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Q13042

- CDC16_HUMAN

UniProt

Q13042 - CDC16_HUMAN

Protein

Cell division cycle protein 16 homolog

Gene

CDC16

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (03 Oct 2003)
      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

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. cell proliferation Source: ProtInc
    3. mitotic cell cycle Source: Reactome
    4. mitotic nuclear division Source: ProtInc
    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 mitosis Source: ProtInc
    10. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, 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 16 homolog
    Alternative name(s):
    Anaphase-promoting complex subunit 6
    Short name:
    APC6
    CDC16 homolog
    Short name:
    CDC16Hs
    Cyclosome subunit 6
    Gene namesi
    Name:CDC16
    Synonyms:ANAPC6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:1720. CDC16.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication
    Note: Colocalizes with CDC27 to the centrosome at all stages of the cell cycle and to the mitotic spindle.

    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. spindle Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26256.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 620620Cell division cycle protein 16 homologPRO_0000106267Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei112 – 1121Phosphoserine1 Publication
    Modified residuei490 – 4901Phosphoserine1 Publication
    Modified residuei560 – 5601Phosphoserine3 Publications
    Modified residuei581 – 5811Phosphothreonine5 Publications
    Modified residuei595 – 5951Phosphoserine1 Publication
    Modified residuei599 – 5991Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylated. Phosphorylation on Ser-560 occurs specifically during mitosis.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13042.
    PaxDbiQ13042.
    PRIDEiQ13042.

    PTM databases

    PhosphoSiteiQ13042.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13042.
    BgeeiQ13042.
    CleanExiHS_CDC16.
    GenevestigatoriQ13042.

    Organism-specific databases

    HPAiHPA042826.

    Interactioni

    Subunit structurei

    The APC/C is composed of at least 12 subunits. Interacts with PPP5C and CDC20.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC26Q8NHZ83EBI-994830,EBI-2555941

    Protein-protein interaction databases

    BioGridi114400. 57 interactions.
    DIPiDIP-36423N.
    IntActiQ13042. 39 interactions.
    MINTiMINT-3026965.
    STRINGi9606.ENSP00000348554.

    Structurei

    Secondary structure

    1
    620
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi234 – 24310
    Helixi247 – 26014
    Turni265 – 2673
    Helixi268 – 27811
    Helixi281 – 29414
    Helixi300 – 31112
    Helixi316 – 32712
    Helixi335 – 34713
    Helixi350 – 36314
    Turni364 – 3663
    Helixi369 – 38012
    Helixi384 – 39512
    Helixi402 – 41413
    Helixi418 – 43215
    Turni433 – 4353
    Turni440 – 4434
    Helixi446 – 45712
    Helixi461 – 47414
    Helixi480 – 49213
    Helixi495 – 5039
    Turni504 – 5085
    Helixi513 – 52412
    Turni525 – 5284

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HYMX-ray2.80B/D/F/H/J/L212-539[»]
    ProteinModelPortaliQ13042.
    SMRiQ13042. Positions 14-529.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13042.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati130 – 16334TPR 1Add
    BLAST
    Repeati299 – 33335TPR 2Add
    BLAST
    Repeati334 – 36734TPR 3Add
    BLAST
    Repeati368 – 40134TPR 4Add
    BLAST
    Repeati403 – 43533TPR 5Add
    BLAST
    Repeati445 – 47834TPR 6Add
    BLAST
    Repeati479 – 51234TPR 7Add
    BLAST

    Sequence similaritiesi

    Belongs to the APC6/CDC16 family.Curated
    Contains 7 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0457.
    HOGENOMiHOG000230908.
    HOVERGENiHBG050857.
    InParanoidiQ13042.
    KOiK03353.
    OMAiHFLFENK.
    OrthoDBiEOG72VH5N.
    PhylomeDBiQ13042.
    TreeFamiTF101054.

