ID   CDKA1_MOUSE             Reviewed;         114 AA.
AC   O35207; B2RV53; Q3SYK3; Q6ZWZ1;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   24-JAN-2024, entry version 139.
DE   RecName: Full=Cyclin-dependent kinase 2-associated protein 1;
DE            Short=CDK2-associated protein 1;
DE   AltName: Full=Deleted in oral cancer 1;
DE            Short=DOC-1;
DE   AltName: Full=Putative oral cancer suppressor;
GN   Name=Cdk2ap1; Synonyms=Cdkap1, Doc1;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
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].
RC   STRAIN=FVB/N-3; TISSUE=Brain, Colon, 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   NUCLEOTIDE SEQUENCE [MRNA] OF 6-114.
RC   TISSUE=Fibroblast;
RA   Wong D.T.W., Tsuji T., Todd R., McBride J.;
RT   "Molecular cloning and characterization of mouse doc-1 oral tumor
RT   suppressor gene.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, AND INTERACTION WITH CDK2.
RX   PubMed=10938106; DOI=10.1128/mcb.20.17.6300-6307.2000;
RA   Shintani S., Ohyama H., Zhang X., McBride J., Matsuo K., Tsuji T., Hu M.G.,
RA   Hu G., Kohno Y., Lerman M., Todd R., Wong D.T.;
RT   "p12(DOC-1) is a novel cyclin-dependent kinase 2-associated protein.";
RL   Mol. Cell. Biol. 20:6300-6307(2000).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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: Inhibitor of cyclin-dependent kinase CDK2 (PubMed:10938106).
CC       Also acts as a component of the histone deacetylase NuRD complex which
CC       participates in the remodeling of chromatin (By similarity).
CC       {ECO:0000250|UniProtKB:O14519, ECO:0000269|PubMed:10938106}.
CC   -!- SUBUNIT: Homodimer (By similarity). Component of the nucleosome
CC       remodeling and deacetylase (NuRD) repressor complex, composed of core
CC       proteins MTA1, MTA2, MTA3, RBBP4, RBBP7, HDAC1, HDAC2, MBD2, MBD3, and
CC       peripherally associated proteins CDK2AP1, CDK2AP2, GATAD2A, GATAD2B,
CC       CHD3, CHD4 and CHD5 (By similarity). The exact stoichiometry of the
CC       NuRD complex is unknown, and some subunits such as MBD2 and MBD3,
CC       GATAD2A and GATAD2B, and CHD3, CHD4 and CHD5 define mutually exclusive
CC       NuRD complexes (By similarity). Interacts with monomeric
CC       unphosphorylated CDK2 (PubMed:10938106). Interacts with CDK2AP2 (By
CC       similarity). Interacts with GATAD2A (By similarity). Interacts with
CC       HDAC1 (By similarity). Interacts with HDAC2 (By similarity). Interacts
CC       with MBD2 (By similarity). Interacts with MBD3 (By similarity).
CC       Interacts with RBBP4 (By similarity). Interacts with RBBP7 (By
CC       similarity). {ECO:0000250|UniProtKB:O14519,
CC       ECO:0000269|PubMed:10938106}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O14519}.
CC       Chromosome {ECO:0000250|UniProtKB:O14519}.
CC   -!- PTM: Phosphorylated in vitro by IKBKE at Ser-45.
CC       {ECO:0000250|UniProtKB:O14519}.
CC   -!- SIMILARITY: Belongs to the CDK2AP family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK004852; BAB23616.1; -; mRNA.
DR   EMBL; AL645849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC083075; AAH83075.1; -; mRNA.
DR   EMBL; BC103772; AAI03773.1; -; mRNA.
DR   EMBL; BC147052; AAI47053.1; -; mRNA.
DR   EMBL; BC147053; AAI47054.1; -; mRNA.
DR   EMBL; AF011644; AAB65752.1; -; mRNA.
DR   CCDS; CCDS39279.1; -.
DR   RefSeq; NP_038840.2; NM_013812.2.
DR   AlphaFoldDB; O35207; -.
DR   SMR; O35207; -.
DR   BioGRID; 199264; 14.
DR   IntAct; O35207; 13.
DR   STRING; 10090.ENSMUSP00000031341; -.
DR   PhosphoSitePlus; O35207; -.
DR   EPD; O35207; -.
DR   MaxQB; O35207; -.
DR   PaxDb; 10090-ENSMUSP00000031341; -.
DR   PeptideAtlas; O35207; -.
DR   ProteomicsDB; 281441; -.
DR   Pumba; O35207; -.
DR   DNASU; 13445; -.
DR   Ensembl; ENSMUST00000031341.11; ENSMUSP00000031341.5; ENSMUSG00000029394.12.
DR   Ensembl; ENSMUST00000104959.2; ENSMUSP00000100565.2; ENSMUSG00000078154.4.
DR   GeneID; 13445; -.
DR   KEGG; mmu:13445; -.
DR   UCSC; uc008zpo.1; mouse.
DR   AGR; MGI:1202069; -.
DR   CTD; 8099; -.
DR   MGI; MGI:1202069; Cdk2ap1.
DR   VEuPathDB; HostDB:ENSMUSG00000029394; -.
DR   VEuPathDB; HostDB:ENSMUSG00000078154; -.
DR   eggNOG; KOG4713; Eukaryota.
DR   GeneTree; ENSGT00940000155149; -.
DR   HOGENOM; CLU_130479_1_0_1; -.
DR   InParanoid; O35207; -.
DR   OMA; CGSHRDF; -.
DR   OrthoDB; 5396585at2759; -.
DR   PhylomeDB; O35207; -.
DR   TreeFam; TF101037; -.
DR   BioGRID-ORCS; 13445; 6 hits in 77 CRISPR screens.
DR   ChiTaRS; Cdk2ap1; mouse.
DR   PRO; PR:O35207; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; O35207; Protein.
DR   Bgee; ENSMUSG00000029394; Expressed in undifferentiated genital tubercle and 62 other cell types or tissues.
DR   ExpressionAtlas; O35207; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0016581; C:NuRD complex; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR   Gene3D; 6.10.140.1300; -; 1.
DR   InterPro; IPR017266; DOC_1/2.
DR   PANTHER; PTHR22607:SF2; CYCLIN-DEPENDENT KINASE 2-ASSOCIATED PROTEIN 1; 1.
DR   PANTHER; PTHR22607; DELETED IN ORAL CANCER 1/CDK2-ASSOCIATED PROTEIN 1; 1.
DR   Pfam; PF09806; CDK2AP; 1.
DR   PIRSF; PIRSF037709; CDK2-associated_p2; 1.
DR   Genevisible; O35207; MM.
PE   1: Evidence at protein level;
KW   Cell cycle; Chromosome; Disulfide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Tumor suppressor.
FT   CHAIN           1..114
FT                   /note="Cyclin-dependent kinase 2-associated protein 1"
FT                   /id="PRO_0000089454"
FT   REGION          18..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          19..24
FT                   /note="Interaction with CDK2AP2"
FT                   /evidence="ECO:0000250|UniProtKB:O14519"
FT   COMPBIAS        19..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         45
FT                   /note="Phosphoserine; by IKKE"
FT                   /evidence="ECO:0000250|UniProtKB:O14519"
FT   DISULFID        104
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   114 AA;  12354 MW;  6421DD87E438F02D CRC64;
     MSYKPNLTAH MPAAALNAGS VHSPSTSMAT SSQYRQLLSD YGPPSLGYTQ GTGNSQVPQS
     KYAELLAIIE ELGKEIRPTY AGSKSAMERL KRGIIHARSL VRECLAETER NARS
//