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Q9UM13 (APC10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Anaphase-promoting complex subunit 10

Short name=APC10
Alternative name(s):
Cyclosome subunit 10
Gene names
Name:ANAPC10
Synonyms:APC10
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Pathway

Protein modification; protein ubiquitination.

Subunit structure

The APC/C is composed of at least 12 subunits. The C-terminus of APC10 binds to CDC27/APC3.

Sequence similarities

Belongs to the APC10 family.

Contains 1 DOC domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 185185Anaphase-promoting complex subunit 10
PRO_0000174011

Regions

Domain1 – 185185DOC

Amino acid modifications

Modified residue1691N6-acetyllysine Ref.8

Natural variations

Natural variant461R → Q. Ref.4
Corresponds to variant rs35257136 [ dbSNP | Ensembl ].
VAR_025200

Experimental info

Sequence conflict61K → R in AAD30527. Ref.1
Sequence conflict1341T → S in CAB45705. Ref.3
Sequence conflict1461Q → L in CAB45705. Ref.3

Secondary structure

.......................... 185
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UM13 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: ACA7F245B3861FF5

FASTA18521,252
        10         20         30         40         50         60 
MTTPNKTPPG ADPKQLERTG TVREIGSQAV WSLSSCKPGF GVDQLRDDNL ETYWQSDGSQ 

        70         80         90        100        110        120 
PHLVNIQFRR KTTVKTLCIY ADYKSDESYT PSKISVRVGN NFHNLQEIRQ LELVEPSGWI 

       130        140        150        160        170        180 
HVPLTDNHKK PTRTFMIQIA VLANHQNGRD THMRQIKIYT PVEESSIGKF PRCTTIDFMM 


YRSIR 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the DOC1/APC10 subunit of the yeast and the human anaphase-promoting complex."
Grossberger R., Gieffers C., Zachariae W., Podtelejnikov A.V., Schleiffer A., Nasmyth K., Mann M., Peters J.-M.
J. Biol. Chem. 274:14500-14507(1999) [PubMed: 10318877] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Identification of human APC10/Doc1 as a subunit of anaphase promoting complex."
Kurasawa Y., Todokoro K.
Oncogene 18:5131-5137(1999) [PubMed: 10498862] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]NIEHS SNPs program
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-46.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Brain.
[7]"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: 18485873] [Abstract]
Cited for: FUNCTION OF THE APC/C.
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-169, MASS SPECTROMETRY.
[9]"Crystal structure of the APC10/DOC1 subunit of the human anaphase-promoting complex."
Wendt K.S., Vodermaier H.C., Jacob U., Gieffers C., Gmachl M., Peters J.-M., Huber R., Sondermann P.
Nat. Struct. Biol. 8:784-788(2001) [PubMed: 11524682] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[10]"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.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF132794 mRNA. Translation: AAD30527.1.
AB012109 mRNA. Translation: BAA86953.1.
AL080090 mRNA. Translation: CAB45705.1.
DQ304649 Genomic DNA. Translation: ABB96248.1.
CH471056 Genomic DNA. Translation: EAX05050.1.
CH471056 Genomic DNA. Translation: EAX05051.1.
BC005217 mRNA. Translation: AAH05217.1.
IPIIPI00007088.
PIRT12476.
RefSeqNP_055700.2. NM_014885.3.
UniGeneHs.480876.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JHJX-ray1.60A3-172[»]
ProteinModelPortalQ9UM13.
SMRQ9UM13. Positions 3-162.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-39885N.
IntActQ9UM13. 12 interactions.
STRINGQ9UM13.

PTM databases

PhosphoSiteQ9UM13.

Polymorphism databases

DMDM34395509.

Proteomic databases

PRIDEQ9UM13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309439; ENSP00000310071; ENSG00000164162.
ENST00000451299; ENSP00000403891; ENSG00000164162.
GeneID10393.
KEGGhsa:10393.
UCSCuc003iju.2. human.

Organism-specific databases

CTD10393.
GeneCardsGC04M145916.
H-InvDBHIX0004537.
HIX0037099.
HGNCHGNC:24077. ANAPC10.
MIM613745. gene.
neXtProtNX_Q9UM13.
PharmGKBPA134938672.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG06692.
GeneTreeENSGT00390000013722.
HOGENOMHBG435437.
HOVERGENHBG050528.
InParanoidQ9UM13.
OMASNHQNGR.
OrthoDBEOG4CVG7X.
PhylomeDBQ9UM13.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.

Gene expression databases

ArrayExpressQ9UM13.
BgeeQ9UM13.
CleanExHS_ANAPC10.
GenevestigatorQ9UM13.
GermOnlineENSG00000164162. Homo sapiens.

Family and domain databases

InterProIPR016901. APC_su10.
IPR004939. APC_su10/DOC_dom.
IPR008979. Galactose-bd-like.
[Graphical view]
KOK03357.
PfamPF03256. APC10. 1 hit.
[Graphical view]
PIRSFPIRSF028841. APC10_sub. 1 hit.
SUPFAMSSF49785. Gal_bind_like. 1 hit.
PROSITEPS51284. DOC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio39374.
SOURCESearch...

Entry information

Entry nameAPC10_HUMAN
AccessionPrimary (citable) accession number: Q9UM13
Secondary accession number(s): D3DNZ7 expand/collapse secondary AC list , Q2V500, Q9UG51, Q9Y5R0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families