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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

Pathwayi: 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

ReactomeiR-HSA-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiQ13042.
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
Proteomesi
  • UP000005640 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

DisGeNETi8881.
OpenTargetsiENSG00000130177.
PharmGKBiPA26256.

Polymorphism and mutation databases

BioMutaiCDC16.
DMDMi37537763.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001062671 – 620Cell division cycle protein 16 homologAdd BLAST620

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei112Phosphoserine1 Publication1
Modified residuei490Phosphoserine1 Publication1
Modified residuei560PhosphoserineCombined sources1 Publication1
Modified residuei581PhosphothreonineCombined sources1 Publication1
Modified residuei595Phosphoserine1 Publication1
Modified residuei599Phosphothreonine1 Publication1

Post-translational modificationi

Phosphorylated. Phosphorylation on Ser-560 occurs specifically during mitosis.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ13042.
MaxQBiQ13042.
PaxDbiQ13042.
PeptideAtlasiQ13042.
PRIDEiQ13042.

PTM databases

iPTMnetiQ13042.
PhosphoSitePlusiQ13042.

Expressioni

Gene expression databases

BgeeiENSG00000130177.
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
CDC26Q8NHZ811EBI-994830,EBI-2555941

Protein-protein interaction databases

BioGridi114400. 158 interactors.
DIPiDIP-36423N.
IntActiQ13042. 53 interactors.
MINTiMINT-3026965.
STRINGi9606.ENSP00000348554.

Structurei

Secondary structure

1620
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi234 – 243Combined sources10
Helixi247 – 260Combined sources14
Turni265 – 267Combined sources3
Helixi268 – 278Combined sources11
Helixi281 – 294Combined sources14
Helixi300 – 311Combined sources12
Helixi316 – 327Combined sources12
Helixi335 – 347Combined sources13
Helixi350 – 363Combined sources14
Turni364 – 366Combined sources3
Helixi369 – 380Combined sources12
Helixi384 – 395Combined sources12
Helixi402 – 414Combined sources13
Helixi418 – 432Combined sources15
Turni433 – 435Combined sources3
Turni440 – 443Combined sources4
Helixi446 – 457Combined sources12
Helixi461 – 474Combined sources14
Helixi480 – 492Combined sources13
Helixi495 – 503Combined sources9
Turni504 – 508Combined sources5
Helixi513 – 524Combined sources12
Turni525 – 528Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HYMX-ray2.80B/D/F/H/J/L212-539[»]
4UI9electron microscopy3.60J/K1-620[»]
5A31electron microscopy4.30J/K1-620[»]
5G04electron microscopy4.00J/K1-620[»]
5G05electron microscopy3.40J/K1-620[»]
5KHRelectron microscopy6.10J/K1-620[»]
5L9Uelectron microscopy6.40J/K1-620[»]
5LCWelectron microscopy4.00J/K1-620[»]
ProteinModelPortaliQ13042.
SMRiQ13042.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13042.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati4 – 33TPR 1Add BLAST30
Repeati37 – 62TPR 2Add BLAST26
Repeati70 – 93TPR 3Add BLAST24
Repeati128 – 159TPR 4Add BLAST32
Repeati164 – 187TPR 5Add BLAST24
Repeati198 – 222TPR 6Add BLAST25
Repeati232 – 260TPR 7Add BLAST29
Repeati267 – 294TPR 8Add BLAST28
Repeati299 – 329TPR 9Add BLAST31
Repeati334 – 362TPR 10Add BLAST29
Repeati369 – 397TPR 11Add BLAST29
Repeati402 – 434TPR 12Add BLAST33
Repeati442 – 474TPR 13Add BLAST33
Repeati479 – 508TPR 14Add BLAST30

