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P30274

- CCNA2_BOVIN

UniProt

P30274 - CCNA2_BOVIN

Protein

Cyclin-A2

Gene

CCNA2

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      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.

    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

    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-SubCell
    2. female pronucleus Source: Ensembl
    3. male pronucleus Source: Ensembl
    4. nucleus Source: AgBase

    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.

    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

    MLGSSAHGPA AREAGSAVTL QQTAFQEDQE NVNPEKAAPA QQPRTRAGLA    50
    VLRAGNSRGP APQRPKTRRV APLKDLPIND EYVPVPPWKA NNKQPAFTIH 100
    VDEAEEEIQK RPTESKKSES EDVLAFNSAV TLPGPRKPLA PLDYPMDGSF 150
    ESPHTMEMSV VLEDEKPVSV NEVPDYHEDI HTYLREMEVK CKPKVGYMKK 200
    QPDITNSMRA ILVDWLVEVG EEYKLQNETL HLAVNYIDRF LSSMSVLRGK 250
    LQLVGTAAML LASKFEEIYP PEVAEFVYIT DDTYTKKQVL RMEHLVLKVL 300
    AFDLAAPTIN QFLTQYFLHQ QPANCKVESL AMFLGELSLI DADPYLKYLP 350
    SVIAAAAFHL ALYTVTGQSW PESLVQKTGY TLETLKPCLL DLHQTYLRAP 400
    QHAQQSIREK YKNSKYHGVS LLNPPETLNV 430
    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.

    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. 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 1, 2014
    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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3