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P24864

- CCNE1_HUMAN

UniProt

P24864 - CCNE1_HUMAN

Protein

G1/S-specific cyclin-E1

Gene

CCNE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Essential for the control of the cell cycle at the G1/S (start) transition.1 Publication

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. cyclin-dependent protein serine/threonine kinase regulator activity Source: Ensembl
    3. kinase activity Source: Ensembl
    4. protein binding Source: UniProtKB
    5. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. androgen receptor signaling pathway Source: UniProtKB
    2. cell division Source: UniProtKB-KW
    3. DNA replication initiation Source: Ensembl
    4. G1/S transition of mitotic cell cycle Source: UniProtKB
    5. mitotic cell cycle Source: Reactome
    6. positive regulation of transcription, DNA-templated Source: UniProtKB
    7. protein phosphorylation Source: MGI
    8. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
    9. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome
    10. Wnt signaling pathway Source: Ensembl

    Keywords - Molecular functioni

    Cyclin

    Keywords - Biological processi

    Cell cycle, Cell division

    Enzyme and pathway databases

    ReactomeiREACT_111214. G0 and Early G1.
    REACT_1625. p53-Dependent G1 DNA Damage Response.
    REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_308. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_683. G1/S-Specific Transcription.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    SignaLinkiP24864.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    G1/S-specific cyclin-E1
    Gene namesi
    Name:CCNE1
    Synonyms:CCNE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:1589. CCNE1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cyclin-dependent protein kinase holoenzyme complex Source: Ensembl
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA96.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 410410G1/S-specific cyclin-E1PRO_0000080449Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei77 – 771Phosphothreonine2 Publications
    Modified residuei103 – 1031Phosphoserine2 Publications
    Modified residuei387 – 3871Phosphoserine3 Publications
    Modified residuei395 – 3951Phosphothreonine; by GSK34 Publications
    Modified residuei399 – 3991Phosphoserine; by CDK22 Publications

    Post-translational modificationi

    Phosphorylation of both Thr-395 by GSK3 and Ser-399 by CDK2 creates a high affinity degron recognized by FBXW7, and accelerates degradation via the ubiquitin proteasome pathway. Phosphorylation at Thr-77 creates a low affinity degron also recognized by FBXW7.5 Publications
    Ubiquitinated by UHRF2; appears to occur independently of phosphorylation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP24864.
    PaxDbiP24864.
    PRIDEiP24864.

    PTM databases

    PhosphoSiteiP24864.

    Miscellaneous databases

    PMAP-CutDBP24864.

    Expressioni

    Tissue specificityi

    Highly expressed in testis and placenta. Low levels in bronchial epithelial cells.1 Publication

    Gene expression databases

    ArrayExpressiP24864.
    BgeeiP24864.
    CleanExiHS_CCNE1.
    GenevestigatoriP24864.

    Organism-specific databases

    HPAiCAB000308.
    CAB016682.
    HPA018169.

    Interactioni

    Subunit structurei

    Interacts with a member of the CDK2/CDK protein kinases to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. Found in a complex with CDK2, CABLES1 and CCNA1 By similarity. Part of a complex consisting of UHRF2, CDK2 and CCNE1. Interacts directly with UHRF2; the interaction ubiquitinates CCNE1 and appears to occur independently of CCNE1 phosphorylation.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRCA1P383982EBI-519526,EBI-349905
    CDK2P2494110EBI-519526,EBI-375096
    CDKN1AP389369EBI-519526,EBI-375077
    CDKN1BP465277EBI-519526,EBI-519280
    FOXM1Q080502EBI-519526,EBI-866480
    UHRF2Q96PU44EBI-519526,EBI-625304

    Protein-protein interaction databases

    BioGridi107338. 73 interactions.
    DIPiDIP-149N.
    IntActiP24864. 14 interactions.
    MINTiMINT-1514839.
    STRINGi9606.ENSP00000262643.

