activated T-cells
(NFAT) translocates into the nucleus to perform its
transcriptional duty. Phosphorylates 2 essential adapter proteins:
the linker for activation of T-cells/LAT protein and LCP2. Then, a
large number of signaling molecules such as VAV1 are recruited and
ultimately lead to lymphokine production, T-cell proliferation and
differentiation (PubMed:12186560, PubMed:12682224,
PubMed:21725281). Phosphorylates TBX21 at 'Tyr-530' and mediates
its interaction with GATA3 (By similarity).
{ECO:0000250|UniProtKB:Q03526, ECO:0000269|PubMed:12186560,
ECO:0000269|PubMed:12682224, ECO:0000269|PubMed:21725281}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Homooligomerizes; this association negatively regulates
kinase activity (By similarity). Interacts with PPIA/CYPA; this
interaction regulates TCR signal strength via a proline-directed
conformational switch in ITK. Interacts with THEMIS (By
similarity). Interacts with FASLG. Interacts with VAV1; this
interaction is important for VAV1 localization and TCR-induced
actin polarization. Interacts with TBX21 (By similarity).
{ECO:0000250|UniProtKB:Q03526, ECO:0000269|PubMed:15308100,
ECO:0000269|PubMed:15661896, ECO:0000269|PubMed:19807924}.
-!- INTERACTION:
P04626:ERBB2; NbExp=2; IntAct=EBI-968552, EBI-641062;
P48023:FASLG; NbExp=3; IntAct=EBI-968552, EBI-495538;
Q13094:LCP2; NbExp=4; IntAct=EBI-968552, EBI-346946;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17060314}.
Nucleus {ECO:0000250|UniProtKB:Q03526}. Note=Localizes in the
vicinity of cell surface receptors in the plasma membrane after
receptor stimulation.
-!- TISSUE SPECIFICITY: T-cell lines and natural killer cell lines.
-!- INDUCTION: Through a myriad of surface receptors including the
TCR/CD3 signaling complex, coreceptors, or chemokine receptors.
{ECO:0000269|PubMed:8504851, ECO:0000269|PubMed:9701039}.
-!- DOMAIN: The N-terminal PH domain allows ITK to be recruited to the
plasma membrane by an activated PI3 kinase. This domain contains
also a proline-rich region (PRR). The adjoining domain is a SH3
domain, which binds to PRR (from itself or from other proteins).
Next, a SH2 domain is required for binding tyrosine-phosphorylated
substrates. In the C-terminal region, the kinase domain is
required for tyrosine phosphorylation.
{ECO:0000269|PubMed:10795735}.
-!- PTM: Phosphorylated at Tyr-512 in the activation loop of the
kinase domain by LCK. Subsequent autophosphorylation at Tyr-180
leads to the kinase activation. The autophosphorylated Tyr-180
lies within the substrate binding sequence of the SH3 domain.
{ECO:0000269|PubMed:12573241, ECO:0000269|PubMed:9312162}.
-!- PTM: Ubiquitinated. {ECO:0000269|PubMed:20596523}.
-!- DISEASE: Lymphoproliferative syndrome 1 (LPFS1) [MIM:613011]: A
rare immunodeficiency characterized by extreme susceptibility to
infection with Epstein-Barr virus (EBV). Inadequate immune
response to EBV can have a fatal outcome. Clinical features
include splenomegaly, lymphadenopathy, anemia, thrombocytopenia,
pancytopenia, recurrent infections. There is an increased risk for
lymphoma. {ECO:0000269|PubMed:19425169}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. TEC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ITKID43329ch5q33.html";
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EMBL; D13720; BAA02873.1; -; mRNA.
EMBL; L10717; AAA36748.1; -; mRNA.
EMBL; S65186; AAB28072.2; -; mRNA.
EMBL; AK312846; BAG35699.1; -; mRNA.
EMBL; CH471062; EAW61608.1; -; Genomic_DNA.
EMBL; BC109077; AAI09078.1; -; mRNA.
EMBL; BC109078; AAI09079.1; -; mRNA.
CCDS; CCDS4336.1; -.
PIR; S33253; S33253.
RefSeq; NP_005537.3; NM_005546.3.
UniGene; Hs.558348; -.
PDB; 1SM2; X-ray; 2.30 A; A/B=357-620.
PDB; 1SNU; X-ray; 2.50 A; A/B=357-620.
PDB; 1SNX; X-ray; 3.20 A; A/B=357-620.
PDB; 2E6I; NMR; -; A=113-169.
