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P20248

- CCNA2_HUMAN

UniProt

P20248 - CCNA2_HUMAN

Protein

Cyclin-A2

Gene

CCNA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (02 Nov 2010)
      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 - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Molecular functioni

    Cyclin

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_111214. G0 and Early G1.
    REACT_1156. Orc1 removal from chromatin.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_1915. G2 Phase.
    REACT_6362. Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
    SignaLinkiP20248.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-A2
    Short name:
    Cyclin-A
    Gene namesi
    Name:CCNA2
    Synonyms:CCN1, CCNA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:1578. CCNA2.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Cytoplasmic when associated with SCAPER.

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. female pronucleus Source: Ensembl
    3. male pronucleus Source: Ensembl
    4. nucleoplasm Source: Reactome
    5. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA94.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 432432Cyclin-A2PRO_0000080338Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei5 – 51Phosphoserine1 Publication
    Modified residuei55 – 551Phosphoserine1 Publication

    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

    MaxQBiP20248.
    PaxDbiP20248.
    PRIDEiP20248.

    PTM databases

    PhosphoSiteiP20248.

    Miscellaneous databases

    PMAP-CutDBP20248.

    Expressioni

    Developmental stagei

    Accumulates steadily during G2 and is abruptly destroyed at mitosis.

    Gene expression databases

    BgeeiP20248.
    CleanExiHS_CCNA2.
    GenevestigatoriP20248.

    Organism-specific databases

    HPAiCAB000114.
    HPA020626.

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P030702EBI-457097,EBI-617698From a different organism.
    CDK2P2494119EBI-457097,EBI-375096
    CDKN1AP389362EBI-457097,EBI-375077
    CDKN1BP4652713EBI-457097,EBI-519280
    UHRF2Q96PU42EBI-457097,EBI-625304

    Protein-protein interaction databases

    BioGridi107331. 71 interactions.
    DIPiDIP-638N.
    IntActiP20248. 27 interactions.
    MINTiMINT-141826.
    STRINGi9606.ENSP00000274026.

    Structurei

    Secondary structure

    1
    432
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi176 – 1783
    Helixi179 – 19214
    Helixi199 – 2024
    Helixi208 – 22417
    Helixi229 – 24315
    Helixi250 – 2523
    Helixi253 – 26816
    Beta strandi269 – 2713
    Helixi275 – 2817
    Turni282 – 2843
    Helixi288 – 30114
    Turni302 – 3043
    Helixi311 – 3199
    Beta strandi322 – 3243
    Helixi327 – 34216
    Helixi344 – 3474
    Helixi352 – 36817
    Helixi374 – 3807
    Helixi384 – 40017
    Helixi401 – 4033
    Helixi408 – 4125
    Beta strandi413 – 4153
    Helixi416 – 4183
    Helixi421 – 4233

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E9HX-ray2.50B/D175-432[»]
    1FINX-ray2.30B/D173-432[»]
    1FVVX-ray2.80B/D173-432[»]
    1GY3X-ray2.70B/D175-432[»]
    1H1PX-ray2.10B/D175-432[»]
    1H1QX-ray2.50B/D175-432[»]
    1H1RX-ray2.00B/D175-432[»]
    1H1SX-ray2.00B/D175-432[»]
    1H24X-ray2.50B/D174-432[»]
    1H25X-ray2.50B/D174-432[»]
    1H26X-ray2.24B/D174-432[»]
    1H27X-ray2.20B/D174-432[»]
    1H28X-ray2.80B/D174-432[»]
    1JSTX-ray2.60B/D175-432[»]
    1JSUX-ray2.30B173-432[»]
    1OGUX-ray2.60B/D174-432[»]
    1OI9X-ray2.10B/D174-432[»]
    1OIUX-ray2.00B/D174-432[»]
    1OIYX-ray2.40B/D174-432[»]
    1OKVX-ray2.40B/D173-432[»]
    1OKWX-ray2.50B/D173-432[»]
    1OL1X-ray2.90B/D173-432[»]
    1OL2X-ray2.60B/D173-432[»]
    1P5EX-ray2.22B/D175-432[»]
    1PKDX-ray2.30B/D175-432[»]
    1QMZX-ray2.20B/D174-432[»]
    1URCX-ray2.60B/D173-432[»]
    1VYWX-ray2.30B/D174-432[»]
    2BKZX-ray2.60B/D174-432[»]
    2BPMX-ray2.40B/D174-432[»]
    2C4GX-ray2.70B/D173-432[»]
    2C5NX-ray2.10B/D174-432[»]
    2C5OX-ray2.10B/D173-432[»]
    2C5VX-ray2.90B/D174-432[»]
    2C5XX-ray2.90B/D174-432[»]
    2C6TX-ray2.61B/D175-432[»]
    2CCHX-ray1.70B/D173-432[»]
    2CCIX-ray2.70B/D175-432[»]
    2CJMX-ray2.30B/D175-432[»]
    2I40X-ray2.80B/D173-432[»]
    2IW6X-ray2.30B/D174-432[»]
    2IW8X-ray2.30B/D174-432[»]
    2IW9X-ray2.00B/D174-432[»]
    2UUEX-ray2.06B/D174-432[»]
    2UZBX-ray2.70B/D175-432[»]
    2UZDX-ray2.72B/D175-432[»]
    2UZEX-ray2.40B/D175-432[»]
    2UZLX-ray2.40B/D175-432[»]
    2V22X-ray2.60B/D174-432[»]
    2WEVX-ray2.30B/D173-432[»]
    2WFYX-ray2.53B/D173-432[»]
    2WHBX-ray2.90B/D173-432[»]
    2WIHX-ray2.50B/D173-432[»]
    2WIPX-ray2.80B/D173-432[»]
    2WMAX-ray2.80B/D174-432[»]
    2WMBX-ray2.60B/D174-432[»]
    2WPAX-ray2.51B/D173-432[»]
    2WXVX-ray2.60B/D173-432[»]
    2X1NX-ray2.75B/D172-432[»]
    3EIDX-ray3.15B/D173-432[»]
    3EJ1X-ray3.22B/D173-432[»]
    3EOCX-ray3.20B/D173-432[»]
    3F5XX-ray2.40B/D177-432[»]
    4BCKX-ray2.05B/D171-432[»]
    4BCMX-ray2.45B/D171-432[»]
    4BCNX-ray2.10B171-432[»]
    D171-431[»]
    4BCPX-ray2.26B/D171-432[»]
    4CFNX-ray2.20B/D175-432[»]
    4CFWX-ray2.45B/D175-432[»]
    4EOIX-ray2.00B/D175-432[»]
    4EOJX-ray1.65B/D175-432[»]
    4EOKX-ray2.57B/D175-432[»]
    4EOLX-ray2.40B/D175-432[»]
    4EOMX-ray2.10B/D175-432[»]
    4EONX-ray2.40B/D175-432[»]
    4EOOX-ray2.10B/D175-432[»]
    4EOPX-ray1.99B/D175-432[»]
    4EOQX-ray2.15B/D175-432[»]
    4EORX-ray2.20B/D175-432[»]
    4EOSX-ray2.57B/D175-432[»]
    4FX3X-ray2.75B/D175-432[»]
    ProteinModelPortaliP20248.
    SMRiP20248. Positions 176-432.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20248.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cyclin family. Cyclin AB subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG5024.
    HOGENOMiHOG000167672.
    HOVERGENiHBG106244.
    InParanoidiP20248.
    KOiK06627.
    OMAiNPEKAAP.
    OrthoDBiEOG7G7KQ0.
    PhylomeDBiP20248.
    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.

