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P30274

- CCNA2_BOVIN

UniProt

P30274 - CCNA2_BOVIN

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Protein

Cyclin-A2

Gene

CCNA2

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 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. mitotic nuclear division Source: UniProtKB-KW
  2. positive regulation of transcription, DNA-templated Source: Ensembl
  3. Ras protein signal transduction Source: Ensembl
  4. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
  5. regulation of G2/M transition of mitotic cell cycle Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_201949. G2 Phase.
REACT_203215. Senescence-Associated Secretory Phenotype (SASP).
REACT_206864. Cyclin A:Cdk2-associated events at S phase entry.
REACT_213030. Orc1 removal from chromatin.
REACT_213075. Regulation of APC/C activators between G1/S and early anaphase.
REACT_214732. DNA Damage/Telomere Stress Induced Senescence.
REACT_223494. SCF(Skp2)-mediated degradation of p27/p21.
REACT_224007. Cyclin A/B1 associated events during G2/M transition.
REACT_226948. G0 and Early G1.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-A2
Short name:
Cyclin-A
Gene namesi
Name:CCNA2
Synonyms:CCNA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Nucleus. Cytoplasm
Note: Cytoplasmic when associated with SCAPER.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. female pronucleus Source: Ensembl
  3. male pronucleus Source: Ensembl
  4. nucleus Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Cyclin-A2PRO_0000080337Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei5 – 51PhosphoserineBy similarity

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

PRIDEiP30274.

Expressioni

Developmental stagei

Accumulates steadily during G2 and is abruptly destroyed at mitosis.

Gene expression databases

ExpressionAtlasiP30274. baseline.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi158986. 5 interactions.
DIPiDIP-693N.
STRINGi9913.ENSBTAP00000006503.

Structurei

Secondary structure

1
430
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi170 – 1723
Turni174 – 1763
Helixi177 – 19014
Turni195 – 1973
Helixi198 – 2003
Helixi206 – 22217
Helixi227 – 24317
Helixi248 – 2503
Helixi251 – 26616
Helixi273 – 2797
Turni280 – 2823
Helixi286 – 29914
Turni300 – 3023
Helixi309 – 3179
Beta strandi320 – 3223
Helixi325 – 34016
Helixi342 – 3454
Helixi350 – 36617
Helixi372 – 3787
Helixi382 – 39817
Helixi399 – 4013
Helixi406 – 4105
Helixi414 – 4163
Helixi419 – 4213

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VINX-ray2.00A170-429[»]
2G9XX-ray2.50B/D170-430[»]
3BHTX-ray2.00B/D169-430[»]
3BHUX-ray2.30B/D169-430[»]
3BHVX-ray2.10B/D169-430[»]
3DDPX-ray2.70B/D169-430[»]
3DDQX-ray1.80B/D169-430[»]
3DOGX-ray2.70B/D169-430[»]
3MY5X-ray2.10B/D169-430[»]
3TNWX-ray2.00B/D169-430[»]
4BCNX-ray2.10D169-430[»]
4BCOX-ray2.05B/D169-429[»]
4BCQX-ray2.40B169-429[»]
D169-430[»]
ProteinModelPortaliP30274.
SMRiP30274. Positions 169-430.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30274.

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclin family. Cyclin AB subfamily.Curated

Phylogenomic databases

eggNOGiCOG5024.
HOGENOMiHOG000167672.
HOVERGENiHBG106244.
InParanoidiP30274.
KOiK06627.

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.

