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Dual specificity testis-specific protein kinase 1 (EC 2 7 12 1) (Testicular protein kinase 1)

 TESK1_MOUSE             Reviewed;         627 AA.
O70146; O70147; Q499W7;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 3.
12-AUG-2020, entry version 169.
RecName: Full=Dual specificity testis-specific protein kinase 1;
EC=2.7.12.1;
AltName: Full=Testicular protein kinase 1;
Name=Tesk1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
STRAIN=129/Sv;
PubMed=9469938; DOI=10.1016/s0378-1119(97)00591-x;
Toshima J., Nakagawara K., Mori M., Noda T., Mizuno K.;
"Structural organization and chromosomal localization of the mouse tesk1
(testis-specific protein kinase 1) gene.";
Gene 206:237-245(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[6]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-338, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Dual specificity protein kinase activity catalyzing
autophosphorylation and phosphorylation of exogenous substrates on both
serine/threonine and tyrosine residues (By similarity). Regulates the
cellular cytoskeleton by enhancing actin stress fiber formation via
phosphorylation of cofilin and by preventing microtubule breakdown via
inhibition of TAOK1/MARKK kinase activity (By similarity). Probably
plays a central role at and after the meiotic phase of spermatogenesis
(By similarity). {ECO:0000250|UniProtKB:Q63572}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.12.1;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- ACTIVITY REGULATION: Activated by autophosphorylation on Ser-215.
Kinase activity is inhibited by SPRED1 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with SPRY4 (By similarity). Interacts with TAOK1;
inhibits TAOK1 kinase activity (By similarity). Interacts with SPRED1
(via C-terminus); inhibits TESK1 kinase activity (By similarity).
{ECO:0000250|UniProtKB:Q15569, ECO:0000250|UniProtKB:Q63572}.
-!- TISSUE SPECIFICITY: Predominantly expressed in testis.
{ECO:0000269|PubMed:9469938}.
-!- DOMAIN: The extracatalytic C-terminal part is highly rich in proline
residues.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; AB003493; BAA25124.1; -; Genomic_DNA.
EMBL; AB003494; BAA25125.1; -; mRNA.
EMBL; AK144302; BAE25822.1; -; mRNA.
EMBL; AL732506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC099699; AAH99699.1; -; mRNA.
CCDS; CCDS18094.1; -.
PIR; JC6534; JC6534.
RefSeq; NP_035701.3; NM_011571.3.
SMR; O70146; -.
BioGRID; 204120; 2.
STRING; 10090.ENSMUSP00000050087; -.
iPTMnet; O70146; -.
PhosphoSitePlus; O70146; -.
SwissPalm; O70146; -.
EPD; O70146; -.
MaxQB; O70146; -.
PaxDb; O70146; -.
PRIDE; O70146; -.
Antibodypedia; 2068; 149 antibodies.
Ensembl; ENSMUST00000060864; ENSMUSP00000050087; ENSMUSG00000028458.
GeneID; 21754; -.
KEGG; mmu:21754; -.
UCSC; uc008spq.2; mouse.
CTD; 7016; -.
MGI; MGI:1201675; Tesk1.
eggNOG; ENOG502QTCP; Eukaryota.
GeneTree; ENSGT00940000157807; -.
HOGENOM; CLU_018577_0_0_1; -.
InParanoid; O70146; -.
KO; K08841; -.
OMA; SPPTWGD; -.
OrthoDB; 219904at2759; -.
PhylomeDB; O70146; -.
TreeFam; TF318014; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
BioGRID-ORCS; 21754; 0 hits in 18 CRISPR screens.
ChiTaRS; Tesk1; mouse.
PRO; PR:O70146; -.
Proteomes; UP000000589; Chromosome 4.
RNAct; O70146; protein.
Bgee; ENSMUSG00000028458; Expressed in testis and 273 other tissues.
ExpressionAtlas; O70146; baseline and differential.
Genevisible; O70146; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISO:MGI.
GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR015782; TESK1.
InterPro; IPR008266; Tyr_kinase_AS.
PANTHER; PTHR46485:SF3; PTHR46485:SF3; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
ATP-binding; Kinase; Magnesium; Manganese; Metal-binding; Methylation;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
CHAIN 1..627
/note="Dual specificity testis-specific protein kinase 1"
/id="PRO_0000086747"
DOMAIN 52..309
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 58..66
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
ACT_SITE 170
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10028"
BINDING 81
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 215
/note="Phosphoserine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:Q63572"
MOD_RES 338
/note="Omega-N-methylarginine"
/evidence="ECO:0000244|PubMed:24129315"
CONFLICT 550
/note="R -> Q (in Ref. 1; BAA25124/BAA25125)"
/evidence="ECO:0000305"
SEQUENCE 627 AA; 68052 MW; 091ADA8CF52A2B50 CRC64;
MAGERPPLRG PGPGEAPGEG PGGAGGGPGR GRPSSYRALR SAVSSLARVD DFDCAEKIGA
GFFSEVYKVR HRQSGQVMVL KMNKLPSNRS NTLREVQLMN RLRHPNILRF MGVCVHQGQL
HALTEYMNGG TLEQLLSSPE PLSWPVRLHL ALDIAQGLRY LHAKGVFHRD LTSKNCLVRR
EDRGFTAVVG DFGLAEKIPV YREGTRKEPL AVVGSPYWMA PEVLRGELYD EKADVFAFGI
VLCELIARVP ADPDYLPRTE DFGLDVPAFR TLVGNDCPLP FLLLAIHCCS MEPSTRAPFT
EITQHLEQIL EQQPEATPLA KPPLTKAPLT YNQGSVPRGG PSATLPRPDP RLSRSRSDLF
LPPSPESPPS WGDNLTRVNP FSLREDLRGG KIKLLDTPCK PATPLPLVPP SPLTSTQLPL
VTTPDILVQP ETPVRRCRSL PSSPELPRRM ETALPGPGPS PMGPTEERMD CEGSSPEPEP
PGLAPQLPLA VATDNFISTC SSASQPWSPR SGPPLNNNPP AVVVNSPQGW AREPWNRAQH
SLPRAAALER TEPSPPPSAP REPEEGLPCP GCCLGPFSFG FLSMCPRPTP AVARYRNLNC
EAGSLLCHRG HHAKPPTPSL QLPGARS


