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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

  1. cell division Source: UniProtKB-KW
  2. G2/M transition of mitotic cell cycle Source: Reactome
  3. mitotic cell cycle Source: Reactome
  4. mitotic G2 DNA damage checkpoint Source: ProtInc
  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. Ras protein signal transduction Source: BHF-UCL
  10. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
  11. regulation of G2/M transition of mitotic cell cycle Source: InterPro
  12. response to estradiol Source: Ensembl
  13. 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 1 Publication. Cytoplasm 1 Publication
Note: Cytoplasmic when associated with SCAPER.

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-A2PRO_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).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. 87 interactions.
DIPiDIP-638N.
IntActiP20248. 27 interactions.
MINTiMINT-141826.
STRINGi9606.ENSP00000274026.

Structurei

Secondary structure

1
432
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi172 – 1743Combined sources
Helixi176 – 1783Combined sources
Helixi179 – 19214Combined sources
Helixi199 – 2024Combined sources
Helixi208 – 22417Combined sources
Helixi229 – 24315Combined sources
Helixi250 – 2523Combined sources
Helixi253 – 26816Combined sources
Beta strandi269 – 2713Combined sources
Helixi275 – 2817Combined sources
Turni282 – 2843Combined sources
Helixi288 – 30114Combined sources
Turni302 – 3043Combined sources
Helixi311 – 3199Combined sources
Beta strandi322 – 3243Combined sources
Helixi327 – 34216Combined sources
Helixi344 – 3474Combined sources
Helixi352 – 36817Combined sources
Helixi374 – 3807Combined sources
Helixi384 – 40017Combined sources
Helixi401 – 4033Combined sources
Helixi408 – 4125Combined sources
Beta strandi413 – 4153Combined sources
Helixi416 – 4183Combined sources
Helixi421 – 4233Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
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[»]
ProteinModelPortaliP20248.
SMRiP20248. Positions 176-432.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20248.

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclin family. Cyclin AB subfamily.Curated

Phylogenomic databases

eggNOGiCOG5024.
GeneTreeiENSGT00760000118939.
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

        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti156 – 1561H → R in CAG28620 (Ref. 3) Curated

Natural variant

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

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_001237.3.
UniGeneiHs.58974.

Genome annotation databases

EnsembliENST00000274026; ENSP00000274026; ENSG00000145386.
ENST00000618014; ENSP00000481380; 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:
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_001237.3.
UniGeneiHs.58974.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
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[»]
ProteinModelPortaliP20248.
SMRiP20248. Positions 176-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107331. 87 interactions.
DIPiDIP-638N.
IntActiP20248. 27 interactions.
MINTiMINT-141826.
STRINGi9606.ENSP00000274026.

Chemistry

BindingDBiP20248.
ChEMBLiCHEMBL3038467.

PTM databases

PhosphoSiteiP20248.

Polymorphism databases

DMDMi311033358.

Proteomic databases

MaxQBiP20248.
PaxDbiP20248.
PRIDEiP20248.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000274026; ENSP00000274026; ENSG00000145386.
ENST00000618014; ENSP00000481380; ENSG00000145386.
GeneIDi890.
KEGGihsa:890.
UCSCiuc003iec.4. human.

Organism-specific databases

CTDi890.
GeneCardsiGC04M122737.
HGNCiHGNC:1578. CCNA2.
HPAiCAB000114.
HPA020626.
MIMi123835. gene.
neXtProtiNX_P20248.
PharmGKBiPA94.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5024.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000167672.
HOVERGENiHBG106244.
InParanoidiP20248.
KOiK06627.
OMAiNPEKAAP.
OrthoDBiEOG7G7KQ0.
PhylomeDBiP20248.
TreeFamiTF101002.

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.

Miscellaneous databases

EvolutionaryTraceiP20248.
GeneWikiiCyclin_A2.
GenomeRNAii890.
NextBioi3682.
PMAP-CutDBP20248.
PROiP20248.
SOURCEiSearch...

Gene expression databases

BgeeiP20248.
CleanExiHS_CCNA2.
GenevestigatoriP20248.

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.
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Publicationsi

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  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: March 4, 2015
This is version 159 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

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 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.