CDK15_MOUSE
ID CDK15_MOUSE Reviewed; 433 AA.
AC Q3V3A1; B2RVR3; B7ZWG3;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cyclin-dependent kinase 15;
DE EC=2.7.11.22 {ECO:0000250|UniProtKB:Q96Q40};
DE AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 7 protein homolog;
DE AltName: Full=Cell division protein kinase 15;
DE AltName: Full=Serine/threonine-protein kinase ALS2CR7;
DE AltName: Full=Serine/threonine-protein kinase PFTAIRE-2;
GN Name=Cdk15; Synonyms=Als2cr7, Pftk2;
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] {ECO:0000305, ECO:0000312|EMBL:BAE20636.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE20636.1};
RC TISSUE=Cerebellum {ECO:0000312|EMBL:BAE20636.1};
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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).
CC -!- FUNCTION: Serine/threonine-protein kinase that acts like an
CC antiapoptotic protein that counters TRAIL/TNFSF10-induced apoptosis by
CC inducing phosphorylation of BIRC5 at 'Thr-34'.
CC {ECO:0000250|UniProtKB:Q96Q40}.
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=2.7.11.22;
CC Evidence={ECO:0000250|UniProtKB:Q96Q40};
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=2.7.11.22; Evidence={ECO:0000250|UniProtKB:Q96Q40};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P28523};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000305};
CC IsoId=Q3V3A1-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q3V3A1-2; Sequence=VSP_052350, VSP_052351;
CC Name=3;
CC IsoId=Q3V3A1-3; Sequence=VSP_038766;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; AK042881; BAE20636.1; -; mRNA.
DR EMBL; AC116995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC147314; AAI47315.1; -; mRNA.
DR EMBL; BC147315; AAI47316.1; -; mRNA.
DR EMBL; BC147758; AAI47759.1; -; mRNA.
DR EMBL; BC147763; AAI47764.1; -; mRNA.
DR EMBL; BC172036; AAI72036.1; -; mRNA.
DR CCDS; CCDS48273.1; -. [Q3V3A1-1]
DR RefSeq; NP_001028545.2; NM_001033373.2. [Q3V3A1-1]
DR RefSeq; XP_006496113.1; XM_006496050.3.
DR AlphaFoldDB; Q3V3A1; -.
DR SMR; Q3V3A1; -.
DR STRING; 10090.ENSMUSP00000124680; -.
DR iPTMnet; Q3V3A1; -.
DR PhosphoSitePlus; Q3V3A1; -.
DR jPOST; Q3V3A1; -.
DR MaxQB; Q3V3A1; -.
DR PaxDb; Q3V3A1; -.
DR PRIDE; Q3V3A1; -.
DR ProteomicsDB; 281290; -. [Q3V3A1-1]
DR ProteomicsDB; 281292; -. [Q3V3A1-3]
DR Antibodypedia; 19940; 256 antibodies from 27 providers.
DR DNASU; 271697; -.
DR Ensembl; ENSMUST00000114248; ENSMUSP00000109886; ENSMUSG00000026023. [Q3V3A1-1]
DR GeneID; 271697; -.
DR KEGG; mmu:271697; -.
DR UCSC; uc007bdq.2; mouse. [Q3V3A1-3]
DR UCSC; uc007bdr.2; mouse. [Q3V3A1-1]
DR UCSC; uc007bds.2; mouse. [Q3V3A1-2]
DR CTD; 65061; -.
DR MGI; MGI:3583944; Cdk15.
DR VEuPathDB; HostDB:ENSMUSG00000026023; -.
DR eggNOG; KOG0594; Eukaryota.
DR GeneTree; ENSGT00940000159606; -.
DR HOGENOM; CLU_000288_181_6_1; -.
DR InParanoid; Q3V3A1; -.
DR OMA; YMAQHPG; -.
DR OrthoDB; 1010560at2759; -.
DR PhylomeDB; Q3V3A1; -.
DR BioGRID-ORCS; 271697; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Cdk15; mouse.
DR PRO; PR:Q3V3A1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3V3A1; protein.
DR Bgee; ENSMUSG00000026023; Expressed in animal zygote and 40 other tissues.
DR ExpressionAtlas; Q3V3A1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR CDD; cd07870; STKc_PFTAIRE2; 1.
DR InterPro; IPR042761; CDK15_STKc.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..433
FT /note="Cyclin-dependent kinase 15"
FT /id="PRO_0000283822"
FT DOMAIN 52..336
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 46..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 58..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..290
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052350"
FT VAR_SEQ 90
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038766"
FT VAR_SEQ 336..398
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052351"
SQ SEQUENCE 433 AA; 48457 MW; 9584802B36C2224F CRC64;
MGQELCAKRL QPGCSCYHRS EGGEAHSCQR SQPGSTEPAV FELTEASSST ASFHPRGLEA
ASAQKLKSKR PRSNSDSFQE ENLRQGLPWK KSLPFGAASS YLNLEKLGEG SYAKVYKGIS
RINGQLVALK VISMNAEEGV PFTAIREASL LKGLKHANIV LLHDIVHTKE TLTFVFEYMH
TDLAQYMSQH PGGLHPHNVR LFMFQLLRGL AYIHHQRVLH RDLKPQNLLL SHLGELKLAD
FGLARAKSIP SQTYSSEVVT LWYRPPDALL GATEYSSELD IWGAGCIFIE MFQGQPLFPG
VSNILEQLEK IWEVLGVPTE DTWPGVSKLP NYNPEWFPPP KPQSLQIVWD RLGGVPEAED
LASQMLKGFP RDRVSAQEAL VHDYFSVLPS QLYQLPDEES LFAVSGVKLK PEMCDLSASY
RKRHHLVGVN KCW
