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Protein

Anaphase-promoting complex subunit 16

Gene

ANAPC16

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).
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit 16
Short name:
APC16
Alternative name(s):
Cyclosome subunit 16
Gene namesi
Name:ANAPC16
Synonyms:C10orf104, CENP-271 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:26976. ANAPC16.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: UniProtKB
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • kinetochore Source: UniProtKB
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Kinetochore, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165548225.

Polymorphism and mutation databases

BioMutaiANAPC16.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 110109Anaphase-promoting complex subunit 16PRO_0000089816Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ96DE5.
MaxQBiQ96DE5.
PaxDbiQ96DE5.
PeptideAtlasiQ96DE5.
PRIDEiQ96DE5.

PTM databases

iPTMnetiQ96DE5.
PhosphoSiteiQ96DE5.

Expressioni

Gene expression databases

BgeeiQ96DE5.
CleanExiHS_C10orf104.
ExpressionAtlasiQ96DE5. baseline and differential.
GenevisibleiQ96DE5. HS.

Organism-specific databases

HPAiHPA037815.

Interactioni

Subunit structurei

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. ANAPC16 associates with the rest of the complex independently of ANAPC2 and ANAPC11.2 Publications

Protein-protein interaction databases

BioGridi125643. 35 interactions.
DIPiDIP-56449N.
IntActiQ96DE5. 25 interactions.
STRINGi9606.ENSP00000299381.

Structurei

Secondary structure

1
110
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi75 – 839Combined sources
Helixi85 – 917Combined sources
Helixi93 – 953Combined sources
Helixi99 – 1024Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RG6X-ray3.30S74-109[»]
4RG9X-ray3.25S74-109[»]
4UI9electron microscopy3.60E1-110[»]
5A31electron microscopy4.30E1-110[»]
5G04electron microscopy4.00E1-110[»]
5G05electron microscopy3.40E1-110[»]
ProteinModelPortaliQ96DE5.
SMRiQ96DE5. Positions 52-107.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 2623Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the APC16 family.Curated

Phylogenomic databases

eggNOGiENOG410IX3S. Eukaryota.
ENOG4111QQQ. LUCA.
GeneTreeiENSGT00390000018109.
HOGENOMiHOG000073535.
HOVERGENiHBG054279.
InParanoidiQ96DE5.
OMAiEADEWKY.
OrthoDBiEOG7JT6ZT.
PhylomeDBiQ96DE5.
TreeFamiTF332754.

Family and domain databases

InterProiIPR029641. APC16.
[Graphical view]
PANTHERiPTHR31564. PTHR31564. 1 hit.
ProDomiPD392219. PD392219. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96DE5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASSSSSSA GGVSGSSVTG SGFSVSDLAP PRKALFTYPK GAGEMLEDGS
60 70 80 90 100
ERFLCESVFS YQVASTLKQV KHDQQVARME KLAGLVEELE ADEWRFKPIE
110
QLLGFTPSSG
Length:110
Mass (Da):11,667
Last modified:December 1, 2001 - v1
Checksum:iF348FA92F4B89E4F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL607035 Genomic DNA. Translation: CAI15909.1.
BC009530 mRNA. Translation: AAH09530.1.
CCDSiCCDS7314.1.
RefSeqiNP_001229475.1. NM_001242546.1.
NP_001229476.1. NM_001242547.1.
NP_775744.1. NM_173473.3.
UniGeneiHs.426296.

Genome annotation databases

EnsembliENST00000299381; ENSP00000299381; ENSG00000166295.
ENST00000621663; ENSP00000477760; ENSG00000166295.
GeneIDi119504.
KEGGihsa:119504.
UCSCiuc001jsv.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL607035 Genomic DNA. Translation: CAI15909.1.
BC009530 mRNA. Translation: AAH09530.1.
CCDSiCCDS7314.1.
RefSeqiNP_001229475.1. NM_001242546.1.
NP_001229476.1. NM_001242547.1.
NP_775744.1. NM_173473.3.
UniGeneiHs.426296.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RG6X-ray3.30S74-109[»]
4RG9X-ray3.25S74-109[»]
4UI9electron microscopy3.60E1-110[»]
5A31electron microscopy4.30E1-110[»]
5G04electron microscopy4.00E1-110[»]
5G05electron microscopy3.40E1-110[»]
ProteinModelPortaliQ96DE5.
SMRiQ96DE5. Positions 52-107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125643. 35 interactions.
DIPiDIP-56449N.
IntActiQ96DE5. 25 interactions.
STRINGi9606.ENSP00000299381.

PTM databases

iPTMnetiQ96DE5.
PhosphoSiteiQ96DE5.

Polymorphism and mutation databases

BioMutaiANAPC16.

Proteomic databases

EPDiQ96DE5.
MaxQBiQ96DE5.
PaxDbiQ96DE5.
PeptideAtlasiQ96DE5.
PRIDEiQ96DE5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000299381; ENSP00000299381; ENSG00000166295.
ENST00000621663; ENSP00000477760; ENSG00000166295.
GeneIDi119504.
KEGGihsa:119504.
UCSCiuc001jsv.4. human.

Organism-specific databases

CTDi119504.
GeneCardsiANAPC16.
HGNCiHGNC:26976. ANAPC16.
HPAiHPA037815.
MIMi613427. gene.
neXtProtiNX_Q96DE5.
PharmGKBiPA165548225.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IX3S. Eukaryota.
ENOG4111QQQ. LUCA.
GeneTreeiENSGT00390000018109.
HOGENOMiHOG000073535.
HOVERGENiHBG054279.
InParanoidiQ96DE5.
OMAiEADEWKY.
OrthoDBiEOG7JT6ZT.
PhylomeDBiQ96DE5.
TreeFamiTF332754.

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).

Miscellaneous databases

ChiTaRSiANAPC16. human.
GenomeRNAii119504.
PROiQ96DE5.
SOURCEiSearch...

Gene expression databases

BgeeiQ96DE5.
CleanExiHS_C10orf104.
ExpressionAtlasiQ96DE5. baseline and differential.
GenevisibleiQ96DE5. HS.

Family and domain databases

InterProiIPR029641. APC16.
[Graphical view]
PANTHERiPTHR31564. PTHR31564. 1 hit.
ProDomiPD392219. PD392219. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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].
    Tissue: Lung.
  3. "The protein composition of mitotic chromosomes determined using multiclassifier combinatorial proteomics."
    Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L., Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T., Earnshaw W.C., Rappsilber J.
    Cell 142:810-821(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  4. Cited for: FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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 nameiAPC16_HUMAN
AccessioniPrimary (citable) accession number: Q96DE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 104 of the entry and version 1 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 10
    Human chromosome 10: 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
  6. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

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.