CCNA2_MESAU
ID CCNA2_MESAU Reviewed; 421 AA.
AC P37881;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cyclin-A2 {ECO:0000305};
DE Short=Cyclin-A {ECO:0000312|EMBL:BAA04128.1};
GN Name=CCNA2 {ECO:0000250|UniProtKB:P20248};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shiraki T., Yamashita K., Nishitani H., Nishimoto T.;
RT "Nucleotide sequence of hamster cyclinA cDNA.";
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cyclin which controls both the G1/S and the G2/M transition
CC phases of the cell cycle. Functions through the formation of specific
CC serine/threonine kinase holoenzyme complexes with the cyclin-dependent
CC protein kinases CDK1 and CDK2. The cyclin subunit confers the substrate
CC specificity of these complexes and differentially interacts with and
CC activates CDK1 and CDK2 throughout the cell cycle.
CC {ECO:0000250|UniProtKB:P20248}.
CC -!- SUBUNIT: Interacts with the CDK1 and CDK2 protein kinases to form
CC serine/threonine kinase holoenzyme complexes. Interacts with CDK1
CC (hyperphosphorylated form in G1 and underphosphorylated forms in S and
CC G2). Interacts with CDK2; the interaction increases from G1 to G2.
CC Interacts (associated with CDK2 but not with CDK1) with SCAPER;
CC regulates the activity of CCNA2/CDK2 by transiently maintaining CCNA2
CC in the cytoplasm. Forms a ternary complex with CDK2 and CDKN1B; CDKN1B
CC inhibits the kinase activity of CDK2 through conformational
CC rearrangements. Interacts with INCA1. {ECO:0000250|UniProtKB:P20248}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P20248}. Cytoplasm
CC {ECO:0000250|UniProtKB:P20248}. Note=Exclusively nuclear during
CC interphase. Detected in the nucleus and the cytoplasm at prophase.
CC Cytoplasmic when associated with SCAPER.
CC {ECO:0000250|UniProtKB:P20248}.
CC -!- PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the anaphase-
CC promoting complex (APC/C), leading to its degradation by the
CC proteasome. Deubiquitinated and stabilized by USP37 enables entry into
CC S phase. {ECO:0000250|UniProtKB:P20248}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; D17295; BAA04128.1; -; mRNA.
DR RefSeq; NP_001268563.1; NM_001281634.1.
DR AlphaFoldDB; P37881; -.
DR SMR; P37881; -.
DR STRING; 10036.XP_005069757.1; -.
DR GeneID; 101835930; -.
DR CTD; 890; -.
DR eggNOG; KOG0654; Eukaryota.
DR OrthoDB; 993640at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0097124; C:cyclin A2-CDK2 complex; IEA:Ensembl.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0001939; C:female pronucleus; IEA:Ensembl.
DR GO; GO:0001940; C:male pronucleus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0044843; P:cell cycle G1/S phase transition; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0016572; P:histone phosphorylation; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:Ensembl.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR032447; Cyclin-A_N.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR Pfam; PF16500; Cyclin_N2; 1.
DR PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Cyclin; Cytoplasm; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..421
FT /note="Cyclin-A2"
FT /id="PRO_0000080339"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P20248"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20248"
SQ SEQUENCE 421 AA; 47327 MW; F5736C97D62667CD CRC64;
MPGSSRQSGR EAGSALLSLQ QEDQENVNPE KAAPDQRARA ALKTGNARGN APQQRLKARR
VAPLKDLSIN DEHVASGPSW KAASKQPAFT IHVDEEEDTQ KIPPEHKEMR CEDALAFNAA
VSLPGARKPL VPLDYPMDGS FESPHAMDMS IVLEEEKPVS VNEVPDYHED IHTYLREMEI
KCKPKVGYMK KQPDITNSMR AILVDWLVEV GEEYKLQNET LHLAVNYIDR FLSSMSVLRG
KLQLVGTAAM LLASKFEEIY PPEVAEFVYI TDDTYSKKQV LRMEHLVLKV LAFDLAAPTV
NQFLNQYFLH QQPANCKVES LAMFLGELSL IDADPYLKYL PSLIAGAAFH LALYTVTGQS
WPESLVQKTG YTLESLKPCL MDLHQTYLRA AQHTQQSIRE KYKHSKYHGV SLLNPPETLN
V
