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P51943

- CCNA2_MOUSE

UniProt

P51943 - CCNA2_MOUSE

Protein

Cyclin-A2

Gene

Ccna2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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

    1. protein binding Source: IntAct
    2. protein kinase binding Source: MGI

    GO - Biological processi

    1. mitotic nuclear division Source: UniProtKB-KW
    2. organ regeneration Source: Ensembl
    3. positive regulation of fibroblast proliferation Source: Ensembl
    4. positive regulation of transcription, DNA-templated Source: MGI
    5. Ras protein signal transduction Source: Ensembl
    6. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
    7. regulation of G2/M transition of mitotic cell cycle Source: InterPro
    8. response to estradiol Source: Ensembl
    9. response to glucagon Source: Ensembl

    Keywords - Molecular functioni

    Cyclin

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_188819. DNA Damage/Telomere Stress Induced Senescence.
    REACT_199110. G0 and Early G1.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_206803. Cyclin A/B1 associated events during G2/M transition.
    REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.
    REACT_227891. G2 Phase.

    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: Chromosome 3

    Organism-specific databases

    MGIiMGI:108069. Ccna2.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. female pronucleus Source: MGI
    3. male pronucleus Source: MGI
    4. nucleus Source: MGI

    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

    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

    ArrayExpressiP51943.
    BgeeiP51943.
    CleanExiMM_CCNA2.
    GenevestigatoriP51943.

    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. 10 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 – 18217
    Helixi189 – 1924
    Helixi198 – 21417
    Helixi219 – 23517
    Helixi240 – 2423
    Helixi243 – 25816
    Helixi265 – 2717
    Beta strandi274 – 2763
    Helixi278 – 29114
    Turni292 – 2943
    Helixi301 – 3088
    Helixi309 – 3113
    Beta strandi312 – 3143
    Helixi317 – 33216
    Helixi334 – 3374
    Helixi342 – 35817
    Helixi364 – 3707
    Helixi374 – 39017
    Helixi391 – 3933
    Helixi398 – 4025
    Helixi406 – 4083
    Helixi411 – 4133

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00740000115500.
    HOGENOMiHOG000167672.
    HOVERGENiHBG106244.
    InParanoidiQ8BRG1.
    KOiK06627.
    OMAiNPEKAAP.
    OrthoDBiEOG7G7KQ0.
    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.

    P51943-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGTSRHSGR DAGSALLSLH QEDQENVNPE KLAPAQQPRA QAVLKAGNVR    50
    GPAPQQKLKT RRVAPLKDLP INDEHVTAGP SWKAVSKQPA FTIHVDEAEE 100
    TQKRPAELKE TECEDALAFN AAVSLPGARK PLTPLDYPMD GSFESPHAMD 150
    MSIVLEDKPV NVNEVPDYQE DIHTYLREME VKCKPKVGYM KRQPDITNSM 200
    RAILVDWLVE VGEEYKLQNE TLHLAVNYID RFLSSMSVLR GKLQLVGTAA 250
    MLLASKFEEI YPPEVAEFVY ITDDTYSKKQ VLRMEHLVLK VLAFDLAAPT 300
    VNQFLTQYFL HLQPANCKVE SLAMFLGELS LIDADPYLKY LPSLIAGAAF 350
    HLALYTVTGQ SWPESLAQQT GYTLESLKPC LVDLHQTYLK APQHAQQSIR 400
    EKYKHSKYHS VSLLNPPETL SV 422
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS17313.1.
    PIRi S37280.
    S38501.
    RefSeqi NP_033958.2. NM_009828.2.
    UniGenei Mm.4189.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QHR X-ray 2.17 B/D 163-422 [» ]
    3QHW X-ray 1.91 B/D 163-422 [» ]
    4I3Z X-ray 2.05 B/D 165-421 [» ]
    4II5 X-ray 2.15 B/D 165-422 [» ]
    ProteinModelPortali P51943.
    SMRi P51943. Positions 163-422.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198545. 10 interactions.
    DIPi DIP-45864N.
    IntActi P51943. 3 interactions.
    STRINGi 10090.ENSMUSP00000029270.

    PTM databases

    PhosphoSitei P51943.

    Proteomic databases

    PaxDbi P51943.
    PRIDEi P51943.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029270 ; ENSMUSP00000029270 ; ENSMUSG00000027715 .
    GeneIDi 12428.
    KEGGi mmu:12428.
    UCSCi uc012cov.1. mouse.

    Organism-specific databases

    CTDi 890.
    MGIi MGI:108069. Ccna2.

    Phylogenomic databases

    eggNOGi COG5024.
    GeneTreei ENSGT00740000115500.
    HOGENOMi HOG000167672.
    HOVERGENi HBG106244.
    InParanoidi Q8BRG1.
    KOi K06627.
    OMAi NPEKAAP.
    OrthoDBi EOG7G7KQ0.
    TreeFami TF101002.

    Enzyme and pathway databases

    Reactomei REACT_188819. DNA Damage/Telomere Stress Induced Senescence.
    REACT_199110. G0 and Early G1.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_206803. Cyclin A/B1 associated events during G2/M transition.
    REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.
    REACT_227891. G2 Phase.

    Miscellaneous databases

    ChiTaRSi CCNA2. mouse.
    NextBioi 281244.
    PROi P51943.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51943.
    Bgeei P51943.
    CleanExi MM_CCNA2.
    Genevestigatori P51943.

    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

    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: October 1, 2014
    This is version 115 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