TOPK_HUMAN
ID TOPK_HUMAN Reviewed; 322 AA.
AC Q96KB5; B4DX68; D3DST2; Q9NPD9; Q9NYL7; Q9NZK6;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Lymphokine-activated killer T-cell-originated protein kinase;
DE EC=2.7.12.2;
DE AltName: Full=Cancer/testis antigen 84;
DE Short=CT84;
DE AltName: Full=MAPKK-like protein kinase;
DE AltName: Full=Nori-3;
DE AltName: Full=PDZ-binding kinase;
DE AltName: Full=Spermatogenesis-related protein kinase;
DE Short=SPK;
DE AltName: Full=T-LAK cell-originated protein kinase;
GN Name=PBK; Synonyms=TOPK;
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] (ISOFORM 1), FUNCTION, PHOSPHORYLATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Lymphoid tissue;
RX PubMed=10781613; DOI=10.1074/jbc.m909629199;
RA Abe Y., Matsumoto S., Kito K., Ueda N.;
RT "Cloning and expression of a novel MAPKK-like protein kinase, lymphokine-
RT activated killer T-cell-originated protein kinase, specifically expressed
RT in the testis and activated lymphoid cells.";
RL J. Biol. Chem. 275:21525-21531(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION, MUTAGENESIS OF
RP 64-LEU-LEU-65; THR-320 AND VAL-322, INTERACTION WITH DLG1, AND VARIANT
RP SER-107.
RX PubMed=10779557; DOI=10.1073/pnas.090102397;
RA Gaudet S., Branton D., Lue R.A.;
RT "Characterization of PDZ-binding kinase, a mitotic kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5167-5172(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP SER-107.
RC TISSUE=Fetal brain;
RX PubMed=11378444; DOI=10.1016/s1357-2725(01)00005-x;
RA Zhao S., Dai J., Zhao W., Xia F., Zhou Z., Wang W., Gu S., Ying K., Xie Y.,
RA Mao Y.;
RT "PDZ-binding kinase participates in spermatogenesis.";
RL Int. J. Biochem. Cell Biol. 33:631-636(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-107.
RC TISSUE=Embryo, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [8]
RP FUNCTION, INTERACTION WITH TP53, AND MUTAGENESIS OF THR-9.
RX PubMed=17482142; DOI=10.1016/j.bbrc.2007.04.125;
RA Nandi A.K., Ford T., Fleksher D., Neuman B., Rapoport A.P.;
RT "Attenuation of DNA damage checkpoint by PBK, a novel mitotic kinase,
RT involves protein-protein interaction with tumor suppressor p53.";
RL Biochem. Biophys. Res. Commun. 358:181-188(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; SER-32 AND SER-59, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-9; SER-32 AND SER-59, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9 AND SER-59, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-169, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [17]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-107 AND LEU-241.
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: Phosphorylates MAP kinase p38. Seems to be active only in
CC mitosis. May also play a role in the activation of lymphoid cells. When
CC phosphorylated, forms a complex with TP53, leading to TP53
CC destabilization and attenuation of G2/M checkpoint during doxorubicin-
CC induced DNA damage. {ECO:0000269|PubMed:10781613,
CC ECO:0000269|PubMed:17482142}.
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=2.7.12.2;
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=2.7.12.2;
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=2.7.12.2;
CC -!- ACTIVITY REGULATION: Activated by phosphorylation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DLG1 and TP53. {ECO:0000269|PubMed:10779557,
CC ECO:0000269|PubMed:17482142}.
CC -!- INTERACTION:
CC Q96KB5; P10398: ARAF; NbExp=3; IntAct=EBI-536853, EBI-365961;
CC Q96KB5; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-536853, EBI-742054;
CC Q96KB5; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-536853, EBI-348259;
CC Q96KB5; P04637: TP53; NbExp=7; IntAct=EBI-536853, EBI-366083;
CC Q96KB5; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-536853, EBI-11035148;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96KB5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96KB5-2; Sequence=VSP_055269;
CC -!- TISSUE SPECIFICITY: Expressed in the testis and placenta. In the
CC testis, restrictedly expressed in outer cell layer of seminiferous
CC tubules. {ECO:0000269|PubMed:10781613, ECO:0000269|PubMed:11378444}.
CC -!- PTM: Phosphorylated; in a cell-cycle dependent manner at mitosis.
CC {ECO:0000269|PubMed:10779557, ECO:0000269|PubMed:10781613}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; AB027249; BAA99576.1; -; mRNA.
DR EMBL; AB027250; BAA99577.1; -; mRNA.
DR EMBL; AF189722; AAF69107.1; -; mRNA.
DR EMBL; AF237709; AAF71521.1; -; mRNA.
DR EMBL; AK027291; BAB55019.1; -; mRNA.
DR EMBL; AK301836; BAG63280.1; -; mRNA.
DR EMBL; AC104997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63536.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63537.1; -; Genomic_DNA.
DR EMBL; BC015191; AAH15191.1; -; mRNA.
DR CCDS; CCDS6063.1; -. [Q96KB5-1]
DR CCDS; CCDS64858.1; -. [Q96KB5-2]
DR RefSeq; NP_001265874.1; NM_001278945.1. [Q96KB5-2]
DR RefSeq; NP_060962.2; NM_018492.3. [Q96KB5-1]
DR RefSeq; XP_006716431.1; XM_006716368.2.
DR PDB; 5J0A; X-ray; 2.74 A; A=23-320, B=19-319.
DR PDBsum; 5J0A; -.
DR AlphaFoldDB; Q96KB5; -.
DR SMR; Q96KB5; -.
DR BioGRID; 120971; 82.
DR IntAct; Q96KB5; 29.
DR MINT; Q96KB5; -.
DR STRING; 9606.ENSP00000428489; -.
DR BindingDB; Q96KB5; -.
DR ChEMBL; CHEMBL4896; -.
DR GuidetoPHARMACOLOGY; 2140; -.
DR GlyGen; Q96KB5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96KB5; -.
DR PhosphoSitePlus; Q96KB5; -.
DR BioMuta; PBK; -.
DR DMDM; 83305809; -.
DR EPD; Q96KB5; -.
DR jPOST; Q96KB5; -.
DR MassIVE; Q96KB5; -.
DR MaxQB; Q96KB5; -.
DR PaxDb; Q96KB5; -.
DR PeptideAtlas; Q96KB5; -.
DR PRIDE; Q96KB5; -.
DR ProteomicsDB; 5416; -.
DR ProteomicsDB; 77056; -. [Q96KB5-1]
DR ABCD; Q96KB5; 2 sequenced antibodies.
DR Antibodypedia; 1595; 584 antibodies from 37 providers.
DR DNASU; 55872; -.
DR Ensembl; ENST00000301905.9; ENSP00000301905.4; ENSG00000168078.10. [Q96KB5-1]
DR Ensembl; ENST00000522944.5; ENSP00000428489.1; ENSG00000168078.10. [Q96KB5-2]
DR GeneID; 55872; -.
DR KEGG; hsa:55872; -.
DR MANE-Select; ENST00000301905.9; ENSP00000301905.4; NM_018492.4; NP_060962.2.
DR UCSC; uc011lap.4; human. [Q96KB5-1]
DR CTD; 55872; -.
DR DisGeNET; 55872; -.
DR GeneCards; PBK; -.
DR HGNC; HGNC:18282; PBK.
DR HPA; ENSG00000168078; Group enriched (lymphoid tissue, testis).
DR MIM; 611210; gene.
DR neXtProt; NX_Q96KB5; -.
DR OpenTargets; ENSG00000168078; -.
DR PharmGKB; PA134925802; -.
DR VEuPathDB; HostDB:ENSG00000168078; -.
DR eggNOG; KOG0192; Eukaryota.
DR GeneTree; ENSGT00720000108839; -.
DR HOGENOM; CLU_044128_1_0_1; -.
DR InParanoid; Q96KB5; -.
DR OMA; TFKMIMD; -.
DR OrthoDB; 1030296at2759; -.
DR PhylomeDB; Q96KB5; -.
DR TreeFam; TF329763; -.
DR PathwayCommons; Q96KB5; -.
DR SignaLink; Q96KB5; -.
DR SIGNOR; Q96KB5; -.
DR BioGRID-ORCS; 55872; 9 hits in 1109 CRISPR screens.
DR ChiTaRS; PBK; human.
DR GeneWiki; PBK_(gene); -.
DR GenomeRNAi; 55872; -.
DR Pharos; Q96KB5; Tchem.
DR PRO; PR:Q96KB5; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96KB5; protein.
DR Bgee; ENSG00000168078; Expressed in ventricular zone and 127 other tissues.
DR ExpressionAtlas; Q96KB5; baseline and differential.
DR Genevisible; Q96KB5; HS.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004706; F:JUN kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0004708; F:MAP kinase kinase activity; IEA:UniProtKB-EC.
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:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
DR GO; GO:0000278; P:mitotic cell cycle; NAS:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IEA:Ensembl.
DR GO; GO:0038066; P:p38MAPK cascade; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:1904291; P:positive regulation of mitotic DNA damage checkpoint; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR CDD; cd14001; PKc_TOPK; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR041989; PKc_TOPK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Isopeptide bond; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation.
FT CHAIN 1..322
FT /note="Lymphokine-activated killer T-cell-originated
FT protein kinase"
FT /id="PRO_0000086763"
FT DOMAIN 32..322
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 320..322
FT /note="PDZ-interaction"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 38..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 169
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 198
FT /note="T -> TAPAFITILLVS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055269"
FT VARIANT 107
FT /note="N -> S (in dbSNP:rs3779620)"
FT /evidence="ECO:0000269|PubMed:10779557,
FT ECO:0000269|PubMed:11378444, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_021162"
FT VARIANT 220
FT /note="E -> D (in dbSNP:rs17057901)"
FT /id="VAR_051676"
FT VARIANT 241
FT /note="M -> L (in dbSNP:rs36086402)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041234"
FT MUTAGEN 9
FT /note="T->E: TP53-binding."
FT /evidence="ECO:0000269|PubMed:17482142"
FT MUTAGEN 64..65
FT /note="KK->AA: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10779557"
FT MUTAGEN 320
FT /note="T->A: Decrease in the binding to DLG1."
FT /evidence="ECO:0000269|PubMed:10779557"
FT MUTAGEN 322
FT /note="V->A: Decrease in the binding to DLG1."
FT /evidence="ECO:0000269|PubMed:10779557"
FT CONFLICT 34
FT /note="F -> I (in Ref. 3; AAF71521)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="K -> E (in Ref. 4; BAB55019)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="D -> N (in Ref. 4; BAB55019)"
FT /evidence="ECO:0000305"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:5J0A"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:5J0A"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:5J0A"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:5J0A"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:5J0A"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:5J0A"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 140..159
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:5J0A"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:5J0A"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:5J0A"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:5J0A"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:5J0A"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 227..242
FT /evidence="ECO:0007829|PDB:5J0A"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:5J0A"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 268..274
FT /evidence="ECO:0007829|PDB:5J0A"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 291..300
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:5J0A"
FT HELIX 311..319
FT /evidence="ECO:0007829|PDB:5J0A"
SQ SEQUENCE 322 AA; 36085 MW; 6BF55789BC204ABE CRC64;
MEGISNFKTP SKLSEKKKSV LCSTPTINIP ASPFMQKLGF GTGVNVYLMK RSPRGLSHSP
WAVKKINPIC NDHYRSVYQK RLMDEAKILK SLHHPNIVGY RAFTEANDGS LCLAMEYGGE
KSLNDLIEER YKASQDPFPA AIILKVALNM ARGLKYLHQE KKLLHGDIKS SNVVIKGDFE
TIKICDVGVS LPLDENMTVT DPEACYIGTE PWKPKEAVEE NGVITDKADI FAFGLTLWEM
MTLSIPHINL SNDDDDEDKT FDESDFDDEA YYAALGTRPP INMEELDESY QKVIELFSVC
TNEDPKDRPS AAHIVEALET DV
