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Protein

Cyclin-A2

Gene

CCNA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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, Host-virus interaction, Mitosis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000145386-MONOMER.
ReactomeiR-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 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-A2
Short name:
Cyclin-A
Gene namesi
Name:CCNA2
Synonyms:CCN1, CCNA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:1578. CCNA2.

Subcellular locationi

GO - Cellular componenti

  • cyclin A2-CDK2 complex Source: Ensembl
  • cytoplasm Source: MGI
  • female pronucleus Source: Ensembl
  • Golgi apparatus Source: HPA
  • male pronucleus Source: Ensembl
  • nucleoplasm Source: HPA
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi890.
OpenTargetsiENSG00000145386.
PharmGKBiPA94.

Chemistry databases

ChEMBLiCHEMBL2582.

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP20248.
MaxQBiP20248.
PaxDbiP20248.
PeptideAtlasiP20248.
PRIDEiP20248.

PTM databases

iPTMnetiP20248.
PhosphoSitePlusiP20248.

Miscellaneous databases

PMAP-CutDBP20248.

Expressioni

Developmental stagei

Accumulates steadily during G2 and is abruptly destroyed at mitosis.

Gene expression databases

BgeeiENSG00000145386.
CleanExiHS_CCNA2.
GenevisibleiP20248. HS.

Organism-specific databases

HPAiCAB000114.
HPA020626.
HPA061793.

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. Interacts with human cytomegalovirus protein UL32 (PubMed:24101496).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P030702EBI-457097,EBI-617698From a different organism.
CDK2P2494124EBI-457097,EBI-375096
CDKN1AP389363EBI-457097,EBI-375077
CDKN1BP4652714EBI-457097,EBI-519280
E7P031292EBI-457097,EBI-866453From a different organism.
UHRF2Q96PU42EBI-457097,EBI-625304

Protein-protein interaction databases

BioGridi107331. 113 interactors.
DIPiDIP-638N.
IntActiP20248. 51 interactors.
MINTiMINT-141826.
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[»]
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

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.

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 → V.Combined sources7 PublicationsCorresponds to variant rs769242dbSNPEnsembl.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

Cross-referencesi

Web resourcesi

NIEHS-SNPs

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.

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[»]
ProteinModelPortaliP20248.
SMRiP20248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107331. 113 interactors.
DIPiDIP-638N.
IntActiP20248. 51 interactors.
MINTiMINT-141826.
STRINGi9606.ENSP00000274026.

Chemistry databases

BindingDBiP20248.
ChEMBLiCHEMBL2582.

PTM databases

iPTMnetiP20248.
PhosphoSitePlusiP20248.

Polymorphism and mutation databases

BioMutaiCCNA2.
DMDMi311033358.

Proteomic databases

EPDiP20248.
MaxQBiP20248.
PaxDbiP20248.
PeptideAtlasiP20248.
PRIDEiP20248.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi890.
DisGeNETi890.
GeneCardsiCCNA2.
HGNCiHGNC:1578. CCNA2.
HPAiCAB000114.
HPA020626.
HPA061793.
MIMi123835. gene.
neXtProtiNX_P20248.
OpenTargetsiENSG00000145386.
PharmGKBiPA94.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000145386-MONOMER.
ReactomeiR-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 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.

Miscellaneous databases

EvolutionaryTraceiP20248.
GeneWikiiCyclin_A2.
GenomeRNAii890.
PMAP-CutDBP20248.
PROiP20248.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000145386.
CleanExiHS_CCNA2.
GenevisibleiP20248. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P20248
Secondary accession number(s): A8K7B6
, Q2M3U6, Q4W5P4, Q6LER8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 2, 2010
Last modified: November 30, 2016
This is version 179 of the entry and version 2 of the sequence. [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

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.