    Structurei

    Secondary structure

    1
    410
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi109 – 1113
    Helixi113 – 12311
    Turni124 – 1263
    Helixi133 – 1364
    Helixi142 – 15817
    Helixi163 – 17917
    Helixi185 – 1873
    Helixi188 – 20316
    Helixi210 – 2156
    Turni216 – 2194
    Helixi223 – 23614
    Turni237 – 2393
    Helixi246 – 25712
    Beta strandi265 – 2673
    Helixi272 – 28716
    Helixi289 – 2935
    Helixi296 – 30611
    Helixi310 – 3167
    Helixi321 – 34121
    Helixi354 – 3596
    Helixi366 – 3705

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W98X-ray2.15B96-378[»]
    ProteinModelPortaliP24864.
    SMRiP24864. Positions 103-372.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24864.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cyclin family. Cyclin E subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG5024.
    HOGENOMiHOG000231743.
    HOVERGENiHBG050834.
    InParanoidiP24864.
    KOiK06626.
    OMAiPLLQPKM.
    OrthoDBiEOG7HB595.
    PhylomeDBiP24864.
    TreeFamiTF101005.

    Family and domain databases

    Gene3Di1.10.472.10. 2 hits.
    InterProiIPR013763. Cyclin-like.
    IPR014400. Cyclin_A/B/D/E/F.
    IPR004367. Cyclin_C-dom.
    IPR028858. Cyclin_E.
    IPR006671. Cyclin_N.
    [Graphical view]
    PANTHERiPTHR10177:SF71. PTHR10177:SF71. 1 hit.
    PfamiPF02984. Cyclin_C. 1 hit.
    PF00134. Cyclin_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001771. Cyclin_A_B_D_E. 1 hit.
    SMARTiSM00385. CYCLIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF47954. SSF47954. 2 hits.
    PROSITEiPS00292. CYCLINS. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform E1L (identifier: P24864-1) [UniParc]FASTAAdd to Basket

    Also known as: E-L

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPRERRERDA KERDTMKEDG GAEFSARSRK RKANVTVFLQ DPDEEMAKID    50
    RTARDQCGSQ PWDNNAVCAD PCSLIPTPDK EDDDRVYPNS TCKPRIIAPS 100
    RGSPLPVLSW ANREEVWKIM LNKEKTYLRD QHFLEQHPLL QPKMRAILLD 150
    WLMEVCEVYK LHRETFYLAQ DFFDRYMATQ ENVVKTLLQL IGISSLFIAA 200
    KLEEIYPPKL HQFAYVTDGA CSGDEILTME LMIMKALKWR LSPLTIVSWL 250
    NVYMQVAYLN DLHEVLLPQY PQQIFIQIAE LLDLCVLDVD CLEFPYGILA 300
    ASALYHFSSS ELMQKVSGYQ WCDIENCVKW MVPFAMVIRE TGSSKLKHFR 350
    GVADEDAHNI QTHRDSLDLL DKARAKKAML SEQNRASPLP SGLLTPPQSG 400
    KKQSSGPEMA 410
    Length:410
    Mass (Da):47,077
    Last modified:July 15, 1998 - v2
    Checksum:i424DF0B253B7047E
    GO
    Isoform E1S (identifier: P24864-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         154-196: Missing.

    Note: Lacks 49 residues within the cyclin box and cannot complex with CDK2.

    Show »
    Length:367
    Mass (Da):41,982
    Checksum:i526E59736D99D3C6
    GO
    Isoform 3 (identifier: P24864-3) [UniParc]FASTAAdd to Basket

    Also known as: E-S

    The sequence of this isoform differs from the canonical sequence as follows:
         1-15: Missing.

