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Protein

Cyclin-A2

Gene

Ccna2

Organism
Mus musculus (Mouse)
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.1 Publication

GO - Molecular functioni

  • protein kinase binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_274086. G0 and Early G1.
REACT_283368. G2 Phase.
REACT_315933. Orc1 removal from chromatin.
REACT_316610. DNA Damage/Telomere Stress Induced Senescence.
REACT_321479. Cyclin A:Cdk2-associated events at S phase entry.
REACT_336745. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_342086. SCF(Skp2)-mediated degradation of p27/p21.
REACT_349749. Cyclin A/B1 associated events during G2/M transition.
REACT_350665. Senescence-Associated Secretory Phenotype (SASP).
REACT_351228. Regulation of APC/C activators between G1/S and early anaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-A2
Short name:
Cyclin-A
Gene namesi
Name:Ccna2
Synonyms:Ccna, Cyca
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:108069. Ccna2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • female pronucleus Source: MGI
  • male pronucleus Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Cyclin-A2PRO_0000080340Add
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

MaxQBiP51943.
PaxDbiP51943.
PRIDEiP51943.

PTM databases

PhosphoSiteiP51943.

Expressioni

Tissue specificityi

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

Developmental stagei

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.

Gene expression databases

BgeeiP51943.
CleanExiMM_CCNA2.
ExpressionAtlasiP51943. baseline and differential.
GenevisibleiP51943. MM.

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. In the testis, interacts only with CDK2. When associated with CDK2 (but not with CDK1), interacts with SCAPER (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Cdk1P114402EBI-846980,EBI-846949
Cdk2P973773EBI-846980,EBI-847048

Protein-protein interaction databases

BioGridi198545. 9 interactions.
DIPiDIP-45864N.
IntActiP51943. 3 interactions.
STRINGi10090.ENSMUSP00000029270.

Structurei

Secondary structure

1
422
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi166 – 18217Combined sources
Helixi189 – 1924Combined sources
Helixi198 – 21417Combined sources
Helixi219 – 23517Combined sources
Helixi240 – 2423Combined sources
Helixi243 – 25816Combined sources
Helixi265 – 2717Combined sources
Beta strandi274 – 2763Combined sources
Helixi278 – 29114Combined sources
Turni292 – 2943Combined sources
Helixi301 – 3088Combined sources
Helixi309 – 3113Combined sources
Beta strandi312 – 3143Combined sources
Helixi317 – 33216Combined sources
Helixi334 – 3374Combined sources
Helixi342 – 35817Combined sources
Helixi364 – 3707Combined sources
Helixi374 – 39017Combined sources
Helixi391 – 3933Combined sources
Helixi398 – 4025Combined sources
Helixi406 – 4083Combined sources
Helixi411 – 4133Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QHRX-ray2.17B/D163-422[»]
3QHWX-ray1.91B/D163-422[»]
4I3ZX-ray2.05B/D165-421[»]
4II5X-ray2.15B/D165-422[»]
ProteinModelPortaliP51943.
SMRiP51943. Positions 163-422.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclin family. Cyclin AB subfamily.Curated

