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UniProtKB - P20248 (CCNA2_HUMAN)

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

  • cyclin-dependent protein serine/threonine kinase regulator activity Source: GO_Central
  • protein domain specific binding Source: CAFA
  • protein kinase binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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-69017 CDK-mediated phosphorylation and removal of Cdc6
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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
ProteomicsDBi53735

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 Expressed in 192 organ(s), highest expression level in oocyte
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). Interacts with INCA1 (PubMed:21540187).6 Publications
(Microbial infection) Interacts with human cytomegalovirus protein UL32.1 Publication

Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi107331, 122 interactors
ComplexPortaliCPX-2004 Cyclin A2-CDK1 complex
CPX-2006 Cyclin A2-CDK2 complex
CORUMiP20248
DIPiDIP-638N
ELMiP20248
IntActiP20248, 56 interactors
MINTiP20248
STRINGi9606.ENSP00000274026

Chemistry databases

BindingDBiP20248

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
IPR039361 Cyclin
IPR032447 Cyclin-A_N
IPR013763 Cyclin-like
IPR036915 Cyclin-like_sf
IPR004367 Cyclin_C-dom
IPR006671 Cyclin_N
PANTHERiPTHR10177 PTHR10177, 1 hit
PfamiView protein in Pfam
PF02984 Cyclin_C, 1 hit
PF00134 Cyclin_N, 1 hit
PF16500 Cyclin_N2, 1 hit
PIRSFiPIRSF001771 Cyclin_A_B_D_E, 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

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[»]
5LMKX-ray2.40B/D175-432[»]
5NEVX-ray2.97B/D174-432[»]
6ATHX-ray1.82B173-432[»]
ProteinModelPortaliP20248
SMRiP20248
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107331, 122 interactors
ComplexPortaliCPX-2004 Cyclin A2-CDK1 complex
CPX-2006 Cyclin A2-CDK2 complex
CORUMiP20248
DIPiDIP-638N
ELMiP20248
IntActiP20248, 56 interactors
MINTiP20248
STRINGi9606.ENSP00000274026

Chemistry databases

BindingDBiP20248
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

PTM databases

iPTMnetiP20248
PhosphoSitePlusiP20248

Polymorphism and mutation databases

BioMutaiCCNA2
DMDMi311033358

Proteomic databases

EPDiP20248
MaxQBiP20248
PaxDbiP20248
PeptideAtlasiP20248
PRIDEiP20248
ProteomicsDBi53735

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
EuPathDBiHostDB:ENSG00000145386.9
GeneCardsiCCNA2
HGNCiHGNC:1578 CCNA2
HPAiCAB000114
HPA020626
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

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-69017 CDK-mediated phosphorylation and removal of Cdc6
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

Miscellaneous databases

EvolutionaryTraceiP20248
GeneWikiiCyclin_A2
GenomeRNAii890
PMAP-CutDBiP20248
PROiPR:P20248
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000145386 Expressed in 192 organ(s), highest expression level in oocyte
CleanExiHS_CCNA2
GenevisibleiP20248 HS

Family and domain databases

CDDicd00043 CYCLIN, 2 hits
InterProiView protein in InterPro
IPR039361 Cyclin
IPR032447 Cyclin-A_N
IPR013763 Cyclin-like
IPR036915 Cyclin-like_sf
IPR004367 Cyclin_C-dom
IPR006671 Cyclin_N
PANTHERiPTHR10177 PTHR10177, 1 hit
PfamiView protein in Pfam
PF02984 Cyclin_C, 1 hit
PF00134 Cyclin_N, 1 hit
PF16500 Cyclin_N2, 1 hit
PIRSFiPIRSF001771 Cyclin_A_B_D_E, 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
ProtoNetiSearch...

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: November 7, 2018
This is version 197 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

Documents

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