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Protein

Anaphase-promoting complex subunit 13

Gene

Anapc13

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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 (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.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit 13
Short name:
APC13
Alternative name(s):
Cyclosome subunit 13
Gene namesi
Name:Anapc13
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1916260. Anapc13.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7474Anaphase-promoting complex subunit 13PRO_0000253981Add
BLAST

Proteomic databases

PaxDbiQ8R034.
PRIDEiQ8R034.

PTM databases

PhosphoSiteiQ8R034.

Expressioni

Gene expression databases

BgeeiQ8R034.
CleanExiMM_ANAPC13.
GenevisibleiQ8R034. 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.By similarity

Protein-protein interaction databases

BioGridi213171. 28 interactions.
IntActiQ8R034. 25 interactions.
STRINGi10090.ENSMUSP00000039761.

Structurei

3D structure databases

ProteinModelPortaliQ8R034.
SMRiQ8R034. Positions 1-67.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the APC13 family.Curated

Phylogenomic databases

eggNOGiENOG410J0AV. Eukaryota.
ENOG4111UJR. LUCA.
GeneTreeiENSGT00390000008673.
HOGENOMiHOG000220858.
HOVERGENiHBG079845.
InParanoidiQ8R034.
KOiK12456.
OMAiLHENTPN.
OrthoDBiEOG7T1RDX.
PhylomeDBiQ8R034.
TreeFamiTF105448.

Family and domain databases

InterProiIPR008401. Apc13p.
[Graphical view]
PfamiPF05839. Apc13p. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R034-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSEVQRDGR ILDLIDDAWR EDKLPYEDVA IPLSELPEPE QDNGGTTESV
60 70
KEQEMKWTDL ALQGLHENVP PAGN
Length:74
Mass (Da):8,346
Last modified:June 1, 2002 - v1
Checksum:iE84F16A13821CB3B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007332 mRNA. Translation: BAC25171.1.
BC028526 mRNA. Translation: AAH28526.1.
CCDSiCCDS40744.1.
RefSeqiNP_852059.1. NM_181394.3.
XP_006511869.1. XM_006511806.2.
XP_006511870.1. XM_006511807.2.
UniGeneiMm.2000.

Genome annotation databases

EnsembliENSMUST00000038673; ENSMUSP00000039761; ENSMUSG00000035048.
ENSMUST00000186693; ENSMUSP00000139762; ENSMUSG00000035048.
ENSMUST00000188398; ENSMUSP00000140325; ENSMUSG00000035048.
ENSMUST00000190279; ENSMUSP00000140967; ENSMUSG00000035048.
GeneIDi69010.
KEGGimmu:69010.
UCSCiuc009rft.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007332 mRNA. Translation: BAC25171.1.
BC028526 mRNA. Translation: AAH28526.1.
CCDSiCCDS40744.1.
RefSeqiNP_852059.1. NM_181394.3.
XP_006511869.1. XM_006511806.2.
XP_006511870.1. XM_006511807.2.
UniGeneiMm.2000.

3D structure databases

ProteinModelPortaliQ8R034.
SMRiQ8R034. Positions 1-67.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213171. 28 interactions.
IntActiQ8R034. 25 interactions.
STRINGi10090.ENSMUSP00000039761.

PTM databases

PhosphoSiteiQ8R034.

Proteomic databases

PaxDbiQ8R034.
PRIDEiQ8R034.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038673; ENSMUSP00000039761; ENSMUSG00000035048.
ENSMUST00000186693; ENSMUSP00000139762; ENSMUSG00000035048.
ENSMUST00000188398; ENSMUSP00000140325; ENSMUSG00000035048.
ENSMUST00000190279; ENSMUSP00000140967; ENSMUSG00000035048.
GeneIDi69010.
KEGGimmu:69010.
UCSCiuc009rft.2. mouse.

Organism-specific databases

CTDi25847.
MGIiMGI:1916260. Anapc13.

Phylogenomic databases

eggNOGiENOG410J0AV. Eukaryota.
ENOG4111UJR. LUCA.
GeneTreeiENSGT00390000008673.
HOGENOMiHOG000220858.
HOVERGENiHBG079845.
InParanoidiQ8R034.
KOiK12456.
OMAiLHENTPN.
OrthoDBiEOG7T1RDX.
PhylomeDBiQ8R034.
TreeFamiTF105448.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiAnapc13. mouse.
NextBioi328395.
PROiQ8R034.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R034.
CleanExiMM_ANAPC13.
GenevisibleiQ8R034. MM.

Family and domain databases

InterProiIPR008401. Apc13p.
[Graphical view]
PfamiPF05839. Apc13p. 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: Pancreas.
  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].
    Tissue: Mammary gland.

Entry informationi

Entry nameiAPC13_MOUSE
AccessioniPrimary (citable) accession number: Q8R034
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: June 1, 2002
Last modified: April 13, 2016
This is version 96 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.