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Tyrosine-protein kinase TXK (EC 2.7.10.2) (Protein-tyrosine kinase 4) (Resting lymphocyte kinase)

 TXK_HUMAN               Reviewed;         527 AA.
P42681; Q14220;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
25-OCT-2017, entry version 171.
RecName: Full=Tyrosine-protein kinase TXK;
EC=2.7.10.2;
AltName: Full=Protein-tyrosine kinase 4;
AltName: Full=Resting lymphocyte kinase;
Name=TXK; Synonyms=PTK4, RLK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-45, AND TISSUE SPECIFICITY.
TISSUE=Blood;
PubMed=7951233; DOI=10.1093/hmg/3.6.897;
Haire R.N., Ohta Y., Lewis J.E., Fu S.M., Kroisel P.M., Litman G.W.;
"TXK, a novel human tyrosine kinase expressed in T cells shares
sequence identity with Tec family kinases and maps to 4p12.";
Hum. Mol. Genet. 3:897-901(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
PubMed=8632917;
Ohta Y., Haire R.N., Amemiya C.T., Litman R.T., Trager T., Riess O.,
Litman G.W.;
"Human Txk: genomic organization, structure and contiguous physical
linkage with the Tec gene.";
Oncogene 12:937-942(1996).
[3]
FUNCTION IN PHOSPHORYLATION OF CTLA4, AND MUTAGENESIS OF LYS-299.
PubMed=9813138; DOI=10.1006/bbrc.1998.9559;
Schneider H., Schwartzberg P.L., Rudd C.E.;
"Resting lymphocyte kinase (Rlk/Txk) phosphorylates the YVKM motif and
regulates PI 3-kinase binding to T-cell antigen CTLA-4.";
Biochem. Biophys. Res. Commun. 252:14-19(1998).
[4]
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=10523612; DOI=10.1084/jem.190.8.1147;
Kashiwakura J., Suzuki N., Nagafuchi H., Takeno M., Takeba Y.,
Shimoyama Y., Sakane T.;
"Txk, a nonreceptor tyrosine kinase of the Tec family, is expressed in
T helper type 1 cells and regulates interferon gamma production in
human T lymphocytes.";
J. Exp. Med. 190:1147-1154(1999).
[5]
FUNCTION IN PHOSPHORYLATION OF PLCG1.
PubMed=11564877; DOI=10.1128/MCB.21.20.6939-6950.2001;
Veri M.C., DeBell K.E., Seminario M.C., DiBaldassarre A., Reischl I.,
Rawat R., Graham L., Noviello C., Rellahan B.L., Miscia S.,
Wange R.L., Bonvini E.;
"Membrane raft-dependent regulation of phospholipase Cgamma-1
activation in T lymphocytes.";
Mol. Cell. Biol. 21:6939-6950(2001).
[6]
AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-91 AND TYR-420, ENZYME
REGULATION, AND MUTAGENESIS OF TYR-91.
PubMed=12081135; DOI=10.1248/bpb.25.718;
Kashiwakura J., Suzuki N., Takeno M., Itoh S., Oku T., Sakane T.,
Nakajin S., Toyoshima S.;
"Evidence of autophosphorylation in Txk: Y91 is an autophosphorylation
site.";
Biol. Pharm. Bull. 25:718-721(2002).
[7]
DNA-BINDING, AND FUNCTION.
PubMed=11859127; DOI=10.4049/jimmunol.168.5.2365;
Takeba Y., Nagafuchi H., Takeno M., Kashiwakura J., Suzuki N.;
"Txk, a member of nonreceptor tyrosine kinase of Tec family, acts as a
Th1 cell-specific transcription factor and regulates IFN-gamma gene
transcription.";
J. Immunol. 168:2365-2370(2002).
[8]
INTERACTION WITH PARP1 AND EEF1A1, FUNCTION IN PHOSPHORYLATION OF
PARP1 AND EEF1A1, SUBCELLULAR LOCATION, AND FUNCTION AS A
TRANSCRIPTION FACTOR.