    Family and domain databases

    Gene3Di1.25.40.10. 2 hits.
    InterProiIPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF00515. TPR_1. 2 hits.
    PF13181. TPR_8. 1 hit.
    [Graphical view]
    SMARTiSM00028. TPR. 4 hits.
    [Graphical view]
    PROSITEiPS50005. TPR. 5 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13042-1) [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

    MNLERLRKRV RQYLDQQQYQ SALFWADKVA SLSREEPQDI YWLAQCLYLT    50
    AQYHRAAHAL RSRKLDKLYE ACRYLAARCH YAAKEHQQAL DVLDMEEPIN 100
    KRLFEKYLKD ESGFKDPSSD WEMSQSSIKS SICLLRGKIY DALDNRTLAT 150
    YSYKEALKLD VYCFEAFDLL TSHHMLTAQE EKELLESLPL SKLCNEEQEL 200
    LRFLFENKLK KYNKPSETVI PESVDGLQEN LDVVVSLAER HYYNCDFKMC 250
    YKLTSVVMEK DPFHASCLPV HIGTLVELNK ANELFYLSHK LVDLYPSNPV 300
    SWFAVGCYYL MVGHKNEHAR RYLSKATTLE KTYGPAWIAY GHSFAVESEH 350
    DQAMAAYFTA AQLMKGCHLP MLYIGLEYGL TNNSKLAERF FSQALSIAPE 400
    DPFVMHEVGV VAFQNGEWKT AEKWFLDALE KIKAIGNEVT VDKWEPLLNN 450
    LGHVCRKLKK YAEALDYHRQ ALVLIPQNAS TYSAIGYIHS LMGNFENAVD 500
    YFHTALGLRR DDTFSVTMLG HCIEMYIGDS EAYIGADIKD KLKCYDFDVH 550
    TMKTLKNIIS PPWDFREFEV EKQTAEETGL TPLETSRKTP DSRPSLEETF 600
    EIEMNESDMM LETSMSDHST 620
    Length:620
    Mass (Da):71,656
    Last modified:October 3, 2003 - v2
    Checksum:iA9C4F24615DF17EB
    GO
    Isoform 2 (identifier: Q13042-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         36-36: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:619
    Mass (Da):71,527
    Checksum:i87D5542D21C14CD6
    GO
    Isoform 3 (identifier: Q13042-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         36-36: Missing.
         367-417: Missing.

    Show »
    Length:568
    Mass (Da):65,860
    Checksum:i0B5B3A3B468B3109
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti138 – 1381K → Q in AAC50200. (PubMed:7736578)Curated
    Sequence conflicti299 – 2991P → L in AAD45156. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei36 – 361Missing in isoform 2 and isoform 3. 1 PublicationVSP_008427
    Alternative sequencei367 – 41751Missing in isoform 3. CuratedVSP_008428Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18291 mRNA. Translation: AAC50200.1.
    AF164598 mRNA. Translation: AAD45156.1.
    AY599074 Genomic DNA. Translation: AAS94323.1.
    AL160396 Genomic DNA. Translation: CAI15810.1.
    AL160396 Genomic DNA. Translation: CAM22287.1.
    CH471085 Genomic DNA. Translation: EAX09237.1.
    CH471085 Genomic DNA. Translation: EAX09244.1.
    BC017244 mRNA. Translation: AAH17244.1.
    CCDSiCCDS9542.2. [Q13042-1]
    PIRiA56519.
    RefSeqiNP_001072113.1. NM_001078645.1. [Q13042-1]
    NP_003894.3. NM_003903.3. [Q13042-1]
    XP_005266261.1. XM_005266204.1. [Q13042-2]
    XP_006720055.1. XM_006719992.1. [Q13042-2]
    UniGeneiHs.374127.

    Genome annotation databases

    EnsembliENST00000252457; ENSP00000252457; ENSG00000130177. [Q13042-2]
    ENST00000356221; ENSP00000348554; ENSG00000130177. [Q13042-1]
    ENST00000360383; ENSP00000353549; ENSG00000130177. [Q13042-1]
    GeneIDi8881.
    KEGGihsa:8881.
    UCSCiuc001vuk.1. human. [Q13042-1]
    uc001vun.1. human. [Q13042-2]
    uc001vuo.1. human. [Q13042-3]

    Polymorphism databases

    DMDMi37537763.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18291 mRNA. Translation: AAC50200.1 .
    AF164598 mRNA. Translation: AAD45156.1 .
    AY599074 Genomic DNA. Translation: AAS94323.1 .
    AL160396 Genomic DNA. Translation: CAI15810.1 .
    AL160396 Genomic DNA. Translation: CAM22287.1 .
    CH471085 Genomic DNA. Translation: EAX09237.1 .
    CH471085 Genomic DNA. Translation: EAX09244.1 .
    BC017244 mRNA. Translation: AAH17244.1 .
    CCDSi CCDS9542.2. [Q13042-1 ]
    PIRi A56519.
    RefSeqi NP_001072113.1. NM_001078645.1. [Q13042-1 ]
    NP_003894.3. NM_003903.3. [Q13042-1 ]
    XP_005266261.1. XM_005266204.1. [Q13042-2 ]
    XP_006720055.1. XM_006719992.1. [Q13042-2 ]
    UniGenei Hs.374127.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HYM X-ray 2.80 B/D/F/H/J/L 212-539 [» ]
    ProteinModelPortali Q13042.
    SMRi Q13042. Positions 14-529.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114400. 57 interactions.
    DIPi DIP-36423N.
    IntActi Q13042. 39 interactions.
    MINTi MINT-3026965.
    STRINGi 9606.ENSP00000348554.

