TXK_HUMAN
ID TXK_HUMAN Reviewed; 527 AA.
AC P42681; Q14220;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Tyrosine-protein kinase TXK;
DE EC=2.7.10.2 {ECO:0000269|PubMed:17177976};
DE AltName: Full=Protein-tyrosine kinase 4;
DE AltName: Full=Resting lymphocyte kinase;
GN Name=TXK; Synonyms=PTK4, RLK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-45, AND TISSUE SPECIFICITY.
RC TISSUE=Blood;
RX PubMed=7951233; DOI=10.1093/hmg/3.6.897;
RA Haire R.N., Ohta Y., Lewis J.E., Fu S.M., Kroisel P.M., Litman G.W.;
RT "TXK, a novel human tyrosine kinase expressed in T cells shares sequence
RT identity with Tec family kinases and maps to 4p12.";
RL Hum. Mol. Genet. 3:897-901(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=8632917;
RA Ohta Y., Haire R.N., Amemiya C.T., Litman R.T., Trager T., Riess O.,
RA Litman G.W.;
RT "Human Txk: genomic organization, structure and contiguous physical linkage
RT with the Tec gene.";
RL Oncogene 12:937-942(1996).
RN [3]
RP FUNCTION IN PHOSPHORYLATION OF CTLA4, AND MUTAGENESIS OF LYS-299.
RX PubMed=9813138; DOI=10.1006/bbrc.1998.9559;
RA Schneider H., Schwartzberg P.L., Rudd C.E.;
RT "Resting lymphocyte kinase (Rlk/Txk) phosphorylates the YVKM motif and
RT regulates PI 3-kinase binding to T-cell antigen CTLA-4.";
RL Biochem. Biophys. Res. Commun. 252:14-19(1998).
RN [4]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=10523612; DOI=10.1084/jem.190.8.1147;
RA Kashiwakura J., Suzuki N., Nagafuchi H., Takeno M., Takeba Y.,
RA Shimoyama Y., Sakane T.;
RT "Txk, a nonreceptor tyrosine kinase of the Tec family, is expressed in T
RT helper type 1 cells and regulates interferon gamma production in human T
RT lymphocytes.";
RL J. Exp. Med. 190:1147-1154(1999).
RN [5]
RP FUNCTION IN PHOSPHORYLATION OF PLCG1.
RX PubMed=11564877; DOI=10.1128/mcb.21.20.6939-6950.2001;
RA Veri M.C., DeBell K.E., Seminario M.C., DiBaldassarre A., Reischl I.,
RA Rawat R., Graham L., Noviello C., Rellahan B.L., Miscia S., Wange R.L.,
RA Bonvini E.;
RT "Membrane raft-dependent regulation of phospholipase Cgamma-1 activation in
RT T lymphocytes.";
RL Mol. Cell. Biol. 21:6939-6950(2001).
RN [6]
RP AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-91 AND TYR-420, ACTIVITY
RP REGULATION, AND MUTAGENESIS OF TYR-91.
RX PubMed=12081135; DOI=10.1248/bpb.25.718;
RA Kashiwakura J., Suzuki N., Takeno M., Itoh S., Oku T., Sakane T.,
RA Nakajin S., Toyoshima S.;
RT "Evidence of autophosphorylation in Txk: Y91 is an autophosphorylation
RT site.";
RL Biol. Pharm. Bull. 25:718-721(2002).
RN [7]
RP FUNCTION.
RX PubMed=11859127; DOI=10.4049/jimmunol.168.5.2365;
RA Takeba Y., Nagafuchi H., Takeno M., Kashiwakura J., Suzuki N.;
RT "Txk, a member of nonreceptor tyrosine kinase of Tec family, acts as a Th1
RT cell-specific transcription factor and regulates IFN-gamma gene
RT transcription.";
RL J. Immunol. 168:2365-2370(2002).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PARP1 AND EEF1A1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17177976; DOI=10.1111/j.1365-2249.2006.03249.x;
RA Maruyama T., Nara K., Yoshikawa H., Suzuki N.;
RT "Txk, a member of the non-receptor tyrosine kinase of the Tec family, forms
RT a complex with poly(ADP-ribose) polymerase 1 and elongation factor 1alpha
RT and regulates interferon-gamma gene transcription in Th1 cells.";
RL Clin. Exp. Immunol. 147:164-175(2007).
RN [9]
RP REVIEW ON FUNCTION.
RX PubMed=19290923; DOI=10.1111/j.1600-065x.2008.00757.x;
RA Readinger J.A., Mueller K.L., Venegas A.M., Horai R., Schwartzberg P.L.;
RT "Tec kinases regulate T-lymphocyte development and function: new insights
RT into the roles of Itk and Rlk/Txk.";
RL Immunol. Rev. 228:93-114(2009).
RN [10]
RP STRUCTURE BY NMR OF 140-251.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH2 domain of human tyrosine-protein kinase
RT TXK.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [11]
RP VARIANTS [LARGE SCALE ANALYSIS] HIS-45; CYS-63 AND GLN-336.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Non-receptor tyrosine kinase that plays a redundant role with
CC ITK in regulation of the adaptive immune response. Regulates the
CC development, function and differentiation of conventional T-cells and
CC nonconventional NKT-cells. When antigen presenting cells (APC) activate
CC T-cell receptor (TCR), a series of phosphorylation leads to the
CC recruitment of TXK to the cell membrane, where it is phosphorylated at
CC Tyr-420. Phosphorylation leads to TXK full activation. Contributes also
CC to signaling from many receptors and participates in multiple
CC downstream pathways, including regulation of the actin cytoskeleton.
CC Like ITK, can phosphorylate PLCG1, leading to its localization in lipid
CC rafts and activation, followed by subsequent cleavage of its
CC substrates. In turn, the endoplasmic reticulum releases calcium in the
CC cytoplasm and the nuclear activator of activated T-cells (NFAT)
CC translocates into the nucleus to perform its transcriptional duty.
CC Plays a role in the positive regulation of IFNG transcription in T-
CC helper 1 cells as part of an IFNG promoter-binding complex with PARP1
CC and EEF1A1 (PubMed:11859127, PubMed:17177976). Within the complex,
CC phosphorylates both PARP1 and EEF1A1 (PubMed:17177976). Phosphorylates
CC also key sites in LCP2 leading to the up-regulation of Th1 preferred
CC cytokine IL-2. Phosphorylates 'Tyr-201' of CTLA4 which leads to the
CC association of PI-3 kinase with the CTLA4 receptor.
CC {ECO:0000269|PubMed:10523612, ECO:0000269|PubMed:11564877,
CC ECO:0000269|PubMed:11859127, ECO:0000269|PubMed:17177976,
CC ECO:0000269|PubMed:9813138}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000269|PubMed:17177976};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation by FYN.
CC {ECO:0000269|PubMed:12081135}.
CC -!- SUBUNIT: Interacts with PARP1 and EEF1A1 (PubMed:17177976). Interacts
CC with SH2D2A (By similarity). Interacts with FYN (By similarity).
CC {ECO:0000250|UniProtKB:P42682, ECO:0000269|PubMed:17177976}.
