UniProtKB - P20248 (CCNA2_HUMAN)
Cyclin-A2
CCNA2
Functioni
GO - Molecular functioni
- cyclin-dependent protein serine/threonine kinase regulator activity Source: UniProtKB
- protein domain specific binding Source: CAFA
- protein kinase binding Source: UniProtKB
GO - Biological processi
- animal organ regeneration Source: Ensembl
- cell cycle G1/S phase transition Source: UniProtKB
- cell division Source: UniProtKB-KW
- cellular response to cocaine Source: Ensembl
- cellular response to estradiol stimulus Source: Ensembl
- cellular response to hypoxia Source: Ensembl
- cellular response to insulin-like growth factor stimulus Source: Ensembl
- cellular response to leptin stimulus Source: Ensembl
- cellular response to luteinizing hormone stimulus Source: Ensembl
- cellular response to nitric oxide Source: Ensembl
- cellular response to platelet-derived growth factor stimulus Source: Ensembl
- cochlea development Source: Ensembl
- G2/M transition of mitotic cell cycle Source: UniProtKB
- histone phosphorylation Source: CAFA
- mitotic cell cycle phase transition Source: GO_Central
- positive regulation of fibroblast proliferation Source: Ensembl
- positive regulation of transcription, DNA-templated Source: Ensembl
- protein deubiquitination Source: Reactome
- Ras protein signal transduction Source: BHF-UCL
- regulation of cyclin-dependent protein serine/threonine kinase activity Source: GO_Central
- regulation of DNA replication Source: UniProtKB
- response to glucagon Source: Ensembl
- viral process Source: UniProtKB-KW
Keywordsi
Molecular function | Cyclin |
Biological process | Cell cycle, Cell division, Host-virus interaction, Mitosis |
Enzyme and pathway databases
PathwayCommonsi | P20248 |
Reactomei | R-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-171319, Telomere Extension By Telomerase 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 |
SignaLinki | P20248 |
SIGNORi | P20248 |
Names & Taxonomyi
Protein namesi | Recommended name: Cyclin-A2ImportedShort name: Cyclin-A1 Publication Alternative name(s): Cyclin A1 Publication |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000145386.9 |
HGNCi | HGNC:1578, CCNA2 |
MIMi | 123835, gene |
neXtProti | NX_P20248 |
Subcellular locationi
Cytosol
- cytosol Source: HPA
Nucleus
- female pronucleus Source: Ensembl
- male pronucleus Source: Ensembl
- nucleoplasm Source: CAFA
- nucleus Source: UniProtKB
Other locations
- cyclin A2-CDK2 complex Source: UniProtKB
- cyclin-dependent protein kinase holoenzyme complex Source: UniProtKB
- cytoplasm Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Organism-specific databases
DisGeNETi | 890 |
OpenTargetsi | ENSG00000145386 |
PharmGKBi | PA94 |
Miscellaneous databases
Pharosi | P20248, Tchem |
Chemistry databases
ChEMBLi | CHEMBL2582 |
DrugBanki | DB08463, (2R)-2-({9-(1-methylethyl)-6-[(4-pyridin-2-ylbenzyl)amino]-9H-purin-2-yl}amino)butan-1-ol DB08285, (2R)-2-{[4-(benzylamino)-8-(1-methylethyl)pyrazolo[1,5-a][1,3,5]triazin-2-yl]amino}butan-1-ol DB07137, (2S)-N-[(3E)-5-Cyclopropyl-3H-pyrazol-3-ylidene]-2-[4-(2-oxo-1-imidazolidinyl)phenyl]propanamide DB07852, 1-(3,5-DICHLOROPHENYL)-5-METHYL-1H-1,2,4-TRIAZOLE-3-CARBOXYLIC ACID DB08527, 1-[4-(AMINOSULFONYL)PHENYL]-1,6-DIHYDROPYRAZOLO[3,4-E]INDAZOLE-3-CARBOXAMIDE DB08355, 1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxylic acid 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 DB02915, 4-(2,4-Dimethyl-1,3-thiazol-5-yl)-N-[4-(trifluoromethyl)phenyl]-2-pyrimidinamine DB02091, 4-(2,4-Dimethyl-Thiazol-5-Yl)-Pyrimidin-2-Ylamine DB08178, 4-(4-methoxy-1H-pyrrolo[2,3-b]pyridin-3-yl)pyrimidin-2-amine DB08182, 4-(4-propoxy-1H-pyrrolo[2,3-b]pyridin-3-yl)pyrimidin-2-amine DB08241, 4-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)--BENZAMIDE DB06844, 