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Q08881

- ITK_HUMAN

UniProt

Q08881 - ITK_HUMAN

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Protein
Tyrosine-protein kinase ITK/TSK
Gene
ITK, EMT, LYK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi121 – 1211Zinc By similarity
Metal bindingi132 – 1321Zinc By similarity
Metal bindingi133 – 1331Zinc By similarity
Metal bindingi143 – 1431Zinc By similarity
Binding sitei391 – 3911ATP By similarity
Active sitei482 – 4821Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri113 – 14937Btk-type
Add
BLAST
Nucleotide bindingi369 – 3779ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. Fc-epsilon receptor signaling pathway Source: Reactome
  2. NK T cell differentiation Source: Ensembl
  3. T cell activation Source: UniProtKB
  4. T cell receptor signaling pathway Source: UniProtKB
  5. activation of phospholipase C activity Source: UniProtKB
  6. adaptive immune response Source: UniProtKB
  7. cellular defense response Source: ProtInc
  8. cytokine production Source: UniProtKB
  9. innate immune response Source: Reactome
  10. interferon-gamma production Source: Ensembl
  11. interleukin-4 production Source: Ensembl
  12. intracellular signal transduction Source: InterPro
  13. peptidyl-tyrosine phosphorylation Source: GOC
  14. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Adaptive immunity, Immunity

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_12623. Generation of second messenger molecules.
REACT_163834. FCERI mediated Ca+2 mobilization.
SignaLinkiQ08881.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase ITK/TSK (EC:2.7.10.2)
Alternative name(s):
Interleukin-2-inducible T-cell kinase
Short name:
IL-2-inducible T-cell kinase
Kinase EMT
T-cell-specific kinase
Tyrosine-protein kinase Lyk
Gene namesi
Name:ITK
Synonyms:EMT, LYK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:6171. ITK.

Subcellular locationi

Cytoplasm
Note: Localizes in the vicinity of cell surface receptors in the plasma membrane after receptor stimulation.1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti335 – 3351R → W in LPFS1; shows nearly undetectable mutant ITK protein consistent with severe protein instability. 1 Publication
Corresponds to variant rs121908191 [ dbSNP | Ensembl ].
VAR_063424

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi288 – 2881P → G: Complete loss of interaction with PPIA/CYPA. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi613011. phenotype.
Orphaneti238505. Autosomal recessive lymphoproliferative disease.
PharmGKBiPA29968.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 620620Tyrosine-protein kinase ITK/TSK
PRO_0000088106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei180 – 1801Phosphotyrosine; by autocatalysis1 Publication
Modified residuei512 – 5121Phosphotyrosine; by LCK1 Publication
Modified residuei565 – 5651Phosphoserine1 Publication

Post-translational modificationi

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.3 Publications
Ubiquitinated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ08881.
PaxDbiQ08881.
PeptideAtlasiQ08881.
PRIDEiQ08881.

PTM databases

PhosphoSiteiQ08881.

Expressioni

Tissue specificityi

T-cell lines and natural killer cell lines.

Inductioni

Through a myriad of surface receptors including the TCR/CD3 signaling complex, coreceptors, or chemokine receptors.2 Publications

Gene expression databases

ArrayExpressiQ08881.
BgeeiQ08881.
CleanExiHS_ITK.
GenevestigatoriQ08881.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ERBB2P046262EBI-968552,EBI-641062
FASLGP480233EBI-968552,EBI-495538

Protein-protein interaction databases

BioGridi109907. 25 interactions.
DIPiDIP-29974N.
IntActiQ08881. 10 interactions.
MINTiMINT-110502.
STRINGi9606.ENSP00000398655.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi127 – 1337
Beta strandi148 – 1525
Beta strandi171 – 1733
Beta strandi175 – 1806
Beta strandi187 – 1893
Beta strandi197 – 2059
Beta strandi208 – 2125
Beta strandi214 – 2163
Beta strandi218 – 2214
Helixi223 – 2253
Beta strandi226 – 2283
Helixi360 – 3623
Beta strandi363 – 3719
Beta strandi372 – 3743
Beta strandi376 – 3827
Turni383 – 3853
Beta strandi386 – 3938
Turni395 – 3973
Helixi400 – 41112
Beta strandi421 – 4255
Beta strandi427 – 43610
Helixi443 – 4486
Turni449 – 4524
Helixi456 – 47520
Helixi485 – 4873
Beta strandi488 – 4903
Helixi492 – 4943
Beta strandi496 – 4983
Helixi503 – 5064
Helixi510 – 5134
Helixi522 – 5243
Helixi527 – 5326
Helixi537 – 55216
Turni553 – 5553
Turni558 – 5614
Helixi564 – 5729
Beta strandi581 – 5833
Helixi585 – 59410
Helixi599 – 6013
Helixi605 – 61713

