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Q13042 (CDC16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CDC16
Synonyms:ANAPC6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length620 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

Pathway

Protein modification; protein ubiquitination.

Subunit structure

The APC/C is composed of at least 12 subunits. Interacts with PPP5C and CDC20. Ref.7 Ref.8

Subcellular location

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

Post-translational modification

Phosphorylated. Phosphorylation on Ser-560 occurs specifically during mitosis. Ref.9

Sequence similarities

Belongs to the APC6/CDC16 family.

Contains 7 TPR repeats.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
Ubl conjugation pathway
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DomainRepeat
TPR repeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

mitosis

Traceable author statement Ref.1. Source: ProtInc

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic spindle assembly checkpoint

Traceable author statement. Source: Reactome

negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein K11-linked ubiquitination

Inferred from direct assay Ref.11. Source: UniProtKB

regulation of mitosis

Traceable author statement Ref.1. Source: ProtInc

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

   Cellular_componentanaphase-promoting complex

Inferred from direct assay Ref.17PubMed 21926987. Source: UniProtKB

centrosome

Inferred from direct assay Ref.1. Source: MGI

cytoplasm

Inferred from direct assay. Source: LIFEdb

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

spindle

Traceable author statement Ref.1. Source: ProtInc

spindle microtubule

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDC26Q8NHZ83EBI-994830,EBI-2555941

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13042-1)

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.
Isoform 2 (identifier: Q13042-2)

The sequence of this isoform differs from the canonical sequence as follows:
     36-36: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q13042-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 620620Cell division cycle protein 16 homolog
PRO_0000106267

Regions

Repeat130 – 16334TPR 1
Repeat299 – 33335TPR 2
Repeat334 – 36734TPR 3
Repeat368 – 40134TPR 4
Repeat403 – 43533TPR 5
Repeat445 – 47834TPR 6
Repeat479 – 51234TPR 7

Amino acid modifications

Modified residue1121Phosphoserine Ref.9
Modified residue4901Phosphoserine Ref.9
Modified residue5601Phosphoserine Ref.9 Ref.12 Ref.15
Modified residue5811Phosphothreonine Ref.9 Ref.10 Ref.12 Ref.14 Ref.15
Modified residue5951Phosphoserine Ref.9
Modified residue5991Phosphothreonine Ref.9

Natural variations

Alternative sequence361Missing in isoform 2 and isoform 3.
VSP_008427
Alternative sequence367 – 41751Missing in isoform 3.
VSP_008428

Experimental info

Sequence conflict1381K → Q in AAC50200. Ref.1
Sequence conflict2991P → L in AAD45156. Ref.2

Secondary structure

.......................................... 620
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 3, 2003. Version 2.
Checksum: A9C4F24615DF17EB

FASTA62071,656
        10         20         30         40         50         60 
MNLERLRKRV RQYLDQQQYQ SALFWADKVA SLSREEPQDI YWLAQCLYLT AQYHRAAHAL 

        70         80         90        100        110        120 
RSRKLDKLYE ACRYLAARCH YAAKEHQQAL DVLDMEEPIN KRLFEKYLKD ESGFKDPSSD 

       130        140        150        160        170        180 
WEMSQSSIKS SICLLRGKIY DALDNRTLAT YSYKEALKLD VYCFEAFDLL TSHHMLTAQE 

       190        200        210        220        230        240 
EKELLESLPL SKLCNEEQEL LRFLFENKLK KYNKPSETVI PESVDGLQEN LDVVVSLAER 

       250        260        270        280        290        300 
HYYNCDFKMC YKLTSVVMEK DPFHASCLPV HIGTLVELNK ANELFYLSHK LVDLYPSNPV 

       310        320        330        340        350        360 
SWFAVGCYYL MVGHKNEHAR RYLSKATTLE KTYGPAWIAY GHSFAVESEH DQAMAAYFTA 

       370        380        390        400        410        420 
AQLMKGCHLP MLYIGLEYGL TNNSKLAERF FSQALSIAPE DPFVMHEVGV VAFQNGEWKT 

       430        440        450        460        470        480 
AEKWFLDALE KIKAIGNEVT VDKWEPLLNN LGHVCRKLKK YAEALDYHRQ ALVLIPQNAS 

       490        500        510        520        530        540 
TYSAIGYIHS LMGNFENAVD YFHTALGLRR DDTFSVTMLG HCIEMYIGDS EAYIGADIKD 

       550        560        570        580        590        600 
KLKCYDFDVH TMKTLKNIIS PPWDFREFEV EKQTAEETGL TPLETSRKTP DSRPSLEETF 

       610        620 
EIEMNESDMM LETSMSDHST 

« Hide

Isoform 2 [UniParc].

Checksum: 87D5542D21C14CD6
Show »

FASTA61971,527
Isoform 3 [UniParc].

Checksum: 0B5B3A3B468B3109
Show »

FASTA56865,860

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA56519.
RefSeqNP_001072113.1. NM_001078645.1.
NP_003894.3. NM_003903.3.
XP_005266261.1. XM_005266204.1.
UniGeneHs.374127.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HYMX-ray2.80B/D/F/H/J/L212-539[»]
ProteinModelPortalQ13042.
SMRQ13042. Positions 14-529.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114400. 57 interactions.
DIPDIP-36423N.
IntActQ13042. 39 interactions.
MINTMINT-3026965.
STRING9606.ENSP00000348554.

PTM databases

PhosphoSiteQ13042.

Polymorphism databases

DMDM37537763.

Proteomic databases

PaxDbQ13042.
PRIDEQ13042.

Protocols and materials databases

DNASU8881.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252457; ENSP00000252457; ENSG00000130177. [Q13042-2]
ENST00000356221; ENSP00000348554; ENSG00000130177. [Q13042-1]
ENST00000360383; ENSP00000353549; ENSG00000130177. [Q13042-1]
GeneID8881.
KEGGhsa:8881.
UCSCuc001vuk.1. human. [Q13042-1]
uc001vun.1. human. [Q13042-2]
uc001vuo.1. human. [Q13042-3]

Organism-specific databases

CTD8881.
GeneCardsGC13P115000.
HGNCHGNC:1720. CDC16.
HPAHPA042826.
MIM603461. gene.
neXtProtNX_Q13042.
PharmGKBPA26256.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0457.
HOGENOMHOG000230908.
HOVERGENHBG050857.
InParanoidQ13042.
KOK03353.
OMAHFLFENK.
OrthoDBEOG72VH5N.
PhylomeDBQ13042.
TreeFamTF101054.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ13042.
BgeeQ13042.
CleanExHS_CDC16.
GenevestigatorQ13042.

Family and domain databases

Gene3D1.25.40.10. 2 hits.
InterProIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF00515. TPR_1. 2 hits.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTSM00028. TPR. 4 hits.
[Graphical view]
PROSITEPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDC16. human.
EvolutionaryTraceQ13042.
GeneWikiCDC16.
GenomeRNAi8881.
NextBio33347.
PROQ13042.
SOURCESearch...

Entry information

Entry nameCDC16_HUMAN
AccessionPrimary (citable) accession number: Q13042
Secondary accession number(s): A2A365 expand/collapse secondary AC list , Q5T8C8, Q96AE6, Q9Y564
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: April 16, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM