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Q9NYG5 (APC11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Anaphase-promoting complex subunit 11

Short name=APC11
Alternative name(s):
Cyclosome subunit 11
Hepatocellular carcinoma-associated RING finger protein
Gene names
Name:ANAPC11
ORF Names:HSPC214
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length84 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. May recruit the E2 ubiquitin-conjugating enzymes to the complex. Ref.7 Ref.8

Pathway

Protein modification; protein ubiquitination.

Subunit structure

The APC/C is composed of at least 12 subunits. Interacts with the cullin domain of ANAPC2. Interacts with UBE2D2. Ref.6 Ref.7

Subcellular location

Cytoplasm. Nucleus Ref.1.

Tissue specificity

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. Ref.1

Domain

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

Post-translational modification

Auto-ubiquitinated.

Sequence similarities

Belongs to the RING-box family.

Contains 1 RING-type zinc finger.

Sequence caution

The sequence AAF36134.1 differs from that shown. Reason: Frameshift at position 67.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandMetal-binding
Zinc
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

mitosis

Traceable author statement Ref.7. Source: UniProtKB

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.8. Source: UniProtKB

protein ubiquitination

Inferred from direct assay Ref.7. Source: UniProtKB

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.7Ref.9PubMed 21926987. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionubiquitin-protein ligase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NYG5-1)

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: Q9NYG5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     38-84: KVPGDDCPLV...MCRQEWKFKE → PLHGESISRC...PDLALAGGAS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8484Anaphase-promoting complex subunit 11
PRO_0000055747

Regions

Zinc finger34 – 7744RING-type

Sites

Metal binding231Zinc 1 By similarity
Metal binding261Zinc 1 By similarity
Metal binding341Zinc 3 By similarity
Metal binding371Zinc 3 By similarity
Metal binding441Zinc 3 By similarity
Metal binding511Zinc 2 By similarity
Metal binding531Zinc 2 By similarity
Metal binding561Zinc 1 By similarity
Metal binding581Zinc 3 By similarity
Metal binding591Zinc 1 By similarity
Metal binding731Zinc 2 By similarity
Metal binding761Zinc 2 By similarity

Natural variations

Alternative sequence38 – 8447KVPGD…WKFKE → PLHGESISRCLGWCPQPVPV LGGRAHPQVPINTASPTPGQ HTGSLMSREESSRSPDPTPP ALDQETSSLLRCTSPWCLDH SCDLFGITDQVSADGPRACR QGARRRLPAGVGPVLPLLPH ALHPQVAARTAGAAALPHVP PGMEVQGVRPDLALAGGAS in isoform 2.
VSP_012347

Experimental info

Mutagenesis231C → S: Greatly reduces autoubiquitination activity; in isoform 1.
Mutagenesis261C → S: Greatly reduces autoubiquitination activity; in isoform 1.
Mutagenesis341C → S: Slightly reduces autoubiquitination activity; in isoform 1.
Mutagenesis371C → S: Slightly reduces autoubiquitination activity; in isoform 1.
Mutagenesis441C → S: Slightly reduces autoubiquitination activity; in isoform 1.
Mutagenesis511C → S: Greatly reduces autoubiquitination activity; in isoform 1.
Mutagenesis531H → S: Greatly reduces autoubiquitination activity; in isoform 1.
Mutagenesis561H → S: Greatly reduces autoubiquitination activity; in isoform 1.
Mutagenesis581H → S: Slightly reduces autoubiquitination activity; in isoform 1.
Mutagenesis591C → S: Greatly reduces autoubiquitination activity; in isoform 1.
Mutagenesis731C → S: Greatly reduces autoubiquitination activity; in isoform 1.
Mutagenesis761C → S: Greatly reduces autoubiquitination activity; in isoform 1.

Sequences

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

Last modified October 1, 2000. Version 1.
Checksum: EACBD5A54FDC11AE

FASTA849,841
        10         20         30         40         50         60 
MKVKIKCWNG VATWLWVAND ENCGICRMAF NGCCPDCKVP GDDCPLVWGQ CSHCFHMHCI 

        70         80 
LKWLHAQQVQ QHCPMCRQEW KFKE 

« Hide

Isoform 2 [UniParc].

Checksum: E28CB66699B5B937
Show »

FASTA19620,644

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a RING-H2 finger protein, ANAPC11, the human homolog of yeast Apc11p."
Chan A.H., Lee S.M.Y., Chim S.S., Kok L.D., Waye M.M.Y., Lee C.Y., Fung K.P., Tsui S.K.W.
J. Cell. Biochem. 83:249-258(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]"Novel human APC11 anaphase-promoting complex subunit."
Li N., Wan T., Zhang W., Cao X.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Umbilical cord blood.
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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 2).
Tissue: Brain, Skin and Testis.
[6]"The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex."
Gmachl M., Gieffers C., Podtelejnikov A.V., Mann M., Peters J.-M.
Proc. Natl. Acad. Sci. U.S.A. 97:8973-8978(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN APC/C COMPLEX.
[7]"APC2 cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex."
Tang Z., Li B., Bharadwaj R., Zhu H., Oezkan E., Hakala K., Deisenhofer J., Yu H.
Mol. Biol. Cell 12:3839-3851(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS, INTERACTION WITH ANAPC2 AND UBE2D2.
[8]"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.
[9]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001002244.1. NM_001002244.2.
NP_001002245.1. NM_001002245.2.
NP_001002246.1. NM_001002246.2.
NP_001002247.1. NM_001002247.2.
NP_001002248.1. NM_001002248.2.
NP_001002249.1. NM_001002249.2.
NP_057560.8. NM_016476.11.
UniGeneHs.534456.

3D structure databases

ProteinModelPortalQ9NYG5.
SMRQ9NYG5. Positions 5-84.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119591. 36 interactions.
IntActQ9NYG5. 11 interactions.
STRING9606.ENSP00000349957.

PTM databases

PhosphoSiteQ9NYG5.

Polymorphism databases

DMDM19924286.

Proteomic databases

PaxDbQ9NYG5.
PRIDEQ9NYG5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344877; 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]
GeneID51529.
KEGGhsa:51529.
UCSCuc002kbv.1. human. [Q9NYG5-1]
uc002kby.1. human. [Q9NYG5-2]

Organism-specific databases

CTD51529.
GeneCardsGC17P079849.
HGNCHGNC:14452. ANAPC11.
HPAHPA021989.
HPA027838.
MIM614534. gene.
neXtProtNX_Q9NYG5.
PharmGKBPA24787.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG316465.
HOGENOMHOG000171951.
HOVERGENHBG097038.
KOK03358.
OMACCPDCPL.
OrthoDBEOG7ZKSDB.
PhylomeDBQ9NYG5.
TreeFamTF354219.

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

BgeeQ9NYG5.
CleanExHS_ANAPC11.
GenevestigatorQ9NYG5.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR024991. Apc11.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF12861. zf-Apc11. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiANAPC11.
GenomeRNAi51529.
NextBio55250.
PROQ9NYG5.
SOURCESearch...

Entry information

Entry nameAPC11_HUMAN
AccessionPrimary (citable) accession number: Q9NYG5
Secondary accession number(s): A8MTT2 expand/collapse secondary AC list , B7ZW64, Q502X9, Q9BW64, Q9P0R2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 126 of the entry and version 1 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

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 17

Human chromosome 17: entries, gene names and cross-references to MIM