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Protein

Anaphase-promoting complex subunit 11

Gene

Anapc11

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

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)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

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

ReactomeiR-MMU-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-MMU-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-MMU-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-MMU-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-MMU-176412. Phosphorylation of the APC/C.
R-MMU-179409. APC-Cdc20 mediated degradation of Nek2A.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit 11
Short name:
APC11
Alternative name(s):
Cyclosome subunit 11
Gene namesi
Name:Anapc11
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1913406. Anapc11.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8484Anaphase-promoting complex subunit 11PRO_0000055748Add
BLAST

Post-translational modificationi

Auto-ubiquitinated.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ9CPX9.
MaxQBiQ9CPX9.
PaxDbiQ9CPX9.
PRIDEiQ9CPX9.

PTM databases

iPTMnetiQ9CPX9.
PhosphoSiteiQ9CPX9.

Expressioni

Gene expression databases

BgeeiQ9CPX9.
GenevisibleiQ9CPX9. MM.

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 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi211257. 3 interactions.
STRINGi10090.ENSMUSP00000026128.

Structurei

3D structure databases

ProteinModelPortaliQ9CPX9.
SMRiQ9CPX9. Positions 17-84.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

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

eggNOGiKOG1493. Eukaryota.
COG5194. LUCA.
GeneTreeiENSGT00550000075186.
HOVERGENiHBG097038.
InParanoidiQ9CPX9.
KOiK03358.
OMAiWNGVASW.
OrthoDBiEOG7ZKSDB.
PhylomeDBiQ9CPX9.
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-ANAPC11. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CPX9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVKIKCWNG VATWLWVAND ENCGICRMAF NGCCPDCKVP GDDCPLVWGQ
60 70 80
CSHCFHMHCI LKWLNAQQVQ QHCPMCRQEW KFKE
Length:84
Mass (Da):9,818
Last modified:June 1, 2001 - v1
Checksum:iEACBD5A194FC11AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003244 mRNA. Translation: BAB22663.1.
AK003612 mRNA. Translation: BAB22890.1.
AK003684 mRNA. Translation: BAB22937.1.
AK045408 mRNA. Translation: BAC32348.1.
AK136358 mRNA. Translation: BAE22944.1.
BC023039 mRNA. Translation: AAH23039.1.
CCDSiCCDS25745.1.
RefSeqiNP_001033319.1. NM_001038230.2.
NP_079665.1. NM_025389.4.
UniGeneiMm.21645.

Genome annotation databases

EnsembliENSMUST00000026128; ENSMUSP00000026128; ENSMUSG00000025135.
ENSMUST00000093140; ENSMUSP00000097714; ENSMUSG00000025135.
GeneIDi66156.
KEGGimmu:66156.
UCSCiuc007mtm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003244 mRNA. Translation: BAB22663.1.
AK003612 mRNA. Translation: BAB22890.1.
AK003684 mRNA. Translation: BAB22937.1.
AK045408 mRNA. Translation: BAC32348.1.
AK136358 mRNA. Translation: BAE22944.1.
BC023039 mRNA. Translation: AAH23039.1.
CCDSiCCDS25745.1.
RefSeqiNP_001033319.1. NM_001038230.2.
NP_079665.1. NM_025389.4.
UniGeneiMm.21645.

3D structure databases

ProteinModelPortaliQ9CPX9.
SMRiQ9CPX9. Positions 17-84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211257. 3 interactions.
STRINGi10090.ENSMUSP00000026128.

PTM databases

iPTMnetiQ9CPX9.
PhosphoSiteiQ9CPX9.

Proteomic databases

EPDiQ9CPX9.
MaxQBiQ9CPX9.
PaxDbiQ9CPX9.
PRIDEiQ9CPX9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026128; ENSMUSP00000026128; ENSMUSG00000025135.
ENSMUST00000093140; ENSMUSP00000097714; ENSMUSG00000025135.
GeneIDi66156.
KEGGimmu:66156.
UCSCiuc007mtm.2. mouse.

Organism-specific databases

CTDi51529.
MGIiMGI:1913406. Anapc11.

Phylogenomic databases

eggNOGiKOG1493. Eukaryota.
COG5194. LUCA.
GeneTreeiENSGT00550000075186.
HOVERGENiHBG097038.
InParanoidiQ9CPX9.
KOiK03358.
OMAiWNGVASW.
OrthoDBiEOG7ZKSDB.
PhylomeDBiQ9CPX9.
TreeFamiTF354219.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-MMU-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-MMU-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-MMU-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-MMU-176412. Phosphorylation of the APC/C.
R-MMU-179409. APC-Cdc20 mediated degradation of Nek2A.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

NextBioi320800.
PROiQ9CPX9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CPX9.
GenevisibleiQ9CPX9. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR024991. Apc11.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF12861. zf-ANAPC11. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina and Embryo.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiAPC11_MOUSE
AccessioniPrimary (citable) accession number: Q9CPX9
Secondary accession number(s): Q3UWH1, Q9CTG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.