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Protein

Tyrosine-protein kinase ITK/TSK

Gene

ITK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi121 – 1211ZincBy similarity
Metal bindingi132 – 1321ZincBy similarity
Metal bindingi133 – 1331ZincBy similarity
Metal bindingi143 – 1431ZincBy similarity
Binding sitei391 – 3911ATPPROSITE-ProRule annotation
Active sitei482 – 4821Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri113 – 14937Btk-typePROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi369 – 3779ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

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.
ReactomeiR-HSA-202433. Generation of second messenger molecules.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
SignaLinkiQ08881.
SIGNORiQ08881.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:6171. ITK.

Subcellular locationi

  • Cytoplasm 1 Publication

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Lymphoproliferative syndrome 1 (LPFS1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:613011
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

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

Chemistry

ChEMBLiCHEMBL2959.
DrugBankiDB06589. Pazopanib.
GuidetoPHARMACOLOGYi2046.

Polymorphism and mutation databases

BioMutaiITK.
DMDMi585361.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 620620Tyrosine-protein kinase ITK/TSKPRO_0000088106Add
BLAST

Amino acid modifications

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

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.2 Publications
Ubiquitinated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ08881.
PaxDbiQ08881.
PeptideAtlasiQ08881.
PRIDEiQ08881.

PTM databases

iPTMnetiQ08881.
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

BgeeiENSG00000113263.
CleanExiHS_ITK.
ExpressionAtlasiQ08881. baseline and differential.
GenevisibleiQ08881. HS.

Organism-specific databases

HPAiCAB026471.

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.By similarity3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi109907. 34 interactions.
DIPiDIP-29974N.
IntActiQ08881. 12 interactions.
MINTiMINT-110502.
STRINGi9606.ENSP00000398655.

Chemistry

BindingDBiQ08881.

Structurei

Secondary structure

1
620
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi127 – 1337Combined sources
Beta strandi148 – 1525Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi175 – 1806Combined sources
Beta strandi187 – 1893Combined sources
Beta strandi197 – 2059Combined sources
Beta strandi208 – 2125Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi218 – 2214Combined sources
Helixi223 – 2253Combined sources
Beta strandi226 – 2283Combined sources
Helixi360 – 3623Combined sources
Beta strandi363 – 3719Combined sources
Beta strandi373 – 3753Combined sources
Beta strandi376 – 3827Combined sources
Turni383 – 3853Combined sources
Beta strandi386 – 3938Combined sources
Turni395 – 3973Combined sources
Helixi400 – 41112Combined sources
Beta strandi421 – 4255Combined sources
Beta strandi427 – 43610Combined sources
Helixi443 – 4486Combined sources
Turni449 – 4524Combined sources
Helixi456 – 47520Combined sources
Helixi485 – 4873Combined sources
Beta strandi488 – 4903Combined sources
Helixi492 – 4943Combined sources
Beta strandi496 – 4983Combined sources
Helixi503 – 5064Combined sources
Helixi510 – 5134Combined sources
Helixi522 – 5243Combined sources
Helixi527 – 5326Combined sources
Helixi537 – 55216Combined sources
Turni553 – 5553Combined sources
Turni558 – 5614Combined sources
Helixi564 – 5729Combined sources
Beta strandi581 – 5833Combined sources
Helixi585 – 59410Combined sources
Helixi599 – 6013Combined sources
Helixi605 – 61713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4PQNX-ray1.71A357-620[»]
4QD6X-ray2.45A/B357-620[»]
4RFMX-ray2.10A357-620[»]
ProteinModelPortaliQ08881.
SMRiQ08881. Positions 1-618.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08881.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 111108PHPROSITE-ProRule annotationAdd
BLAST
Domaini171 – 23161SH3PROSITE-ProRule annotationAdd
BLAST
Domaini239 – 338100SH2PROSITE-ProRule annotationAdd
BLAST
Domaini363 – 615253Protein kinasePROSITE-ProRule annotationAdd
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

Belongs to the protein kinase superfamily. Tyr protein kinase family. TEC subfamily.PROSITE-ProRule annotation
Contains 1 Btk-type zinc finger.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Zinc finger

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

Keywords - Domaini

SH2 domain, SH3 domain, Zinc-finger

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000233859.
HOVERGENiHBG008761.
InParanoidiQ08881.
KOiK07363.
OMAiRTQRGLF.
OrthoDBiEOG091G0D46.
PhylomeDBiQ08881.
TreeFamiTF351634.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
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.
SSF50729. SSF50729. 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