PDB; 2LMJ; NMR; -; A=171-231.
PDB; 2YUQ; NMR; -; A=162-239.
PDB; 3MIY; X-ray; 1.67 A; A/B=357-620.
PDB; 3MJ1; X-ray; 1.72 A; A=357-620.
PDB; 3MJ2; X-ray; 1.90 A; A=357-620.
PDB; 3QGW; X-ray; 2.10 A; A/B=357-620.
PDB; 3QGY; X-ray; 2.10 A; A/B=357-620.
PDB; 3T9T; X-ray; 1.65 A; A=354-620.
PDB; 3V5J; X-ray; 2.59 A; A/B=357-620.
PDB; 3V5L; X-ray; 1.86 A; A/B/C/D=357-620.
PDB; 3V8T; X-ray; 2.00 A; A/B=357-620.
PDB; 3V8W; X-ray; 2.27 A; A/B=357-620.
PDB; 4HCT; X-ray; 1.48 A; A=354-620.
PDB; 4HCU; X-ray; 1.43 A; A=354-620.
PDB; 4HCV; X-ray; 1.48 A; A=354-620.
PDB; 4KIO; X-ray; 2.18 A; A/B/C/D=357-620.
PDB; 4L7S; X-ray; 2.03 A; A/B=357-620.
PDB; 4M0Y; X-ray; 1.70 A; A=354-620.
PDB; 4M0Z; X-ray; 2.00 A; A=354-620.
PDB; 4M12; X-ray; 2.15 A; A=354-620.
PDB; 4M13; X-ray; 1.85 A; A=354-620.
PDB; 4M14; X-ray; 1.55 A; A=354-620.
PDB; 4M15; X-ray; 1.52 A; A=354-620.
PDB; 4MF0; X-ray; 2.67 A; A/B=357-620.
PDB; 4MF1; X-ray; 2.11 A; A/B=357-620.
PDB; 4PP9; X-ray; 2.58 A; A/B=357-620.
PDB; 4PPA; X-ray; 2.67 A; A/B=357-620.
PDB; 4PPB; X-ray; 2.82 A; A/B=357-620.
PDB; 4PPC; X-ray; 2.95 A; A/B=357-620.
PDB; 4PQN; X-ray; 1.71 A; A=357-620.
PDB; 4QD6; X-ray; 2.45 A; A/B=357-620.
PDB; 4RFM; X-ray; 2.10 A; A=357-620.
PDBsum; 1SM2; -.
PDBsum; 1SNU; -.
PDBsum; 1SNX; -.
PDBsum; 2E6I; -.
PDBsum; 2LMJ; -.
PDBsum; 2YUQ; -.
PDBsum; 3MIY; -.
PDBsum; 3MJ1; -.
PDBsum; 3MJ2; -.
PDBsum; 3QGW; -.
PDBsum; 3QGY; -.
PDBsum; 3T9T; -.
PDBsum; 3V5J; -.
PDBsum; 3V5L; -.
PDBsum; 3V8T; -.
PDBsum; 3V8W; -.
PDBsum; 4HCT; -.
PDBsum; 4HCU; -.
PDBsum; 4HCV; -.
PDBsum; 4KIO; -.
PDBsum; 4L7S; -.
PDBsum; 4M0Y; -.
PDBsum; 4M0Z; -.
PDBsum; 4M12; -.
PDBsum; 4M13; -.
PDBsum; 4M14; -.
PDBsum; 4M15; -.
PDBsum; 4MF0; -.
PDBsum; 4MF1; -.
PDBsum; 4PP9; -.
PDBsum; 4PPA; -.
PDBsum; 4PPB; -.
PDBsum; 4PPC; -.
PDBsum; 4PQN; -.
PDBsum; 4QD6; -.
PDBsum; 4RFM; -.
ProteinModelPortal; Q08881; -.
SMR; Q08881; -.
BioGrid; 109907; 35.
CORUM; Q08881; -.
DIP; DIP-29974N; -.
IntAct; Q08881; 14.
MINT; Q08881; -.
STRING; 9606.ENSP00000398655; -.
BindingDB; Q08881; -.
ChEMBL; CHEMBL2959; -.
DrugBank; DB06589; Pazopanib.
DrugBank; DB02010; Staurosporine.
GuidetoPHARMACOLOGY; 2046; -.
iPTMnet; Q08881; -.
PhosphoSitePlus; Q08881; -.
BioMuta; ITK; -.
DMDM; 585361; -.