PubMed=17177976; DOI=10.1111/j.1365-2249.2006.03249.x;
Maruyama T., Nara K., Yoshikawa H., Suzuki N.;
"Txk, a member of the non-receptor tyrosine kinase of the Tec family,
forms a complex with poly(ADP-ribose) polymerase 1 and elongation
factor 1alpha and regulates interferon-gamma gene transcription in Th1
cells.";
Clin. Exp. Immunol. 147:164-175(2007).
[9]
REVIEW ON FUNCTION.
PubMed=19290923; DOI=10.1111/j.1600-065X.2008.00757.x;
Readinger J.A., Mueller K.L., Venegas A.M., Horai R.,
Schwartzberg P.L.;
"Tec kinases regulate T-lymphocyte development and function: new
insights into the roles of Itk and Rlk/Txk.";
Immunol. Rev. 228:93-114(2009).
[10]
STRUCTURE BY NMR OF 140-251.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SH2 domain of human tyrosine-protein kinase
TXK.";
Submitted (OCT-2006) to the PDB data bank.
[11]
VARIANTS [LARGE SCALE ANALYSIS] HIS-45; CYS-63 AND GLN-336.
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).
-!- FUNCTION: Non-receptor tyrosine kinase that plays a redundant role
with ITK 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 TXK to the cell membrane, where it is
phosphorylated at Tyr-420. Phosphorylation leads to TXK full
activation. Contributes also to signaling from many receptors and
participates in multiple downstream pathways, including regulation
of the actin cytoskeleton. Like ITK, can phosphorylate PLCG1,
leading to its localization in lipid rafts and activation,
followed by 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. With PARP1 and
EEF1A1, TXK forms a complex that acts as a T-helper 1 (Th1) cell-
specific transcription factor and binds the promoter of IFNG to
directly regulate its transcription, and is thus involved
importantly in Th1 cytokine production. Phosphorylates both PARP1
and EEF1A1. Phosphorylates also key sites in LCP2 leading to the
up-regulation of Th1 preferred cytokine IL-2. Phosphorylates 'Tyr-
201' of CTLA4 which leads to the association of PI-3 kinase with
the CTLA4 receptor. {ECO:0000269|PubMed:10523612,
ECO:0000269|PubMed:11564877, ECO:0000269|PubMed:11859127,
ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:9813138}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Activated by phosphorylation by FYN.
{ECO:0000269|PubMed:12081135}.
-!- SUBUNIT: Interacts with PARP1 and EEF1A1. Interacts with SH2D2A
(By similarity). {ECO:0000250}.
-!- INTERACTION:
P10721:KIT; NbExp=3; IntAct=EBI-7877438, EBI-1379503;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17177976}.
Nucleus {ECO:0000269|PubMed:17177976}. Cell membrane
{ECO:0000269|PubMed:17177976}; Peripheral membrane protein
{ECO:0000269|PubMed:17177976}. Note=Localizes in the vicinity of
cell surface receptors in the plasma membrane after receptor
stimulation. Translocates into the nucleus and enhances IFN-gamma
gene transcription in T-cells.
-!- TISSUE SPECIFICITY: Expressed in T-cells and some myeloid cell
lines. Expressed in Th1/Th0 cells with IFN-gamma-producing
potential. {ECO:0000269|PubMed:10523612,
ECO:0000269|PubMed:7951233}.
-!- PTM: Phosphorylated at Tyr-420 by FYN. Autophosphorylation at Tyr-
91 is critical for the activation of TXK, leading to the up-
regulation of IFN-gamma gene transcription.
{ECO:0000269|PubMed:12081135}.
-!- PTM: The cysteine string at the N-terminus is palmitoylated and
required for the proper subcellular location. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. TEC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- CAUTION: Unlike the other TEC subfamily members, TXK is activated
independently of the activity of phosphatidylinositol 3-kinase,
consistent with its lack of a PH domain. Membrane association is
performed through palmitoylation at the N-terminus. {ECO:0000305}.
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EMBL; L27071; AAA74557.1; -; mRNA.