Phylogenomic databases

eggNOGiCOG5024.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000167672.
HOVERGENiHBG106244.
InParanoidiP51943.
KOiK06627.
OMAiNPEKAAP.
OrthoDBiEOG7G7KQ0.
TreeFamiTF101002.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
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]
SMARTiSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51943-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGTSRHSGR DAGSALLSLH QEDQENVNPE KLAPAQQPRA QAVLKAGNVR
60 70 80 90 100
GPAPQQKLKT RRVAPLKDLP INDEHVTAGP SWKAVSKQPA FTIHVDEAEE
110 120 130 140 150
TQKRPAELKE TECEDALAFN AAVSLPGARK PLTPLDYPMD GSFESPHAMD
160 170 180 190 200
MSIVLEDKPV NVNEVPDYQE DIHTYLREME VKCKPKVGYM KRQPDITNSM
210 220 230 240 250
RAILVDWLVE VGEEYKLQNE TLHLAVNYID RFLSSMSVLR GKLQLVGTAA
260 270 280 290 300
MLLASKFEEI YPPEVAEFVY ITDDTYSKKQ VLRMEHLVLK VLAFDLAAPT
310 320 330 340 350
VNQFLTQYFL HLQPANCKVE SLAMFLGELS LIDADPYLKY LPSLIAGAAF
360 370 380 390 400
HLALYTVTGQ SWPESLAQQT GYTLESLKPC LVDLHQTYLK APQHAQQSIR
410 420
EKYKHSKYHS VSLLNPPETL SV
Length:422
Mass (Da):47,269
Last modified:July 27, 2011 - v2
Checksum:i1818B92552E4D0D1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti127 – 1271G → A in CAA81331 (PubMed:8575639).Curated
Sequence conflicti127 – 1271G → A in CAA53212 (PubMed:8565853).Curated
Sequence conflicti391 – 3911A → P in CAA53212 (PubMed:8565853).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS17313.1.
PIRiS37280.
S38501.
RefSeqiNP_033958.2. NM_009828.2.
UniGeneiMm.4189.

Genome annotation databases

EnsembliENSMUST00000029270; ENSMUSP00000029270; ENSMUSG00000027715.
GeneIDi12428.
KEGGimmu:12428.
UCSCiuc012cov.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS17313.1.
PIRiS37280.
S38501.
RefSeqiNP_033958.2. NM_009828.2.
UniGeneiMm.4189.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QHRX-ray2.17B/D163-422[»]
3QHWX-ray1.91B/D163-422[»]
4I3ZX-ray2.05B/D165-421[»]
4II5X-ray2.15B/D165-422[»]
ProteinModelPortaliP51943.
SMRiP51943. Positions 163-422.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198545. 9 interactions.
DIPiDIP-45864N.
IntActiP51943. 3 interactions.
STRINGi10090.ENSMUSP00000029270.

PTM databases

PhosphoSiteiP51943.

Proteomic databases

MaxQBiP51943.
PaxDbiP51943.
PRIDEiP51943.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029270; ENSMUSP00000029270; ENSMUSG00000027715.
GeneIDi12428.
KEGGimmu:12428.
UCSCiuc012cov.1. mouse.

Organism-specific databases

CTDi890.
MGIiMGI:108069. Ccna2.

Phylogenomic databases

eggNOGiCOG5024.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000167672.
HOVERGENiHBG106244.
InParanoidiP51943.
KOiK06627.
OMAiNPEKAAP.
OrthoDBiEOG7G7KQ0.
TreeFamiTF101002.

Enzyme and pathway databases

ReactomeiREACT_274086. G0 and Early G1.
REACT_283368. G2 Phase.
REACT_315933. Orc1 removal from chromatin.
REACT_316610. DNA Damage/Telomere Stress Induced Senescence.
REACT_321479. Cyclin A:Cdk2-associated events at S phase entry.
REACT_336745. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_342086. SCF(Skp2)-mediated degradation of p27/p21.
REACT_349749. Cyclin A/B1 associated events during G2/M transition.
REACT_350665. Senescence-Associated Secretory Phenotype (SASP).
REACT_351228. Regulation of APC/C activators between G1/S and early anaphase.

Miscellaneous databases

ChiTaRSiCcna2. mouse.
NextBioi281244.
PROiP51943.
SOURCEiSearch...

Gene expression databases

BgeeiP51943.
CleanExiMM_CCNA2.
ExpressionAtlasiP51943. baseline and differential.
GenevisibleiP51943. MM.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
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]
SMARTiSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiCCNA2_MOUSE
AccessioniPrimary (citable) accession number: P51943
Secondary accession number(s): Q61459, Q8BRG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 122 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.