    P20248-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGNSAPGPA TREAGSALLA LQQTALQEDQ ENINPEKAAP VQQPRTRAAL    50
    AVLKSGNPRG LAQQQRPKTR RVAPLKDLPV NDEHVTVPPW KANSKQPAFT 100
    IHVDEAEKEA QKKPAESQKI EREDALAFNS AISLPGPRKP LVPLDYPMDG 150
    SFESPHTMDM SIILEDEKPV SVNEVPDYHE DIHTYLREME VKCKPKVGYM 200
    KKQPDITNSM RAILVDWLVE VGEEYKLQNE TLHLAVNYID RFLSSMSVLR 250
    GKLQLVGTAA MLLASKFEEI YPPEVAEFVY ITDDTYTKKQ VLRMEHLVLK 300
    VLTFDLAAPT VNQFLTQYFL HQQPANCKVE SLAMFLGELS LIDADPYLKY 350
    LPSVIAGAAF HLALYTVTGQ SWPESLIRKT GYTLESLKPC LMDLHQTYLK 400
    APQHAQQSIR EKYKNSKYHG VSLLNPPETL NL 432
    Length:432
    Mass (Da):48,551
    Last modified:November 2, 2010 - v2
    Checksum:i97763A2897DD35F4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti156 – 1561H → R in CAG28620. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti163 – 1631I → V.8 Publications
    Corresponds to variant rs769242 [ dbSNP | Ensembl ].
    VAR_018819

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51688 mRNA. Translation: CAA35986.1.
    X68303 Genomic DNA. Translation: CAA48375.1.
    CR407692 mRNA. Translation: CAG28620.1.
    AF518006 Genomic DNA. Translation: AAM54042.1.
    AK291931 mRNA. Translation: BAF84620.1.
    AC079341 Genomic DNA. Translation: AAY40969.1.
    CH471056 Genomic DNA. Translation: EAX05246.1.
    BC104783 mRNA. Translation: AAI04784.1.
    BC104787 mRNA. Translation: AAI04788.1.
    CCDSiCCDS3723.1.
    PIRiS08277.
    RefSeqiNP_001228.1. NM_001237.3.
    UniGeneiHs.58974.

    Genome annotation databases

    EnsembliENST00000274026; ENSP00000274026; ENSG00000145386.
    GeneIDi890.
    KEGGihsa:890.
    UCSCiuc003iec.4. human.

