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Protein

Cyclin-A2

Gene

CCNA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Cyclin which controls both the G1/S and the G2/M transition phases of the cell cycle. Functions through the formation of specific serine/threonine protein kinase holoenzyme complexes with the cyclin-dependent protein kinases CDK1 or CDK2. The cyclin subunit confers the substrate specificity of these complexes and differentially interacts with and activates CDK1 and CDK2 throughout the cell cycle.1 Publication

GO - Molecular functioni

  • protein domain specific binding Source: CAFA
  • protein kinase binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionCyclin
Biological processCell cycle, Cell division, Host-virus interaction, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-1362300 Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1
R-HSA-1538133 G0 and Early G1
R-HSA-170145 Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-176408 Regulation of APC/C activators between G1/S and early anaphase
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-5689880 Ub-specific processing proteases
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-6804116 TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-6804757 Regulation of TP53 Degradation
R-HSA-68911 G2 Phase
R-HSA-68949 Orc1 removal from chromatin
R-HSA-69273 Cyclin A/B1/B2 associated events during G2/M transition
R-HSA-69563 p53-Dependent G1 DNA Damage Response
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
SignaLinkiP20248
SIGNORiP20248

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-A2Imported
Short name:
Cyclin-A1 Publication
Alternative name(s):
Cyclin A1 Publication
Gene namesi
Name:CCNA2Imported
Synonyms:CCN1Imported, CCNAImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000145386.9
HGNCiHGNC:1578 CCNA2
MIMi123835 gene
neXtProtiNX_P20248

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi890
OpenTargetsiENSG00000145386
PharmGKBiPA94

Chemistry databases

ChEMBLiCHEMBL2582
DrugBankiDB08463 (2R)-2-({9-(1-methylethyl)-6-[(4-pyridin-2-ylbenzyl)amino]-9H-purin-2-yl}amino)butan-1-ol
DB07137 (2S)-N-[(3Z)-5-CYCLOPROPYL-3H-PYRAZOL-3-YLIDENE]-2-[4-(2-OXOIMIDAZOLIDIN-1-YL)PHENYL]PROPANAMIDE
DB06948 2-ANILINO-6-CYCLOHEXYLMETHOXYPURINE
DB08248 3-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)-BENZENESULFONAMIDE
DB08309 3-({2-[(4-{[6-(CYCLOHEXYLMETHOXY)-9H-PURIN-2-YL]AMINO}PHENYL)SULFONYL]ETHYL}AMINO)PROPAN-1-OL
DB08241 4-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)--BENZAMIDE
DB08572 4-{[4-AMINO-6-(CYCLOHEXYLMETHOXY)-5-NITROSOPYRIMIDIN-2-YL]AMINO}BENZAMIDE
DB07203 6-CYCLOHEXYLMETHOXY-2-(3'-CHLOROANILINO) PURINE
DB08233 6-CYCLOHEXYLMETHYLOXY-2-(4'-HYDROXYANILINO)PURINE
DB02407 6-O-Cyclohexylmethyl Guanine
DB02833 [4-(2-Amino-4-Methyl-Thiazol-5-Yl)-Pyrimidin-2-Yl]-(3-Nitro-Phenyl)-Amine
DB06944 N-(3-cyclopropyl-1H-pyrazol-5-yl)-2-(2-naphthyl)acetamide
DB07126 O6-CYCLOHEXYLMETHOXY-2-(4'-SULPHAMOYLANILINO) PURINE

Polymorphism and mutation databases

BioMutaiCCNA2
DMDMi311033358

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000803381 – 432Cyclin-A2Add BLAST432

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei5PhosphoserineCombined sources1
Modified residuei55PhosphoserineCombined sources1

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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP20248
MaxQBiP20248
PaxDbiP20248
PeptideAtlasiP20248
PRIDEiP20248

PTM databases

iPTMnetiP20248
PhosphoSitePlusiP20248

Miscellaneous databases

PMAP-CutDBiP20248

Expressioni

Developmental stagei

Accumulates steadily during G2 and is abruptly destroyed at mitosis. Not detected during the G1 phase of the cell cycle. It accumulates during the DNA synthesis/S phase and disappears as cells progress into mitosis, between prophase and metaphase (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000145386
CleanExiHS_CCNA2
GenevisibleiP20248 HS

Organism-specific databases

HPAiCAB000114
HPA020626

Interactioni

Subunit structurei

Interacts with the CDK1 and CDK2 protein kinases to form serine/threonine kinase holoenzyme complexes (PubMed:1312467, PubMed:7630397, PubMed:8684460, PubMed:8756328). Interacts with CDK1 (hyperphosphorylated form in G1 and underphosphorylated forms in S and G2) (PubMed:1312467). Interacts with CDK2; the interaction increases from G1 to G2 (PubMed:1312467). Interacts (associated with CDK2 but not with CDK1) with SCAPER; regulates the activity of CCNA2/CDK2 by transiently maintaining CCNA2 in the cytoplasm (PubMed:17698606). Forms a ternary complex with CDK2 and CDKN1B; CDKN1B inhibits the kinase activity of CDK2 through conformational rearrangements (PubMed:8684460).5 Publications
(Microbial infection) Interacts with human cytomegalovirus protein UL32.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein domain specific binding Source: CAFA
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107331, 121 interactors
CORUMiP20248
DIPiDIP-638N
ELMiP20248
IntActiP20248, 57 interactors
MINTiP20248
STRINGi9606.ENSP00000274026

