CDCA2_MOUSE
ID CDCA2_MOUSE Reviewed; 982 AA.
AC Q14B71; Q8BSQ1; Q8CD75;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Cell division cycle-associated protein 2;
GN Name=Cdca2;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 157-982 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Forelimb, and Testis;
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] OF 157-982 (ISOFORM 1).
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-296, AND IDENTIFICATION BY
RP 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: Regulator of chromosome structure during mitosis required for
CC condensin-depleted chromosomes to retain their compact architecture
CC through anaphase. Acts by mediating the recruitment of phopsphatase
CC PP1-gamma subunit (PPP1CC) to chromatin at anaphase and into the
CC following interphase. At anaphase onset, its association with chromatin
CC targets a pool of PPP1CC to dephosphorylate substrates (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PPP1CC. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Excluded from the
CC nucleolus. Present in nucleoplasm throughout the G1, S and G2 stages of
CC the cell cycle. During M phase, it becomes diffuse throughout the cell
CC as the nuclear membrane breaks down, and faintly accumulates later on
CC metaphase chromatin. As the cell progresses to anaphase, it accumulates
CC on chromatin (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14B71-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14B71-2; Sequence=VSP_025600, VSP_025601;
CC -!- PTM: Phosphorylated by CDK1. May regulate its subcellular location (By
CC similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI16299.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI16300.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC27343.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK031083; BAC27245.1; -; mRNA.
DR EMBL; AK031313; BAC27343.1; ALT_INIT; mRNA.
DR EMBL; AC093020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC116298; AAI16299.1; ALT_INIT; mRNA.
DR EMBL; BC116299; AAI16300.1; ALT_INIT; mRNA.
DR CCDS; CCDS36962.2; -. [Q14B71-1]
DR RefSeq; NP_001103632.1; NM_001110162.1. [Q14B71-1]
DR RefSeq; NP_780593.3; NM_175384.4. [Q14B71-1]
DR RefSeq; XP_006518483.1; XM_006518420.3. [Q14B71-1]
DR AlphaFoldDB; Q14B71; -.
DR SMR; Q14B71; -.
DR STRING; 10090.ENSMUSP00000117847; -.
DR iPTMnet; Q14B71; -.
DR PhosphoSitePlus; Q14B71; -.
DR EPD; Q14B71; -.
DR jPOST; Q14B71; -.
DR MaxQB; Q14B71; -.
DR PaxDb; Q14B71; -.
DR PeptideAtlas; Q14B71; -.
DR PRIDE; Q14B71; -.
DR ProteomicsDB; 281139; -. [Q14B71-1]
DR ProteomicsDB; 281140; -. [Q14B71-2]
DR Antibodypedia; 10001; 143 antibodies from 27 providers.
DR DNASU; 108912; -.
DR Ensembl; ENSMUST00000150006; ENSMUSP00000117847; ENSMUSG00000048922. [Q14B71-1]
DR Ensembl; ENSMUST00000163100; ENSMUSP00000127571; ENSMUSG00000048922. [Q14B71-1]
DR GeneID; 108912; -.
DR KEGG; mmu:108912; -.
DR UCSC; uc007ulb.2; mouse. [Q14B71-1]
DR UCSC; uc007uld.2; mouse. [Q14B71-2]
DR CTD; 157313; -.
DR MGI; MGI:1919787; Cdca2.
DR VEuPathDB; HostDB:ENSMUSG00000048922; -.
DR eggNOG; ENOG502S079; Eukaryota.
DR GeneTree; ENSGT00940000154352; -.
DR HOGENOM; CLU_011968_0_0_1; -.
DR InParanoid; Q14B71; -.
DR OMA; CDCSEDV; -.
DR OrthoDB; 290017at2759; -.
DR PhylomeDB; Q14B71; -.
DR TreeFam; TF336000; -.
DR BioGRID-ORCS; 108912; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Cdca2; mouse.
