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Protein

Cyclin-A1

Gene

Ccna1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

May be involved in the control of the cell cycle at the G1/S (start) and G2/M (mitosis) transitions. May primarily function in the control of the germline meiotic cell cycle and additionally in the control of mitotic cell cycle in some somatic cells (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-RNO-113510. E2F mediated regulation of DNA replication.
R-RNO-1538133. G0 and Early G1.
R-RNO-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-RNO-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-RNO-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-RNO-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-RNO-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-RNO-5693607. Processing of DNA double-strand break ends.
R-RNO-68911. G2 Phase.
R-RNO-68949. Orc1 removal from chromatin.
R-RNO-69205. G1/S-Specific Transcription.
R-RNO-69273. Cyclin A/B1 associated events during G2/M transition.
R-RNO-69656. Cyclin A:Cdk2-associated events at S phase entry.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-A1
Gene namesi
Name:Ccna1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi1310639. Ccna1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 421421Cyclin-A1PRO_0000342166Add
BLAST

Post-translational modificationi

Polyubiquitinated via 'Lys-11'-linked ubiquitin by the anaphase-promoting complex (APC/C), leading to its degradation by the proteasome. Deubiquitinated and stabilized by USP37 enables entry into S phase (By similarity).By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ6AY13.

Expressioni

Gene expression databases

GenevisibleiQ6AY13. RN.

Interactioni

Subunit structurei

Interacts with the CDK2 and the CDC2 protein kinases to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. Does not bind CDK4 and CDK5 (in vitro). The cyclin A1-CDK2 complex interacts with transcription factor E2F-1 and RB proteins. Found in a complex with CDK2, CABLES1 and CCNE1. Interacts with INCA1 and KLHDC9 (By similarity).By similarity

Protein-protein interaction databases

BioGridi254866. 3 interactions.
STRINGi10116.ENSRNOP00000039931.

Structurei

3D structure databases

ProteinModelPortaliQ6AY13.
SMRiQ6AY13. Positions 161-420.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclin family. Cyclin AB subfamily.Curated

Phylogenomic databases

eggNOGiKOG0654. Eukaryota.
COG5024. LUCA.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000167672.
HOVERGENiHBG106244.
InParanoidiQ6AY13.
KOiK06627.
OMAiAEIRHRP.
OrthoDBiEOG7G7KQ0.
PhylomeDBiQ6AY13.
TreeFamiTF101002.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
SM01332. Cyclin_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6AY13-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRHSSKSGV ALPPVGQGPD ACQMLTRAQL GQDPPQRTVL GVLTENEQYR
60 70 80 90 100
RACGQEIATI RCFSGSENVF PAAGKKVLPD NGVSEPAKHG FDIYMDDPEQ
110 120 130 140 150
GDRDSCPGRE GIVFEDVYEV DTSMLKSDLH FLLDFNTVSP MLVDSTAHAQ
160 170 180 190 200
SEEATDFGSD VINVTEYAEE IHRYLREAEV RHRPKAHYMR KQPDITEGMR
210 220 230 240 250
AILVDWLVEV GEEYKLRTET LYLAVNFLDR FLSCMSVLRG KLQLVGTAAI
260 270 280 290 300
LLASKYEEIY PPDVDEFVYI TDDTYTKRQL LRMEHLLLKV LAFDLTVPTT
310 320 330 340 350
NQFLLQYLRR QGVCIRTENL AKYVAELSLL EADPFLKYLP SLVAAAAYCL
360 370 380 390 400
ANYIVNRHFW PETLAAFTGY SLNEIVPCLS ELHKACLSIP HRPQQAIREK
410 420
YKASKYLHVS LMEPPVVLPL Q
Length:421
Mass (Da):47,695
Last modified:September 13, 2004 - v1
Checksum:iC0277433FB6D1C8E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079234 mRNA. Translation: AAH79234.1.
RefSeqiNP_001011949.1. NM_001011949.1.
XP_006232421.1. XM_006232359.2.
XP_006232422.1. XM_006232360.2.
XP_006232423.1. XM_006232361.2.
XP_008759209.1. XM_008760987.1.
XP_008759210.1. XM_008760988.1.
UniGeneiRn.102823.

Genome annotation databases

EnsembliENSRNOT00000040002; ENSRNOP00000039931; ENSRNOG00000014052.
GeneIDi295052.
KEGGirno:295052.
UCSCiRGD:1310639. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079234 mRNA. Translation: AAH79234.1.
RefSeqiNP_001011949.1. NM_001011949.1.
XP_006232421.1. XM_006232359.2.
XP_006232422.1. XM_006232360.2.
XP_006232423.1. XM_006232361.2.
XP_008759209.1. XM_008760987.1.
XP_008759210.1. XM_008760988.1.
UniGeneiRn.102823.

3D structure databases

ProteinModelPortaliQ6AY13.
SMRiQ6AY13. Positions 161-420.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi254866. 3 interactions.
STRINGi10116.ENSRNOP00000039931.

Proteomic databases

PaxDbiQ6AY13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000040002; ENSRNOP00000039931; ENSRNOG00000014052.
GeneIDi295052.
KEGGirno:295052.
UCSCiRGD:1310639. rat.

Organism-specific databases

CTDi8900.
RGDi1310639. Ccna1.

Phylogenomic databases

eggNOGiKOG0654. Eukaryota.
COG5024. LUCA.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000167672.
HOVERGENiHBG106244.
InParanoidiQ6AY13.
KOiK06627.
OMAiAEIRHRP.
OrthoDBiEOG7G7KQ0.
PhylomeDBiQ6AY13.
TreeFamiTF101002.

Enzyme and pathway databases

ReactomeiR-RNO-113510. E2F mediated regulation of DNA replication.
R-RNO-1538133. G0 and Early G1.
R-RNO-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-RNO-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-RNO-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-RNO-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-RNO-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-RNO-5693607. Processing of DNA double-strand break ends.
R-RNO-68911. G2 Phase.
R-RNO-68949. Orc1 removal from chromatin.
R-RNO-69205. G1/S-Specific Transcription.
R-RNO-69273. Cyclin A/B1 associated events during G2/M transition.
R-RNO-69656. Cyclin A:Cdk2-associated events at S phase entry.

Miscellaneous databases

NextBioi638902.
PROiQ6AY13.

Gene expression databases

GenevisibleiQ6AY13. RN.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
SM01332. Cyclin_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.

Entry informationi

Entry nameiCCNA1_RAT
AccessioniPrimary (citable) accession number: Q6AY13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: September 13, 2004
Last modified: May 11, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.