EMBL; U34379; AAB60412.1; -; Genomic_DNA.
EMBL; U34367; AAB60412.1; JOINED; Genomic_DNA.
EMBL; U34368; AAB60412.1; JOINED; Genomic_DNA.
EMBL; U34369; AAB60412.1; JOINED; Genomic_DNA.
EMBL; U34370; AAB60412.1; JOINED; Genomic_DNA.
EMBL; U34371; AAB60412.1; JOINED; Genomic_DNA.
EMBL; U34372; AAB60412.1; JOINED; Genomic_DNA.
EMBL; U34373; AAB60412.1; JOINED; Genomic_DNA.
EMBL; U34374; AAB60412.1; JOINED; Genomic_DNA.
EMBL; U34375; AAB60412.1; JOINED; Genomic_DNA.
EMBL; U34376; AAB60412.1; JOINED; Genomic_DNA.
EMBL; U34377; AAB60412.1; JOINED; Genomic_DNA.
EMBL; U34378; AAB60412.1; JOINED; Genomic_DNA.
CCDS; CCDS3480.1; -.
PIR; I84483; I84483.
RefSeq; NP_003319.2; NM_003328.2.
UniGene; Hs.479669; -.
PDB; 2DM0; NMR; -; A=140-251.
PDBsum; 2DM0; -.
ProteinModelPortal; P42681; -.
SMR; P42681; -.
BioGrid; 113145; 4.
IntAct; P42681; 19.
MINT; MINT-1493369; -.
STRING; 9606.ENSP00000264316; -.
BindingDB; P42681; -.
ChEMBL; CHEMBL4367; -.
GuidetoPHARMACOLOGY; 2268; -.
iPTMnet; P42681; -.
PhosphoSitePlus; P42681; -.
BioMuta; TXK; -.
DMDM; 116242835; -.
PaxDb; P42681; -.
PeptideAtlas; P42681; -.
PRIDE; P42681; -.
DNASU; 7294; -.
Ensembl; ENST00000264316; ENSP00000264316; ENSG00000074966.
GeneID; 7294; -.
KEGG; hsa:7294; -.
UCSC; uc003gxx.4; human.
CTD; 7294; -.
DisGeNET; 7294; -.
EuPathDB; HostDB:ENSG00000074966.10; -.
GeneCards; TXK; -.
H-InvDB; HIX0031512; -.
HGNC; HGNC:12434; TXK.
HPA; HPA062482; -.
MIM; 600058; gene.
neXtProt; NX_P42681; -.
OpenTargets; ENSG00000074966; -.
PharmGKB; PA37090; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000119011; -.
HOGENOM; HOG000233859; -.
HOVERGEN; HBG008761; -.
InParanoid; P42681; -.
KO; K08016; -.
OMA; PIKWSPP; -.
OrthoDB; EOG091G0D46; -.
PhylomeDB; P42681; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
SignaLink; P42681; -.
SIGNOR; P42681; -.
ChiTaRS; TXK; human.
EvolutionaryTrace; P42681; -.
GeneWiki; TXK_(gene); -.
GenomeRNAi; 7294; -.
PRO; PR:P42681; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000074966; -.
CleanEx; HS_TXK; -.
ExpressionAtlas; P42681; baseline and differential.
Genevisible; P42681; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001012; F:RNA polymerase II regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0007202; P:activation of phospholipase C activity; ISS:UniProtKB.
GO; GO:0002250; P:adaptive immune response; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0001816; P:cytokine production; ISS:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0010543; P:regulation of platelet activation; IBA:GO_Central.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0042246; P:tissue regeneration; IBA:GO_Central.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd10398; SH2_Tec_Txk; 1.
CDD; cd11907; SH3_TXK; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011009; Kinase-like_dom.
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.
InterPro; IPR001452; SH3_domain.
InterPro; IPR035870; Txk_SH2.
InterPro; IPR035579; TXK_SH3.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00109; TYRKINASE.
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; 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.
