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P30260

- CDC27_HUMAN

UniProt

P30260 - CDC27_HUMAN

Protein

Cell division cycle protein 27 homolog

Gene

CDC27

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 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein phosphatase binding Source: BHF-UCL

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. cell proliferation Source: ProtInc
    3. metaphase/anaphase transition of mitotic cell cycle Source: MGI
    4. mitotic cell cycle Source: Reactome
    5. mitotic spindle assembly checkpoint Source: Reactome
    6. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    7. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    8. protein K11-linked ubiquitination Source: UniProtKB
    9. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_150471. Separation of Sister Chromatids.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_6904. Phosphorylation of the APC/C.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell division cycle protein 27 homolog
    Alternative name(s):
    Anaphase-promoting complex subunit 3
    Short name:
    APC3
    CDC27 homolog
    Short name:
    CDC27Hs
    H-NUC
    Gene namesi
    Name:CDC27
    Synonyms:ANAPC3, D0S1430E, D17S978E
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:1728. CDC27.

    Subcellular locationi

    GO - Cellular componenti

    1. anaphase-promoting complex Source: UniProtKB
    2. centrosome Source: MGI
    3. cytoplasm Source: LIFEdb
    4. cytosol Source: Reactome
    5. nucleoplasm Source: Reactome
    6. nucleus Source: BHF-UCL
    7. spindle Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi821 – 8211S → A: Abolishes binding to MCPH1. 1 Publication

    Organism-specific databases

    PharmGKBiPA26261.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 824824Cell division cycle protein 27 homologPRO_0000106273Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei205 – 2051Phosphothreonine2 Publications
    Modified residuei209 – 2091Phosphothreonine1 Publication
    Modified residuei244 – 2441Phosphothreonine1 Publication
    Modified residuei291 – 2911Phosphoserine1 Publication
    Modified residuei313 – 3131Phosphothreonine1 Publication
    Modified residuei339 – 3391Phosphoserine1 Publication
    Modified residuei366 – 3661Phosphothreonine1 Publication
    Modified residuei386 – 3861Phosphoserine1 Publication
    Modified residuei426 – 4261Phosphoserine2 Publications
    Modified residuei430 – 4301Phosphothreonine1 Publication
    Modified residuei435 – 4351Phosphoserine1 Publication
    Modified residuei438 – 4381Phosphoserine1 Publication
    Modified residuei446 – 4461Phosphothreonine2 Publications
    Modified residuei821 – 8211Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated. Phosphorylation on Ser-426 and Thr-446 occurs specifically during mitosis.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP30260.
    PaxDbiP30260.
    PRIDEiP30260.

    PTM databases

    PhosphoSiteiP30260.

    Expressioni

    Gene expression databases

    ArrayExpressiP30260.
    BgeeiP30260.
    CleanExiHS_CDC27.
    GenevestigatoriP30260.

    Organism-specific databases

    HPAiCAB004357.
    CAB016315.
    HPA028129.
    HPA052399.

    Interactioni

    Subunit structurei

    The APC/C is composed of at least 12 subunits. Interacts with RB. Interacts with FAM168B/MANI By similarity. Interacts with MCPH1.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC20Q128346EBI-994813,EBI-367462
    CDH1P128302EBI-994813,EBI-727477
    FBXO5Q9UKT42EBI-994813,EBI-852298
    FZR1Q9UM118EBI-994813,EBI-724997
    MAD2L2Q9UI952EBI-994813,EBI-77889
    NCK1P163333EBI-994813,EBI-389883
    NEK2P519552EBI-994813,EBI-633182
    PTENP604847EBI-994813,EBI-696162

    Protein-protein interaction databases

    BioGridi107431. 88 interactions.
    DIPiDIP-36422N.
    IntActiP30260. 44 interactions.
    MINTiMINT-86425.
    STRINGi9606.ENSP00000399255.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3T1NX-ray2.60C/D821-824[»]
    ProteinModelPortaliP30260.
    SMRiP30260. Positions 487-780.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati84 – 11431TPR 1Add
    BLAST
    Repeati115 – 14834TPR 2Add
    BLAST
    Repeati499 – 53234TPR 3Add
    BLAST
    Repeati567 – 60034TPR 4Add
    BLAST
    Repeati602 – 63433TPR 5Add
    BLAST
    Repeati635 – 66834TPR 6Add
    BLAST
    Repeati670 – 70233TPR 7Add
    BLAST
    Repeati704 – 73633TPR 8Add
    BLAST
    Repeati737 – 77034TPR 9Add
    BLAST

    Sequence similaritiesi

    Belongs to the APC3/CDC27 family.Curated
    Contains 9 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0457.
    HOGENOMiHOG000231056.
    HOVERGENiHBG050859.
    InParanoidiP30260.
    KOiK03350.
    OMAiNSCTTQV.
    OrthoDBiEOG751NDX.
    PhylomeDBiP30260.
    TreeFamiTF101058.