Chemistry databases

BindingDBiP20248

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi172 – 174Combined sources3
Helixi176 – 178Combined sources3
Helixi179 – 192Combined sources14
Helixi199 – 202Combined sources4
Helixi208 – 224Combined sources17
Helixi229 – 243Combined sources15
Helixi250 – 252Combined sources3
Helixi253 – 268Combined sources16
Beta strandi269 – 271Combined sources3
Helixi275 – 281Combined sources7
Turni282 – 284Combined sources3
Helixi288 – 301Combined sources14
Turni302 – 304Combined sources3
Helixi311 – 319Combined sources9
Beta strandi322 – 324Combined sources3
Helixi327 – 342Combined sources16
Helixi344 – 347Combined sources4
Helixi352 – 368Combined sources17
Helixi374 – 380Combined sources7
Helixi384 – 400Combined sources17
Helixi401 – 403Combined sources3
Helixi408 – 412Combined sources5
Beta strandi413 – 415Combined sources3
Helixi416 – 418Combined sources3
Helixi421 – 423Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E9HX-ray2.50B/D175-432[»]
1FINX-ray2.30B/D173-432[»]
1FVVX-ray2.80B/D173-432[»]
1GY3X-ray2.70B/D175-432[»]
1H1PX-ray2.10B/D175-432[»]
1H1QX-ray2.50B/D175-432[»]
1H1RX-ray2.00B/D175-432[»]
1H1SX-ray2.00B/D175-432[»]
1H24X-ray2.50B/D174-432[»]
1H25X-ray2.50B/D174-432[»]
1H26X-ray2.24B/D174-432[»]
1H27X-ray2.20B/D174-432[»]
1H28X-ray2.80B/D174-432[»]
1JSTX-ray2.60B/D175-432[»]
1JSUX-ray2.30B173-432[»]
1OGUX-ray2.60B/D174-432[»]
1OI9X-ray2.10B/D174-432[»]
1OIUX-ray2.00B/D174-432[»]
1OIYX-ray2.40B/D174-432[»]
1OKVX-ray2.40B/D173-432[»]
1OKWX-ray2.50B/D173-432[»]
1OL1X-ray2.90B/D173-432[»]
1OL2X-ray2.60B/D173-432[»]
1P5EX-ray2.22B/D175-432[»]
1PKDX-ray2.30B/D175-432[»]
1QMZX-ray2.20B/D174-432[»]
1URCX-ray2.60B/D173-432[»]
1VYWX-ray2.30B/D174-432[»]
2BKZX-ray2.60B/D174-432[»]
2BPMX-ray2.40B/D174-432[»]
2C4GX-ray2.70B/D173-432[»]
2C5NX-ray2.10B/D174-432[»]
2C5OX-ray2.10B/D173-432[»]
2C5VX-ray2.90B/D174-432[»]
2C5XX-ray2.90B/D174-432[»]
2C6TX-ray2.61B/D175-432[»]
2CCHX-ray1.70B/D173-432[»]
2CCIX-ray2.70B/D175-432[»]
2CJMX-ray2.30B/D175-432[»]
2I40X-ray2.80B/D173-432[»]
2IW6X-ray2.30B/D174-432[»]
2IW8X-ray2.30B/D174-432[»]
2IW9X-ray2.00B/D174-432[»]
2UUEX-ray2.06B/D174-432[»]
2UZBX-ray2.70B/D175-432[»]
2UZDX-ray2.72B/D175-432[»]
2UZEX-ray2.40B/D175-432[»]
2UZLX-ray2.40B/D175-432[»]
2V22X-ray2.60B/D174-432[»]
2WEVX-ray2.30B/D173-432[»]
2WFYX-ray2.53B/D173-432[»]
2WHBX-ray2.90B/D173-432[»]
2WIHX-ray2.50B/D173-432[»]
2WIPX-ray2.80B/D173-432[»]
2WMAX-ray2.80B/D174-432[»]
2WMBX-ray2.60B/D174-432[»]
2WPAX-ray2.51B/D173-432[»]
2WXVX-ray2.60B/D173-432[»]
2X1NX-ray2.75B/D172-432[»]
3EIDX-ray3.15B/D173-432[»]
3EJ1X-ray3.22B/D173-432[»]
3EOCX-ray3.20B/D173-432[»]
3F5XX-ray2.40B/D177-432[»]
4BCKX-ray2.05B/D171-432[»]
4BCMX-ray2.45B/D171-432[»]
4BCNX-ray2.10B171-432[»]
D171-431[»]
4BCPX-ray2.26B/D171-432[»]
4CFMX-ray2.85B/D175-432[»]
4CFNX-ray2.20B/D175-432[»]
4CFUX-ray2.20B172-432[»]
D173-432[»]
4CFVX-ray2.00B/D172-432[»]
4CFWX-ray2.45B/D175-432[»]
4CFXX-ray3.50B/D173-432[»]
4EOIX-ray2.00B/D175-432[»]
4EOJX-ray1.65B/D175-432[»]
4EOKX-ray2.57B/D175-432[»]
4EOLX-ray2.40B/D175-432[»]
4EOMX-ray2.10B/D175-432[»]
4EONX-ray2.40B/D175-432[»]
4EOOX-ray2.10B/D175-432[»]
4EOPX-ray1.99B/D175-432[»]
4EOQX-ray2.15B/D175-432[»]
4EORX-ray2.20B/D175-432[»]
4EOSX-ray2.57B/D175-432[»]
4FX3X-ray2.75B/D175-432[»]
5CYIX-ray2.00B/D174-432[»]
5IF1X-ray2.61B/D174-432[»]
5LMKX-ray2.40B/D175-432[»]
5NEVX-ray2.97B/D174-432[»]
ProteinModelPortaliP20248
SMRiP20248
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20248