    Polymorphism databases

    DMDMi311033358.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51688 mRNA. Translation: CAA35986.1 .
    X68303 Genomic DNA. Translation: CAA48375.1 .
    CR407692 mRNA. Translation: CAG28620.1 .
    AF518006 Genomic DNA. Translation: AAM54042.1 .
    AK291931 mRNA. Translation: BAF84620.1 .
    AC079341 Genomic DNA. Translation: AAY40969.1 .
    CH471056 Genomic DNA. Translation: EAX05246.1 .
    BC104783 mRNA. Translation: AAI04784.1 .
    BC104787 mRNA. Translation: AAI04788.1 .
    CCDSi CCDS3723.1.
    PIRi S08277.
    RefSeqi NP_001228.1. NM_001237.3.
    UniGenei Hs.58974.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E9H X-ray 2.50 B/D 175-432 [» ]
    1FIN X-ray 2.30 B/D 173-432 [» ]
    1FVV X-ray 2.80 B/D 173-432 [» ]
    1GY3 X-ray 2.70 B/D 175-432 [» ]
    1H1P X-ray 2.10 B/D 175-432 [» ]
    1H1Q X-ray 2.50 B/D 175-432 [» ]
    1H1R X-ray 2.00 B/D 175-432 [» ]
    1H1S X-ray 2.00 B/D 175-432 [» ]
    1H24 X-ray 2.50 B/D 174-432 [» ]
    1H25 X-ray 2.50 B/D 174-432 [» ]
    1H26 X-ray 2.24 B/D 174-432 [» ]
    1H27 X-ray 2.20 B/D 174-432 [» ]
    1H28 X-ray 2.80 B/D 174-432 [» ]
    1JST X-ray 2.60 B/D 175-432 [» ]
    1JSU X-ray 2.30 B 173-432 [» ]
    1OGU X-ray 2.60 B/D 174-432 [» ]
    1OI9 X-ray 2.10 B/D 174-432 [» ]
    1OIU X-ray 2.00 B/D 174-432 [» ]
    1OIY X-ray 2.40 B/D 174-432 [» ]
    1OKV X-ray 2.40 B/D 173-432 [» ]
    1OKW X-ray 2.50 B/D 173-432 [» ]
    1OL1 X-ray 2.90 B/D 173-432 [» ]
    1OL2 X-ray 2.60 B/D 173-432 [» ]
    1P5E X-ray 2.22 B/D 175-432 [» ]
    1PKD X-ray 2.30 B/D 175-432 [» ]
    1QMZ X-ray 2.20 B/D 174-432 [» ]
    1URC X-ray 2.60 B/D 173-432 [» ]
    1VYW X-ray 2.30 B/D 174-432 [» ]
    2BKZ X-ray 2.60 B/D 174-432 [» ]
    2BPM X-ray 2.40 B/D 174-432 [» ]
    2C4G X-ray 2.70 B/D 173-432 [» ]
    2C5N X-ray 2.10 B/D 174-432 [» ]
    2C5O X-ray 2.10 B/D 173-432 [» ]
    2C5V X-ray 2.90 B/D 174-432 [» ]
    2C5X X-ray 2.90 B/D 174-432 [» ]
    2C6T X-ray 2.61 B/D 175-432 [» ]
    2CCH X-ray 1.70 B/D 173-432 [» ]
    2CCI X-ray 2.70 B/D 175-432 [» ]
    2CJM X-ray 2.30 B/D 175-432 [» ]
    2I40 X-ray 2.80 B/D 173-432 [» ]
    2IW6 X-ray 2.30 B/D 174-432 [» ]
    2IW8 X-ray 2.30 B/D 174-432 [» ]
    2IW9 X-ray 2.00 B/D 174-432 [» ]
    2UUE X-ray 2.06 B/D 174-432 [» ]
    2UZB X-ray 2.70 B/D 175-432 [» ]
    2UZD X-ray 2.72 B/D 175-432 [» ]
    2UZE X-ray 2.40 B/D 175-432 [» ]
    2UZL X-ray 2.40 B/D 175-432 [» ]
    2V22 X-ray 2.60 B/D 174-432 [» ]
    2WEV X-ray 2.30 B/D 173-432 [» ]
    2WFY X-ray 2.53 B/D 173-432 [» ]
    2WHB X-ray 2.90 B/D 173-432 [» ]
    2WIH X-ray 2.50 B/D 173-432 [» ]
    2WIP X-ray 2.80 B/D 173-432 [» ]
    2WMA X-ray 2.80 B/D 174-432 [» ]
    2WMB X-ray 2.60 B/D 174-432 [» ]
    2WPA X-ray 2.51 B/D 173-432 [» ]
    2WXV X-ray 2.60 B/D 173-432 [» ]
    2X1N X-ray 2.75 B/D 172-432 [» ]
    3EID X-ray 3.15 B/D 173-432 [» ]
    3EJ1 X-ray 3.22 B/D 173-432 [» ]
    3EOC X-ray 3.20 B/D 173-432 [» ]
    3F5X X-ray 2.40 B/D 177-432 [» ]
    4BCK X-ray 2.05 B/D 171-432 [» ]
    4BCM X-ray 2.45 B/D 171-432 [» ]
    4BCN X-ray 2.10 B 171-432 [» ]
    D 171-431 [» ]
    4BCP X-ray 2.26 B/D 171-432 [» ]
    4CFN X-ray 2.20 B/D 175-432 [» ]
    4CFW X-ray 2.45 B/D 175-432 [» ]
    4EOI X-ray 2.00 B/D 175-432 [» ]
    4EOJ X-ray 1.65 B/D 175-432 [» ]
    4EOK X-ray 2.57 B/D 175-432 [» ]
    4EOL X-ray 2.40 B/D 175-432 [» ]
    4EOM X-ray 2.10 B/D 175-432 [» ]
    4EON X-ray 2.40 B/D 175-432 [» ]
    4EOO X-ray 2.10 B/D 175-432 [» ]
    4EOP X-ray 1.99 B/D 175-432 [» ]
    4EOQ X-ray 2.15 B/D 175-432 [» ]
    4EOR X-ray 2.20 B/D 175-432 [» ]
    4EOS X-ray 2.57 B/D 175-432 [» ]
    4FX3 X-ray 2.75 B/D 175-432 [» ]
    ProteinModelPortali P20248.
    SMRi P20248. Positions 176-432.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107331. 71 interactions.
    DIPi DIP-638N.
    IntActi P20248. 27 interactions.
    MINTi MINT-141826.
    STRINGi 9606.ENSP00000274026.

