ID   CKS1_MOUSE              Reviewed;          79 AA.
AC   P61025; P33551; Q6ZWX7;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 1.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=Cyclin-dependent kinases regulatory subunit 1;
DE            Short=CKS-1;
DE   AltName: Full=Sid 1334;
GN   Name=Cks1b; Synonyms=Cks1, Sid1334;
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].
RA   Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT   "Mouse cks1 sid1334.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
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=C57BL/6J; 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: Binds to the catalytic subunit of the cyclin dependent
CC       kinases and is essential for their biological function. {ECO:0000250}.
CC   -!- SUBUNIT: Forms a homohexamer that can probably bind six kinase
CC       subunits. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CKS family. {ECO:0000305}.
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DR   EMBL; AB025409; BAA84694.1; -; mRNA.
DR   EMBL; AK010414; BAC25295.1; -; mRNA.
DR   EMBL; AK011782; BAB27837.1; -; mRNA.
DR   EMBL; BC076579; AAH76579.1; -; mRNA.
DR   CCDS; CCDS38493.1; -.
DR   RefSeq; NP_058600.1; NM_016904.1.
DR   AlphaFoldDB; P61025; -.
DR   SMR; P61025; -.
DR   BioGRID; 207564; 2.
DR   STRING; 10090.ENSMUSP00000029679; -.
DR   iPTMnet; P61025; -.
DR   PhosphoSitePlus; P61025; -.
DR   EPD; P61025; -.
DR   MaxQB; P61025; -.
DR   PaxDb; 10090-ENSMUSP00000029679; -.
DR   PeptideAtlas; P61025; -.
DR   ProteomicsDB; 281634; -.
DR   Pumba; P61025; -.
DR   Antibodypedia; 47036; 283 antibodies from 26 providers.
DR   DNASU; 54124; -.
DR   Ensembl; ENSMUST00000029679.4; ENSMUSP00000029679.4; ENSMUSG00000028044.7.
DR   GeneID; 54124; -.
DR   KEGG; mmu:54124; -.
DR   UCSC; uc008pzl.1; mouse.
DR   AGR; MGI:1889208; -.
DR   CTD; 1163; -.
DR   MGI; MGI:1889208; Cks1b.
DR   VEuPathDB; HostDB:ENSMUSG00000028044; -.
DR   eggNOG; KOG3484; Eukaryota.
DR   GeneTree; ENSGT00950000182971; -.
DR   HOGENOM; CLU_140546_2_0_1; -.
DR   InParanoid; P61025; -.
DR   OMA; HYANHKP; -.
DR   OrthoDB; 204504at2759; -.
DR   PhylomeDB; P61025; -.
DR   TreeFam; TF101142; -.
DR   Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR   BioGRID-ORCS; 54124; 9 hits in 82 CRISPR screens.
DR   ChiTaRS; Cks1b; mouse.
DR   PRO; PR:P61025; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P61025; Protein.
DR   Bgee; ENSMUSG00000028044; Expressed in endocardial cushion and 247 other cell types or tissues.
DR   ExpressionAtlas; P61025; baseline and differential.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0048144; P:fibroblast proliferation; IGI:MGI.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IGI:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IGI:MGI.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR   Gene3D; 3.30.170.10; Cyclin-dependent kinase, regulatory subunit; 1.
DR   InterPro; IPR000789; Cyclin-dep_kinase_reg-sub.
DR   InterPro; IPR036858; Cyclin-dep_kinase_reg-sub_sf.
DR   PANTHER; PTHR23415:SF50; CYCLIN-DEPENDENT KINASES REGULATORY SUBUNIT 1; 1.
DR   PANTHER; PTHR23415; CYCLIN-DEPENDENT KINASES REGULATORY SUBUNIT/60S RIBOSOME SUBUNIT BIOGENESIS PROTEIN NIP7; 1.
DR   Pfam; PF01111; CKS; 1.
DR   PRINTS; PR00296; CYCLINKINASE.
DR   SMART; SM01084; CKS; 1.
DR   SUPFAM; SSF55637; Cell cycle regulatory proteins; 1.
DR   PROSITE; PS00944; CKS_1; 1.
DR   PROSITE; PS00945; CKS_2; 1.
DR   Genevisible; P61025; MM.
PE   3: Inferred from homology;
KW   Acetylation; Cell cycle; Cell division; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P61024"
FT   CHAIN           2..79
FT                   /note="Cyclin-dependent kinases regulatory subunit 1"
FT                   /id="PRO_0000206236"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P61024"
SQ   SEQUENCE   79 AA;  9660 MW;  E64207B140FA38D5 CRC64;
     MSHKQIYYSD KYDDEEFEYR HVMLPKDIAK LVPKTHLMSE SEWRNLGVQQ SQGWVHYMIH
     EPEPHILLFR RPLPKKPKK
//