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Protein

Anaphase-promoting complex subunit 11

Gene

ANAPC11

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

Functioni

Together with the cullin protein ANAPC2, constitutes the catalytic 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. May recruit the E2 ubiquitin-conjugating enzymes to the complex.2 Publications

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi23Zinc 1By similarity1
Metal bindingi26Zinc 1By similarity1
Metal bindingi34Zinc 3By similarity1
Metal bindingi37Zinc 3By similarity1
Metal bindingi44Zinc 3By similarity1
Metal bindingi51Zinc 2By similarity1
Metal bindingi53Zinc 2By similarity1
Metal bindingi56Zinc 1By similarity1
Metal bindingi58Zinc 3By similarity1
Metal bindingi59Zinc 1By similarity1
Metal bindingi73Zinc 2By similarity1
Metal bindingi76Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri34 – 77RING-typePROSITE-ProRule annotationAdd BLAST44

GO - Molecular functioni

  • cullin family protein binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: MGI
  • ubiquitin-ubiquitin ligase activity Source: MGI

GO - Biological processi

Keywordsi

Biological processCell cycle, Cell division, Mitosis, Ubl conjugation pathway
LigandMetal-binding, Zinc

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.
SIGNORiQ9NYG5.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit 11
Short name:
APC11
Alternative name(s):
Cyclosome subunit 11
Hepatocellular carcinoma-associated RING finger protein
Gene namesi
Name:ANAPC11
ORF Names:HSPC214
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:14452. ANAPC11.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: UniProtKB
  • cytosol Source: Reactome
  • nucleolus Source: HPA
  • nucleoplasm Source: HPA

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23C → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication1
Mutagenesisi26C → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication1
Mutagenesisi34C → S: Slightly reduces autoubiquitination activity; in isoform 1. 1 Publication1
Mutagenesisi37C → S: Slightly reduces autoubiquitination activity; in isoform 1. 1 Publication1
Mutagenesisi44C → S: Slightly reduces autoubiquitination activity; in isoform 1. 1 Publication1
Mutagenesisi51C → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication1
Mutagenesisi53H → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication1
Mutagenesisi56H → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication1
Mutagenesisi58H → S: Slightly reduces autoubiquitination activity; in isoform 1. 1 Publication1
Mutagenesisi59C → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication1
Mutagenesisi73C → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication1
Mutagenesisi76C → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication1

Organism-specific databases

DisGeNETi51529.
OpenTargetsiENSG00000141552.
PharmGKBiPA24787.

Polymorphism and mutation databases

BioMutaiANAPC11.
DMDMi19924286.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000557471 – 84Anaphase-promoting complex subunit 11Add BLAST84

Post-translational modificationi

Auto-ubiquitinated.

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ9NYG5.
MaxQBiQ9NYG5.
PeptideAtlasiQ9NYG5.
PRIDEiQ9NYG5.

PTM databases

iPTMnetiQ9NYG5.
PhosphoSitePlusiQ9NYG5.

Expressioni

Tissue specificityi

Expressed at high levels in skeletal muscle and heart; in moderate levels in brain, kidney, and liver; and at low levels in colon, thymus, spleen, small intestine, placenta, lung and peripheral blood leukocyte.1 Publication

Gene expression databases

BgeeiENSG00000141552.
CleanExiHS_ANAPC11.
ExpressionAtlasiQ9NYG5. baseline and differential.
GenevisibleiQ9NYG5. HS.

Organism-specific databases

HPAiHPA021989.
HPA027838.

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. Interacts with the cullin domain of ANAPC2. Interacts with UBE2D2.3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • cullin family protein binding Source: MGI

Protein-protein interaction databases

BioGridi119591. 33 interactors.
DIPiDIP-52741N.
IntActiQ9NYG5. 27 interactors.

Structurei

Secondary structure

184
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Beta strandi19 – 22Combined sources4
Turni24 – 26Combined sources3
Helixi35 – 37Combined sources3
Turni38 – 41Combined sources4
Beta strandi46 – 49Combined sources4
Beta strandi50 – 52Combined sources3
Beta strandi54 – 56Combined sources3
Helixi57 – 67Combined sources11
Beta strandi68 – 70Combined sources3
Beta strandi76 – 79Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MT5NMR-A17-84[»]
4R2YX-ray1.76A/B/C/D17-84[»]
4UI9electron microscopy3.60B1-84[»]
5A31electron microscopy4.30B1-84[»]
5G04electron microscopy4.00B1-84[»]
5G05electron microscopy3.40B1-84[»]
5JG6X-ray2.00A/D17-84[»]
5KHRelectron microscopy6.10B1-84[»]
5KHUelectron microscopy4.80B1-84[»]
5L9Telectron microscopy6.40B1-84[»]
5L9Uelectron microscopy6.40B1-84[»]
5LCWelectron microscopy4.00B1-84[»]
ProteinModelPortaliQ9NYG5.
SMRiQ9NYG5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The RING-type zinc finger domain coordinates an additional third zinc ion.

