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P20248

- CCNA2_HUMAN

UniProt

P20248 - CCNA2_HUMAN

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Protein
Cyclin-A2
Gene
CCNA2, CCN1, CCNA
Organism
Homo sapiens (Human)
Status
Reviewed - 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 - Molecular functioni

  1. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. G2/M transition of mitotic cell cycle Source: Reactome
  2. Ras protein signal transduction Source: BHF-UCL
  3. mitotic G2 DNA damage checkpoint Source: ProtInc
  4. mitotic cell cycle Source: Reactome
  5. mitotic nuclear division Source: UniProtKB-KW
  6. organ regeneration Source: Ensembl
  7. positive regulation of fibroblast proliferation Source: Ensembl
  8. positive regulation of transcription, DNA-templated Source: Ensembl
  9. regulation of G2/M transition of mitotic cell cycle Source: InterPro
  10. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
  11. response to estradiol Source: Ensembl
  12. response to glucagon Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_111214. G0 and Early G1.
REACT_1156. Orc1 removal from chromatin.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_1915. G2 Phase.
REACT_6362. Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinkiP20248.

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
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:1578. CCNA2.

Subcellular locationi

Nucleus. Cytoplasm
Note: Cytoplasmic when associated with SCAPER.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. female pronucleus Source: Ensembl
  3. male pronucleus Source: Ensembl
  4. nucleoplasm Source: Reactome
  5. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA94.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Cyclin-A2
PRO_0000080338Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei5 – 51Phosphoserine1 Publication
Modified residuei55 – 551Phosphoserine1 Publication

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.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP20248.
PaxDbiP20248.
PRIDEiP20248.

PTM databases

PhosphoSiteiP20248.

Miscellaneous databases

PMAP-CutDBP20248.

Expressioni

Developmental stagei

Accumulates steadily during G2 and is abruptly destroyed at mitosis.

Gene expression databases

BgeeiP20248.
CleanExiHS_CCNA2.
GenevestigatoriP20248.

Organism-specific databases

HPAiCAB000114.
HPA020626.

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
P030702EBI-457097,EBI-617698From a different organism.
CDK2P2494119EBI-457097,EBI-375096
CDKN1AP389362EBI-457097,EBI-375077
CDKN1BP4652713EBI-457097,EBI-519280
UHRF2Q96PU42EBI-457097,EBI-625304

Protein-protein interaction databases

BioGridi107331. 71 interactions.
DIPiDIP-638N.
IntActiP20248. 27 interactions.
MINTiMINT-141826.
STRINGi9606.ENSP00000274026.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi176 – 1783
Helixi179 – 19214
Helixi199 – 2024
Helixi208 – 22417
Helixi229 – 24315
Helixi250 – 2523
Helixi253 – 26816
Beta strandi269 – 2713
Helixi275 – 2817
Turni282 – 2843
Helixi288 – 30114
Turni302 – 3043
Helixi311 – 3199
Beta strandi322 – 3243
Helixi327 – 34216
Helixi344 – 3474
Helixi352 – 36817
Helixi374 – 3807
Helixi384 – 40017
Helixi401 – 4033
Helixi408 – 4125
Beta strandi413 – 4153
Helixi416 – 4183
Helixi421 – 4233

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4CFNX-ray2.20B/D175-432[»]
4CFWX-ray2.45B/D175-432[»]
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[»]
ProteinModelPortaliP20248.
SMRiP20248. Positions 176-432.

Miscellaneous databases

EvolutionaryTraceiP20248.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5024.
HOGENOMiHOG000167672.
HOVERGENiHBG106244.
InParanoidiP20248.
KOiK06627.
OMAiNPEKAAP.
OrthoDBiEOG7G7KQ0.
PhylomeDBiP20248.
TreeFamiTF101002.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E/F.
IPR015453. Cyclin_A_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.
[Graphical view]
PIRSFiPIRSF001771. Cyclin_A_B_D_E. 1 hit.
SMARTiSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20248-1 [UniParc]FASTAAdd to Basket

« Hide

MLGNSAPGPA TREAGSALLA LQQTALQEDQ ENINPEKAAP VQQPRTRAAL    50
AVLKSGNPRG LAQQQRPKTR RVAPLKDLPV NDEHVTVPPW KANSKQPAFT 100
IHVDEAEKEA QKKPAESQKI EREDALAFNS AISLPGPRKP LVPLDYPMDG 150
SFESPHTMDM SIILEDEKPV SVNEVPDYHE DIHTYLREME VKCKPKVGYM 200
KKQPDITNSM RAILVDWLVE VGEEYKLQNE TLHLAVNYID RFLSSMSVLR 250
GKLQLVGTAA MLLASKFEEI YPPEVAEFVY ITDDTYTKKQ VLRMEHLVLK 300
VLTFDLAAPT VNQFLTQYFL HQQPANCKVE SLAMFLGELS LIDADPYLKY 350
LPSVIAGAAF HLALYTVTGQ SWPESLIRKT GYTLESLKPC LMDLHQTYLK 400
APQHAQQSIR EKYKNSKYHG VSLLNPPETL NL 432
Length:432
Mass (Da):48,551
Last modified:November 2, 2010 - v2
Checksum:i97763A2897DD35F4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti163 – 1631I → V.8 Publications
Corresponds to variant rs769242 [ dbSNP | Ensembl ].
VAR_018819

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti156 – 1561H → R in CAG28620. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_001237.3.
UniGeneiHs.58974.

