Reviewed, UniProtKB/Swiss-Prot Q9NYG5 (APC11_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	84 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase that controls progression through mitosis and the G1 phase of the cell cycle. May recruit the E2 ubiquitin-conjugating enzymes to the complex. Ref.6
Pathway	Protein modification; protein ubiquitination.
Subunit structure	The APC/C is composed of at least 11 subunits. Interacts with the cullin domain of ANAPC2. Interacts with UBE2D2. Ref.6
Subcellular location	Cytoplasm. Nucleus.
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 process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Ref.6 Traceable author statement. Source: UniProtKB negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome protein ubiquitination Ref.6 Inferred from direct assay. Source: UniProtKB
Cellular component	anaphase-promoting complex Ref.6 Inferred from direct assay. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 84	84	Anaphase-promoting complex subunit 11		PRO_0000055747
Regions
	Zinc finger	34 – 77	44	RING-type
Sites
	Metal binding	23	1	Zinc 1 By similarity
	Metal binding	26	1	Zinc 1 By similarity
	Metal binding	34	1	Zinc 3 By similarity
	Metal binding	37	1	Zinc 3 By similarity
	Metal binding	44	1	Zinc 3 By similarity
	Metal binding	51	1	Zinc 2 By similarity
	Metal binding	53	1	Zinc 2 By similarity
	Metal binding	56	1	Zinc 1 By similarity
	Metal binding	58	1	Zinc 3 By similarity
	Metal binding	59	1	Zinc 1 By similarity
	Metal binding	73	1	Zinc 2 By similarity
	Metal binding	76	1	Zinc 2 By similarity
Natural variations
	Alternative sequence	38 – 84	47	KVPGD…WKFKE → PLHGESISRCLGWCPQPVPV LGGRAHPQVPINTASPTPGQ HTGSLMSREESSRSPDPTPP ALDQETSSLLRCTSPWCLDH SCDLFGITDQVSADGPRACR QGARRRLPAGVGPVLPLLPH ALHPQVAARTAGAAALPHVP PGMEVQGVRPDLALAGGAS in isoform 2.		VSP_012347
Experimental info
	Mutagenesis	23	1	C → S: Greatly reduces autoubiquitination activity; in isoform 1.
	Mutagenesis	26	1	C → S: Greatly reduces autoubiquitination activity; in isoform 1.
	Mutagenesis	34	1	C → S: Slightly reduces autoubiquitination activity; in isoform 1.
	Mutagenesis	37	1	C → S: Slightly reduces autoubiquitination activity; in isoform 1.
	Mutagenesis	44	1	C → S: Slightly reduces autoubiquitination activity; in isoform 1.
	Mutagenesis	51	1	C → S: Greatly reduces autoubiquitination activity; in isoform 1.
	Mutagenesis	53	1	H → S: Greatly reduces autoubiquitination activity; in isoform 1.
	Mutagenesis	56	1	H → S: Greatly reduces autoubiquitination activity; in isoform 1.
	Mutagenesis	58	1	H → S: Slightly reduces autoubiquitination activity; in isoform 1.
	Mutagenesis	59	1	C → S: Greatly reduces autoubiquitination activity; in isoform 1.
	Mutagenesis	73	1	C → S: Greatly reduces autoubiquitination activity; in isoform 1.
	Mutagenesis	76	1	C → S: Greatly reduces autoubiquitination activity; in isoform 1.

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: EACBD5A54FDC11AE	FASTA	84	9,841
	10 20 30 40 50 60 MKVKIKCWNG VATWLWVAND ENCGICRMAF NGCCPDCKVP GDDCPLVWGQ CSHCFHMHCI 70 80 LKWLHAQQVQ QHCPMCRQEW KFKE
	Isoform 2. Checksum: E28CB66699B5B937	FASTA	196	20,644
	10 20 30 40 50 60 MKVKIKCWNG VATWLWVAND ENCGICRMAF NGCCPDCPLH GESISRCLGW CPQPVPVLGG 70 80 90 100 110 120 RAHPQVPINT ASPTPGQHTG SLMSREESSR SPDPTPPALD QETSSLLRCT SPWCLDHSCD 130 140 150 160 170 180 LFGITDQVSA DGPRACRQGA RRRLPAGVGP VLPLLPHALH PQVAARTAGA AALPHVPPGM 190 EVQGVRPDLA LAGGAS

References

	« Hide 'large scale' referencesShow '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: 11573242] [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. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Umbilical cord blood.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Brain, Skin and Testis.
[5]	"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: 10922056] [Abstract] Cited for: IDENTIFICATION IN APC/C COMPLEX.
[6]	"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: 11739784] [Abstract] Cited for: FUNCTION, MUTAGENESIS, INTERACTION WITH ANAPC2 AND UBE2D2.
[7]	"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: 16364912] [Abstract] Cited for: ELECTRON MICROSCOPY OF THE APC/C.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF247565 mRNA. Translation: AAF65816.1. AF247789 mRNA. Translation: AAL95694.1. AF151048 mRNA. Translation: AAF36134.1. Frameshift. 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.
IPI	IPI00000722. IPI00787159.
RefSeq	NP_001002244.1. NP_001002245.1. NP_001002246.1. NP_001002247.1. NP_001002248.1. NP_001002249.1. NP_057560.8.
UniGene	Hs.534456
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9NYG5.
Proteomic databases
PRIDE	Q9NYG5.
Genome annotation databases
Ensembl	ENST00000344877; ENSP00000339695; ENSG00000141552; Homo sapiens. [Genome view] ENST00000392376; ENSP00000376181; ENSG00000141552; Homo sapiens. [Genome view] ENST00000392377; ENSP00000376182; ENSG00000141552; Homo sapiens. [Genome view] ENST00000400717; ENSP00000383552; ENSG00000141552; Homo sapiens. [Genome view] ENST00000429613; ENSP00000412535; ENSG00000141552; Homo sapiens. [Genome view] ENST00000443513; ENSP00000409564; ENSG00000141552; Homo sapiens. [Genome view] ENST00000448458; ENSP00000396147; ENSG00000141552; Homo sapiens. [Genome view]
GeneID	51529.
KEGG	hsa:51529.
UCSC	uc002kbv.1. human. uc002kby.1. human.
Organism-specific databases
CTD	51529.
GeneCards	GC17P077442. GC17P077443.
H-InvDB	HIX0014260.
HGNC	HGNC:14452. ANAPC11.
HPA	HPA021989.
PharmGKB	PA24787.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q9NYG5.
OMA	PHALHPQ
OrthoDB	EOG9Z6581
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_8017. APC-Cdc20 mediated degradation of Nek2A. REACT_9035. APC/C:Cdh1-mediated degradation of Skp2.
Gene expression databases
ArrayExpress	Q9NYG5.
Bgee	Q9NYG5.
CleanEx	HS_ANAPC11.
Genevestigator	Q9NYG5.
GermOnline	ENSG00000141552. Homo sapiens.
Family and domain databases
InterPro	IPR001841. Znf_RING. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APC11_HUMAN

Accession

Primary (citable) accession number: Q9NYG5
Secondary accession number(s): B7ZW64 , Q502X9, Q9BW64, Q9P0R2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	October 1, 2000
Last modified:	November 24, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.