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Protein

Cell division cycle protein 16 homolog

Gene

CDC16

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Pathway: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Biological processi

Complete GO annotation...

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_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
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.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
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 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:1720. CDC16.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: UniProtKB
  • centrosome Source: MGI
  • cytoplasm Source: LIFEdb
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • spindle Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26256.

Polymorphism and mutation databases

BioMutaiCDC16.
DMDMi37537763.

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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13042.
PaxDbiQ13042.
PRIDEiQ13042.

PTM databases

PhosphoSiteiQ13042.

Expressioni

Gene expression databases

BgeeiQ13042.
CleanExiHS_CDC16.
ExpressionAtlasiQ13042. baseline and differential.
GenevisibleiQ13042. HS.

Organism-specific databases

HPAiHPA042826.

Interactioni

Subunit structurei

V-shaped homodimer. Interacts with CDC26. The mammalian APC/C is composed of 14 distinct subunits that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa. Interacts with PPP5C and CDC20.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC26Q8NHZ88EBI-994830,EBI-2555941

Protein-protein interaction databases

BioGridi114400. 62 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 – 24310Combined sources
Helixi247 – 26014Combined sources
Turni265 – 2673Combined sources
Helixi268 – 27811Combined sources
Helixi281 – 29414Combined sources
Helixi300 – 31112Combined sources
Helixi316 – 32712Combined sources
Helixi335 – 34713Combined sources
Helixi350 – 36314Combined sources
Turni364 – 3663Combined sources
Helixi369 – 38012Combined sources
Helixi384 – 39512Combined sources
Helixi402 – 41413Combined sources
Helixi418 – 43215Combined sources
Turni433 – 4353Combined sources
Turni440 – 4434Combined sources
Helixi446 – 45712Combined sources
Helixi461 – 47414Combined sources
Helixi480 – 49213Combined sources
Helixi495 – 5039Combined sources
Turni504 – 5085Combined sources
Helixi513 – 52412Combined sources
Turni525 – 5284Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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
Repeati4 – 3330TPR 1Add
BLAST
Repeati37 – 6226TPR 2Add
BLAST
Repeati70 – 9324TPR 3Add
BLAST
Repeati128 – 15932TPR 4Add
BLAST
Repeati164 – 18724TPR 5Add
BLAST
Repeati198 – 22225TPR 6Add
BLAST
Repeati232 – 26029TPR 7Add
BLAST
Repeati267 – 29428TPR 8Add
BLAST
Repeati299 – 32931TPR 9Add
BLAST
Repeati334 – 36229TPR 10Add
BLAST
Repeati369 – 39729TPR 11Add
BLAST
Repeati402 – 43433TPR 12Add
BLAST
Repeati442 – 47433TPR 13Add
BLAST
Repeati479 – 50830TPR 14Add
BLAST

Domaini

TPR repeats 1-7 mediate homodimerization, while the C-terminal TPR repeats bind to CDC26, burying its hydrophobic N-terminus.1 Publication

Sequence similaritiesi

Belongs to the APC6/CDC16 family.Curated
Contains 14 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00510000047327.
HOGENOMiHOG000230908.
HOVERGENiHBG050857.
InParanoidiQ13042.
KOiK03353.
OMAiACQYLAA.
OrthoDBiEOG72VH5N.
PhylomeDBiQ13042.
TreeFamiTF101054.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MNLERLRKRV RQYLDQQQYQ SALFWADKVA SLSREEPQDI YWLAQCLYLT
60 70 80 90 100
AQYHRAAHAL RSRKLDKLYE ACRYLAARCH YAAKEHQQAL DVLDMEEPIN
110 120 130 140 150
KRLFEKYLKD ESGFKDPSSD WEMSQSSIKS SICLLRGKIY DALDNRTLAT
160 170 180 190 200
YSYKEALKLD VYCFEAFDLL TSHHMLTAQE EKELLESLPL SKLCNEEQEL
210 220 230 240 250
LRFLFENKLK KYNKPSETVI PESVDGLQEN LDVVVSLAER HYYNCDFKMC
260 270 280 290 300
YKLTSVVMEK DPFHASCLPV HIGTLVELNK ANELFYLSHK LVDLYPSNPV
310 320 330 340 350
SWFAVGCYYL MVGHKNEHAR RYLSKATTLE KTYGPAWIAY GHSFAVESEH
360 370 380 390 400
DQAMAAYFTA AQLMKGCHLP MLYIGLEYGL TNNSKLAERF FSQALSIAPE
410 420 430 440 450
DPFVMHEVGV VAFQNGEWKT AEKWFLDALE KIKAIGNEVT VDKWEPLLNN
460 470 480 490 500
LGHVCRKLKK YAEALDYHRQ ALVLIPQNAS TYSAIGYIHS LMGNFENAVD
510 520 530 540 550
YFHTALGLRR DDTFSVTMLG HCIEMYIGDS EAYIGADIKD KLKCYDFDVH
560 570 580 590 600
TMKTLKNIIS PPWDFREFEV EKQTAEETGL TPLETSRKTP DSRPSLEETF
610 620
EIEMNESDMM LETSMSDHST
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
Isoform 4 (identifier: Q13042-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: Missing.