CC -!- INTERACTION:
CC P42681; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-7877438, EBI-11524851;
CC P42681; P46108: CRK; NbExp=3; IntAct=EBI-7877438, EBI-886;
CC P42681; O60496: DOK2; NbExp=3; IntAct=EBI-7877438, EBI-1046024;
CC P42681; Q16828: DUSP6; NbExp=3; IntAct=EBI-7877438, EBI-746870;
CC P42681; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-7877438, EBI-2349927;
CC P42681; Q13322-4: GRB10; NbExp=3; IntAct=EBI-7877438, EBI-12353035;
CC P42681; P62993: GRB2; NbExp=3; IntAct=EBI-7877438, EBI-401755;
CC P42681; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-7877438, EBI-11522367;
CC P42681; Q9H2S9: IKZF4; NbExp=3; IntAct=EBI-7877438, EBI-1640423;
CC P42681; O75564-2: JRK; NbExp=3; IntAct=EBI-7877438, EBI-17181882;
CC P42681; P10721: KIT; NbExp=3; IntAct=EBI-7877438, EBI-1379503;
CC P42681; O43639: NCK2; NbExp=3; IntAct=EBI-7877438, EBI-713635;
CC P42681; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-7877438, EBI-9090282;
CC P42681; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-7877438, EBI-3957793;
CC P42681; Q9NYW8: RBAK; NbExp=3; IntAct=EBI-7877438, EBI-1210429;
CC P42681; O14543: SOCS3; NbExp=3; IntAct=EBI-7877438, EBI-714146;
CC P42681; O14544: SOCS6; NbExp=3; IntAct=EBI-7877438, EBI-3929549;
CC P42681; Q9UGK3: STAP2; NbExp=3; IntAct=EBI-7877438, EBI-1553984;
CC P42681; Q8IZW8: TNS4; NbExp=3; IntAct=EBI-7877438, EBI-7543499;
CC P42681; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-7877438, EBI-6427977;
CC P42681; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-7877438, EBI-10240849;
CC P42681; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-7877438, EBI-5667516;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17177976}. Nucleus
CC {ECO:0000269|PubMed:17177976}. Cell membrane
CC {ECO:0000269|PubMed:17177976}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17177976}. Note=Localizes in the vicinity of cell
CC surface receptors in the plasma membrane after receptor stimulation.
CC Translocates into the nucleus and enhances IFN-gamma gene transcription
CC in T-cells.
CC -!- TISSUE SPECIFICITY: Expressed in T-cells and some myeloid cell lines.
CC Expressed in Th1/Th0 cells with IFN-gamma-producing potential.
CC {ECO:0000269|PubMed:10523612, ECO:0000269|PubMed:7951233}.
CC -!- PTM: Phosphorylated at Tyr-420 by FYN. Autophosphorylation at Tyr-91 is
CC critical for the activation of TXK, leading to the up-regulation of
CC IFN-gamma gene transcription. {ECO:0000269|PubMed:12081135}.
CC -!- PTM: The cysteine string at the N-terminus is palmitoylated and
CC required for the proper subcellular location. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. TEC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Unlike the other TEC subfamily members, TXK is activated
CC independently of the activity of phosphatidylinositol 3-kinase,
CC consistent with its lack of a PH domain. Membrane association is
CC performed through palmitoylation at the N-terminus. {ECO:0000305}.
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DR EMBL; L27071; AAA74557.1; -; mRNA.
DR EMBL; U34379; AAB60412.1; -; Genomic_DNA.
DR EMBL; U34367; AAB60412.1; JOINED; Genomic_DNA.
DR EMBL; U34368; AAB60412.1; JOINED; Genomic_DNA.
DR EMBL; U34369; AAB60412.1; JOINED; Genomic_DNA.
DR EMBL; U34370; AAB60412.1; JOINED; Genomic_DNA.
DR EMBL; U34371; AAB60412.1; JOINED; Genomic_DNA.
DR EMBL; U34372; AAB60412.1; JOINED; Genomic_DNA.
DR EMBL; U34373; AAB60412.1; JOINED; Genomic_DNA.
DR EMBL; U34374; AAB60412.1; JOINED; Genomic_DNA.
DR EMBL; U34375; AAB60412.1; JOINED; Genomic_DNA.
DR EMBL; U34376; AAB60412.1; JOINED; Genomic_DNA.
DR EMBL; U34377; AAB60412.1; JOINED; Genomic_DNA.
DR EMBL; U34378; AAB60412.1; JOINED; Genomic_DNA.
DR CCDS; CCDS3480.1; -.
DR PIR; I84483; I84483.
DR RefSeq; NP_003319.2; NM_003328.2.
DR PDB; 2DM0; NMR; -; A=140-251.
DR PDBsum; 2DM0; -.
DR AlphaFoldDB; P42681; -.
DR SMR; P42681; -.
DR BioGRID; 113145; 39.
DR IntAct; P42681; 85.
DR MINT; P42681; -.
DR STRING; 9606.ENSP00000264316; -.
DR BindingDB; P42681; -.
DR ChEMBL; CHEMBL4367; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB15035; Zanubrutinib.
DR DrugCentral; P42681; -.
DR GuidetoPHARMACOLOGY; 2268; -.
DR iPTMnet; P42681; -.