        10         20         30         40         50
MNNFILLEEQ LIKKSQQKRR TSPSNFKVRF FVLTKASLAY FEDRHGKKRT
60 70 80 90 100
LKGSIELSRI KCVEIVKSDI SIPCHYKYPF QVVHDNYLLY VFAPDRESRQ
110 120 130 140 150
RWVLALKEET RNNNSLVPKY HPNFWMDGKW RCCSQLEKLA TGCAQYDPTK
160 170 180 190 200
NASKKPLPPT PEDNRRPLWE PEETVVIALY DYQTNDPQEL ALRRNEEYCL
210 220 230 240 250
LDSSEIHWWR VQDRNGHEGY VPSSYLVEKS PNNLETYEWY NKSISRDKAE
260 270 280 290 300
KLLLDTGKEG AFMVRDSRTA GTYTVSVFTK AVVSENNPCI KHYHIKETND
310 320 330 340 350
NPKRYYVAEK YVFDSIPLLI NYHQHNGGGL VTRLRYPVCF GRQKAPVTAG
360 370 380 390 400
LRYGKWVIDP SELTFVQEIG SGQFGLVHLG YWLNKDKVAI KTIREGAMSE
410 420 430 440 450
EDFIEEAEVM MKLSHPKLVQ LYGVCLEQAP ICLVFEFMEH GCLSDYLRTQ
460 470 480 490 500
RGLFAAETLL GMCLDVCEGM AYLEEACVIH RDLAARNCLV GENQVIKVSD
510 520 530 540 550
FGMTRFVLDD QYTSSTGTKF PVKWASPEVF SFSRYSSKSD VWSFGVLMWE
560 570 580 590 600
VFSEGKIPYE NRSNSEVVED ISTGFRLYKP RLASTHVYQI MNHCWKERPE
610 620
DRPAFSRLLR QLAEIAESGL
Length:620
Mass (Da):71,831
Last modified:October 1, 1994 - v1
Checksum:iDAE396BD2309319D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1722PE → GS AA sequence (PubMed:12573241).Curated
Sequence conflicti331 – 3311V → W in AAB28072 (PubMed:8364206).Curated

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
Corresponds to variant rs779372373 [ dbSNP | Ensembl ].
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 databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4PQNX-ray1.71A357-620[»]
4QD6X-ray2.45A/B357-620[»]
4RFMX-ray2.10A357-620[»]
ProteinModelPortaliQ08881.
SMRiQ08881. Positions 1-618.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109907. 34 interactions.
DIPiDIP-29974N.
IntActiQ08881. 12 interactions.
MINTiMINT-110502.
STRINGi9606.ENSP00000398655.

Chemistry

BindingDBiQ08881.
ChEMBLiCHEMBL2959.
DrugBankiDB06589. Pazopanib.
GuidetoPHARMACOLOGYi2046.

PTM databases

iPTMnetiQ08881.
PhosphoSiteiQ08881.

Polymorphism and mutation databases

BioMutaiITK.
DMDMi585361.

Proteomic databases

MaxQBiQ08881.
PaxDbiQ08881.
PeptideAtlasiQ08881.
PRIDEiQ08881.

Protocols and materials databases

DNASUi3702.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000422843; ENSP00000398655; ENSG00000113263.
GeneIDi3702.
KEGGihsa:3702.
UCSCiuc003lwo.2. human.

Organism-specific databases

CTDi3702.
GeneCardsiITK.
HGNCiHGNC:6171. ITK.
HPAiCAB026471.
MalaCardsiITK.
MIMi186973. gene.
613011. phenotype.
neXtProtiNX_Q08881.
Orphaneti238505. Autosomal recessive lymphoproliferative disease.
PharmGKBiPA29968.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000233859.
HOVERGENiHBG008761.
InParanoidiQ08881.
KOiK07363.
OMAiRTQRGLF.
OrthoDBiEOG091G0D46.
PhylomeDBiQ08881.
TreeFamiTF351634.

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiR-HSA-202433. Generation of second messenger molecules.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
SignaLinkiQ08881.
SIGNORiQ08881.

Miscellaneous databases

ChiTaRSiITK. human.
EvolutionaryTraceiQ08881.
GeneWikiiITK_(gene).
GenomeRNAii3702.
PROiQ08881.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000113263.
CleanExiHS_ITK.
ExpressionAtlasiQ08881. baseline and differential.
GenevisibleiQ08881. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
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.
SSF50729. SSF50729. 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]
ProtoNetiSearch...

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 7, 2016
This is version 181 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.