4-[(7-OXO-7H-THIAZOLO[5,4-E]INDOL-8-YLMETHYL)-AMINO]-N-PYRIDIN-2-YL-BENZENESULFONAMIDE DB08219, 4-Methyl-5-[(2Z)-2-{[4-(4-morpholinyl)phenyl]imino}-2,5-dihydro-4-pyrimidinyl]-1,3-thiazol-2-amine DB07533, 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]-2-FURYL}-N-METHYLBENZENESULFONAMIDE DB07538, 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}-2-(TRIFLUOROMETHYL)BENZENESULFONAMIDE DB07534, 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}BENZENESULFONAMIDE DB07539, 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}BENZOIC ACID DB08572, 4-{[4-AMINO-6-(CYCLOHEXYLMETHOXY)-5-NITROSOPYRIMIDIN-2-YL]AMINO}BENZAMIDE DB07688, 4-{[5-(CYCLOHEXYLOXY)[1,2,4]TRIAZOLO[1,5-A]PYRIMIDIN-7-YL]AMINO}BENZENESULFONAMIDE DB07471, 5-[5,6-BIS(METHYLOXY)-1H-BENZIMIDAZOL-1-YL]-3-{[1-(2-CHLOROPHENYL)ETHYL]OXY}-2-THIOPHENECARBOXAMIDE 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 DB08218, HYDROXY(OXO)(3-{[(2Z)-4-[3-(1H-1,2,4-TRIAZOL-1-YLMETHYL)PHENYL]PYRIMIDIN-2(5H)-YLIDENE]AMINO}PHENYL)AMMONIUM DB06944, N-(3-cyclopropyl-1H-pyrazol-5-yl)-2-(2-naphthyl)acetamide DB07562, N-[4-(2,4-DIMETHYL-THIAZOL-5-YL)-PYRIMIDIN-2-YL]-N',N'-DIMETHYL-BENZENE-1,4-DIAMINE DB07164, N-cyclopropyl-4-pyrazolo[1,5-b]pyridazin-3-ylpyrimidin-2-amine DB07126, O6-CYCLOHEXYLMETHOXY-2-(4'-SULPHAMOYLANILINO) PURINE DB08694, Variolin B |
DrugCentrali | P20248 |
Polymorphism and mutation databases
BioMutai | CCNA2 |
DMDMi | 311033358 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000080338 | 1 – 432 | Cyclin-A2Add BLAST | 432 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineCombined sources | 1 | |
Modified residuei | 5 | PhosphoserineCombined sources | 1 | |
Modified residuei | 55 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | P20248 |
jPOSTi | P20248 |
MassIVEi | P20248 |
MaxQBi | P20248 |
PaxDbi | P20248 |
PeptideAtlasi | P20248 |
PRIDEi | P20248 |
ProteomicsDBi | 53735 |
PTM databases
iPTMneti | P20248 |
MetOSitei | P20248 |
PhosphoSitePlusi | P20248 |
Expressioni
Developmental stagei
Gene expression databases
Bgeei | ENSG00000145386, Expressed in ventricular zone and 205 other tissues |
Genevisiblei | P20248, HS |
Organism-specific databases
HPAi | ENSG00000145386, Tissue enriched (lymphoid) |
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 PublicationBinary interactionsi
Hide detailsP20248
GO - Molecular functioni
- protein domain specific binding Source: CAFA
- protein kinase binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 107331, 132 interactors |
ComplexPortali | CPX-2004, Cyclin A2-CDK1 complex CPX-2006, Cyclin A2-CDK2 complex |
CORUMi | P20248 |
DIPi | DIP-638N |
ELMi | P20248 |
IntActi | P20248, 77 interactors |
MINTi | P20248 |
STRINGi | 9606.ENSP00000274026 |
Chemistry databases
BindingDBi | P20248 |
Miscellaneous databases
RNActi | P20248, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P20248 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P20248 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0654, Eukaryota |
GeneTreei | ENSGT00940000155372 |
HOGENOMi | CLU_020695_3_2_1 |
InParanoidi | P20248 |
OMAi | LMPCVED |
OrthoDBi | 993640at2759 |
PhylomeDBi | P20248 |
TreeFami | TF101002 |
Family and domain databases
CDDi | cd00043, CYCLIN, 2 hits |
IDEALi | IID00032 |
InterProi | View protein in InterPro IPR039361, Cyclin IPR032447, Cyclin-A_N IPR013763, Cyclin-like IPR036915, Cyclin-like_sf IPR004367, Cyclin_C-dom IPR006671, Cyclin_N |
PANTHERi | PTHR10177, PTHR10177, 1 hit |
Pfami | View protein in Pfam PF02984, Cyclin_C, 1 hit PF00134, Cyclin_N, 1 hit PF16500, Cyclin_N2, 1 hit |
PIRSFi | PIRSF001771, Cyclin_A_B_D_E, 1 hit |
SMARTi | View protein in SMART SM00385, CYCLIN, 2 hits SM01332, Cyclin_C, 1 hit |
SUPFAMi | SSF47954, SSF47954, 2 hits |
PROSITEi | View protein in PROSITE PS00292, CYCLINS, 1 hit |
i Sequence
Sequence statusi: Complete.
