Reviewed, UniProtKB/Swiss-Prot Q9UM13 (APC10_HUMAN)

Names and origin

Protein names

Recommended name:
    Anaphase-promoting complex subunit 10
      Short name=APC10
Alternative name(s):
    Cyclosome subunit 10

Gene names

Name:	ANAPC10
Synonyms:	APC10

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle.
Subunit structure	The APC is composed of at least 11 subunits. The C-terminus of APC10 binds to CDC27/APC3.
Sequence similarities	Belongs to the APC10 family. Contains 1 DOC domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Coding sequence diversity	Polymorphism
PTM	Acetylation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	G2/M transition of mitotic cell cycle Ref.1 Traceable author statement. Source: ProtInc anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW mitotic anaphase Ref.1 Traceable author statement. Source: ProtInc negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome regulation of mitotic metaphase/anaphase transition Inferred from electronic annotation. Source: InterPro
Cellular component	anaphase-promoting complex Ref.1 Non-traceable author statement. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	protein binding Ref.1 Non-traceable author statement. Source: UniProtKB ubiquitin-protein ligase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 185

185

Anaphase-promoting complex subunit 10

PRO_0000174011

Regions

Domain

1 – 185

185

DOC

Amino acid modifications

Modified residue

169

1

N6-acetyllysine Ref.6

Natural variations

Natural variant

46

1

R → Q: dbSNP rs35257136.

VAR_025200

Experimental info

Sequence conflict

6

1

K → R in AAD30527. Ref.1

Sequence conflict

134

1

T → S in CAB45705. Ref.3

Sequence conflict

146

1

Q → L in CAB45705. Ref.3

Secondary structure

1

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185

Helix Strand Turn

Details...

Helix

13 – 18

6

Beta strand

21 – 24

4

Helix

26 – 28

3

Beta strand

29 – 34

6

Helix

43 – 46

4

Beta strand

58 – 74

17

Beta strand

76 – 82

7

Helix

83 – 86

4

Helix

87 – 89

3

Beta strand

90 – 101

12

Beta strand

106 – 112

7

Beta strand

117 – 123

7

Beta strand

129 – 144

16

Helix

145 – 147

3

Beta strand

155 – 161

7

Sequences

	Sequence		Length	Mass (Da)
	Q9UM13-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: ACA7F245B3861FF5	FASTA	185	21,252
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[6]	"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.
[7]	"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).
[8]	"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.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF132794 mRNA. Translation: AAD30527.1.
AB012109 mRNA. Translation: BAA86953.1.
AL080090 mRNA. Translation: CAB45705.1.
DQ304649 Genomic DNA. Translation: ABB96248.1.
BC005217 mRNA. Translation: AAH05217.1.

IPI

IPI00007088.

PIR

T12476.

RefSeq

NP_055700.2.

UniGene

Hs.480876

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JHJ	X-ray	1.60	A	3-172	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9UM13.

PTM databases

PhosphoSite

Q9UM13.

Proteomic databases

PRIDE

Q9UM13.

Genome annotation databases

Ensembl

ENST00000309439; ENSP00000310071; ENSG00000164162; Homo sapiens. [Genome view]
ENST00000451299; ENSP00000403891; ENSG00000164162; Homo sapiens. [Genome view]

GeneID

10393.

KEGG

hsa:10393.

UCSC

uc003iju.2. human.

Organism-specific databases

CTD

10393.

GeneCards

GC04M146135.

H-InvDB

HIX0004537.
HIX0037099.

HGNC

HGNC:24077. ANAPC10.

PharmGKB

PA134938672.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9UM13.

HOVERGEN

Q9UM13.

OMA

SNHQNGR

OrthoDB

EOG9TQPVB

Enzyme and pathway databases

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
REACT_9035. APC/C:Cdh1-mediated degradation of Skp2.

Gene expression databases

ArrayExpress

Q9UM13.

Bgee

Q9UM13.

CleanEx

HS_ANAPC10.

Genevestigator

Q9UM13.

GermOnline

ENSG00000164162. Homo sapiens.

Family and domain databases

InterPro

IPR004939. APC10.
IPR016901. APC10_subgroup.
IPR008979. Galactose-bd-like.
[Graphical view]

PANTHER

PTHR12936. APC10. 1 hit.

Pfam

PF03256. APC10. 1 hit.
[Graphical view]

PIRSF

PIRSF028841. APC10_sub. 1 hit.

PROSITE

PS51284. DOC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

39374.

Entry information

Entry name

APC10_HUMAN

Accession

Primary (citable) accession number: Q9UM13
Secondary accession number(s): Q2V500, Q9UG51, Q9Y5R0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2003
Last sequence update:	May 1, 2000
Last modified:	November 24, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.