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SM2X-ray2.30A/B357-620[»]
1SNUX-ray2.50A/B357-620[»]
1SNXX-ray3.20A/B357-620[»]
2E6INMR-A113-169[»]
2LMJNMR-A171-231[»]
2YUQNMR-A162-239[»]
3MIYX-ray1.67A/B357-620[»]
3MJ1X-ray1.72A357-620[»]
3MJ2X-ray1.90A357-620[»]
3QGWX-ray2.10A/B357-620[»]
3QGYX-ray2.10A/B357-620[»]
3T9TX-ray1.65A354-620[»]
3V5JX-ray2.59A/B357-620[»]
3V5LX-ray1.86A/B/C/D357-620[»]
3V8TX-ray2.00A/B357-620[»]
3V8WX-ray2.27A/B357-620[»]
4HCTX-ray1.48A354-620[»]
4HCUX-ray1.43A354-620[»]
4HCVX-ray1.48A354-620[»]
4KIOX-ray2.18A/B/C/D357-620[»]
4L7SX-ray2.03A/B357-620[»]
4M0YX-ray1.70A354-620[»]
4M0ZX-ray2.00A354-620[»]
4M12X-ray2.15A354-620[»]
4M13X-ray1.85A354-620[»]
4M14X-ray1.55A354-620[»]
4M15X-ray1.52A354-620[»]
4MF0X-ray2.67A/B357-620[»]
4MF1X-ray2.11A/B357-620[»]
4PP9X-ray2.58A/B357-620[»]
4PPAX-ray2.67A/B357-620[»]
4PPBX-ray2.82A/B357-620[»]
4PPCX-ray2.95A/B357-620[»]
ProteinModelPortaliQ08881.
SMRiQ08881. Positions 1-618.

Miscellaneous databases

EvolutionaryTraceiQ08881.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 111108PH
Add
BLAST
Domaini171 – 23161SH3
Add
BLAST
Domaini239 – 338100SH2
Add
BLAST
Domaini363 – 615253Protein kinase
Add
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Contains 1 PH domain.
Contains 1 SH2 domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH2 domain, SH3 domain, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233859.
HOVERGENiHBG008761.
InParanoidiQ08881.
KOiK07363.
OMAiRRNEEYC.
OrthoDBiEOG7KM5SC.
PhylomeDBiQ08881.
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.
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.

Q08881-1 [UniParc]FASTAAdd to Basket

« Hide

MNNFILLEEQ LIKKSQQKRR TSPSNFKVRF FVLTKASLAY FEDRHGKKRT    50
LKGSIELSRI KCVEIVKSDI SIPCHYKYPF QVVHDNYLLY VFAPDRESRQ 100
RWVLALKEET RNNNSLVPKY HPNFWMDGKW RCCSQLEKLA TGCAQYDPTK 150
NASKKPLPPT PEDNRRPLWE PEETVVIALY DYQTNDPQEL ALRRNEEYCL 200
LDSSEIHWWR VQDRNGHEGY VPSSYLVEKS PNNLETYEWY NKSISRDKAE 250
KLLLDTGKEG AFMVRDSRTA GTYTVSVFTK AVVSENNPCI KHYHIKETND 300
NPKRYYVAEK YVFDSIPLLI NYHQHNGGGL VTRLRYPVCF GRQKAPVTAG 350
LRYGKWVIDP SELTFVQEIG SGQFGLVHLG YWLNKDKVAI KTIREGAMSE 400
EDFIEEAEVM MKLSHPKLVQ LYGVCLEQAP ICLVFEFMEH GCLSDYLRTQ 450
RGLFAAETLL GMCLDVCEGM AYLEEACVIH RDLAARNCLV GENQVIKVSD 500
FGMTRFVLDD QYTSSTGTKF PVKWASPEVF SFSRYSSKSD VWSFGVLMWE 550
VFSEGKIPYE NRSNSEVVED ISTGFRLYKP RLASTHVYQI MNHCWKERPE 600
DRPAFSRLLR QLAEIAESGL 620
Length:620
Mass (Da):71,831
Last modified:October 1, 1994 - v1
Checksum:iDAE396BD2309319D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191R → K in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_041710
Natural varianti23 – 231P → L in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_041711
Natural varianti193 – 1931R → Q.
Corresponds to variant rs17054374 [ dbSNP | Ensembl ].
VAR_051696
Natural varianti335 – 3351R → W in LPFS1; shows nearly undetectable mutant ITK protein consistent with severe protein instability. 1 Publication
Corresponds to variant rs121908191 [ dbSNP | Ensembl ].
VAR_063424
Natural varianti451 – 4511R → Q in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041712
Natural varianti581 – 5811R → W.1 Publication
Corresponds to variant rs34482255 [ dbSNP | Ensembl ].
VAR_041713
Natural varianti587 – 5871V → I.1 Publication
Corresponds to variant rs56005928 [ dbSNP | Ensembl ].
VAR_041714

