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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi23 – 231Zinc 1By similarity
Metal bindingi26 – 261Zinc 1By similarity
Metal bindingi34 – 341Zinc 3By similarity
Metal bindingi37 – 371Zinc 3By similarity
Metal bindingi44 – 441Zinc 3By similarity
Metal bindingi51 – 511Zinc 2By similarity
Metal bindingi53 – 531Zinc 2By similarity
Metal bindingi56 – 561Zinc 1By similarity
Metal bindingi58 – 581Zinc 3By similarity
Metal bindingi59 – 591Zinc 1By similarity
Metal bindingi73 – 731Zinc 2By similarity
Metal bindingi76 – 761Zinc 2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri34 – 7744RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • cullin family protein binding Source: MGI
  • ubiquitin protein ligase activity Source: MGI
  • ubiquitin-ubiquitin ligase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_150471. Separation of Sister Chromatids.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_6904. Phosphorylation of the APC/C.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
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
ProteomesiUP000005640 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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231C → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication
Mutagenesisi26 – 261C → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication
Mutagenesisi34 – 341C → S: Slightly reduces autoubiquitination activity; in isoform 1. 1 Publication
Mutagenesisi37 – 371C → S: Slightly reduces autoubiquitination activity; in isoform 1. 1 Publication
Mutagenesisi44 – 441C → S: Slightly reduces autoubiquitination activity; in isoform 1. 1 Publication
Mutagenesisi51 – 511C → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication
Mutagenesisi53 – 531H → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication
Mutagenesisi56 – 561H → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication
Mutagenesisi58 – 581H → S: Slightly reduces autoubiquitination activity; in isoform 1. 1 Publication
Mutagenesisi59 – 591C → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication
Mutagenesisi73 – 731C → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication
Mutagenesisi76 – 761C → S: Greatly reduces autoubiquitination activity; in isoform 1. 1 Publication

Organism-specific databases

PharmGKBiPA24787.

Polymorphism and mutation databases

BioMutaiANAPC11.
DMDMi19924286.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8484Anaphase-promoting complex subunit 11PRO_0000055747Add
BLAST

Post-translational modificationi

Auto-ubiquitinated.

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ9NYG5.
PaxDbiQ9NYG5.
PRIDEiQ9NYG5.

PTM databases

PhosphoSiteiQ9NYG5.

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

BgeeiQ9NYG5.
CleanExiHS_ANAPC11.
ExpressionAtlasiQ9NYG5. baseline.
GenevestigatoriQ9NYG5.

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

Protein-protein interaction databases

BioGridi119591. 33 interactions.
DIPiDIP-52741N.
IntActiQ9NYG5. 12 interactions.
STRINGi9606.ENSP00000349957.

Structurei

Secondary structure

1
84
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni24 – 263Combined sources
Helixi35 – 373Combined sources
Turni38 – 414Combined sources
Beta strandi46 – 494Combined sources
Beta strandi50 – 523Combined sources
Beta strandi54 – 563Combined sources
Helixi57 – 6711Combined sources
Beta strandi76 – 794Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MT5NMR-A17-84[»]
4R2YX-ray1.76A/B/C/D17-84[»]
ProteinModelPortaliQ9NYG5.
SMRiQ9NYG5. Positions 17-84.
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
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri34 – 7744RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG316465.
GeneTreeiENSGT00550000075186.
HOGENOMiHOG000171951.
HOVERGENiHBG097038.
InParanoidiQ9NYG5.
KOiK03358.
OMAiCCPDCPL.
OrthoDBiEOG7ZKSDB.
PhylomeDBiQ9NYG5.
TreeFamiTF354219.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR024991. Apc11.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF12861. zf-Apc11. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei38 – 8447KVPGD…WKFKE → PLHGESISRCLGWCPQPVPV LGGRAHPQVPINTASPTPGQ HTGSLMSREESSRSPDPTPP ALDQETSSLLRCTSPWCLDH SCDLFGITDQVSADGPRACR QGARRRLPAGVGPVLPLLPH ALHPQVAARTAGAAALPHVP PGMEVQGVRPDLALAGGAS in isoform 2. 1 PublicationVSP_012347Add
BLAST

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.1. human. [Q9NYG5-1]
uc002kby.1. human. [Q9NYG5-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MT5NMR-A17-84[»]
4R2YX-ray1.76A/B/C/D17-84[»]
ProteinModelPortaliQ9NYG5.
SMRiQ9NYG5. Positions 17-84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119591. 33 interactions.
DIPiDIP-52741N.
IntActiQ9NYG5. 12 interactions.
STRINGi9606.ENSP00000349957.

PTM databases

PhosphoSiteiQ9NYG5.

Polymorphism and mutation databases

BioMutaiANAPC11.
DMDMi19924286.

Proteomic databases

MaxQBiQ9NYG5.
PaxDbiQ9NYG5.
PRIDEiQ9NYG5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.1. human. [Q9NYG5-1]
uc002kby.1. human. [Q9NYG5-2]

Organism-specific databases

CTDi51529.
GeneCardsiGC17P079849.
HGNCiHGNC:14452. ANAPC11.
HPAiHPA021989.
HPA027838.
MIMi614534. gene.
neXtProtiNX_Q9NYG5.
PharmGKBiPA24787.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG316465.
GeneTreeiENSGT00550000075186.
HOGENOMiHOG000171951.
HOVERGENiHBG097038.
InParanoidiQ9NYG5.
KOiK03358.
OMAiCCPDCPL.
OrthoDBiEOG7ZKSDB.
PhylomeDBiQ9NYG5.
TreeFamiTF354219.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_150471. Separation of Sister Chromatids.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_6904. Phosphorylation of the APC/C.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.

Miscellaneous databases

GeneWikiiANAPC11.
GenomeRNAii51529.
NextBioi55250.
PROiQ9NYG5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NYG5.
CleanExiHS_ANAPC11.
ExpressionAtlasiQ9NYG5. baseline.
GenevestigatoriQ9NYG5.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR024991. Apc11.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF12861. zf-Apc11. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.
  10. "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 nameiAPC11_HUMAN
AccessioniPrimary (citable) accession number: Q9NYG5
Secondary accession number(s): A8MTT2
, B7ZW64, Q502X9, Q9BW64, Q9P0R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: October 1, 2000
Last modified: May 27, 2015
This is version 139 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 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

External Data

Dasty 3

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 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.