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   24-JAN-2024, entry version 170.
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; 9913-ENSBTAP00000006503; -.
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; 5474295at2759; -.
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:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR   CDD; cd20561; CYCLIN_CCNA2_rpt1; 1.
DR   CDD; cd20564; CYCLIN_CCNA2_rpt2; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR032447; Cyclin-A_N.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR046965; Cyclin_A/B-like.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR048258; Cyclins_cyclin-box.
DR   PANTHER; PTHR10177:SF444; CYCLIN-A2; 1.
DR   PANTHER; PTHR10177; CYCLINS; 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; Cyclin-like; 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
//