    Family and domain databases

    InterProiIPR013026. TPR-contain_dom.
    IPR001440. TPR_1.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF00515. TPR_1. 4 hits.
    PF07719. TPR_2. 1 hit.
    [Graphical view]
    SMARTiSM00028. TPR. 8 hits.
    [Graphical view]
    PROSITEiPS50005. TPR. 8 hits.
    PS50293. TPR_REGION. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30260-1) [UniParc]FASTAAdd to Basket

    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

    MTVLQEPVQA AIWQALNHYA YRDAVFLAER LYAEVHSEEA LFLLATCYYR    50
    SGKAYKAYRL LKGHSCTTPQ CKYLLAKCCV DLSKLAEGEQ ILSGGVFNKQ 100
    KSHDDIVTEF GDSACFTLSL LGHVYCKTDR LAKGSECYQK SLSLNPFLWS 150
    PFESLCEIGE KPDPDQTFKF TSLQNFSNCL PNSCTTQVPN HSLSHRQPET 200
    VLTETPQDTI ELNRLNLESS NSKYSLNTDS SVSYIDSAVI SPDTVPLGTG 250
    TSILSKQVQN KPKTGRSLLG GPAALSPLTP SFGILPLETP SPGDGSYLQN 300
    YTNTPPVIDV PSTGAPSKKS VARIGQTGTK SVFSQSGNSR EVTPILAQTQ 350
    SSGPQTSTTP QVLSPTITSP PNALPRRSSR LFTSDSSTTK ENSKKLKMKF 400
    PPKIPNRKTK SKTNKGGITQ PNINDSLEIT KLDSSIISEG KISTITPQIQ 450
    AFNLQKAAAE GLMSLLREMG KGYLALCSYN CKEAINILSH LPSHHYNTGW 500
    VLCQIGRAYF ELSEYMQAER IFSEVRRIEN YRVEGMEIYS TTLWHLQKDV 550
    ALSVLSKDLT DMDKNSPEAW CAAGNCFSLQ REHDIAIKFF QRAIQVDPNY 600
    AYAYTLLGHE FVLTEELDKA LACFRNAIRV NPRHYNAWYG LGMIYYKQEK 650
    FSLAEMHFQK ALDINPQSSV LLCHIGVVQH ALKKSEKALD TLNKAIVIDP 700
    KNPLCKFHRA SVLFANEKYK SALQELEELK QIVPKESLVY FLIGKVYKKL 750
    GQTHLALMNF SWAMDLDPKG ANNQIKEAID KRYLPDDEEP ITQEEQIMGT 800
    DESQESSMTD ADDTQLHAAE SDEF 824
    Length:824
    Mass (Da):91,867
    Last modified:December 1, 2000 - v2
    Checksum:iE6C8F59C1EF1DCBA
    GO
    Isoform 2 (identifier: P30260-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         319-319: K → KTFRVLQ

    Note: No experimental confirmation available. May be due to competing acceptor splice site.

    Show »
    Length:830
    Mass (Da):92,612
    Checksum:i00CE7174F8165CA1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti403 – 4031K → E in AAH11656. (PubMed:15489334)Curated
    Sequence conflicti460 – 4601Missing in AAA60471. (PubMed:8234252)Curated
    Sequence conflicti715 – 7151A → R in AAA60471. (PubMed:8234252)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti270 – 2701G → A in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035861
    Natural varianti320 – 3201S → P.
    Corresponds to variant rs3208653 [ dbSNP | Ensembl ].
    VAR_052613
    Natural varianti496 – 4961Y → H.
    Corresponds to variant rs13666 [ dbSNP | Ensembl ].
    VAR_014489

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei319 – 3191K → KTFRVLQ in isoform 2. 1 PublicationVSP_047225

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00001 mRNA. Translation: AAA60471.1.
    S78234 mRNA. Translation: AAB34378.1.
    AY518321 Genomic DNA. Translation: AAR89911.1.
    AC002558 Genomic DNA. No translation available.
    CH471231 Genomic DNA. Translation: EAW57687.1.
    BC011656 mRNA. Translation: AAH11656.1.
    CCDSiCCDS11509.1. [P30260-1]
    CCDS45720.1. [P30260-2]
    PIRiI52835.
    RefSeqiNP_001107563.1. NM_001114091.2. [P30260-2]
    NP_001247.3. NM_001256.4. [P30260-1]
    UniGeneiHs.463295.

    Genome annotation databases

    EnsembliENST00000066544; ENSP00000066544; ENSG00000004897. [P30260-1]
    ENST00000531206; ENSP00000434614; ENSG00000004897. [P30260-2]
    GeneIDi996.
    KEGGihsa:996.
    UCSCiuc002ild.4. human. [P30260-1]
    uc002ile.4. human.