1: Evidence at protein level;
3D-structure; Adaptive immunity; ATP-binding; Cell membrane;
Complete proteome; Cytoplasm; DNA-binding; Immunity; Kinase;
Lipoprotein; Membrane; Nucleotide-binding; Nucleus; Palmitate;
Phosphoprotein; Polymorphism; Reference proteome; SH2 domain;
SH3 domain; Transcription; Transcription regulation; Transferase;
Tyrosine-protein kinase.
CHAIN 1 527 Tyrosine-protein kinase TXK.
/FTId=PRO_0000088175.
DOMAIN 82 142 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 150 246 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 271 527 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 277 285 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 68 73 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 14 19 Poly-Cys.
ACT_SITE 390 390 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 299 299 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 91 91 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12081135}.
MOD_RES 420 420 Phosphotyrosine; by FYN and
autocatalysis.
{ECO:0000269|PubMed:12081135}.
VARIANT 45 45 R -> H (in dbSNP:rs7658300).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:7951233}.
/FTId=VAR_028368.
VARIANT 63 63 R -> C (in dbSNP:rs41265727).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041869.
VARIANT 336 336 R -> Q (in dbSNP:rs11724347).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_028369.
MUTAGEN 91 91 Y->A: Reduces expression levels if IFN-
gamma. {ECO:0000269|PubMed:12081135}.
MUTAGEN 299 299 K->A: Impairs kinase activity.
{ECO:0000269|PubMed:9813138}.
STRAND 148 151 {ECO:0000244|PDB:2DM0}.
HELIX 157 167 {ECO:0000244|PDB:2DM0}.
STRAND 175 178 {ECO:0000244|PDB:2DM0}.
STRAND 181 189 {ECO:0000244|PDB:2DM0}.
STRAND 193 197 {ECO:0000244|PDB:2DM0}.
STRAND 200 207 {ECO:0000244|PDB:2DM0}.
STRAND 213 218 {ECO:0000244|PDB:2DM0}.
HELIX 224 231 {ECO:0000244|PDB:2DM0}.
STRAND 237 239 {ECO:0000244|PDB:2DM0}.
SEQUENCE 527 AA; 61258 MW; BCCA081F4155CAA6 CRC64;
MILSSYNTIQ SVFCCCCCCS VQKRQMRTQI SLSTDEELPE KYTQRRRPWL SQLSNKKQSN
TGRVQPSKRK PLPPLPPSEV AEEKIQVKAL YDFLPREPCN LALRRAEEYL ILEKYNPHWW
KARDRLGNEG LIPSNYVTEN KITNLEIYEW YHRNITRNQA EHLLRQESKE GAFIVRDSRH
LGSYTISVFM GARRSTEAAI KHYQIKKNDS GQWYVAERHA FQSIPELIWY HQHNAAGLMT
RLRYPVGLMG SCLPATAGFS YEKWEIDPSE LAFIKEIGSG QFGVVHLGEW RSHIQVAIKA
INEGSMSEED FIEEAKVMMK LSHSKLVQLY GVCIQRKPLY IVTEFMENGC LLNYLRENKG
KLRKEMLLSV CQDICEGMEY LERNGYIHRD LAARNCLVSS TCIVKISDFG MTRYVLDDEY
VSSFGAKFPI KWSPPEVFLF NKYSSKSDVW SFGVLMWEVF TEGKMPFENK SNLQVVEAIS
EGFRLYRPHL APMSIYEVMY SCWHEKPEGR PTFAELLRAV TEIAETW


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10-782-55014 Cytoplasmic tyrosine-protein kinase BMX - EC 2.7.10.2; Bone marrow tyrosine kinase gene in chromosome X protein; Epithelial and endothelial tyrosine kinase; ETK; NTK38 N_A 0.02 mg
10-782-55014 Cytoplasmic tyrosine-protein kinase BMX - EC 2.7.10.2; Bone marrow tyrosine kinase gene in chromosome X protein; Epithelial and endothelial tyrosine kinase; ETK; NTK38 N_A 0.001 mg


 

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