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 156 | H → R in CAG28620 (Ref. 3) Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_018819 | 163 | I → 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 |
CCDSi | CCDS3723.1 |
PIRi | S08277 |
RefSeqi | NP_001228.1, NM_001237.4 |
Genome annotation databases
Ensembli | ENST00000274026; ENSP00000274026; ENSG00000145386 ENST00000618014; ENSP00000481380; ENSG00000145386 |
GeneIDi | 890 |
KEGGi | hsa:890 |
UCSCi | uc003iec.5, human |
Keywords - Coding sequence diversityi
PolymorphismSimilar 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 |
CCDSi | CCDS3723.1 |
PIRi | S08277 |
RefSeqi | NP_001228.1, NM_001237.4 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1E9H | X-ray | 2.50 | B/D | 175-432 | [»] | |
1FIN | X-ray | 2.30 | B/D | 173-432 | [»] | |
1FVV | X-ray | 2.80 | B/D | 173-432 | [»] | |
1GY3 | X-ray | 2.70 | B/D | 175-432 | [»] | |
1H1P | X-ray | 2.10 | B/D | 175-432 | [»] | |
1H1Q | X-ray | 2.50 | B/D | 175-432 | [»] | |
1H1R | X-ray | 2.00 | B/D | 175-432 | [»] | |
1H1S | X-ray | 2.00 | B/D | 175-432 | [»] | |
1H24 | X-ray | 2.50 | B/D | 174-432 | [»] | |
1H25 | X-ray | 2.50 | B/D | 174-432 | [»] | |
1H26 | X-ray | 2.24 | B/D | 174-432 | [»] | |
1H27 | X-ray | 2.20 | B/D | 174-432 | [»] | |
1H28 | X-ray | 2.80 | B/D | 174-432 | [»] | |
1JST | X-ray | 2.60 | B/D | 175-432 | [»] | |
1JSU | X-ray | 2.30 | B | 173-432 | [»] | |
1OGU | X-ray | 2.60 | B/D | 174-432 | [»] | |
1OI9 | X-ray | 2.10 | B/D | 174-432 | [»] | |
1OIU | X-ray | 2.00 | B/D | 174-432 | [»] | |
1OIY | X-ray | 2.40 | B/D | 174-432 | [»] | |
1OKV | X-ray | 2.40 | B/D | 173-432 | [»] | |
1OKW | X-ray | 2.50 | B/D | 173-432 | [»] | |
1OL1 | X-ray | 2.90 | B/D | 173-432 | [»] | |
1OL2 | X-ray | 2.60 | B/D | 173-432 | [»] | |
1P5E | X-ray | 2.22 | B/D | 175-432 | [»] | |
1PKD | X-ray | 2.30 | B/D | 175-432 | [»] | |
1QMZ | X-ray | 2.20 | B/D | 174-432 | [»] | |
1URC | X-ray | 2.60 | B/D | 173-432 | [»] | |
1VYW | X-ray | 2.30 | B/D | 174-432 | [»] | |
2BKZ | X-ray | 2.60 | B/D | 174-432 | [»] | |
2BPM | X-ray | 2.40 | B/D | 174-432 | [»] | |
2C4G | X-ray | 2.70 | B/D | 173-432 | [»] | |
2C5N | X-ray | 2.10 | B/D | 174-432 | [»] | |
2C5O | X-ray | 2.10 | B/D | 173-432 | [»] | |
2C5V | X-ray | 2.90 | B/D | 174-432 | [»] | |
2C5X | X-ray | 2.90 | B/D | 174-432 | [»] | |
2C6T | X-ray | 2.61 | B/D | 175-432 | [»] | |
2CCH | X-ray | 1.70 | B/D | 173-432 | [»] | |
2CCI | X-ray | 2.70 | B/D | 175-432 | [»] | |
2CJM | X-ray | 2.30 | B/D | 175-432 | [»] | |
2I40 | X-ray | 2.80 | B/D | 173-432 | [»] | |
2IW6 | X-ray | 2.30 | B/D | 174-432 | [»] | |
2IW8 | X-ray | 2.30 | B/D | 174-432 | [»] | |
2IW9 | X-ray | 2.00 | B/D | 174-432 | [»] | |