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1722PE → GS AA sequence 1 Publication
Sequence conflicti331 – 3311V → W in AAB28072. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D13720 mRNA. Translation: BAA02873.1.
L10717 mRNA. Translation: AAA36748.1.
S65186 mRNA. Translation: AAB28072.2.
AK312846 mRNA. Translation: BAG35699.1.
CH471062 Genomic DNA. Translation: EAW61608.1.
BC109077 mRNA. Translation: AAI09078.1.
BC109078 mRNA. Translation: AAI09079.1.
CCDSiCCDS4336.1.
PIRiS33253.
RefSeqiNP_005537.3. NM_005546.3.
UniGeneiHs.558348.

Genome annotation databases

EnsembliENST00000422843; ENSP00000398655; ENSG00000113263.
GeneIDi3702.
KEGGihsa:3702.
UCSCiuc003lwo.1. human.

Polymorphism databases

DMDMi585361.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D13720 mRNA. Translation: BAA02873.1 .
L10717 mRNA. Translation: AAA36748.1 .
S65186 mRNA. Translation: AAB28072.2 .
AK312846 mRNA. Translation: BAG35699.1 .
CH471062 Genomic DNA. Translation: EAW61608.1 .
BC109077 mRNA. Translation: AAI09078.1 .
BC109078 mRNA. Translation: AAI09079.1 .
CCDSi CCDS4336.1.
PIRi S33253.
RefSeqi NP_005537.3. NM_005546.3.
UniGenei Hs.558348.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SM2 X-ray 2.30 A/B 357-620 [» ]
1SNU X-ray 2.50 A/B 357-620 [» ]
1SNX X-ray 3.20 A/B 357-620 [» ]
2E6I NMR - A 113-169 [» ]
2LMJ NMR - A 171-231 [» ]
2YUQ NMR - A 162-239 [» ]
3MIY X-ray 1.67 A/B 357-620 [» ]
3MJ1 X-ray 1.72 A 357-620 [» ]
3MJ2 X-ray 1.90 A 357-620 [» ]
3QGW X-ray 2.10 A/B 357-620 [» ]
3QGY X-ray 2.10 A/B 357-620 [» ]
3T9T X-ray 1.65 A 354-620 [» ]
3V5J X-ray 2.59 A/B 357-620 [» ]
3V5L X-ray 1.86 A/B/C/D 357-620 [» ]
3V8T X-ray 2.00 A/B 357-620 [» ]
3V8W X-ray 2.27 A/B 357-620 [» ]
4HCT X-ray 1.48 A 354-620 [» ]
4HCU X-ray 1.43 A 354-620 [» ]
4HCV X-ray 1.48 A 354-620 [» ]
4KIO X-ray 2.18 A/B/C/D 357-620 [» ]
4L7S X-ray 2.03 A/B 357-620 [» ]
4M0Y X-ray 1.70 A 354-620 [» ]
4M0Z X-ray 2.00 A 354-620 [» ]
4M12 X-ray 2.15 A 354-620 [» ]
4M13 X-ray 1.85 A 354-620 [» ]
4M14 X-ray 1.55 A 354-620 [» ]
4M15 X-ray 1.52 A 354-620 [» ]
4MF0 X-ray 2.67 A/B 357-620 [» ]
4MF1 X-ray 2.11 A/B 357-620 [» ]
4PP9 X-ray 2.58 A/B 357-620 [» ]
4PPA X-ray 2.67 A/B 357-620 [» ]
4PPB X-ray 2.82 A/B 357-620 [» ]
4PPC X-ray 2.95 A/B 357-620 [» ]
ProteinModelPortali Q08881.
SMRi Q08881. Positions 1-618.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109907. 25 interactions.
DIPi DIP-29974N.
IntActi Q08881. 10 interactions.
MINTi MINT-110502.
STRINGi 9606.ENSP00000398655.

Chemistry

BindingDBi Q08881.
ChEMBLi CHEMBL2959.
GuidetoPHARMACOLOGYi 2046.

PTM databases

PhosphoSitei Q08881.

Polymorphism databases

DMDMi 585361.

Proteomic databases

MaxQBi Q08881.
PaxDbi Q08881.
PeptideAtlasi Q08881.
PRIDEi Q08881.

Protocols and materials databases

DNASUi 3702.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000422843 ; ENSP00000398655 ; ENSG00000113263 .
GeneIDi 3702.
KEGGi hsa:3702.
UCSCi uc003lwo.1. human.

