TESK1_HUMAN
ID TESK1_HUMAN Reviewed; 626 AA.
AC Q15569; Q8IXZ8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Dual specificity testis-specific protein kinase 1;
DE EC=2.7.12.1;
DE AltName: Full=Testicular protein kinase 1;
GN Name=TESK1;
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].
RC TISSUE=Hepatoma;
RX PubMed=8537404; DOI=10.1074/jbc.270.52.31331;
RA Toshima J., Ohashi K., Okano I., Nunoue K., Kishioka M., Kuma K.,
RA Miyata T., Hirai M., Baba T., Mizuno K.;
RT "Identification and characterization of a novel protein kinase, TESK1,
RT specifically expressed in testicular germ cells.";
RL J. Biol. Chem. 270:31331-31337(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH YWHAB.
RX PubMed=11555644; DOI=10.1074/jbc.m104620200;
RA Toshima J.Y., Toshima J., Watanabe T., Mizuno K.;
RT "Binding of 14-3-3beta regulates the kinase activity and subcellular
RT localization of testicular protein kinase 1.";
RL J. Biol. Chem. 276:43471-43481(2001).
RN [6]
RP INTERACTION WITH SPRY4.
RX PubMed=12027893; DOI=10.1046/j.1432-1033.2002.02921.x;
RA Leeksma O.C., van Achterberg T.A.E., Tsumura Y., Toshima J., Eldering E.,
RA Kroes W.G.M., Mellink C., Spaargaren M., Mizuno K., Pannekoek H.,
RA de Vries C.J.M.;
RT "Human sprouty 4, a new ras antagonist on 5q31, interacts with the dual
RT specificity kinase TESK1.";
RL Eur. J. Biochem. 269:2546-2556(2002).
RN [7]
RP FUNCTION, INTERACTION WITH SPRY4, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-175.
RX PubMed=15584898; DOI=10.1042/bj20041181;
RA Tsumura Y., Toshima J., Leeksma O.C., Ohashi K., Mizuno K.;
RT "Sprouty-4 negatively regulates cell spreading by inhibiting the kinase
RT activity of testicular protein kinase.";
RL Biochem. J. 387:627-637(2005).
RN [8]
RP INTERACTION WITH PARVA.
RX PubMed=15817463; DOI=10.1074/jbc.m500752200;
RA LaLonde D.P., Brown M.C., Bouverat B.P., Turner C.E.;
RT "Actopaxin interacts with TESK1 to regulate cell spreading on
RT fibronectin.";
RL J. Biol. Chem. 280:21680-21688(2005).
RN [9]
RP INTERACTION WITH SPRED1.
RX PubMed=17974561; DOI=10.1074/jbc.m705457200;
RA Chandramouli S., Yu C.Y., Yusoff P., Lao D.H., Leong H.F., Mizuno K.,
RA Guy G.R.;
RT "Tesk1 interacts with Spry2 to abrogate its inhibition of ERK
RT phosphorylation downstream of receptor tyrosine kinase signaling.";
RL J. Biol. Chem. 283:1679-1691(2008).
RN [10]
RP INTERACTION WITH SPRED1.
RX PubMed=18216281; DOI=10.1091/mbc.e07-07-0730;
RA Johne C., Matenia D., Li X.Y., Timm T., Balusamy K., Mandelkow E.M.;
RT "Spred1 and TESK1--two new interaction partners of the kinase MARKK/TAO1
RT that link the microtubule and actin cytoskeleton.";
RL Mol. Biol. Cell 19:1391-1403(2008).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25849865; DOI=10.1038/ncomms7781;
RA Kim J., Jo H., Hong H., Kim M.H., Kim J.M., Lee J.K., Heo W.D., Kim J.;
RT "Actin remodelling factors control ciliogenesis by regulating YAP/TAZ
RT activity and vesicle trafficking.";
RL Nat. Commun. 6:6781-6781(2015).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=30115939; DOI=10.1038/s41598-018-30115-3;
RA Wang L., Buckley A.F., Spurney R.F.;
RT "Regulation of cofilin phosphorylation in glomerular podocytes by testis
RT specific kinase 1 (TESK1).";
RL Sci. Rep. 8:12286-12286(2018).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] TYR-539.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [14]
RP VARIANTS [LARGE SCALE ANALYSIS] TYR-539 AND SER-574.