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EIAAB41994 Dual specificity testis-specific protein kinase 1,Rat,Rattus norvegicus,Tesk1,Testicular protein kinase 1
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Pathways :
WP1493: Carbon assimilation C4 pathway
WP1049: G Protein Signaling Pathways
WP1692: Protein export
WP73: G Protein Signaling Pathways
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WP1659: Glycine, serine and threonine metabolism
WP2218: sGC
WP1438: Influenza A virus infection
WP1700: Selenoamino acid metabolism
WP931: G Protein Signaling Pathways
WP1531: Vitamin D synthesis
WP1713: Two-component system
WP1665: Limonene and pinene degradation
WP232: G Protein Signaling Pathways
WP1675: Nitrogen metabolism
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1613: 1,4-Dichlorobenzene degradation
WP1888: Post-translational protein modification
WP1624: Bacterial secretion system
WP1939: Unfolded Protein Response
WP1681: Pantothenate and CoA biosynthesis
WP32: Translation Factors
WP1690: Propanoate metabolism
WP525: Mitochondrial Unfolded-Protein Response

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[CDKN3 CDI1 CIP2 KAP] Cyclin-dependent kinase inhibitor 3 (EC 3.1.3.16) (EC 3.1.3.48) (CDK2-associated dual-specificity phosphatase) (Cyclin-dependent kinase interactor 1) (Cyclin-dependent kinase-interacting protein 2) (Kinase-associated phosphatase)
[Tssk3 Stk22c Stk22d] Testis-specific serine/threonine-protein kinase 3 (TSK-3) (TSSK-3) (Testis-specific kinase 3) (EC 2.7.11.1) (Serine/threonine-protein kinase 22C)
[MAP2K6 MEK6 MKK6 PRKMK6 SKK3] Dual specificity mitogen-activated protein kinase kinase 6 (MAP kinase kinase 6) (MAPKK 6) (EC 2.7.12.2) (MAPK/ERK kinase 6) (MEK 6) (Stress-activated protein kinase kinase 3) (SAPK kinase 3) (SAPKK-3) (SAPKK3)
[Akap1 Akap] A-kinase anchor protein 1, mitochondrial (Dual specificity A-kinase-anchoring protein 1) (D-AKAP-1) (Protein kinase A-anchoring protein 1) (PRKA1) (Spermatid A-kinase anchor protein) (S-AKAP)
[DSTYK KIAA0472 RIP5 RIPK5 SGK496 HDCMD38P] Dual serine/threonine and tyrosine protein kinase (EC 2.7.12.1) (Dusty protein kinase) (Dusty PK) (RIP-homologous kinase) (Receptor-interacting serine/threonine-protein kinase 5) (Sugen kinase 496) (SgK496)
[Akap1 Akap] A-kinase anchor protein 1, mitochondrial (A-kinase anchor protein 121 kDa) (AKAP 121) (Dual specificity A-kinase-anchoring protein 1) (D-AKAP-1) (Protein kinase A-anchoring protein 1) (PRKA1) (Spermatid A-kinase anchor protein 84) (S-AKAP84)

Bibliography :
[12027893] Human sprouty 4, a new ras antagonist on 5q31, interacts with the dual specificity kinase TESK1.
[10207045] Dual specificity protein kinase activity of testis-specific protein kinase 1 and its regulation by autophosphorylation of serine-215 within the activation loop.