    Show »
    Length:395
    Mass (Da):45,150
    Checksum:i4E55D1F80BCFB3EB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91D → K no nucleotide entry (PubMed:7739542)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1515Missing in isoform 3. 3 PublicationsVSP_037381Add
    BLAST
    Alternative sequencei154 – 19643Missing in isoform E1S. CuratedVSP_001253Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74093 mRNA. No translation available.
    M73812 mRNA. No translation available.
    AK291549 mRNA. Translation: BAF84238.1.
    AF518727 Genomic DNA. Translation: AAM54043.1.
    BC035498 mRNA. Translation: AAH35498.1.
    X95406 Genomic DNA. Translation: CAA64687.1.
    X95406 Genomic DNA. Translation: CAA64688.1.
    AH003247 Genomic DNA. Translation: AAA83269.1.
    CCDSiCCDS12419.1. [P24864-1]
    PIRiA40270.
    RefSeqiNP_001229.1. NM_001238.2. [P24864-1]
    XP_006723520.1. XM_006723457.1. [P24864-3]
    UniGeneiHs.244723.

    Genome annotation databases

    EnsembliENST00000262643; ENSP00000262643; ENSG00000105173. [P24864-1]
    ENST00000444983; ENSP00000410179; ENSG00000105173. [P24864-3]
    GeneIDi898.
    KEGGihsa:898.
    UCSCiuc002nsn.3. human. [P24864-1]

    Polymorphism databases

    DMDMi3041657.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74093 mRNA. No translation available.
    M73812 mRNA. No translation available.
    AK291549 mRNA. Translation: BAF84238.1 .
    AF518727 Genomic DNA. Translation: AAM54043.1 .
    BC035498 mRNA. Translation: AAH35498.1 .
    X95406 Genomic DNA. Translation: CAA64687.1 .
    X95406 Genomic DNA. Translation: CAA64688.1 .
    AH003247 Genomic DNA. Translation: AAA83269.1 .
    CCDSi CCDS12419.1. [P24864-1 ]
    PIRi A40270.
    RefSeqi NP_001229.1. NM_001238.2. [P24864-1 ]
    XP_006723520.1. XM_006723457.1. [P24864-3 ]
    UniGenei Hs.244723.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1W98 X-ray 2.15 B 96-378 [» ]
    ProteinModelPortali P24864.
    SMRi P24864. Positions 103-372.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107338. 73 interactions.
    DIPi DIP-149N.
    IntActi P24864. 14 interactions.
    MINTi MINT-1514839.
    STRINGi 9606.ENSP00000262643.

    Chemistry

    BindingDBi P24864.
    ChEMBLi CHEMBL1907605.

    PTM databases

    PhosphoSitei P24864.

    Polymorphism databases

    DMDMi 3041657.

    Proteomic databases

    MaxQBi P24864.
    PaxDbi P24864.
    PRIDEi P24864.

    Protocols and materials databases

    DNASUi 898.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262643 ; ENSP00000262643 ; ENSG00000105173 . [P24864-1 ]
    ENST00000444983 ; ENSP00000410179 ; ENSG00000105173 . [P24864-3 ]
    GeneIDi 898.
    KEGGi hsa:898.
    UCSCi uc002nsn.3. human. [P24864-1 ]

    Organism-specific databases

    CTDi 898.
    GeneCardsi GC19P030302.
    HGNCi HGNC:1589. CCNE1.
    HPAi CAB000308.
    CAB016682.
    HPA018169.
    MIMi 123837. gene.
    neXtProti NX_P24864.
    PharmGKBi PA96.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5024.
    HOGENOMi HOG000231743.
    HOVERGENi HBG050834.
    InParanoidi P24864.
    KOi K06626.
    OMAi PLLQPKM.
    OrthoDBi EOG7HB595.
    PhylomeDBi P24864.
    TreeFami TF101005.

    Enzyme and pathway databases

    Reactomei REACT_111214. G0 and Early G1.
    REACT_1625. p53-Dependent G1 DNA Damage Response.
    REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_308. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_683. G1/S-Specific Transcription.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    SignaLinki P24864.

    Miscellaneous databases

    EvolutionaryTracei P24864.
    GeneWikii Cyclin_E1.
    GenomeRNAii 898.
    NextBioi 3708.
    PMAP-CutDB P24864.
    PROi P24864.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P24864.
    Bgeei P24864.
    CleanExi HS_CCNE1.
    Genevestigatori P24864.