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: Dual specificity protein kinase activity catalyzing
CC autophosphorylation and phosphorylation of exogenous substrates on both
CC serine/threonine and tyrosine residues (By similarity). Regulates the
CC cellular cytoskeleton by enhancing actin stress fiber formation via
CC phosphorylation of cofilin and by preventing microtubule breakdown via
CC inhibition of TAOK1/MARKK kinase activity (By similarity). Inhibits
CC podocyte motility via regulation of actin cytoskeletal dynamics and
CC phosphorylation of CFL1 (By similarity). Positively regulates integrin-
CC mediated cell spreading, via phosphorylation of cofilin
CC (PubMed:15584898). Suppresses ciliogenesis via multiple pathways;
CC phosphorylation of CFL1, suppression of ciliary vesicle directional
CC trafficking to the ciliary base, and by facilitating YAP1 nuclear
CC localization where it acts as a transcriptional corepressor of the
CC TEAD4 target genes AURKA and PLK1 (PubMed:25849865). Probably plays a
CC central role at and after the meiotic phase of spermatogenesis (By
CC similarity). {ECO:0000250|UniProtKB:O70146,
CC ECO:0000250|UniProtKB:Q63572, ECO:0000269|PubMed:15584898,
CC ECO:0000269|PubMed:25849865}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.1;
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=2.7.12.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by autophosphorylation on Ser-220.
CC Kinase activity is inhibited by SPRED1. {ECO:0000250|UniProtKB:Q63572}.
CC -!- SUBUNIT: Interacts (via both C- and N-termini) with SPRY4 (via C-
CC terminus); the interaction inhibits TESK1 kinase activity
CC (PubMed:12027893, PubMed:15584898). Interacts with TAOK1; the
CC interaction inhibits TAOK1 kinase activity (By similarity). Interacts
CC (via C-terminus) with SPRED1 (via C-terminus); the interaction inhibits
CC TESK1 kinase activity (PubMed:18216281). Interacts (via C-terminus)
CC with PARVA/PARVIN (via C-terminus); the interaction inhibits TESK1
CC kinase activity (PubMed:15817463). Interacts with YWHAB/14-3-3 beta;
CC the interaction is dependent on the phosphorylation of TESK1 Ser-437
CC and inhibits TESK1 kinase activity (PubMed:11555644). Interacts with
CC SPRY1, SPRY3 and SPRED2 (PubMed:17974561). Interacts (via C-terminus)
CC with SPRY2 (via C-terminus); the interaction disrupts SPRY2 interaction
CC with PPP2CA/PP2A-C, possibly by vesicular sequestration of SPRY2
CC (PubMed:17974561). Therefore dephosphorylation of SPRY2 by the
CC serine/threonine-protein phosphatase 2A (PP2A) holoenzyme is lost,
CC inhibiting its interaction with GRB2 (PubMed:17974561).
CC {ECO:0000250|UniProtKB:Q63572, ECO:0000269|PubMed:11555644,
CC ECO:0000269|PubMed:12027893, ECO:0000269|PubMed:15584898,
CC ECO:0000269|PubMed:15817463, ECO:0000269|PubMed:17974561,
CC ECO:0000269|PubMed:18216281}.
CC -!- INTERACTION:
CC Q15569; Q9C004: SPRY4; NbExp=4; IntAct=EBI-354852, EBI-354861;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15584898}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63572}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:25849865}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q63572}. Note=Colocalizes with SPRY4 in
CC vesicular spots in the cytoplasm (PubMed:15584898). Localized to F-
CC actin-rich lamellipodia at the cell periphery following fibronectin-
CC mediated cell adhesion of Schwann cells (By similarity).