    Polymorphism databases

    DMDMi12644198.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00001 mRNA. Translation: AAA60471.1 .
    S78234 mRNA. Translation: AAB34378.1 .
    AY518321 Genomic DNA. Translation: AAR89911.1 .
    AC002558 Genomic DNA. No translation available.
    CH471231 Genomic DNA. Translation: EAW57687.1 .
    BC011656 mRNA. Translation: AAH11656.1 .
    CCDSi CCDS11509.1. [P30260-1 ]
    CCDS45720.1. [P30260-2 ]
    PIRi I52835.
    RefSeqi NP_001107563.1. NM_001114091.2. [P30260-2 ]
    NP_001247.3. NM_001256.4. [P30260-1 ]
    UniGenei Hs.463295.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3T1N X-ray 2.60 C/D 821-824 [» ]
    ProteinModelPortali P30260.
    SMRi P30260. Positions 487-780.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107431. 88 interactions.
    DIPi DIP-36422N.
    IntActi P30260. 44 interactions.
    MINTi MINT-86425.
    STRINGi 9606.ENSP00000399255.

    PTM databases

    PhosphoSitei P30260.

    Polymorphism databases

    DMDMi 12644198.

    Proteomic databases

    MaxQBi P30260.
    PaxDbi P30260.
    PRIDEi P30260.

    Protocols and materials databases

    DNASUi 996.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000066544 ; ENSP00000066544 ; ENSG00000004897 . [P30260-1 ]
    ENST00000531206 ; ENSP00000434614 ; ENSG00000004897 . [P30260-2 ]
    GeneIDi 996.
    KEGGi hsa:996.
    UCSCi uc002ild.4. human. [P30260-1 ]
    uc002ile.4. human.

    Organism-specific databases

    CTDi 996.
    GeneCardsi GC17M045195.
    H-InvDB HIX0176461.
    HGNCi HGNC:1728. CDC27.
    HPAi CAB004357.
    CAB016315.
    HPA028129.
    HPA052399.
    MIMi 116946. gene.
    neXtProti NX_P30260.
    PharmGKBi PA26261.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0457.
    HOGENOMi HOG000231056.
    HOVERGENi HBG050859.
    InParanoidi P30260.
    KOi K03350.
    OMAi NSCTTQV.
    OrthoDBi EOG751NDX.
    PhylomeDBi P30260.
    TreeFami TF101058.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_150471. Separation of Sister Chromatids.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_6904. Phosphorylation of the APC/C.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi CDC27. human.
    GeneWikii CDC27.
    GenomeRNAii 996.
    NextBioi 4184.
    PROi P30260.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30260.
    Bgeei P30260.
    CleanExi HS_CDC27.
    Genevestigatori P30260.

    Family and domain databases

    InterProi IPR013026. TPR-contain_dom.
    IPR001440. TPR_1.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF00515. TPR_1. 4 hits.
    PF07719. TPR_2. 1 hit.
    [Graphical view ]
    SMARTi SM00028. TPR. 8 hits.
    [Graphical view ]
    PROSITEi PS50005. TPR. 8 hits.
    PS50293. TPR_REGION. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Linking yeast genetics to mammalian genomes: identification and mapping of the human homolog of CDC27 via the expressed sequence tag (EST) data base."
      Tugendreich S., Boguski M.S., Seldin M., Hieter P.A.
      Proc. Natl. Acad. Sci. U.S.A. 90:10031-10035(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Identification of a human homologue of yeast nuc2 which interacts with the retinoblastoma protein in a specific manner."
      Chen P.L., Ueng Y.C., Durfee T., Chen K.C., Yang-Feng T., Lee W.H.
      Cell Growth Differ. 6:199-210(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. NIEHS SNPs program
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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 2).
      Tissue: Uterus.
    7. "Mitotic regulation of the human anaphase-promoting complex by phosphorylation."
      Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J., Peters J.-M.
      EMBO J. 22:6598-6609(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-205; THR-209; THR-244; SER-291; THR-313; SER-426; THR-430; SER-435 AND THR-446.
    8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex."
      Jin L., Williamson A., Banerjee S., Philipp I., Rape M.
      Cell 133:653-665(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE APC/C.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205; SER-339; SER-426; SER-438 AND THR-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a cryo-electron microscopy model of vertebrate APC/C."
      Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A., Engel A., Peters J.-M., Stark H.
      Mol. Cell 20:867-879(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ELECTRON MICROSCOPY OF THE APC/C.
    16. "Molecular basis for the association of microcephalin (MCPH1) protein with the cell division cycle protein 27 (Cdc27) subunit of the anaphase-promoting complex."
      Singh N., Wiltshire T.D., Thompson J.R., Mer G., Couch F.J.
      J. Biol. Chem. 287:2854-2862(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 821-824 IN COMPLEX WITH MCPH1, PHOSPHORYLATION AT SER-821, MUTAGENESIS OF SER-821.
    17. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-270.

    Entry informationi

    Entry nameiCDC27_HUMAN
    AccessioniPrimary (citable) accession number: P30260
    Secondary accession number(s): G3V1C4, Q16349, Q96F35
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: December 1, 2000
    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 17
      Human chromosome 17: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3