MaxQB; Q08881; -.
PaxDb; Q08881; -.
PeptideAtlas; Q08881; -.
PRIDE; Q08881; -.
ProteomicsDB; 58650; -.
DNASU; 3702; -.
Ensembl; ENST00000422843; ENSP00000398655; ENSG00000113263.
GeneID; 3702; -.
KEGG; hsa:3702; -.
UCSC; uc003lwo.2; human.
CTD; 3702; -.
DisGeNET; 3702; -.
EuPathDB; HostDB:ENSG00000113263.12; -.
GeneCards; ITK; -.
HGNC; HGNC:6171; ITK.
MalaCards; ITK; -.
MIM; 186973; gene.
MIM; 613011; phenotype.
neXtProt; NX_Q08881; -.
OpenTargets; ENSG00000113263; -.
Orphanet; 238505; Autosomal recessive lymphoproliferative disease.
PharmGKB; PA29968; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000119011; -.
HOGENOM; HOG000233859; -.
HOVERGEN; HBG008761; -.
InParanoid; Q08881; -.
KO; K07363; -.
OMA; RYPVCSW; -.
OrthoDB; EOG091G0D46; -.
PhylomeDB; Q08881; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
SignaLink; Q08881; -.
SIGNOR; Q08881; -.
ChiTaRS; ITK; human.
EvolutionaryTrace; Q08881; -.
GeneWiki; ITK_(gene); -.
GenomeRNAi; 3702; -.
PRO; PR:Q08881; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113263; -.
CleanEx; HS_ITK; -.
ExpressionAtlas; Q08881; baseline and differential.
Genevisible; Q08881; HS.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0007202; P:activation of phospholipase C activity; ISS:UniProtKB.
GO; GO:0002250; P:adaptive immune response; ISS:UniProtKB.
GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
GO; GO:0001816; P:cytokine production; ISS:UniProtKB.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0032609; P:interferon-gamma production; IEA:Ensembl.
GO; GO:0032633; P:interleukin-4 production; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0001865; P:NK T cell differentiation; IBA:GO_Central.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0042110; P:T cell activation; TAS:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd11908; SH3_ITK; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035583; ITK_SH3.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001562; Znf_Btk_motif.
Pfam; PF00779; BTK; 1.
Pfam; PF00169; PH; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00107; BTK; 1.
SMART; SM00233; PH; 1.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
PROSITE; PS51113; ZF_BTK; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; ATP-binding; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation; Immunity;
Kinase; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; SH2 domain; SH3 domain; Transferase;
Tyrosine-protein kinase; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 620 Tyrosine-protein kinase ITK/TSK.
/FTId=PRO_0000088106.
DOMAIN 4 111 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 171 231 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 239 338 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 363 615 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 113 149 Btk-type. {ECO:0000255|PROSITE-
ProRule:PRU00432}.
NP_BIND 369 377 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 482 482 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
METAL 121 121 Zinc. {ECO:0000250}.
METAL 132 132 Zinc. {ECO:0000250}.
METAL 133 133 Zinc. {ECO:0000250}.
METAL 143 143 Zinc. {ECO:0000250}.
BINDING 391 391 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 180 180 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12573241}.
MOD_RES 512 512 Phosphotyrosine; by LCK.
{ECO:0000244|PubMed:19690332}.
MOD_RES 565 565 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
VARIANT 19 19 R -> K (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041710.
VARIANT 23 23 P -> L (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041711.
VARIANT 193 193 R -> Q (in dbSNP:rs17054374).
/FTId=VAR_051696.
VARIANT 335 335 R -> W (in LPFS1; shows nearly
undetectable mutant ITK protein
consistent with severe protein
instability; dbSNP:rs121908191).
{ECO:0000269|PubMed:19425169}.
/FTId=VAR_063424.
VARIANT 451 451 R -> Q (in a gastric adenocarcinoma
sample; somatic mutation;
dbSNP:rs779372373).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041712.
VARIANT 581 581 R -> W (in dbSNP:rs34482255).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041713.
VARIANT 587 587 V -> I (in dbSNP:rs56005928).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041714.
MUTAGEN 288 288 P->G: Complete loss of interaction with
PPIA/CYPA. {ECO:0000269|PubMed:15308100}.
CONFLICT 171 172 PE -> GS (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 331 331 V -> W (in Ref. 2; AAB28072).
{ECO:0000305}.
STRAND 127 133 {ECO:0000244|PDB:2E6I}.