DR PRO; PR:Q14B71; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q14B71; protein.
DR Bgee; ENSMUSG00000048922; Expressed in manus and 150 other tissues.
DR ExpressionAtlas; Q14B71; baseline and differential.
DR Genevisible; Q14B71; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IDA:MGI.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:MGI.
DR GO; GO:0051983; P:regulation of chromosome segregation; IBA:GO_Central.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IBA:GO_Central.
DR InterPro; IPR033064; CDCA2.
DR InterPro; IPR029334; PP1-bd.
DR PANTHER; PTHR21603:SF16; PTHR21603:SF16; 1.
DR Pfam; PF15276; PP1_bind; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Isopeptide bond; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..982
FT /note="Cell division cycle-associated protein 2"
FT /id="PRO_0000287696"
FT DOMAIN 379..436
FT /note="PP1-binding"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT REGION 75..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..545
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT MOD_RES 309
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT MOD_RES 402
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT MOD_RES 913
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT MOD_RES 950
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT CROSSLNK 741
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT VAR_SEQ 341..392
FT /note="ESNLCDDGAHLISYPSNSCKEGRAGRENCKTPGCLNPRKRKRVTFGEDLSPE
FT -> VRVTLPKAKEFRDVCFRAVREIHVSHWCAGKPSLVCHFLKSQYYSEIGSVFK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025600"
FT VAR_SEQ 393..982
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025601"
FT CONFLICT 391
FT /note="P -> H (in Ref. 1; BAC27343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 982 AA; 106366 MW; 6DA939D78072A66C CRC64;
MDASSHDKPL SESKECVLNN SENDVFRLGT EPFVTPQKHV ADATPNLCTP DTFKSPLDFT
TVTVEQLGIT PESFVKTSSG KSTSSLQKAR RRSTVGVRGS PETNCLIRFI AQQRNLKKAV
LSPLAREPHF EGSPRLYRNA SVLRERMSAF RSAFHSIQET KMASSPSAAE ADGESRISDL
TRKEDLLEYQ QSGFPVNSSS KRRRISSQDS PDNYLSGTKA LADEACAGGA STDLAEKSPD
IGSAQPGCMA APLPELRETS QGLAVTDCVE GPVTPLSSGT ATATRSPETP MCGSSSPSAK
TTATRSPATP VCGSSTPSAK TFVLRSVLKK PGKLFSENGK ESNLCDDGAH LISYPSNSCK
EGRAGRENCK TPGCLNPRKR KRVTFGEDLS PEVFDESLPA NTPLCKGGTP VRPRTVKTTS
PLQSPVHEQF LQPNFDDKEE NLENIEPPQG SFANLSLSKS SLSETPPGTN TCSSLNKDEE
IICSIVRPTR TSQRRKQTLS STGVCSSYTT QAEPRKEKMS RRKSREKKHT SAALPKKKQV
LKSYRKKKKG KKDVEKCFYG PRDIASKKPL LSPIPELPEV SEATPLADCT QGTSSDDFNK
CGQLEEVNSF EIPTQRKRRL PQKADSPELD PAHHQSQVSD KCCYLLPLTT ASERGPNAST
RDTGSEGNTR AESKCQSAKE PKPGTKMESG LVPRASVTQD HIVSKNPKPL GSPQSQDLFK
AGQNLENPCE ILIVSESMNL KCEKESECLA PQGSLQGSPV STDSKRDLNC SEDVLIQNIK
EPASHSENVG RKCAGNGSPG SGRERKWRRR TVCCGGQSSY LEQNGNPASS CSGENFVEIS
LESVQLIEEL SNTIEQSFQR TSSKTKVRRS TRLQRDLENT GLVWLSPSPS TLQKPRRRMT
ICTLDSRGFE CPSSKEETIS SGQNPGPLPA VSGSESQGVG SSALPRKRRS LCGSTLTDAN
SATQPPDCKR KPSLKGESAQ LP