    Chemistry

    BindingDBi P20248.
    ChEMBLi CHEMBL2582.

    PTM databases

    PhosphoSitei P20248.

    Polymorphism databases

    DMDMi 311033358.

    Proteomic databases

    MaxQBi P20248.
    PaxDbi P20248.
    PRIDEi P20248.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000274026 ; ENSP00000274026 ; ENSG00000145386 .
    GeneIDi 890.
    KEGGi hsa:890.
    UCSCi uc003iec.4. human.

    Organism-specific databases

    CTDi 890.
    GeneCardsi GC04M122737.
    HGNCi HGNC:1578. CCNA2.
    HPAi CAB000114.
    HPA020626.
    MIMi 123835. gene.
    neXtProti NX_P20248.
    PharmGKBi PA94.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5024.
    HOGENOMi HOG000167672.
    HOVERGENi HBG106244.
    InParanoidi P20248.
    KOi K06627.
    OMAi NPEKAAP.
    OrthoDBi EOG7G7KQ0.
    PhylomeDBi P20248.
    TreeFami TF101002.

    Enzyme and pathway databases

    Reactomei REACT_111214. G0 and Early G1.
    REACT_1156. Orc1 removal from chromatin.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_1915. G2 Phase.
    REACT_6362. Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
    SignaLinki P20248.

    Miscellaneous databases

    EvolutionaryTracei P20248.
    GeneWikii Cyclin_A2.
    GenomeRNAii 890.
    NextBioi 3682.
    PMAP-CutDB P20248.
    PROi P20248.
    SOURCEi Search...

    Gene expression databases

    Bgeei P20248.
    CleanExi HS_CCNA2.
    Genevestigatori P20248.

    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. "Hepatitis B virus integration in a cyclin A gene in a hepatocellular carcinoma."
      Wang J., Chenivesse X., Henglein B., Brechot C.
      Nature 343:555-557(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-163.
    2. "Structure and cell cycle-regulated transcription of the human cyclin A gene."
      Henglein B., Chenivesse X., Wang D., Eick D., Brechot C.
      Proc. Natl. Acad. Sci. U.S.A. 91:5490-5494(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-163.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-163.
    4. NIEHS SNPs program
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-163.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-163.
    6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-163.
    8. "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], VARIANT VAL-163.
      Tissue: Brain.
    9. "SCAPER, a novel cyclin A-interacting protein that regulates cell cycle progression."
      Tsang W.Y., Wang L., Chen Z., Sanchez I., Dynlacht B.D.
      J. Cell Biol. 178:621-633(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCAPER, SUBCELLULAR LOCATION.
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry."
      Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G., Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.
      Mol. Cell 42:511-523(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP37.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex."
      Jeffrey P.D., Russo A.A., Polyak K., Gibbs E., Hurwitz J., Massague J., Pavletich N.P.
      Nature 376:313-320(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 173-432 COMPLEXED WITH CDK2.
    15. "Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex."
      Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.
      Nature 382:325-331(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 173-432 IN CDK2/KIP1 COMPLEX.
    16. "Structural basis of cyclin-dependent kinase activation by phosphorylation."
      Russo A.A., Jeffrey P.D., Pavletich N.P.
      Nat. Struct. Biol. 3:696-700(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 173-432 COMPLEXED WITH CDK2.
    17. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiCCNA2_HUMAN
    AccessioniPrimary (citable) accession number: P20248
    Secondary accession number(s): A8K7B6
    , Q2M3U6, Q4W5P4, Q6LER8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 154 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3