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P51943 (CCNA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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, Cyca
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length422 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. Ref.6

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. In the testis, interacts only with CDK2. 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.

Tissue specificity

Ubiquitous. In the testis, expressed in germ cells and in the ovary, in both germline and somatic cells.

Developmental stage

Accumulates steadily during G2 and is abruptly destroyed at mitosis. Expressed in spermatogonia and is most abundant in preleptotene spermatocytes, cells which will enter the meiotic pathway.

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.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Nucleus
   Molecular functionCyclin
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRas protein signal transduction

Inferred from electronic annotation. Source: Ensembl

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

organ regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 16137671. Source: MGI

regulation of G2/M transition of mitotic cell cycle

Inferred from electronic annotation. Source: InterPro

regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: InterPro

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to glucagon

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15159393. Source: MGI

female pronucleus

Inferred from direct assay PubMed 16137671. Source: MGI

male pronucleus

Inferred from direct assay PubMed 16137671. Source: MGI

nucleus

Inferred from direct assay PubMed 15159393. Source: MGI

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 19592082. Source: IntAct

protein kinase binding

Inferred from physical interaction PubMed 11981756. Source: MGI

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Cyclin-A2
PRO_0000080340

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue51Phosphoserine By similarity

Experimental info

Sequence conflict1271G → A in CAA81331. Ref.1
Sequence conflict1271G → A in CAA53212. Ref.2
Sequence conflict3911A → P in CAA53212. Ref.2

Secondary structure

........................................ 422
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51943 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 1818B92552E4D0D1

FASTA42247,269
        10         20         30         40         50         60 
MPGTSRHSGR DAGSALLSLH QEDQENVNPE KLAPAQQPRA QAVLKAGNVR GPAPQQKLKT 

        70         80         90        100        110        120 
RRVAPLKDLP INDEHVTAGP SWKAVSKQPA FTIHVDEAEE TQKRPAELKE TECEDALAFN 

       130        140        150        160        170        180 
AAVSLPGARK PLTPLDYPMD GSFESPHAMD MSIVLEDKPV NVNEVPDYQE DIHTYLREME 

       190        200        210        220        230        240 
VKCKPKVGYM KRQPDITNSM RAILVDWLVE VGEEYKLQNE TLHLAVNYID RFLSSMSVLR 

       250        260        270        280        290        300 
GKLQLVGTAA MLLASKFEEI YPPEVAEFVY ITDDTYSKKQ VLRMEHLVLK VLAFDLAAPT 

       310        320        330        340        350        360 
VNQFLTQYFL HLQPANCKVE SLAMFLGELS LIDADPYLKY LPSLIAGAAF HLALYTVTGQ 

       370        380        390        400        410        420 
SWPESLAQQT GYTLESLKPC LVDLHQTYLK APQHAQQSIR EKYKHSKYHS VSLLNPPETL 


SV 

« Hide

References

« Hide 'large scale' references
[1]"The developmentally restricted pattern of expression in the male germ line of a murine cyclin A, cyclin A2, suggests roles in both mitotic and meiotic cell cycles."
Ravnik S.E., Wolgemuth D.J.
Dev. Biol. 173:69-78(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"A distinct cyclin A is expressed in germ cells in the mouse."
Sweeney C., Murphy M., Kubelka M., Ravnik S.E., Hawkins C.F., Wolgemuth D.J., Carrington M.
Development 122:53-64(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Thymus.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
[6]"Regulation of meiosis during mammalian spermatogenesis: the A-type cyclins and their associated cyclin-dependent kinases are differentially expressed in the germ-cell lineage."
Ravnik S.E., Wolgemuth D.J.
Dev. Biol. 207:408-418(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: Swiss Webster.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z26580 mRNA. Translation: CAA81331.1.
X75483 mRNA. Translation: CAA53212.1.
AK044924 mRNA. Translation: BAC32144.1.
CH466530 Genomic DNA. Translation: EDL35081.1.
BC052730 mRNA. Translation: AAH52730.1.
CCDSCCDS17313.1.
PIRS37280.
S38501.
RefSeqNP_033958.2. NM_009828.2.
UniGeneMm.4189.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QHRX-ray2.17B/D163-422[»]
3QHWX-ray1.91B/D163-422[»]
4I3ZX-ray2.05B/D165-421[»]
4II5X-ray2.15B/D165-422[»]
ProteinModelPortalP51943.
SMRP51943. Positions 163-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198545. 10 interactions.
DIPDIP-45864N.
IntActP51943. 3 interactions.
STRING10090.ENSMUSP00000029270.

PTM databases

PhosphoSiteP51943.

Proteomic databases

PaxDbP51943.
PRIDEP51943.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029270; ENSMUSP00000029270; ENSMUSG00000027715.
GeneID12428.
KEGGmmu:12428.
UCSCuc012cov.1. mouse.

Organism-specific databases

CTD890.
MGIMGI:108069. Ccna2.

Phylogenomic databases

eggNOGCOG5024.
GeneTreeENSGT00740000115500.
HOGENOMHOG000167672.
HOVERGENHBG106244.
InParanoidQ8BRG1.
KOK06627.
OMANPEKAAP.
OrthoDBEOG7G7KQ0.
TreeFamTF101002.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.

Gene expression databases

ArrayExpressP51943.
BgeeP51943.
CleanExMM_CCNA2.
GenevestigatorP51943.

Family and domain databases

Gene3D1.10.472.10. 2 hits.
InterProIPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E/F.
IPR015453. Cyclin_A_chordates.
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

ChiTaRSCCNA2. mouse.
NextBio281244.
PROP51943.
SOURCESearch...

Entry information

Entry nameCCNA2_MOUSE
AccessionPrimary (citable) accession number: P51943
Secondary accession number(s): Q61459, Q8BRG1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 113 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot