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P30274 (CCNA2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-A2

Short name=Cyclin-A
Gene names
Name:CCNA2
Synonyms:CCNA
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.

Subunit structure

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.

Subcellular location

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

Developmental stage

Accumulates steadily during G2 and is abruptly destroyed at mitosis.

Post-translational modification

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.

Sequence similarities

Belongs to the cyclin family. Cyclin AB subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430Cyclin-A2
PRO_0000080337

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue51Phosphoserine By similarity

Experimental info

Sequence conflict241A → E in CAA48398. Ref.2
Sequence conflict1071Missing in CAA48398. Ref.2

Secondary structure

........................................... 430
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30274 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: FACA1B8E770E997F

FASTA43048,262
        10         20         30         40         50         60 
MLGSSAHGPA AREAGSAVTL QQTAFQEDQE NVNPEKAAPA QQPRTRAGLA VLRAGNSRGP 

        70         80         90        100        110        120 
APQRPKTRRV APLKDLPIND EYVPVPPWKA NNKQPAFTIH VDEAEEEIQK RPTESKKSES 

       130        140        150        160        170        180 
EDVLAFNSAV TLPGPRKPLA PLDYPMDGSF ESPHTMEMSV VLEDEKPVSV NEVPDYHEDI 

       190        200        210        220        230        240 
HTYLREMEVK CKPKVGYMKK QPDITNSMRA ILVDWLVEVG EEYKLQNETL HLAVNYIDRF 

       250        260        270        280        290        300 
LSSMSVLRGK LQLVGTAAML LASKFEEIYP PEVAEFVYIT DDTYTKKQVL RMEHLVLKVL 

       310        320        330        340        350        360 
AFDLAAPTIN QFLTQYFLHQ QPANCKVESL AMFLGELSLI DADPYLKYLP SVIAAAAFHL 

       370        380        390        400        410        420 
ALYTVTGQSW PESLVQKTGY TLETLKPCLL DLHQTYLRAP QHAQQSIREK YKNSKYHGVS 

       430 
LLNPPETLNV 

« Hide

References

« Hide 'large scale' references
[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]"The crystal structure of cyclin A."
Brown N.R., Noble M.E.M., Endicott J.A., Garman E.F., Wakatsuki S., Mitchell E., Rasmussen B., Hunt T., Johnson L.N.
Structure 3:1235-1247(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 179-430.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC118203 mRNA. Translation: AAI18204.1.
X68321 mRNA. Translation: CAA48398.1.
PIRS24788.
RefSeqNP_001068591.1. NM_001075123.1.
UniGeneBt.87491.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VINX-ray2.00A170-429[»]
2G9XX-ray2.50B/D170-429[»]
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[»]
ProteinModelPortalP30274.
SMRP30274. Positions 169-430.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid158986. 5 interactions.
DIPDIP-693N.
STRING9913.ENSBTAP00000006503.

Proteomic databases

PRIDEP30274.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281667.
KEGGbta:281667.

Organism-specific databases

CTD890.

Phylogenomic databases

eggNOGCOG5024.
HOGENOMHOG000167672.
HOVERGENHBG106244.
InParanoidP30274.
KOK06627.

Family and domain databases

Gene3D1.10.472.10. 2 hits.
InterProIPR013763. Cyclin-like.
IPR015453. Cyclin_A.
IPR014400. Cyclin_A/B/D/E.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERPTHR10177:SF69. PTHR10177:SF69. 1 hit.
PfamPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFPIRSF001771. Cyclin_A_B_D_E. 1 hit.
SMARTSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMSSF47954. SSF47954. 2 hits.
PROSITEPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP30274.
NextBio20805598.

Entry information

Entry nameCCNA2_BOVIN
AccessionPrimary (citable) accession number: P30274
Secondary accession number(s): Q17QS7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references