CC {ECO:0000250|UniProtKB:Q63572, ECO:0000269|PubMed:15584898}.
CC -!- TISSUE SPECIFICITY: Expressed in podocytes and renal tubular cells in
CC the kidney (at protein level). {ECO:0000269|PubMed:30115939}.
CC -!- DOMAIN: The extracatalytic C-terminal part is highly rich in proline
CC residues.
CC -!- PTM: Autophosphorylated on serine and tyrosine residues.
CC {ECO:0000250|UniProtKB:Q63572}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; D50863; BAA09459.1; -; mRNA.
DR EMBL; AL357874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58375.1; -; Genomic_DNA.
DR EMBL; BC038448; AAH38448.1; -; mRNA.
DR EMBL; BC067130; AAH67130.1; -; mRNA.
DR CCDS; CCDS6580.1; -.
DR RefSeq; NP_001305159.1; NM_001318230.1.
DR RefSeq; NP_006276.2; NM_006285.2.
DR AlphaFoldDB; Q15569; -.
DR SMR; Q15569; -.
DR BioGRID; 112875; 14.
DR IntAct; Q15569; 21.
DR MINT; Q15569; -.
DR STRING; 9606.ENSP00000481045; -.
DR BindingDB; Q15569; -.
DR ChEMBL; CHEMBL5604; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q15569; -.
DR GuidetoPHARMACOLOGY; 2239; -.
DR iPTMnet; Q15569; -.
DR PhosphoSitePlus; Q15569; -.
DR BioMuta; TESK1; -.
DR DMDM; 209572684; -.
DR EPD; Q15569; -.
DR jPOST; Q15569; -.
DR MassIVE; Q15569; -.
DR PaxDb; Q15569; -.
DR PeptideAtlas; Q15569; -.
DR PRIDE; Q15569; -.
DR ProteomicsDB; 60637; -.
DR Antibodypedia; 2068; 152 antibodies from 27 providers.
DR DNASU; 7016; -.
DR Ensembl; ENST00000336395.6; ENSP00000338127.5; ENSG00000107140.16.
DR Ensembl; ENST00000620767.4; ENSP00000481045.1; ENSG00000107140.16.
DR GeneID; 7016; -.
DR KEGG; hsa:7016; -.
DR MANE-Select; ENST00000336395.6; ENSP00000338127.5; NM_006285.3; NP_006276.2.
DR UCSC; uc003zxa.4; human.
DR CTD; 7016; -.
DR DisGeNET; 7016; -.
DR GeneCards; TESK1; -.
DR HGNC; HGNC:11731; TESK1.
DR HPA; ENSG00000107140; Low tissue specificity.
DR MIM; 601782; gene.
DR neXtProt; NX_Q15569; -.
DR OpenTargets; ENSG00000107140; -.
DR PharmGKB; PA36448; -.
DR VEuPathDB; HostDB:ENSG00000107140; -.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR GeneTree; ENSGT00940000157807; -.
DR HOGENOM; CLU_018577_0_0_1; -.
DR InParanoid; Q15569; -.
DR OMA; SPPTWGD; -.
DR OrthoDB; 219904at2759; -.
DR PhylomeDB; Q15569; -.
DR TreeFam; TF318014; -.
DR BRENDA; 2.7.10.2; 2681.
DR PathwayCommons; Q15569; -.
DR Reactome; R-HSA-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR SignaLink; Q15569; -.
DR SIGNOR; Q15569; -.
DR BioGRID-ORCS; 7016; 32 hits in 1114 CRISPR screens.
DR ChiTaRS; TESK1; human.
DR GeneWiki; TESK1; -.
DR GenomeRNAi; 7016; -.
DR Pharos; Q15569; Tchem.
DR PRO; PR:Q15569; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q15569; protein.
DR Bgee; ENSG00000107140; Expressed in right testis and 177 other tissues.