Organism-specific databases

CTDi 3702.
GeneCardsi GC05P156607.
HGNCi HGNC:6171. ITK.
MIMi 186973. gene.
613011. phenotype.
neXtProti NX_Q08881.
Orphaneti 238505. Autosomal recessive lymphoproliferative disease.
PharmGKBi PA29968.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233859.
HOVERGENi HBG008761.
InParanoidi Q08881.
KOi K07363.
OMAi RRNEEYC.
OrthoDBi EOG7KM5SC.
PhylomeDBi Q08881.
TreeFami TF351634.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_12623. Generation of second messenger molecules.
REACT_163834. FCERI mediated Ca+2 mobilization.
SignaLinki Q08881.

Miscellaneous databases

EvolutionaryTracei Q08881.
GeneWikii ITK_(gene).
GenomeRNAii 3702.
NextBioi 14507.
PROi Q08881.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q08881.
Bgeei Q08881.
CleanExi HS_ITK.
Genevestigatori Q08881.

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.
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

« Hide 'large scale' publications
  1. "A novel human tyrosine kinase gene inducible in T cells by interleukin 2."
    Tanaka N., Asao H., Ohtani K., Nakamura M., Sugamura K.
    FEBS Lett. 324:1-5(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
  2. "Identification, cloning, and characterization of a novel human T-cell-specific tyrosine kinase located at the hematopoietin complex on chromosome 5q."
    Gibson S., Leung B., Squire J.A., Hill M., Arima N., Goss P., Hogg D., Mills G.B.
    Blood 82:1561-1572(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Thymus.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thymus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
  6. "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 171-192, PHOSPHORYLATION AT TYR-180.
  7. "Lck phosphorylates the activation loop tyrosine of the Itk kinase domain and activates Itk kinase activity."
    Heyeck S.D., Wilcox H.M., Bunnell S.C., Berg L.J.
    J. Biol. Chem. 272:25401-25408(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY LCK.
  8. "CD2-mediated activation of the Tec-family tyrosine kinase ITK is controlled by proline-rich stretch-4 of the CD2 cytoplasmic tail."
    King P.D., Sadra A., Teng J.M., Bell G.M., Dupont B.
    Int. Immunol. 10:1009-1016(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  9. "Tec kinases: a family with multiple roles in immunity."
    Yang W.C., Collette Y., Nunes J.A., Olive D.
    Immunity 12:373-382(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  10. "Phosphorylation of the linker for activation of T-cells by Itk promotes recruitment of Vav."
    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.
    Biochemistry 41:10732-10740(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF LAT.
  11. "Inducible T cell tyrosine kinase regulates actin-dependent cytoskeletal events induced by the T cell antigen receptor."
    Grasis J.A., Browne C.D., Tsoukas C.D.
    J. Immunol. 170:3971-3976(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Cyclophilin A regulates TCR signal strength in CD4+ T cells via a proline-directed conformational switch in Itk."
    Colgan J., Asmal M., Neagu M., Yu B., Schneidkraut J., Lee Y., Sokolskaja E., Andreotti A., Luban J.
    Immunity 21:189-201(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPIA/CYPA, MUTAGENESIS OF PRO-288.
  14. "Kinase-independent functions for Itk in TCR-induced regulation of Vav and the actin cytoskeleton."
    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.
    J. Immunol. 174:1385-1392(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VAV1.
  15. "Tec kinase Itk forms membrane clusters specifically in the vicinity of recruiting receptors."
    Qi Q., Sahu N., August A.
    J. Biol. Chem. 281:38529-38534(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "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.
  17. "SH2-dependent autophosphorylation within the Tec family kinase Itk."
    Joseph R.E., Severin A., Min L., Fulton D.B., Andreotti A.H.
    J. Mol. Biol. 391:164-177(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION.
  18. "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-512 AND SER-565, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "Development and validation of a method for profiling post-translational modification activities using protein microarrays."
    Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
    PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  20. Cited for: FUNCTION IN PHOSPHORYLATION OF LCP2.
  21. "Solution structure of the BTK motif and the SH3 domain of tyrosine-protein kinase ITK from human."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 113-239.
  22. "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] LYS-19; LEU-23; GLN-451; TRP-581 AND ILE-587.
  23. "Girls homozygous for an IL-2-inducible T cell kinase mutation that leads to protein deficiency develop fatal EBV-associated lymphoproliferation."
    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.
    J. Clin. Invest. 119:1350-1358(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LPFS1 TRP-335, CHARACTERIZATION OF VARIANT LPSA1 TRP-335.

Entry informationi

Entry nameiITK_HUMAN
AccessioniPrimary (citable) accession number: Q08881
Secondary accession number(s): B2R752, Q32ML7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: September 3, 2014
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 5
    Human chromosome 5: 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

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