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

eggNOGiKOG1173. Eukaryota.
ENOG410XNY1. LUCA.
GeneTreeiENSGT00510000047327.
HOGENOMiHOG000230908.
HOVERGENiHBG050857.
InParanoidiQ13042.
KOiK03353.
OMAiQFIDMRR.
OrthoDBiEOG091G0HW1.
PhylomeDBiQ13042.
TreeFamiTF101054.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
SMARTiSM00028. TPR. 6 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti138K → Q in AAC50200 (PubMed:7736578).Curated1
Sequence conflicti299P → L in AAD45156 (Ref. 2) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0572701 – 94Missing in isoform 4. 1 PublicationAdd BLAST94
Alternative sequenceiVSP_00842736Missing in isoform 2 and isoform 3. 1 Publication1
Alternative sequenceiVSP_008428367 – 417Missing in isoform 3. CuratedAdd BLAST51

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.
CCDSiCCDS81786.1. [Q13042-2]
CCDS81787.1. [Q13042-4]
CCDS9542.2. [Q13042-1]
PIRiA56519.
RefSeqiNP_001072113.1. NM_001078645.2. [Q13042-1]
NP_001305446.1. NM_001318517.2. [Q13042-2]
NP_001305447.1. NM_001318518.2. [Q13042-3]
NP_001317030.1. NM_001330101.1.
NP_001317033.1. NM_001330104.1.
NP_001317034.1. NM_001330105.1.
NP_003894.3. NM_003903.4. [Q13042-1]
XP_016876322.1. XM_017020833.1. [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]

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.
CCDSiCCDS81786.1. [Q13042-2]
CCDS81787.1. [Q13042-4]
CCDS9542.2. [Q13042-1]
PIRiA56519.
RefSeqiNP_001072113.1. NM_001078645.2. [Q13042-1]
NP_001305446.1. NM_001318517.2. [Q13042-2]
NP_001305447.1. NM_001318518.2. [Q13042-3]
NP_001317030.1. NM_001330101.1.
NP_001317033.1. NM_001330104.1.
NP_001317034.1. NM_001330105.1.
NP_003894.3. NM_003903.4. [Q13042-1]
XP_016876322.1. XM_017020833.1. [Q13042-4]
UniGeneiHs.374127.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HYMX-ray2.80B/D/F/H/J/L212-539[»]
4UI9electron microscopy3.60J/K1-620[»]
5A31electron microscopy4.30J/K1-620[»]
5G04electron microscopy4.00J/K1-620[»]
5G05electron microscopy3.40J/K1-620[»]
5KHRelectron microscopy6.10J/K1-620[»]
5L9Uelectron microscopy6.40J/K1-620[»]
5LCWelectron microscopy4.00J/K1-620[»]
ProteinModelPortaliQ13042.
SMRiQ13042.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114400. 158 interactors.
DIPiDIP-36423N.
IntActiQ13042. 53 interactors.
MINTiMINT-3026965.
STRINGi9606.ENSP00000348554.

PTM databases

iPTMnetiQ13042.
PhosphoSitePlusiQ13042.

Polymorphism and mutation databases

BioMutaiCDC16.
DMDMi37537763.

Proteomic databases

EPDiQ13042.
MaxQBiQ13042.
PaxDbiQ13042.
PeptideAtlasiQ13042.
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]

Organism-specific databases

CTDi8881.
DisGeNETi8881.
GeneCardsiCDC16.
HGNCiHGNC:1720. CDC16.
HPAiHPA042826.
MIMi603461. gene.
neXtProtiNX_Q13042.
OpenTargetsiENSG00000130177.
PharmGKBiPA26256.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1173. Eukaryota.
ENOG410XNY1. LUCA.
GeneTreeiENSGT00510000047327.
HOGENOMiHOG000230908.
HOVERGENiHBG050857.
InParanoidiQ13042.
KOiK03353.
OMAiQFIDMRR.
OrthoDBiEOG091G0HW1.
PhylomeDBiQ13042.
TreeFamiTF101054.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiQ13042.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000130177.
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.
IPR019734. TPR_repeat.
[Graphical view]
SMARTiSM00028. TPR. 6 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
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 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

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 one 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.