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Q12157 (APC11_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Anaphase-promoting complex subunit 11

EC=6.3.2.-
Gene names
Name:APC11
Ordered Locus Names:YDL008W
ORF Names:D2900
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length165 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably catalytic subunit of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. APC11 is required to recruit the ubiquitin-conjugating enzyme E2 to the APC/C. Ref.4

Pathway

Protein modification; protein ubiquitination.

Subunit structure

The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. Ref.3

Miscellaneous

Present with 377 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 RING-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 165165Anaphase-promoting complex subunit 11
PRO_0000055751

Regions

Zinc finger52 – 9544RING-type; atypical

Experimental info

Mutagenesis101S → R in APC11-13; G2/M cell cycle arrest at 37 degrees Celsius. Ref.4
Mutagenesis411C → A: Loss of function. Ref.4
Mutagenesis441C → A: Loss of function. Ref.4
Mutagenesis811W → A: Loss of function. Ref.4
Mutagenesis911C → A: Loss of function. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q12157 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 99F8E8C6BC841934

FASTA16518,865
        10         20         30         40         50         60 
MKVKINEVHS VFAWSWHIPS TSDEDAANND PIGNDEDEDV CGICRASYNG TCPSCKFPGD 

        70         80         90        100        110        120 
QCPLVIGLCH HNFHDHCIYR WLDTPTSKGL CPMCRQTFQL QKGLAINDAH VQKFVEIVSR 

       130        140        150        160 
RREEMIEEGV AEEFVDFDEP IRQNTDNPIG RQQVDTILDE DFLLR 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Mass spectrometric analysis of the anaphase-promoting complex from yeast: identification of a subunit related to cullins."
Zachariae W., Shevchenko A., Andrews P.D., Ciosk R., Galova M., Stark M.J., Mann M., Nasmyth K.
Science 279:1216-1219(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
[4]"The APC11 RING-H2 finger mediates E2-dependent ubiquitination."
Leverson J.D., Joazeiro C.A., Page A.M., Huang H., Hieter P., Hunter T.
Mol. Biol. Cell 11:2315-2325(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-10; CYS-41; CYS-44; TRP-81 AND CYS-91.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z74056 Genomic DNA. Translation: CAA98564.1.
Z48432 Genomic DNA. Translation: CAA88351.1.
BK006938 Genomic DNA. Translation: DAA11839.1.
PIRS52511.
RefSeqNP_010276.3. NM_001180067.3.

3D structure databases

ProteinModelPortalQ12157.
SMRQ12157. Positions 5-102.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32044. 46 interactions.
DIPDIP-1130N.
IntActQ12157. 15 interactions.
MINTMINT-2785255.
STRING4932.YDL008W.

Proteomic databases

PaxDbQ12157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL008W; YDL008W; YDL008W.
GeneID851554.
KEGGsce:YDL008W.

Organism-specific databases

CYGDYDL008w.
SGDS000002166. APC11.

Phylogenomic databases

eggNOGCOG5194.
GeneTreeENSGT00550000075186.
HOGENOMHOG000171951.
KOK03358.
OMAGICRASY.
OrthoDBEOG73Z363.

Enzyme and pathway databases

BioCycYEAST:G3O-29439-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorQ12157.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR024991. Apc11.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR024766. Znf_RING_H2.
[Graphical view]
PfamPF12861. zf-Apc11. 1 hit.
PF12678. zf-rbx1. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968976.

Entry information

Entry nameAPC11_YEAST
AccessionPrimary (citable) accession number: Q12157
Secondary accession number(s): D6VRX9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways