ID TOPK_MOUSE Reviewed; 330 AA.
AC Q9JJ78; Q922V2; Q9D184;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 165.
DE RecName: Full=Lymphokine-activated killer T-cell-originated protein kinase;
DE EC=2.7.12.2;
DE AltName: Full=PDZ-binding kinase;
DE AltName: Full=T-LAK cell-originated protein kinase;
GN Name=Pbk; Synonyms=Topk;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetus;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland, and Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
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:0000250}.
CC -!- PTM: Phosphorylated; in a cell-cycle dependent manner at mitosis.
CC {ECO:0000250}.
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; AB041882; BAA99578.1; -; mRNA.
DR EMBL; AK003838; BAB23029.1; -; mRNA.
DR EMBL; AK076121; BAC36199.1; -; mRNA.
DR EMBL; BC006754; AAH06754.1; -; mRNA.
DR EMBL; BC020099; AAH20099.1; -; mRNA.
DR CCDS; CCDS27215.1; -.
DR RefSeq; NP_075698.1; NM_023209.2.
DR RefSeq; XP_006519320.1; XM_006519257.3.
DR AlphaFoldDB; Q9JJ78; -.
DR SMR; Q9JJ78; -.
DR BioGRID; 206338; 7.
DR IntAct; Q9JJ78; 1.
DR MINT; Q9JJ78; -.
DR STRING; 10090.ENSMUSP00000022612; -.
DR iPTMnet; Q9JJ78; -.
DR PhosphoSitePlus; Q9JJ78; -.
DR SwissPalm; Q9JJ78; -.
DR EPD; Q9JJ78; -.
DR jPOST; Q9JJ78; -.
DR MaxQB; Q9JJ78; -.
DR PaxDb; 10090-ENSMUSP00000022612; -.
DR PeptideAtlas; Q9JJ78; -.
DR ProteomicsDB; 259289; -.
DR Pumba; Q9JJ78; -.
DR Antibodypedia; 1595; 659 antibodies from 37 providers.
DR DNASU; 52033; -.
DR Ensembl; ENSMUST00000022612.10; ENSMUSP00000022612.4; ENSMUSG00000022033.10.
DR GeneID; 52033; -.
DR KEGG; mmu:52033; -.
DR UCSC; uc007ujo.1; mouse.
DR AGR; MGI:1289156; -.
DR CTD; 55872; -.
DR MGI; MGI:1289156; Pbk.
DR VEuPathDB; HostDB:ENSMUSG00000022033; -.
DR eggNOG; KOG0192; Eukaryota.
DR GeneTree; ENSGT00720000108839; -.
DR HOGENOM; CLU_044128_0_0_1; -.
DR InParanoid; Q9JJ78; -.
DR OMA; KDSQDPF; -.
DR OrthoDB; 5474002at2759; -.
DR PhylomeDB; Q9JJ78; -.
DR TreeFam; TF329763; -.
DR BioGRID-ORCS; 52033; 1 hit in 81 CRISPR screens.
DR ChiTaRS; Pbk; mouse.
DR PRO; PR:Q9JJ78; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9JJ78; Protein.
DR Bgee; ENSMUSG00000022033; Expressed in dorsal pancreas and 233 other cell types or tissues.
DR ExpressionAtlas; Q9JJ78; baseline and differential.
DR Genevisible; Q9JJ78; MM.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IDA:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0034644; P:cellular response to UV; IMP:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IMP:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IMP:MGI.
DR CDD; cd14001; PKc_TOPK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR43289:SF35; LYMPHOKINE-ACTIVATED KILLER T-CELL-ORIGINATED PROTEIN KINASE-RELATED; 1.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Isopeptide bond; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Ubl conjugation.
FT CHAIN 1..330
FT /note="Lymphokine-activated killer T-cell-originated
FT protein kinase"
FT /id="PRO_0000086764"
FT DOMAIN 31..330
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 37..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 63
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:0000250|UniProtKB:Q96KB5"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96KB5"
FT MOD_RES 23
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96KB5"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KB5"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 168
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96KB5"
FT CONFLICT 123
FT /note="N -> D (in Ref. 2; BAB23029)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 36745 MW; D274A4DB44CFEEE0 CRC64;
MEGINNFKTP NKSEKRKSVL CSTPCVNIPA SPFMQKLGFG TGVSVYLMKR SPRGLSHSPW
AVKKISLLCD DHYRTVYQKR LTDEAKILKN LNHPNIIGYR AFTEASDGSL CLAMEYGGEK
SLNDLIEERN KDSGSPFPAA VILRVALHMA RGLKYLHQEK KLLHGDIKSS NVVIKGDFET
IKICDVGVSL PLDENMTVTD PEACYIGTEP WKPKEALEEN GIITDKADVF AFGLTLWEMM
TLCIPHVNLP DDDVDEDATF DESDFDDEAY YAALGTRPSI NMEELDDSYQ KAIELFCVCT
NEDPKDRPSA AHIVEALELD GQCCGLSSKH
//