Sequence similaritiesi

Belongs to the RING-box family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri34 – 77RING-typePROSITE-ProRule annotationAdd BLAST44

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00550000075186.
HOGENOMiHOG000171951.
HOVERGENiHBG097038.
InParanoidiQ9NYG5.
KOiK03358.
OMAiCCPDCPL.
PhylomeDBiQ9NYG5.
TreeFamiTF354219.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiView protein in InterPro
IPR024991. Apc11.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
PfamiView protein in Pfam
PF12861. zf-ANAPC11. 1 hit.
PROSITEiView protein in PROSITE
PS50089. ZF_RING_2. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NYG5-1) [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
MKVKIKCWNG VATWLWVAND ENCGICRMAF NGCCPDCKVP GDDCPLVWGQ
60 70 80
CSHCFHMHCI LKWLHAQQVQ QHCPMCRQEW KFKE
Length:84
Mass (Da):9,841
Last modified:October 1, 2000 - v1
Checksum:iEACBD5A54FDC11AE
GO
Isoform 2 (identifier: Q9NYG5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     38-84: KVPGDDCPLV...MCRQEWKFKE → PLHGESISRC...PDLALAGGAS

Note: No experimental confirmation available.
Show »
Length:196
Mass (Da):20,644
Checksum:iE28CB66699B5B937
GO

Sequence cautioni

The sequence AAF36134 differs from that shown. Reason: Frameshift at position 67.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01234738 – 84KVPGD…WKFKE → PLHGESISRCLGWCPQPVPV LGGRAHPQVPINTASPTPGQ HTGSLMSREESSRSPDPTPP ALDQETSSLLRCTSPWCLDH SCDLFGITDQVSADGPRACR QGARRRLPAGVGPVLPLLPH ALHPQVAARTAGAAALPHVP PGMEVQGVRPDLALAGGAS in isoform 2. 1 PublicationAdd BLAST47

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF247565 mRNA. Translation: AAF65816.1.
AF247789 mRNA. Translation: AAL95694.1.
AF151048 mRNA. Translation: AAF36134.1. Frameshift.
AC145207 Genomic DNA. No translation available.
BC000607 mRNA. Translation: AAH00607.2.
BC066308 mRNA. Translation: AAH66308.1.
BC095454 mRNA. Translation: AAH95454.1.
BC104641 mRNA. Translation: AAI04642.1.
BC171892 mRNA. Translation: AAI71892.1.
BC171898 mRNA. Translation: AAI71898.1.
BC171899 mRNA. Translation: AAI71899.1.
BC171900 mRNA. Translation: AAI71900.1.
CCDSiCCDS11789.1. [Q9NYG5-1]
CCDS32769.1. [Q9NYG5-2]
RefSeqiNP_001002244.1. NM_001002244.2. [Q9NYG5-2]
NP_001002245.1. NM_001002245.2. [Q9NYG5-1]
NP_001002246.1. NM_001002246.2. [Q9NYG5-1]
NP_001002247.1. NM_001002247.2. [Q9NYG5-1]
NP_001002248.1. NM_001002248.2. [Q9NYG5-1]
NP_001002249.1. NM_001002249.2. [Q9NYG5-1]
NP_001276343.1. NM_001289414.1. [Q9NYG5-1]
NP_001276344.1. NM_001289415.1. [Q9NYG5-1]
NP_001276345.1. NM_001289416.1. [Q9NYG5-1]
NP_001276346.1. NM_001289417.1. [Q9NYG5-1]
NP_001276349.1. NM_001289420.1.
NP_057560.8. NM_016476.11. [Q9NYG5-1]
UniGeneiHs.534456.

Genome annotation databases

EnsembliENST00000344877; ENSP00000339695; ENSG00000141552. [Q9NYG5-1]
ENST00000357385; ENSP00000349957; ENSG00000141552. [Q9NYG5-2]
ENST00000392376; ENSP00000376181; ENSG00000141552. [Q9NYG5-1]
ENST00000571024; ENSP00000461648; ENSG00000141552. [Q9NYG5-1]
ENST00000571570; ENSP00000458143; ENSG00000141552. [Q9NYG5-1]
ENST00000571874; ENSP00000459200; ENSG00000141552. [Q9NYG5-1]
ENST00000572639; ENSP00000460678; ENSG00000141552. [Q9NYG5-1]
ENST00000572851; ENSP00000458265; ENSG00000141552. [Q9NYG5-1]
ENST00000574924; ENSP00000460064; ENSG00000141552. [Q9NYG5-1]
ENST00000575195; ENSP00000458515; ENSG00000141552. [Q9NYG5-1]
ENST00000577747; ENSP00000463567; ENSG00000141552. [Q9NYG5-1]
ENST00000578550; ENSP00000464615; ENSG00000141552. [Q9NYG5-1]
ENST00000579978; ENSP00000463640; ENSG00000141552. [Q9NYG5-1]
ENST00000583839; ENSP00000463598; ENSG00000141552. [Q9NYG5-1]
GeneIDi51529.
KEGGihsa:51529.
UCSCiuc002kbv.3. human. [Q9NYG5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiAPC11_HUMAN
AccessioniPrimary (citable) accession number: Q9NYG5
Secondary accession number(s): A8MTT2
, B7ZW64, Q502X9, Q9BW64, Q9P0R2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: October 1, 2000
Last modified: August 30, 2017
This is version 162 of the entry and version 1 of the sequence. See 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 17
    Human chromosome 17: 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