2UUE | X-ray | 2.06 | B/D | 174-432 | [»] | |
2UZB | X-ray | 2.70 | B/D | 175-432 | [»] | |
2UZD | X-ray | 2.72 | B/D | 175-432 | [»] | |
2UZE | X-ray | 2.40 | B/D | 175-432 | [»] | |
2UZL | X-ray | 2.40 | B/D | 175-432 | [»] | |
2V22 | X-ray | 2.60 | B/D | 174-432 | [»] | |
2WEV | X-ray | 2.30 | B/D | 173-432 | [»] | |
2WFY | X-ray | 2.53 | B/D | 173-432 | [»] | |
2WHB | X-ray | 2.90 | B/D | 173-432 | [»] | |
2WIH | X-ray | 2.50 | B/D | 173-432 | [»] | |
2WIP | X-ray | 2.80 | B/D | 173-432 | [»] | |
2WMA | X-ray | 2.80 | B/D | 174-432 | [»] | |
2WMB | X-ray | 2.60 | B/D | 174-432 | [»] | |
2WPA | X-ray | 2.51 | B/D | 173-432 | [»] | |
2WXV | X-ray | 2.60 | B/D | 173-432 | [»] | |
2X1N | X-ray | 2.75 | B/D | 172-432 | [»] | |
3EID | X-ray | 3.15 | B/D | 173-432 | [»] | |
3EJ1 | X-ray | 3.22 | B/D | 173-432 | [»] | |
3EOC | X-ray | 3.20 | B/D | 173-432 | [»] | |
3F5X | X-ray | 2.40 | B/D | 177-432 | [»] | |
4BCK | X-ray | 2.05 | B/D | 171-432 | [»] | |
4BCM | X-ray | 2.45 | B/D | 171-432 | [»] | |
4BCN | X-ray | 2.10 | B | 171-432 | [»] | |
D | 171-431 | [»] | ||||
4BCP | X-ray | 2.26 | B/D | 171-432 | [»] | |
4CFM | X-ray | 2.85 | B/D | 175-432 | [»] | |
4CFN | X-ray | 2.20 | B/D | 175-432 | [»] | |
4CFU | X-ray | 2.20 | B | 172-432 | [»] | |
D | 173-432 | [»] | ||||
4CFV | X-ray | 2.00 | B/D | 172-432 | [»] | |
4CFW | X-ray | 2.45 | B/D | 175-432 | [»] | |
4CFX | X-ray | 3.50 | B/D | 173-432 | [»] | |
4EOI | X-ray | 2.00 | B/D | 175-432 | [»] | |
4EOJ | X-ray | 1.65 | B/D | 175-432 | [»] | |
4EOK | X-ray | 2.57 | B/D | 175-432 | [»] | |
4EOL | X-ray | 2.40 | B/D | 175-432 | [»] | |
4EOM | X-ray | 2.10 | B/D | 175-432 | [»] | |
4EON | X-ray | 2.40 | B/D | 175-432 | [»] | |
4EOO | X-ray | 2.10 | B/D | 175-432 | [»] | |
4EOP | X-ray | 1.99 | B/D | 175-432 | [»] | |
4EOQ | X-ray | 2.15 | B/D | 175-432 | [»] | |
4EOR | X-ray | 2.20 | B/D | 175-432 | [»] | |
4EOS | X-ray | 2.57 | B/D | 175-432 | [»] | |
4FX3 | X-ray | 2.75 | B/D | 175-432 | [»] | |
5CYI | X-ray | 2.00 | B/D | 174-432 | [»] | |
5IF1 | X-ray | 2.61 | B/D | 174-432 | [»] | |
5LMK | X-ray | 2.40 | B/D | 175-432 | [»] | |
5NEV | X-ray | 2.97 | B/D | 174-432 | [»] | |
6ATH | X-ray | 1.82 | B | 173-432 | [»] | |
6GVA | X-ray | 2.15 | B | 175-432 | [»] | |
6P3W | X-ray | 2.54 | B/D | 176-432 | [»] | |
6Q6G | electron microscopy | 3.20 | S | 1-432 | [»] | |
6Q6H | electron microscopy | 3.20 | S | 1-432 | [»] | |
6RIJ | X-ray | 2.20 | B/D | 175-432 | [»] | |
SMRi | P20248 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 107331, 132 interactors |
ComplexPortali | CPX-2004, Cyclin A2-CDK1 complex CPX-2006, Cyclin A2-CDK2 complex |
CORUMi | P20248 |
DIPi | DIP-638N |
ELMi | P20248 |
IntActi | P20248, 77 interactors |