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclin family. Cyclin AB subfamily.Curated

Phylogenomic databases

eggNOGiKOG0654 Eukaryota
COG5024 LUCA
GeneTreeiENSGT00760000118939
HOGENOMiHOG000167672
HOVERGENiHBG106244
InParanoidiP20248
KOiK06627
OMAiTMDISIV
OrthoDBiEOG091G090I
PhylomeDBiP20248
TreeFamiTF101002

Family and domain databases

CDDicd00043 CYCLIN, 2 hits
InterProiView protein in InterPro
IPR032447 Cyclin-A_N
IPR013763 Cyclin-like
IPR036915 Cyclin-like_sf
IPR004367 Cyclin_C-dom
IPR006671 Cyclin_N
PfamiView protein in Pfam
PF02984 Cyclin_C, 1 hit
PF00134 Cyclin_N, 1 hit
PF16500 Cyclin_N2, 1 hit
SMARTiView protein in SMART
SM00385 CYCLIN, 2 hits
SM01332 Cyclin_C, 1 hit
SUPFAMiSSF47954 SSF47954, 2 hits
PROSITEiView protein in PROSITE
PS00292 CYCLINS, 1 hit

Sequencei

Sequence statusi: Complete.

P20248-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGNSAPGPA TREAGSALLA LQQTALQEDQ ENINPEKAAP VQQPRTRAAL
60 70 80 90 100
AVLKSGNPRG LAQQQRPKTR RVAPLKDLPV NDEHVTVPPW KANSKQPAFT
110 120 130 140 150
IHVDEAEKEA QKKPAESQKI EREDALAFNS AISLPGPRKP LVPLDYPMDG
160 170 180 190 200
SFESPHTMDM SIILEDEKPV SVNEVPDYHE DIHTYLREME VKCKPKVGYM
210 220 230 240 250
KKQPDITNSM RAILVDWLVE VGEEYKLQNE TLHLAVNYID RFLSSMSVLR
260 270 280 290 300
GKLQLVGTAA MLLASKFEEI YPPEVAEFVY ITDDTYTKKQ VLRMEHLVLK
310 320 330 340 350
VLTFDLAAPT VNQFLTQYFL HQQPANCKVE SLAMFLGELS LIDADPYLKY
360 370 380 390 400
LPSVIAGAAF HLALYTVTGQ SWPESLIRKT GYTLESLKPC LMDLHQTYLK
410 420 430
APQHAQQSIR EKYKNSKYHG VSLLNPPETL NL
Length:432
Mass (Da):48,551
Last modified:November 2, 2010 - v2
Checksum:i97763A2897DD35F4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti156H → R in CAG28620 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_018819163I → VCombined sources7 PublicationsCorresponds to variant dbSNP:rs769242Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51688 mRNA Translation: CAA35986.1
X68303 Genomic DNA Translation: CAA48375.1
CR407692 mRNA Translation: CAG28620.1
AF518006 Genomic DNA Translation: AAM54042.1
AK291931 mRNA Translation: BAF84620.1
AC079341 Genomic DNA Translation: AAY40969.1
CH471056 Genomic DNA Translation: EAX05246.1
BC104783 mRNA Translation: AAI04784.1
BC104787 mRNA Translation: AAI04788.1
CCDSiCCDS3723.1
PIRiS08277
RefSeqiNP_001228.1, NM_001237.4
UniGeneiHs.58974

Genome annotation databases

EnsembliENST00000274026; ENSP00000274026; ENSG00000145386
ENST00000618014; ENSP00000481380; ENSG00000145386
GeneIDi890
KEGGihsa:890
UCSCiuc003iec.5 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCCNA2_HUMAN
AccessioniPrimary (citable) accession number: P20248
Secondary accession number(s): A8K7B6
, Q2M3U6, Q4W5P4, Q6LER8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 2, 2010
Last modified: March 28, 2018
This is version 191 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health