DR Genevisible; Q15569; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0004672; F:protein kinase activity; IMP:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051650; P:establishment of vesicle localization; IMP:UniProtKB.
DR GO; GO:1902018; P:negative regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0042326; P:negative regulation of phosphorylation; ISS:UniProtKB.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISS:ARUK-UCL.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; ISS:ARUK-UCL.
DR GO; GO:0090521; P:podocyte cell migration; ISS:UniProtKB.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:ARUK-UCL.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISS:ARUK-UCL.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
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; IPR015782; TESK1.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR46485:SF3; PTHR46485:SF3; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
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.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Cytoplasm; Cytoskeleton; Kinase; Magnesium;
KW Manganese; Metal-binding; Methylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..626
FT /note="Dual specificity testis-specific protein kinase 1"
FT /id="PRO_0000086746"
FT DOMAIN 57..314
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..524
FT /note="Required for interaction with YWHAB"
FT /evidence="ECO:0000250|UniProtKB:Q63572"
FT REGION 423..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..626
FT /note="Required for interaction with SPRED1 and SPRY2.
FT Required for TESK1-mediated dephosphorylation of SPRY2 and
FT SPRY2 inhibition of ERK phosphorylation"
FT /evidence="ECO:0000250|UniProtKB:Q63572"
FT REGION 527..624
FT /note="Required for interaction with PARVA"
FT /evidence="ECO:0000250|UniProtKB:Q63572"
FT REGION 529..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 63..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 220
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q63572"
FT MOD_RES 338
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O70146"
FT VARIANT 539
FT /note="H -> Y (in breast cancer samples; infiltrating
FT ductal carcinoma; somatic mutation; dbSNP:rs1373248755)"
FT /evidence="ECO:0000269|PubMed:16959974,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_035638"
FT VARIANT 574
FT /note="G -> S (in dbSNP:rs55673450)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041213"
FT MUTAGEN 175
FT /note="D->A: Abolishes inhibition of SPRY4-mediated
FT repression of cell spreading. No effect on interaction with
FT SPRY4 or colocalization with SPRY4 at vesicular spots in
FT the cytoplasm."
FT /evidence="ECO:0000269|PubMed:15584898"
FT CONFLICT 43
FT /note="A -> V (in Ref. 1; BAA09459)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 626 AA; 67684 MW; 32F78E5E6AEDB0E5 CRC64;
MAGERPPLRG PGPGPGEVPG EGPPGPGGTG GGPGRGRPSS YRALRSAVSS LARVDDFHCA
EKIGAGFFSE VYKVRHRQSG QVMVLKMNKL PSNRGNTLRE VQLMNRLRHP NILRFMGVCV
HQGQLHALTE YMNGGTLEQL LSSPEPLSWP VRLHLALDIA RGLRYLHSKG VFHRDLTSKN
CLVRREDRGF TAVVGDFGLA EKIPVYREGA RKEPLAVVGS PYWMAPEVLR GELYDEKADV
FAFGIVLCEL IARVPADPDY LPRTEDFGLD VPAFRTLVGD DCPLPFLLLA IHCCNLEPST
RAPFTEITQH LEWILEQLPE PAPLTRTALT HNQGSVARGG PSATLPRPDP RLSRSRSDLF
LPPSPESPPN WGDNLTRVNP FSLREDLRGG KIKLLDTPSK PVLPLVPPSP FPSTQLPLVT
TPETLVQPGT PARRCRSLPS SPELPRRMET ALPGPGPPAV GPSAEEKMEC EGSSPEPEPP
GPAPQLPLAV ATDNFISTCS SASQPWSPRS GPVLNNNPPA VVVNSPQGWA GEPWNRAQHS
LPRAAALERT EPSPPPSAPR EPDEGLPCPG CCLGPFSFGF LSMCPRPTPA VARYRNLNCE
AGSLLCHRGH HAKPPTPSLQ LPGARS