STRAND 148 152 {ECO:0000244|PDB:2E6I}.
STRAND 171 173 {ECO:0000244|PDB:2YUQ}.
STRAND 175 180 {ECO:0000244|PDB:2LMJ}.
STRAND 187 189 {ECO:0000244|PDB:2YUQ}.
STRAND 197 205 {ECO:0000244|PDB:2LMJ}.
STRAND 208 212 {ECO:0000244|PDB:2LMJ}.
STRAND 214 216 {ECO:0000244|PDB:2LMJ}.
STRAND 218 221 {ECO:0000244|PDB:2LMJ}.
HELIX 223 225 {ECO:0000244|PDB:2LMJ}.
STRAND 226 228 {ECO:0000244|PDB:2LMJ}.
HELIX 360 362 {ECO:0000244|PDB:4HCU}.
STRAND 363 371 {ECO:0000244|PDB:4HCU}.
STRAND 373 375 {ECO:0000244|PDB:4KIO}.
STRAND 376 382 {ECO:0000244|PDB:4HCU}.
TURN 383 385 {ECO:0000244|PDB:4HCU}.
STRAND 386 393 {ECO:0000244|PDB:4HCU}.
TURN 395 397 {ECO:0000244|PDB:3T9T}.
HELIX 400 411 {ECO:0000244|PDB:4HCU}.
STRAND 421 425 {ECO:0000244|PDB:4HCU}.
STRAND 427 436 {ECO:0000244|PDB:4HCU}.
HELIX 443 448 {ECO:0000244|PDB:4HCU}.
TURN 449 452 {ECO:0000244|PDB:4HCU}.
HELIX 456 475 {ECO:0000244|PDB:4HCU}.
HELIX 485 487 {ECO:0000244|PDB:4HCU}.
STRAND 488 490 {ECO:0000244|PDB:4HCU}.
HELIX 492 494 {ECO:0000244|PDB:4HCU}.
STRAND 496 498 {ECO:0000244|PDB:4HCU}.
HELIX 503 506 {ECO:0000244|PDB:4HCU}.
HELIX 510 513 {ECO:0000244|PDB:4HCU}.
HELIX 522 524 {ECO:0000244|PDB:4HCU}.
HELIX 527 532 {ECO:0000244|PDB:4HCU}.
HELIX 537 552 {ECO:0000244|PDB:4HCU}.
TURN 553 555 {ECO:0000244|PDB:4PQN}.
TURN 558 561 {ECO:0000244|PDB:4HCU}.
HELIX 564 572 {ECO:0000244|PDB:4HCU}.
STRAND 581 583 {ECO:0000244|PDB:3V8W}.
HELIX 585 594 {ECO:0000244|PDB:4HCU}.
HELIX 599 601 {ECO:0000244|PDB:4HCU}.
HELIX 605 617 {ECO:0000244|PDB:4HCU}.
SEQUENCE 620 AA; 71831 MW; DAE396BD2309319D CRC64;
MNNFILLEEQ LIKKSQQKRR TSPSNFKVRF FVLTKASLAY FEDRHGKKRT LKGSIELSRI
KCVEIVKSDI SIPCHYKYPF QVVHDNYLLY VFAPDRESRQ RWVLALKEET RNNNSLVPKY
HPNFWMDGKW RCCSQLEKLA TGCAQYDPTK NASKKPLPPT PEDNRRPLWE PEETVVIALY
DYQTNDPQEL ALRRNEEYCL LDSSEIHWWR VQDRNGHEGY VPSSYLVEKS PNNLETYEWY
NKSISRDKAE KLLLDTGKEG AFMVRDSRTA GTYTVSVFTK AVVSENNPCI KHYHIKETND
NPKRYYVAEK YVFDSIPLLI NYHQHNGGGL VTRLRYPVCF GRQKAPVTAG LRYGKWVIDP
SELTFVQEIG SGQFGLVHLG YWLNKDKVAI KTIREGAMSE EDFIEEAEVM MKLSHPKLVQ
LYGVCLEQAP ICLVFEFMEH GCLSDYLRTQ RGLFAAETLL GMCLDVCEGM AYLEEACVIH
RDLAARNCLV GENQVIKVSD FGMTRFVLDD QYTSSTGTKF PVKWASPEVF SFSRYSSKSD
VWSFGVLMWE VFSEGKIPYE NRSNSEVVED ISTGFRLYKP RLASTHVYQI MNHCWKERPE
DRPAFSRLLR QLAEIAESGL


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