Note: No experimental confirmation available.
Show »
Length:526
Mass (Da):60,371
Checksum:i0F077329FB0AA56B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381K → Q in AAC50200 (PubMed:7736578).Curated
Sequence conflicti299 – 2991P → L in AAD45156 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9494Missing in isoform 4. 1 PublicationVSP_057270Add
BLAST
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:
EMBLi
GenBanki
DDBJi
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.
CH471085 Genomic DNA. Translation: EAX09245.1.
BC010875 mRNA. Translation: AAH10875.1.
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]
XP_006720056.1. XM_006719993.1. [Q13042-4]
UniGeneiHs.374127.

Genome annotation databases

EnsembliENST00000252457; ENSP00000252457; ENSG00000130177. [Q13042-2]
ENST00000356221; ENSP00000348554; ENSG00000130177. [Q13042-1]
ENST00000360383; ENSP00000353549; ENSG00000130177. [Q13042-1]
ENST00000375308; ENSP00000364457; ENSG00000130177. [Q13042-4]
ENST00000375310; ENSP00000364459; ENSG00000130177. [Q13042-4]
GeneIDi8881.
KEGGihsa:8881.
UCSCiuc001vuk.1. human. [Q13042-1]
uc001vun.1. human. [Q13042-2]
uc001vuo.1. human. [Q13042-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
CH471085 Genomic DNA. Translation: EAX09245.1.
BC010875 mRNA. Translation: AAH10875.1.
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]
XP_006720056.1. XM_006719993.1. [Q13042-4]
UniGeneiHs.374127.

3D structure databases

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

Protein-protein interaction databases

BioGridi114400. 62 interactions.
DIPiDIP-36423N.
IntActiQ13042. 39 interactions.
MINTiMINT-3026965.
STRINGi9606.ENSP00000348554.

PTM databases

PhosphoSiteiQ13042.

Polymorphism and mutation databases

BioMutaiCDC16.
DMDMi37537763.

Proteomic databases

MaxQBiQ13042.
PaxDbiQ13042.
PRIDEiQ13042.

Protocols and materials databases

DNASUi8881.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000252457; ENSP00000252457; ENSG00000130177. [Q13042-2]
ENST00000356221; ENSP00000348554; ENSG00000130177. [Q13042-1]
ENST00000360383; ENSP00000353549; ENSG00000130177. [Q13042-1]
ENST00000375308; ENSP00000364457; ENSG00000130177. [Q13042-4]
ENST00000375310; ENSP00000364459; ENSG00000130177. [Q13042-4]
GeneIDi8881.
KEGGihsa:8881.
UCSCiuc001vuk.1. human. [Q13042-1]
uc001vun.1. human. [Q13042-2]
uc001vuo.1. human. [Q13042-3]

Organism-specific databases

CTDi8881.
GeneCardsiGC13P115000.
HGNCiHGNC:1720. CDC16.
HPAiHPA042826.
MIMi603461. gene.
neXtProtiNX_Q13042.
PharmGKBiPA26256.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00510000047327.
HOGENOMiHOG000230908.
HOVERGENiHBG050857.
InParanoidiQ13042.
KOiK03353.
OMAiACQYLAA.
OrthoDBiEOG72VH5N.
PhylomeDBiQ13042.
TreeFamiTF101054.

Enzyme and pathway databases

UniPathwayiUPA00143.
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_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
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.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.

Miscellaneous databases

ChiTaRSiCDC16. human.
EvolutionaryTraceiQ13042.
GeneWikiiCDC16.
GenomeRNAii8881.
NextBioi33347.
PROiQ13042.
SOURCEiSearch...

Gene expression databases

BgeeiQ13042.
CleanExiHS_CDC16.
ExpressionAtlasiQ13042. baseline and differential.
GenevisibleiQ13042. HS.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORMS 1 AND 4).
    Tissue: Lung and 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.
  18. "Insights into anaphase promoting complex TPR subdomain assembly from a CDC26-APC6 structure."
    Wang J., Dye B.T., Rajashankar K.R., Kurinov I., Schulman B.A.
    Nat. Struct. Mol. Biol. 16:987-989(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 212-539 IN COMPLEX WITH CDC26, TPR REPEATS, SUBUNIT.
  19. "Molecular architecture and mechanism of the anaphase-promoting complex."
    Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.
    Nature 513:388-393(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE APC/C, SUBUNIT.

Entry informationi

Entry nameiCDC16_HUMAN
AccessioniPrimary (citable) accession number: Q13042
Secondary accession number(s): A2A365
, Q5T8C8, Q7Z651, Q96AE6, Q9Y564
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: June 24, 2015
This is version 143 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.