CCNA1_RAT
ID CCNA1_RAT Reviewed; 421 AA.
AC Q6AY13;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Cyclin-A1;
GN Name=Ccna1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
CC -!- FUNCTION: May be involved in the control of the cell cycle at the G1/S
CC (start) and G2/M (mitosis) transitions. May primarily function in the
CC control of the germline meiotic cell cycle and additionally in the
CC control of mitotic cell cycle in some somatic cells (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the CDK2 and the CDC2 protein kinases to form a
CC serine/threonine kinase holoenzyme complex. The cyclin subunit imparts
CC substrate specificity to the complex. Does not bind CDK4 and CDK5 (in
CC vitro). The cyclin A1-CDK2 complex interacts with transcription factor
CC E2F-1 and RB proteins. Found in a complex with CDK2, CABLES1 and CCNE1.
CC Interacts with INCA1 and KLHDC9 (By similarity).
CC {ECO:0000250|UniProtKB:P78396, ECO:0000250|UniProtKB:Q61456}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; BC079234; AAH79234.1; -; mRNA.
DR RefSeq; NP_001011949.1; NM_001011949.1.
DR RefSeq; XP_006232421.1; XM_006232359.3.
DR RefSeq; XP_006232422.1; XM_006232360.3.
DR RefSeq; XP_006232423.1; XM_006232361.3.
DR RefSeq; XP_008759209.1; XM_008760987.2.
DR RefSeq; XP_008759210.1; XM_008760988.2.
DR RefSeq; XP_017446238.1; XM_017590749.1.
DR RefSeq; XP_017446239.1; XM_017590750.1.
DR AlphaFoldDB; Q6AY13; -.
DR SMR; Q6AY13; -.
DR BioGRID; 254866; 3.
DR ComplexPortal; CPX-2063; Cyclin A1-CDK1 complex.
DR ComplexPortal; CPX-2067; Cyclin A1-CDK2 complex.
DR STRING; 10116.ENSRNOP00000039931; -.
DR PhosphoSitePlus; Q6AY13; -.
DR PaxDb; Q6AY13; -.
DR Ensembl; ENSRNOT00000040002; ENSRNOP00000039931; ENSRNOG00000014052.
DR GeneID; 295052; -.
DR KEGG; rno:295052; -.
DR UCSC; RGD:1310639; rat.
DR CTD; 8900; -.
DR RGD; 1310639; Ccna1.
DR eggNOG; KOG0654; Eukaryota.
DR GeneTree; ENSGT00940000157940; -.
DR HOGENOM; CLU_020695_3_2_1; -.
DR InParanoid; Q6AY13; -.
DR OMA; YKSSKYC; -.
DR OrthoDB; 993640at2759; -.
DR PhylomeDB; Q6AY13; -.
DR TreeFam; TF101002; -.
DR Reactome; R-RNO-1538133; G0 and Early G1.
DR Reactome; R-RNO-171319; Telomere Extension By Telomerase.
DR Reactome; R-RNO-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-RNO-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-RNO-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-RNO-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-RNO-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR Reactome; R-RNO-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-RNO-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-RNO-6804757; Regulation of TP53 Degradation.
DR Reactome; R-RNO-68911; G2 Phase.
DR Reactome; R-RNO-68949; Orc1 removal from chromatin.
DR Reactome; R-RNO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-RNO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-RNO-69563; p53-Dependent G1 DNA Damage Response.
DR Reactome; R-RNO-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR PRO; PR:Q6AY13; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000014052; Expressed in testis and 11 other tissues.
DR Genevisible; Q6AY13; RN.
DR GO; GO:0097123; C:cyclin A1-CDK2 complex; ISO:RGD.
DR GO; GO:0097124; C:cyclin A2-CDK2 complex; IBA:GO_Central.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:UniProt.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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:0010033; P:response to organic substance; IEA:UniProt.
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 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 Cell cycle; Cell division; Cyclin; Mitosis; Nucleus; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..421
FT /note="Cyclin-A1"
FT /id="PRO_0000342166"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 421 AA; 47695 MW; C0277433FB6D1C8E CRC64;
MRRHSSKSGV ALPPVGQGPD ACQMLTRAQL GQDPPQRTVL GVLTENEQYR RACGQEIATI
RCFSGSENVF PAAGKKVLPD NGVSEPAKHG FDIYMDDPEQ GDRDSCPGRE GIVFEDVYEV
DTSMLKSDLH FLLDFNTVSP MLVDSTAHAQ SEEATDFGSD VINVTEYAEE IHRYLREAEV
RHRPKAHYMR KQPDITEGMR AILVDWLVEV GEEYKLRTET LYLAVNFLDR FLSCMSVLRG
KLQLVGTAAI LLASKYEEIY PPDVDEFVYI TDDTYTKRQL LRMEHLLLKV LAFDLTVPTT
NQFLLQYLRR QGVCIRTENL AKYVAELSLL EADPFLKYLP SLVAAAAYCL ANYIVNRHFW
PETLAAFTGY SLNEIVPCLS ELHKACLSIP HRPQQAIREK YKASKYLHVS LMEPPVVLPL
Q