P30274-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLGSSAHGPA AREAGSAVTL QQTAFQEDQE NVNPEKAAPA QQPRTRAGLA
60 70 80 90 100
VLRAGNSRGP APQRPKTRRV APLKDLPIND EYVPVPPWKA NNKQPAFTIH
110 120 130 140 150
VDEAEEEIQK RPTESKKSES EDVLAFNSAV TLPGPRKPLA PLDYPMDGSF
160 170 180 190 200
ESPHTMEMSV VLEDEKPVSV NEVPDYHEDI HTYLREMEVK CKPKVGYMKK
210 220 230 240 250
QPDITNSMRA ILVDWLVEVG EEYKLQNETL HLAVNYIDRF LSSMSVLRGK
260 270 280 290 300
LQLVGTAAML LASKFEEIYP PEVAEFVYIT DDTYTKKQVL RMEHLVLKVL
310 320 330 340 350
AFDLAAPTIN QFLTQYFLHQ QPANCKVESL AMFLGELSLI DADPYLKYLP
360 370 380 390 400
SVIAAAAFHL ALYTVTGQSW PESLVQKTGY TLETLKPCLL DLHQTYLRAP
410 420 430
QHAQQSIREK YKNSKYHGVS LLNPPETLNV
Length:430
Mass (Da):48,262
Last modified:October 17, 2006 - v2
Checksum:iFACA1B8E770E997F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241A → E in CAA48398. (PubMed:1333843)Curated
Sequence conflicti107 – 1071Missing in CAA48398. (PubMed:1333843)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC118203 mRNA. Translation: AAI18204.1.
X68321 mRNA. Translation: CAA48398.1.
PIRiS24788.
RefSeqiNP_001068591.1. NM_001075123.1.
UniGeneiBt.87491.

Genome annotation databases

GeneIDi281667.
KEGGibta:281667.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC118203 mRNA. Translation: AAI18204.1 .
X68321 mRNA. Translation: CAA48398.1 .
PIRi S24788.
RefSeqi NP_001068591.1. NM_001075123.1.
UniGenei Bt.87491.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1VIN X-ray 2.00 A 170-429 [» ]
2G9X X-ray 2.50 B/D 170-430 [» ]
3BHT X-ray 2.00 B/D 169-430 [» ]
3BHU X-ray 2.30 B/D 169-430 [» ]
3BHV X-ray 2.10 B/D 169-430 [» ]
3DDP X-ray 2.70 B/D 169-430 [» ]
3DDQ X-ray 1.80 B/D 169-430 [» ]
3DOG X-ray 2.70 B/D 169-430 [» ]
3MY5 X-ray 2.10 B/D 169-430 [» ]
3TNW X-ray 2.00 B/D 169-430 [» ]
4BCN X-ray 2.10 D 169-430 [» ]
4BCO X-ray 2.05 B/D 169-429 [» ]
4BCQ X-ray 2.40 B 169-429 [» ]
D 169-430 [» ]
ProteinModelPortali P30274.
SMRi P30274. Positions 169-430.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 158986. 5 interactions.
DIPi DIP-693N.
STRINGi 9913.ENSBTAP00000006503.

Proteomic databases

PRIDEi P30274.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 281667.
KEGGi bta:281667.

Organism-specific databases

CTDi 890.

Phylogenomic databases

eggNOGi COG5024.
HOGENOMi HOG000167672.
HOVERGENi HBG106244.
InParanoidi P30274.
KOi K06627.

Enzyme and pathway databases

Reactomei REACT_201949. G2 Phase.
REACT_203215. Senescence-Associated Secretory Phenotype (SASP).
REACT_206864. Cyclin A:Cdk2-associated events at S phase entry.
REACT_213030. Orc1 removal from chromatin.
REACT_213075. Regulation of APC/C activators between G1/S and early anaphase.
REACT_214732. DNA Damage/Telomere Stress Induced Senescence.
REACT_223494. SCF(Skp2)-mediated degradation of p27/p21.
REACT_224007. Cyclin A/B1 associated events during G2/M transition.
REACT_226948. G0 and Early G1.

Miscellaneous databases

EvolutionaryTracei P30274.
NextBioi 20805598.

Gene expression databases

ExpressionAtlasi P30274. baseline.

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. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Thalamus.
  2. "Identification of the domains in cyclin A required for binding to, and activation of, p34cdc2 and p32cdk2 protein kinase subunits."
    Kobayashi H., Stewart E., Poon R., Adamczewski J.P., Gannon J., Hunt T.
    Mol. Biol. Cell 3:1279-1294(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-430.
    Tissue: Lymphocyte.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 179-430.

Entry informationi

Entry nameiCCNA2_BOVIN
AccessioniPrimary (citable) accession number: P30274
Secondary accession number(s): Q17QS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 17, 2006
Last modified: October 29, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3