CCNA2_BOVIN
ID CCNA2_BOVIN Reviewed; 430 AA.
AC P30274; Q17QS7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 164.
DE RecName: Full=Cyclin-A2 {ECO:0000305};
DE Short=Cyclin-A {ECO:0000303|PubMed:1333843};
GN Name=CCNA2 {ECO:0000250|UniProtKB:P20248};
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=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-430.
RC TISSUE=Lymphocyte;
RX PubMed=1333843; DOI=10.1091/mbc.3.11.1279;
RA Kobayashi H., Stewart E., Poon R., Adamczewski J.P., Gannon J., Hunt T.;
RT "Identification of the domains in cyclin A required for binding to, and
RT activation of, p34cdc2 and p32cdk2 protein kinase subunits.";
RL Mol. Biol. Cell 3:1279-1294(1992).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 179-430.
RX PubMed=8591034; DOI=10.1016/s0969-2126(01)00259-3;
RA Brown N.R., Noble M.E.M., Endicott J.A., Garman E.F., Wakatsuki S.,
RA Mitchell E., Rasmussen B., Hunt T., Johnson L.N.;
RT "The crystal structure of cyclin A.";
RL Structure 3:1235-1247(1995).
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 -!- INTERACTION:
CC P30274; P24941: CDK2; Xeno; NbExp=2; IntAct=EBI-15688654, EBI-375096;
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; BC118203; AAI18204.1; -; mRNA.
DR EMBL; X68321; CAA48398.1; -; mRNA.
DR PIR; S24788; S24788.
DR RefSeq; NP_001068591.1; NM_001075123.1.
DR PDB; 1VIN; X-ray; 2.00 A; A=170-429.
DR PDB; 2G9X; X-ray; 2.50 A; B/D=170-430.
DR PDB; 3BHT; X-ray; 2.00 A; B/D=169-430.
DR PDB; 3BHU; X-ray; 2.30 A; B/D=169-430.
DR PDB; 3BHV; X-ray; 2.10 A; B/D=169-430.
DR PDB; 3DDP; X-ray; 2.70 A; B/D=169-430.
DR PDB; 3DDQ; X-ray; 1.80 A; B/D=169-430.
DR PDB; 3DOG; X-ray; 2.70 A; B/D=169-430.
DR PDB; 3MY5; X-ray; 2.10 A; B/D=169-430.
DR PDB; 3TNW; X-ray; 2.00 A; B/D=169-430.
DR PDB; 4BCN; X-ray; 2.10 A; D=169-430.
DR PDB; 4BCO; X-ray; 2.05 A; B/D=169-429.
DR PDB; 4BCQ; X-ray; 2.40 A; B=169-429, D=169-430.
DR PDB; 6GUB; X-ray; 2.52 A; B/D=170-430.
DR PDB; 6GUC; X-ray; 2.00 A; B/D=170-430.
DR PDB; 6GUE; X-ray; 1.99 A; B/D=169-430.
DR PDB; 6GUF; X-ray; 2.65 A; B/D=170-430.
DR PDBsum; 1VIN; -.
DR PDBsum; 2G9X; -.
DR PDBsum; 3BHT; -.
DR PDBsum; 3BHU; -.
DR PDBsum; 3BHV; -.
DR PDBsum; 3DDP; -.
DR PDBsum; 3DDQ; -.
DR PDBsum; 3DOG; -.
DR PDBsum; 3MY5; -.
DR PDBsum; 3TNW; -.
DR PDBsum; 4BCN; -.
DR PDBsum; 4BCO; -.
DR PDBsum; 4BCQ; -.
DR PDBsum; 6GUB; -.
DR PDBsum; 6GUC; -.
DR PDBsum; 6GUE; -.
DR PDBsum; 6GUF; -.
DR AlphaFoldDB; P30274; -.
DR SMR; P30274; -.
DR BioGRID; 158986; 5.
DR DIP; DIP-693N; -.
DR IntAct; P30274; 3.
DR STRING; 9913.ENSBTAP00000006503; -.
DR BindingDB; P30274; -.
DR ChEMBL; CHEMBL4106153; -.
DR PaxDb; P30274; -.
DR PRIDE; P30274; -.
DR GeneID; 281667; -.
DR KEGG; bta:281667; -.
DR CTD; 890; -.
DR eggNOG; KOG0654; Eukaryota.
DR HOGENOM; CLU_020695_3_2_1; -.
DR InParanoid; P30274; -.
DR OrthoDB; 993640at2759; -.
DR EvolutionaryTrace; P30274; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0097124; C:cyclin A2-CDK2 complex; IBA:GO_Central.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
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:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Cyclin; Cytoplasm;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..430
FT /note="Cyclin-A2"
FT /id="PRO_0000080337"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..121
FT /note="Basic and acidic 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"
FT CONFLICT 24
FT /note="A -> E (in Ref. 2; CAA48398)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="Missing (in Ref. 2; CAA48398)"
FT /evidence="ECO:0000305"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3DDQ"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 177..190
FT /evidence="ECO:0007829|PDB:3DDQ"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:3BHV"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 206..222
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 227..243
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 251..266
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:3DDQ"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 286..299
FT /evidence="ECO:0007829|PDB:3DDQ"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:3DDQ"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:1VIN"
FT HELIX 325..340
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 350..366
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 372..378
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 382..398
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 406..410
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:3DDQ"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:3DDQ"
SQ SEQUENCE 430 AA; 48262 MW; FACA1B8E770E997F CRC64;
MLGSSAHGPA AREAGSAVTL QQTAFQEDQE NVNPEKAAPA QQPRTRAGLA VLRAGNSRGP
APQRPKTRRV APLKDLPIND EYVPVPPWKA NNKQPAFTIH VDEAEEEIQK RPTESKKSES
EDVLAFNSAV TLPGPRKPLA PLDYPMDGSF ESPHTMEMSV VLEDEKPVSV NEVPDYHEDI
HTYLREMEVK CKPKVGYMKK QPDITNSMRA ILVDWLVEVG EEYKLQNETL HLAVNYIDRF
LSSMSVLRGK LQLVGTAAML LASKFEEIYP PEVAEFVYIT DDTYTKKQVL RMEHLVLKVL
AFDLAAPTIN QFLTQYFLHQ QPANCKVESL AMFLGELSLI DADPYLKYLP SVIAAAAFHL
ALYTVTGQSW PESLVQKTGY TLETLKPCLL DLHQTYLRAP QHAQQSIREK YKNSKYHGVS
LLNPPETLNV