Genome annotation databases

EnsembliENST00000274026; ENSP00000274026; ENSG00000145386.
GeneIDi890.
KEGGihsa:890.
UCSCiuc003iec.4. human.

Polymorphism databases

DMDMi311033358.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_001237.3.
UniGenei Hs.58974.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4CFN X-ray 2.20 B/D 175-432 [» ]
4CFW X-ray 2.45 B/D 175-432 [» ]
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 [» ]
ProteinModelPortali P20248.
SMRi P20248. Positions 176-432.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107331. 71 interactions.
DIPi DIP-638N.
IntActi P20248. 27 interactions.
MINTi MINT-141826.
STRINGi 9606.ENSP00000274026.

Chemistry

BindingDBi P20248.
ChEMBLi CHEMBL2582.

PTM databases

PhosphoSitei P20248.

Polymorphism databases

DMDMi 311033358.

Proteomic databases

MaxQBi P20248.
PaxDbi P20248.
PRIDEi P20248.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000274026 ; ENSP00000274026 ; ENSG00000145386 .
GeneIDi 890.
KEGGi hsa:890.
UCSCi uc003iec.4. human.

Organism-specific databases

CTDi 890.
GeneCardsi GC04M122737.
HGNCi HGNC:1578. CCNA2.
HPAi CAB000114.
HPA020626.
MIMi 123835. gene.
neXtProti NX_P20248.
PharmGKBi PA94.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5024.
HOGENOMi HOG000167672.
HOVERGENi HBG106244.
InParanoidi P20248.
KOi K06627.
OMAi NPEKAAP.
OrthoDBi EOG7G7KQ0.
PhylomeDBi P20248.
TreeFami TF101002.

Enzyme and pathway databases

Reactomei REACT_111214. G0 and Early G1.
REACT_1156. Orc1 removal from chromatin.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_1915. G2 Phase.
REACT_6362. Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinki P20248.

Miscellaneous databases

EvolutionaryTracei P20248.
GeneWikii Cyclin_A2.
GenomeRNAii 890.
NextBioi 3682.
PMAP-CutDB P20248.
PROi P20248.
SOURCEi Search...

Gene expression databases

Bgeei P20248.
CleanExi HS_CCNA2.
Genevestigatori P20248.

Family and domain databases

Gene3Di 1.10.472.10. 2 hits.
InterProi IPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E/F.
IPR015453. Cyclin_A_chordates.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view ]
PANTHERi PTHR10177:SF69. PTHR10177:SF69. 1 hit.
Pfami PF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF001771. Cyclin_A_B_D_E. 1 hit.
SMARTi SM00385. CYCLIN. 2 hits.
[Graphical view ]
SUPFAMi SSF47954. SSF47954. 2 hits.
PROSITEi PS00292. CYCLINS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Hepatitis B virus integration in a cyclin A gene in a hepatocellular carcinoma."
    Wang J., Chenivesse X., Henglein B., Brechot C.
    Nature 343:555-557(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-163.
  2. "Structure and cell cycle-regulated transcription of the human cyclin A gene."
    Henglein B., Chenivesse X., Wang D., Eick D., Brechot C.
    Proc. Natl. Acad. Sci. U.S.A. 91:5490-5494(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-163.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-163.
  4. NIEHS SNPs program
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-163.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-163.
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-163.
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-163.
    Tissue: Brain.
  9. "SCAPER, a novel cyclin A-interacting protein that regulates cell cycle progression."
    Tsang W.Y., Wang L., Chen Z., Sanchez I., Dynlacht B.D.
    J. Cell Biol. 178:621-633(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCAPER, SUBCELLULAR LOCATION.
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry."
    Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G., Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.
    Mol. Cell 42:511-523(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP37.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex."
    Jeffrey P.D., Russo A.A., Polyak K., Gibbs E., Hurwitz J., Massague J., Pavletich N.P.
    Nature 376:313-320(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 173-432 COMPLEXED WITH CDK2.
  15. "Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex."
    Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.
    Nature 382:325-331(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 173-432 IN CDK2/KIP1 COMPLEX.
  16. "Structural basis of cyclin-dependent kinase activation by phosphorylation."
    Russo A.A., Jeffrey P.D., Pavletich N.P.
    Nat. Struct. Biol. 3:696-700(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 173-432 COMPLEXED WITH CDK2.
  17. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

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: September 3, 2014
This is version 153 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

External Data

Dasty 3

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