    PTM databases

    PhosphoSitei Q13042.

    Polymorphism databases

    DMDMi 37537763.

    Proteomic databases

    MaxQBi Q13042.
    PaxDbi Q13042.
    PRIDEi Q13042.

    Protocols and materials databases

    DNASUi 8881.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000252457 ; ENSP00000252457 ; ENSG00000130177 . [Q13042-2 ]
    ENST00000356221 ; ENSP00000348554 ; ENSG00000130177 . [Q13042-1 ]
    ENST00000360383 ; ENSP00000353549 ; ENSG00000130177 . [Q13042-1 ]
    GeneIDi 8881.
    KEGGi hsa:8881.
    UCSCi uc001vuk.1. human. [Q13042-1 ]
    uc001vun.1. human. [Q13042-2 ]
    uc001vuo.1. human. [Q13042-3 ]

    Organism-specific databases

    CTDi 8881.
    GeneCardsi GC13P115000.
    HGNCi HGNC:1720. CDC16.
    HPAi HPA042826.
    MIMi 603461. gene.
    neXtProti NX_Q13042.
    PharmGKBi PA26256.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0457.
    HOGENOMi HOG000230908.
    HOVERGENi HBG050857.
    InParanoidi Q13042.
    KOi K03353.
    OMAi HFLFENK.
    OrthoDBi EOG72VH5N.
    PhylomeDBi Q13042.
    TreeFami TF101054.

    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 CDC16. human.
    EvolutionaryTracei Q13042.
    GeneWikii CDC16.
    GenomeRNAii 8881.
    NextBioi 33347.
    PROi Q13042.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13042.
    Bgeei Q13042.
    CleanExi HS_CDC16.
    Genevestigatori Q13042.

    Family and domain databases

    Gene3Di 1.25.40.10. 2 hits.
    InterProi IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF00515. TPR_1. 2 hits.
    PF13181. TPR_8. 1 hit.
    [Graphical view ]
    SMARTi SM00028. TPR. 4 hits.
    [Graphical view ]
    PROSITEi PS50005. TPR. 5 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "CDC27Hs colocalizes with CDC16Hs to the centrosome and mitotic spindle and is essential for the metaphase to anaphase transition."
      Tugendreich S., Tomkiel J., Earnshaw W., Hieter P.
      Cell 81:261-268(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION.
      Tissue: Brain.
    2. "The differential splicing variants of human CDC16 mRNA."
      Zhou P.K., Rigaud O.
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 3).
    3. NIEHS SNPs program
      Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [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 1).
      Tissue: Skin.
    7. "The serine/threonine phosphatase PP5 interacts with CDC16 and CDC27, two tetratricopeptide repeat-containing subunits of the anaphase-promoting complex."
      Ollendorff V., Donoghue D.J.
      J. Biol. Chem. 272:32011-32018(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP5C.
    8. "Mammalian p55CDC mediates association of the spindle checkpoint protein Mad2 with the cyclosome/anaphase-promoting complex, and is involved in regulating anaphase onset and late mitotic events."
      Kallio M., Weinstein J., Daum J.R., Burke D.J., Gorbsky G.J.
      J. Cell Biol. 141:1393-1406(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDC20.
    9. "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 SER-112; SER-490; SER-560; THR-581; SER-595 AND THR-599.
    10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-581, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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.
    12. "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-560 AND THR-581, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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-581, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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-560 AND THR-581, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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.

    Entry informationi

    Entry nameiCDC16_HUMAN
    AccessioniPrimary (citable) accession number: Q13042
    Secondary accession number(s): A2A365
    , Q5T8C8, Q96AE6, Q9Y564
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2003
    Last sequence update: October 3, 2003
    Last modified: October 1, 2014
    This is version 134 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 13
      Human chromosome 13: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3