ID   CDCA2_BOVIN             Reviewed;        1011 AA.
AC   Q29RT4;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Cell division cycle-associated protein 2;
GN   Name=CDCA2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- PTM: Phosphorylated by CDK1. May regulate its subcellular location (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; BC114031; AAI14032.1; -; mRNA.
DR   RefSeq; NP_001039659.1; NM_001046194.1.
DR   AlphaFoldDB; Q29RT4; -.
DR   SMR; Q29RT4; -.
DR   STRING; 9913.ENSBTAP00000054520; -.
DR   PaxDb; Q29RT4; -.
DR   PRIDE; Q29RT4; -.
DR   GeneID; 515287; -.
DR   KEGG; bta:515287; -.
DR   CTD; 157313; -.
DR   eggNOG; ENOG502S079; Eukaryota.
DR   InParanoid; Q29RT4; -.
DR   OrthoDB; 290017at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005694; C:chromosome; IBA:GO_Central.
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:0035307; P:positive regulation of protein dephosphorylation; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Isopeptide bond; Mitosis; Nucleus;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..1011
FT                   /note="Cell division cycle-associated protein 2"
FT                   /id="PRO_0000287694"
FT   DOMAIN          380..440
FT                   /note="PP1-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          522..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          790..835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          896..1011
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..544
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..949
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        968..987
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        989..1011
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         125
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT   MOD_RES         130
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT   MOD_RES         209
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT   MOD_RES         293
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT   MOD_RES         310
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT   MOD_RES         313
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT   MOD_RES         391
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT   MOD_RES         398
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT   MOD_RES         403
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT   MOD_RES         428
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT   MOD_RES         583
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT   MOD_RES         702
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT   MOD_RES         747
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT   MOD_RES         967
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
FT   CROSSLNK        753
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q69YH5"
SQ   SEQUENCE   1011 AA;  110998 MW;  26D693548980701B CRC64;
     MDTCSQESEP LQTKESPINN AGKTPLVLGN GKLVTPHKQA AEMTPNCYTS ETFKSPLNFS
     TVTVEQLGIS PESFVNNSSG KSSPYLKKSR RRSTVGLRGL PETNHLIRFV AEQRSLKNAS
     LTQTSPFQGS PALYRNVYSL REQMSAFHLA FNSIKENEKM TDCPEFSEAE GVFKTRGSTK
     KESLGECQLS EFSAQSSSKR RRLSSPSSSD VNLTDAVDLQ ACGVNMAACP STDMKCAVET
     CAGLSQKSSA SGLNLQCGCL MNESPLLSEL TEASSGIQDA ASVEERGSND AVSVDKCTEV
     STDTAPEVRS LVTPLCQKDL PSSKTFVLRS VLKKPAVKLC VESLQEHLDN LYNDETCPSL
     TSSLANSCKE QTAALPNTKK RKRVTFGEDL SPEVLDESLP ANTPLRKGQT PVRKKDLSSL
     SPPLLEQSPV PEWLPQPNFD DKEENLENIE PLQVSFAVLS SLNMSSIAET LSGTDTSASS
     SNHENIAPFR VGRATRTSDR RSKLISFSQE SVCNLLNAEA QPCKEKKTNR RKSQESKHAD
     KVLPRKNRVL KGCKKKKGKG KRKGVQKSLY GERDLASKKP LLSPIPELPE VSETPLVGSL
     VRRTYPDDFN SNGKFEEMML PKRENLLSQD PEDWQVIQGF NKDNASESCS SDMKSSSSFS
     NATFEQDANI NSIEMDENEN IPKAITLESE NERKTGTECE NSHISCTLVT VTPVVSDNPK
     PDFPLQSQEL SAAGQNVENL FQIVKISEDM NIKCEKQSGF SVIPEDKLQT EHLIPDSQKE
     CDCSEDVLTD QRKVSKSQGE DLGRNSAASC SGVSDRERKY RGHSVGGSDG PGLHLERTNN
     LQTSYSMSSL VEISLENSEL CKDLSDSIEQ SLQRTKSETK VRRSLRLQKS LEREGGLVWV
     SPPPPPASCT SQRTKRRTVG TLDSRGFEPV SSRQDPCTLP STSSEENGEG FTAAPDASLP
     GKRRRRSFCT STLANPKSTT QSRGCKRRSF LGQKRENTLQ ETSRESDLSE N