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Protein

Cyclin-A2

Gene

CCNA2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-A2
Short name:
Cyclin-A
Gene namesi
Name:CCNA2
Synonyms:CCNA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000803371 – 430Cyclin-A2Add BLAST430

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei5PhosphoserineBy similarity1

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

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP30274.
PRIDEiP30274.

Expressioni

Developmental stagei

Accumulates steadily during G2 and is abruptly destroyed at mitosis.

Gene expression databases

BgeeiENSBTAG00000004943.

Interactioni

Subunit structurei

Interacts with the CDK1 and CDK2 protein kinases to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. When associated with CDK2 (but not with CDK1), interacts with SCAPER (By similarity).By similarity

Protein-protein interaction databases

BioGridi158986. 5 interactors.
DIPiDIP-693N.
STRINGi9913.ENSBTAP00000006503.

Structurei

Secondary structure

1430
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi170 – 172Combined sources3
Turni174 – 176Combined sources3
Helixi177 – 190Combined sources14
Turni195 – 197Combined sources3
Helixi198 – 200Combined sources3
Helixi206 – 222Combined sources17
Helixi227 – 243Combined sources17
Helixi248 – 250Combined sources3
Helixi251 – 266Combined sources16
Helixi273 – 279Combined sources7
Turni280 – 282Combined sources3
Helixi286 – 299Combined sources14
Turni300 – 302Combined sources3
Helixi309 – 317Combined sources9
Beta strandi320 – 322Combined sources3
Helixi325 – 340Combined sources16
Helixi342 – 345Combined sources4
Helixi350 – 366Combined sources17
Helixi372 – 378Combined sources7
Helixi382 – 398Combined sources17
Helixi399 – 401Combined sources3
Helixi406 – 410Combined sources5
Helixi414 – 416Combined sources3
Helixi419 – 421Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VINX-ray2.00A170-429[»]
2G9XX-ray2.50B/D170-430[»]
3BHTX-ray2.00B/D169-430[»]
3BHUX-ray2.30B/D169-430[»]
3BHVX-ray2.10B/D169-430[»]
3DDPX-ray2.70B/D169-430[»]
3DDQX-ray1.80B/D169-430[»]
3DOGX-ray2.70B/D169-430[»]
3MY5X-ray2.10B/D169-430[»]
3TNWX-ray2.00B/D169-430[»]
4BCNX-ray2.10D169-430[»]
4BCOX-ray2.05B/D169-429[»]
4BCQX-ray2.40B169-429[»]
D169-430[»]
ProteinModelPortaliP30274.
SMRiP30274.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30274.

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclin family. Cyclin AB subfamily.Curated

Phylogenomic databases

eggNOGiKOG0654. Eukaryota.
COG5024. LUCA.
HOGENOMiHOG000167672.
HOVERGENiHBG106244.
InParanoidiP30274.
KOiK06627.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR032447. Cyclin-A_N.
IPR013763. Cyclin-like.
IPR015453. Cyclin_A2_chordates.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10177:SF69. PTHR10177:SF69. 1 hit.
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
PF16500. Cyclin_N2. 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.

P30274-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGSSAHGPA AREAGSAVTL QQTAFQEDQE NVNPEKAAPA QQPRTRAGLA
60 70 80 90 100
VLRAGNSRGP APQRPKTRRV APLKDLPIND EYVPVPPWKA NNKQPAFTIH
110 120 130 140 150
VDEAEEEIQK RPTESKKSES EDVLAFNSAV TLPGPRKPLA PLDYPMDGSF
160 170 180 190 200
ESPHTMEMSV VLEDEKPVSV NEVPDYHEDI HTYLREMEVK CKPKVGYMKK
210 220 230 240 250
QPDITNSMRA ILVDWLVEVG EEYKLQNETL HLAVNYIDRF LSSMSVLRGK
260 270 280 290 300
LQLVGTAAML LASKFEEIYP PEVAEFVYIT DDTYTKKQVL RMEHLVLKVL
310 320 330 340 350
AFDLAAPTIN QFLTQYFLHQ QPANCKVESL AMFLGELSLI DADPYLKYLP
360 370 380 390 400
SVIAAAAFHL ALYTVTGQSW PESLVQKTGY TLETLKPCLL DLHQTYLRAP
410 420 430
QHAQQSIREK YKNSKYHGVS LLNPPETLNV
Length:430
Mass (Da):48,262
Last modified:October 17, 2006 - v2
Checksum:iFACA1B8E770E997F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti24A → E in CAA48398 (PubMed:1333843).Curated1
Sequence conflicti107Missing in CAA48398 (PubMed:1333843).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC118203 mRNA. Translation: AAI18204.1.
X68321 mRNA. Translation: CAA48398.1.
PIRiS24788.
RefSeqiNP_001068591.1. NM_001075123.1.
UniGeneiBt.87491.

Genome annotation databases

GeneIDi281667.
KEGGibta:281667.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC118203 mRNA. Translation: AAI18204.1.
X68321 mRNA. Translation: CAA48398.1.
PIRiS24788.
RefSeqiNP_001068591.1. NM_001075123.1.
UniGeneiBt.87491.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VINX-ray2.00A170-429[»]
2G9XX-ray2.50B/D170-430[»]
3BHTX-ray2.00B/D169-430[»]
3BHUX-ray2.30B/D169-430[»]
3BHVX-ray2.10B/D169-430[»]
3DDPX-ray2.70B/D169-430[»]
3DDQX-ray1.80B/D169-430[»]
3DOGX-ray2.70B/D169-430[»]
3MY5X-ray2.10B/D169-430[»]
3TNWX-ray2.00B/D169-430[»]
4BCNX-ray2.10D169-430[»]
4BCOX-ray2.05B/D169-429[»]
4BCQX-ray2.40B169-429[»]
D169-430[»]
ProteinModelPortaliP30274.
SMRiP30274.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi158986. 5 interactors.
DIPiDIP-693N.
STRINGi9913.ENSBTAP00000006503.

Proteomic databases

PaxDbiP30274.
PRIDEiP30274.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281667.
KEGGibta:281667.

Organism-specific databases

CTDi890.

Phylogenomic databases

eggNOGiKOG0654. Eukaryota.
COG5024. LUCA.
HOGENOMiHOG000167672.
HOVERGENiHBG106244.
InParanoidiP30274.
KOiK06627.

Miscellaneous databases

EvolutionaryTraceiP30274.

Gene expression databases

BgeeiENSBTAG00000004943.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR032447. Cyclin-A_N.
IPR013763. Cyclin-like.
IPR015453. Cyclin_A2_chordates.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10177:SF69. PTHR10177:SF69. 1 hit.
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
PF16500. Cyclin_N2. 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...

Entry informationi

Entry nameiCCNA2_BOVIN
AccessioniPrimary (citable) accession number: P30274
Secondary accession number(s): Q17QS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 17, 2006
Last modified: November 2, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.