    Family and domain databases

    Gene3Di 1.10.472.10. 2 hits.
    InterProi IPR013763. Cyclin-like.
    IPR014400. Cyclin_A/B/D/E/F.
    IPR004367. Cyclin_C-dom.
    IPR028858. Cyclin_E.
    IPR006671. Cyclin_N.
    [Graphical view ]
    PANTHERi PTHR10177:SF71. PTHR10177:SF71. 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. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47954. SSF47954. 2 hits.
    PROSITEi PS00292. CYCLINS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of three novel human cyclins by rescue of G1 cyclin (Cln) function in yeast."
      Lew D.J., Dulic V., Reed S.I.
      Cell 66:1197-1206(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    2. "Human cyclin E, a new cyclin that interacts with two members of the CDC2 gene family."
      Koff A., Cross F., Fisher A., Schumacher J., le Guellec K., Philippe M., Roberts J.M.
      Cell 66:1217-1228(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    3. "Human cyclin E, a nuclear protein essential for the G1-to-S phase transition."
      Ohtsubo M., Theodoras A.M., Schumacher J., Roberts J.M., Pagano M.
      Mol. Cell. Biol. 15:2612-2624(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS E1L AND 3), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
    4. "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] (ISOFORM E1L).
      Tissue: Placenta.
    5. NIEHS SNPs program
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "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] (ISOFORM E1L).
      Tissue: Placenta.
    7. "Regulation of cyclin E transcription by E2Fs and retinoblastoma protein."
      Geng Y., Eaton E.N., Picon M., Roberts J.M., Lundberg A.S., Gifford A., Sardet C., Weinberg R.A.
      Oncogene 12:1173-1180(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
    8. "Molecular cloning and chromosomal localization of the human cyclin C (CCNC) and cyclin E (CCNE) genes: deletion of the CCNC gene in human tumors."
      Li H., Lahti J.M., Valentine M., Saito M., Reed S.I., Look A.T., Kidd V.J.
      Genomics 32:253-259(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 281-370.
    9. "Alternative splicing of human cyclin E."
      Sewing A., Roenicke V., Buerger C., Funk M., Mueller R.
      J. Cell Sci. 107:581-588(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING.
    10. "Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E."
      Won K.A., Reed S.I.
      EMBO J. 15:4182-4193(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-395.
    11. "Cyclin E2, a novel human G1 cyclin and activating partner of CDK2 and CDK3, is induced by viral oncoproteins."
      Zariwala M., Liu J., Xiong Y.
      Oncogene 17:2787-2798(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    12. "Multisite phosphorylation by Cdk2 and GSK3 controls cyclin E degradation."
      Welcker M., Singer J., Loeb K.R., Grim J., Bloecher A., Gurien-West M., Clurman B.E., Roberts J.M.
      Mol. Cell 12:381-392(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-77; SER-387; THR-395 AND SER-399.
    13. Cited for: IDENTIFICATION IN A COMPLEX WITH UHRF2 AND CDK2.
    14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-387 AND THR-395, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "NIRF constitutes a nodal point in the cell cycle network and is a candidate tumor suppressor."
      Mori T., Ikeda D.D., Fukushima T., Takenoshita S., Kochi H.
      Cell Cycle 10:3284-3299(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH UHRF2.
    18. "The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2-independent roles."
      Honda R., Lowe E.D., Dubinina E., Skamnaki V., Cook A., Brown N.R., Johnson L.N.
      EMBO J. 24:452-463(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 96-378 IN COMPLEX WITH CDK2.
    19. "Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases."
      Hao B., Oehlmann S., Sowa M.E., Harper J.W., Pavletich N.P.
      Mol. Cell 26:131-143(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 73-80 IN COMPLEX WITH SKP1 AND FBXW7, PHOSPHORYLATION AT THR-77; THR-395 AND SER-399.

    Entry informationi

    Entry nameiCCNE1_HUMAN
    AccessioniPrimary (citable) accession number: P24864
    Secondary accession number(s): A8K684
    , Q14091, Q8NFG1, Q92501, Q9UD21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 158 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 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3