MINTi | P20248 |
STRINGi | 9606.ENSP00000274026 |
Chemistry databases
BindingDBi | P20248 |
ChEMBLi | CHEMBL2582 |
DrugBanki | DB08463, (2R)-2-({9-(1-methylethyl)-6-[(4-pyridin-2-ylbenzyl)amino]-9H-purin-2-yl}amino)butan-1-ol DB08285, (2R)-2-{[4-(benzylamino)-8-(1-methylethyl)pyrazolo[1,5-a][1,3,5]triazin-2-yl]amino}butan-1-ol DB07137, (2S)-N-[(3E)-5-Cyclopropyl-3H-pyrazol-3-ylidene]-2-[4-(2-oxo-1-imidazolidinyl)phenyl]propanamide DB07852, 1-(3,5-DICHLOROPHENYL)-5-METHYL-1H-1,2,4-TRIAZOLE-3-CARBOXYLIC ACID DB08527, 1-[4-(AMINOSULFONYL)PHENYL]-1,6-DIHYDROPYRAZOLO[3,4-E]INDAZOLE-3-CARBOXAMIDE DB08355, 1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxylic acid 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 DB02915, 4-(2,4-Dimethyl-1,3-thiazol-5-yl)-N-[4-(trifluoromethyl)phenyl]-2-pyrimidinamine DB02091, 4-(2,4-Dimethyl-Thiazol-5-Yl)-Pyrimidin-2-Ylamine DB08178, 4-(4-methoxy-1H-pyrrolo[2,3-b]pyridin-3-yl)pyrimidin-2-amine DB08182, 4-(4-propoxy-1H-pyrrolo[2,3-b]pyridin-3-yl)pyrimidin-2-amine DB08241, 4-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)--BENZAMIDE DB06844, 4-[(7-OXO-7H-THIAZOLO[5,4-E]INDOL-8-YLMETHYL)-AMINO]-N-PYRIDIN-2-YL-BENZENESULFONAMIDE DB08219, 4-Methyl-5-[(2Z)-2-{[4-(4-morpholinyl)phenyl]imino}-2,5-dihydro-4-pyrimidinyl]-1,3-thiazol-2-amine DB07533, 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]-2-FURYL}-N-METHYLBENZENESULFONAMIDE DB07538, 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}-2-(TRIFLUOROMETHYL)BENZENESULFONAMIDE DB07534, 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}BENZENESULFONAMIDE DB07539, 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}BENZOIC ACID DB08572, 4-{[4-AMINO-6-(CYCLOHEXYLMETHOXY)-5-NITROSOPYRIMIDIN-2-YL]AMINO}BENZAMIDE DB07688, 4-{[5-(CYCLOHEXYLOXY)[1,2,4]TRIAZOLO[1,5-A]PYRIMIDIN-7-YL]AMINO}BENZENESULFONAMIDE DB07471, 5-[5,6-BIS(METHYLOXY)-1H-BENZIMIDAZOL-1-YL]-3-{[1-(2-CHLOROPHENYL)ETHYL]OXY}-2-THIOPHENECARBOXAMIDE 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 DB08218, HYDROXY(OXO)(3-{[(2Z)-4-[3-(1H-1,2,4-TRIAZOL-1-YLMETHYL)PHENYL]PYRIMIDIN-2(5H)-YLIDENE]AMINO}PHENYL)AMMONIUM DB06944, N-(3-cyclopropyl-1H-pyrazol-5-yl)-2-(2-naphthyl)acetamide DB07562, N-[4-(2,4-DIMETHYL-THIAZOL-5-YL)-PYRIMIDIN-2-YL]-N',N'-DIMETHYL-BENZENE-1,4-DIAMINE DB07164, N-cyclopropyl-4-pyrazolo[1,5-b]pyridazin-3-ylpyrimidin-2-amine DB07126, O6-CYCLOHEXYLMETHOXY-2-(4'-SULPHAMOYLANILINO) PURINE DB08694, Variolin B |
DrugCentrali | P20248 |
PTM databases
iPTMneti | P20248 |
MetOSitei | P20248 |
PhosphoSitePlusi | P20248 |
Polymorphism and mutation databases
BioMutai | CCNA2 |
DMDMi | 311033358 |
Proteomic databases
EPDi | P20248 |
jPOSTi | P20248 |
MassIVEi | P20248 |
MaxQBi | P20248 |