DR PhosphoSitePlus; P42681; -.
DR BioMuta; TXK; -.
DR DMDM; 116242835; -.
DR MassIVE; P42681; -.
DR PaxDb; P42681; -.
DR PeptideAtlas; P42681; -.
DR PRIDE; P42681; -.
DR ProteomicsDB; 55527; -.
DR Antibodypedia; 23802; 274 antibodies from 34 providers.
DR DNASU; 7294; -.
DR Ensembl; ENST00000264316.9; ENSP00000264316.4; ENSG00000074966.11.
DR GeneID; 7294; -.
DR KEGG; hsa:7294; -.
DR MANE-Select; ENST00000264316.9; ENSP00000264316.4; NM_003328.3; NP_003319.2.
DR UCSC; uc003gxx.4; human.
DR CTD; 7294; -.
DR DisGeNET; 7294; -.
DR GeneCards; TXK; -.
DR HGNC; HGNC:12434; TXK.
DR HPA; ENSG00000074966; Tissue enhanced (epididymis, lymphoid tissue).
DR MIM; 600058; gene.
DR neXtProt; NX_P42681; -.
DR OpenTargets; ENSG00000074966; -.
DR PharmGKB; PA37090; -.
DR VEuPathDB; HostDB:ENSG00000074966; -.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000160857; -.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; P42681; -.
DR OMA; GDVRHYQ; -.
DR OrthoDB; 1047190at2759; -.
DR PhylomeDB; P42681; -.
DR TreeFam; TF351634; -.
DR BRENDA; 2.7.10.2; 2681.
DR PathwayCommons; P42681; -.
DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR SignaLink; P42681; -.
DR SIGNOR; P42681; -.
DR BioGRID-ORCS; 7294; 20 hits in 1108 CRISPR screens.
DR ChiTaRS; TXK; human.
DR EvolutionaryTrace; P42681; -.
DR GeneWiki; TXK_(gene); -.
DR GenomeRNAi; 7294; -.
DR Pharos; P42681; Tchem.
DR PRO; PR:P42681; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P42681; protein.
DR Bgee; ENSG00000074966; Expressed in granulocyte and 108 other tissues.
DR ExpressionAtlas; P42681; baseline and differential.
DR Genevisible; P42681; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
DR GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IDA:GO_Central.
DR GO; GO:0010543; P:regulation of platelet activation; IBA:GO_Central.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0042246; P:tissue regeneration; IBA:GO_Central.
DR CDD; cd10398; SH2_Tec_Txk; 1.
DR CDD; cd11907; SH3_TXK; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035870; Txk_SH2.
DR InterPro; IPR035579; TXK_SH3.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; ATP-binding; Cell membrane; Cytoplasm;
KW Immunity; Kinase; Lipoprotein; Membrane; Nucleotide-binding; Nucleus;
KW Palmitate; Phosphoprotein; Reference proteome; SH2 domain; SH3 domain;
KW Transcription; Transcription regulation; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..527
FT /note="Tyrosine-protein kinase TXK"
FT /id="PRO_0000088175"
FT DOMAIN 82..142
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 150..246
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 271..527
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 35..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 68..73
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 47..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 390
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 277..285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 91
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12081135"
FT MOD_RES 420
FT /note="Phosphotyrosine; by FYN and autocatalysis"
FT /evidence="ECO:0000269|PubMed:12081135"
FT VARIANT 45
FT /note="R -> H (in dbSNP:rs7658300)"
FT /evidence="ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:7951233"
FT /id="VAR_028368"
FT VARIANT 63
FT /note="R -> C (in dbSNP:rs41265727)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041869"
FT VARIANT 336
FT /note="R -> Q (in dbSNP:rs11724347)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_028369"
FT MUTAGEN 91
FT /note="Y->A: Reduces expression levels if IFN-gamma."
FT /evidence="ECO:0000269|PubMed:12081135"
FT MUTAGEN 299
FT /note="K->A: Impairs kinase activity."
FT /evidence="ECO:0000269|PubMed:9813138"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:2DM0"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:2DM0"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:2DM0"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:2DM0"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:2DM0"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:2DM0"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:2DM0"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:2DM0"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:2DM0"
SQ 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