PaxDbi | P20248 |
PeptideAtlasi | P20248 |
PRIDEi | P20248 |
ProteomicsDBi | 53735 |
Protocols and materials databases
Antibodypediai | 3665, 760 antibodies |
Genome annotation databases
Ensembli | ENST00000274026; ENSP00000274026; ENSG00000145386 ENST00000618014; ENSP00000481380; ENSG00000145386 |
GeneIDi | 890 |
KEGGi | hsa:890 |
UCSCi | uc003iec.5, human |
Organism-specific databases
CTDi | 890 |
DisGeNETi | 890 |
EuPathDBi | HostDB:ENSG00000145386.9 |
GeneCardsi | CCNA2 |
HGNCi | HGNC:1578, CCNA2 |
HPAi | ENSG00000145386, Tissue enriched (lymphoid) |
MIMi | 123835, gene |
neXtProti | NX_P20248 |
OpenTargetsi | ENSG00000145386 |
PharmGKBi | PA94 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0654, Eukaryota |
GeneTreei | ENSGT00940000155372 |
HOGENOMi | CLU_020695_3_2_1 |
InParanoidi | P20248 |
OMAi | LMPCVED |
OrthoDBi | 993640at2759 |
PhylomeDBi | P20248 |
TreeFami | TF101002 |
Enzyme and pathway databases
PathwayCommonsi | P20248 |
Reactomei | R-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-171319, Telomere Extension By Telomerase 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 |
SignaLinki | P20248 |
SIGNORi | P20248 |
Miscellaneous databases
BioGRID-ORCSi | 890, 732 hits in 853 CRISPR screens |
EvolutionaryTracei | P20248 |
GeneWikii | Cyclin_A2 |
GenomeRNAii | 890 |
Pharosi | P20248, Tchem |
PROi | PR:P20248 |
RNActi | P20248, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000145386, Expressed in ventricular zone and 205 other tissues |
Genevisiblei | P20248, HS |
Family and domain databases
CDDi | cd00043, CYCLIN, 2 hits |
IDEALi | IID00032 |
InterProi | View protein in InterPro IPR039361, Cyclin IPR032447, Cyclin-A_N IPR013763, Cyclin-like IPR036915, Cyclin-like_sf IPR004367, Cyclin_C-dom IPR006671, Cyclin_N |
PANTHERi | PTHR10177, PTHR10177, 1 hit |
Pfami | View protein in Pfam PF02984, Cyclin_C, 1 hit PF00134, Cyclin_N, 1 hit PF16500, Cyclin_N2, 1 hit |
PIRSFi | PIRSF001771, Cyclin_A_B_D_E, 1 hit |
SMARTi | View protein in SMART SM00385, CYCLIN, 2 hits SM01332, Cyclin_C, 1 hit |
SUPFAMi | SSF47954, SSF47954, 2 hits |
PROSITEi | View protein in PROSITE PS00292, CYCLINS, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CCNA2_HUMAN | |
Accessioni | P20248Primary (citable) accession number: P20248 Secondary accession number(s): A8K7B6 Q6LER8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1991 |
Last sequence update: | November 2, 2010 | |
Last modified: | December 2, 2020 | |
This is version 213 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Reference proteomeDocuments
- Human chromosome 4
Human chromosome 4: entries, gene names and cross-references to MIM - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations