Q9UJX3 (APC7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Anaphase-promoting complex subunit 7
Short name=APC7

Alternative name(s):
Cyclosome subunit 7

Gene names

Name:	ANAPC7
Synonyms:	APC7

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	599 AA.
Sequence status	Complete.
Protein existence	Evidence 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.4
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Homodimer. The APC/C is composed of at least 12 subunits. Ref.1 Ref.7
Sequence similarities	Belongs to the APC7 family. Contains 7 TPR repeats.
Caution	It is uncertain whether Met-1 or Met-35 is the initiator.
Sequence caution	The sequence AAH17316.2 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Coding sequence diversity	Alternative splicing
Domain	Repeat TPR repeat
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic cell cycle spindle assembly checkpoint Traceable author statement. Source: Reactome negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome protein K11-linked ubiquitination Inferred from direct assay Ref.4. Source: UniProtKB
Cellular component	anaphase-promoting complex Inferred from direct assay Ref.6. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular function	protein phosphatase binding Inferred from physical interaction. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UJX3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UJX3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     537-599: SLDPNDQKSLEGMQKMEKEESPTDATQEEDVDDMEGSGEEGDLEGSDSEAAQWADQEQWFGMQ → R

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 599

599

Anaphase-promoting complex subunit 7

PRO_0000106261

Regions

Repeat

77 – 110

34

TPR 1

Repeat

169 – 202

34

TPR 2

Repeat

271 – 304

34

TPR 3

Repeat

373 – 406

34

TPR 4

Repeat

441 – 475

35

TPR 5

Repeat

476 – 508

33

TPR 6

Repeat

509 – 542

34

TPR 7

Natural variations

Alternative sequence

537 – 599

63

SLDPN…WFGMQ → R in isoform 2.

VSP_039043

Experimental info

Mutagenesis

56

1

L → R: Loss of homodimerization; when associated with K-60. Ref.7

Mutagenesis

60

1

L → K: Loss of homodimerization; when associated with R-56. Ref.7

Sequence conflict

184

1

Q → R in AAF05754. Ref.1

Sequence conflict

302

1

P → L in AAF05754. Ref.1

Sequence conflict

537

1

S → R in CAB70828. Ref.3

Secondary structure

1

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599

Helix Strand Turn

Details...

Helix

37 – 46

10

Helix

50 – 66

17

Helix

73 – 89

17

Helix

93 – 108

16

Helix

135 – 148

14

Helix

152 – 159

8

Helix

164 – 166

3

Helix

169 – 178

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 20, 2010. Version 4. Checksum: D187A1D9DA41DE2C	FASTA	599	66,855
	10 20 30 40 50 60 MDPGDAAILE SSLRILYRLF ESVLPPLPAA LQSRMNVIDH VRDMAAAGLH SNVRLLSSLL 70 80 90 100 110 120 LTMSNNNPEL FSPPQKYQLL VYHADSLFHD KEYRNAVSKY TMALQQKKAL SKTSKVRPST 130 140 150 160 170 180 GNSASTPQSQ CLPSEIEVKY KMAECYTMLK QDKDAIAILD GIPSRQRTPK INMMLANLYK 190 200 210 220 230 240 KAGQERPSVT SYKEVLRQCP LALDAILGLL SLSVKGAEVA SMTMNVIQTV PNLDWLSVWI 250 260 270 280 290 300 KAYAFVHTGD NSRAISTICS LEKKSLLRDN VDLLGSLADL YFRAGDNKNS VLKFEQAQML 310 320 330 340 350 360 DPYLIKGMDV YGYLLAREGR LEDVENLGCR LFNISDQHAE PWVVSGCHSF YSKRYSRALY 370 380 390 400 410 420 LGAKAIQLNS NSVQALLLKG AALRNMGRVQ EAIIHFREAI RLAPCRLDCY EGLIECYLAS 430 440 450 460 470 480 NSIREAMVMA NNVYKTLGAN AQTLTLLATV CLEDPVTQEK AKTLLDKALT QRPDYIKAVV 490 500 510 520 530 540 KKAELLSREQ KYEDGIALLR NALANQSDCV LHRILGDFLV AVNEYQEAMD QYSIALSLDP 550 560 570 580 590 NDQKSLEGMQ KMEKEESPTD ATQEEDVDDM EGSGEEGDLE GSDSEAAQWA DQEQWFGMQ
	Isoform 2 [UniParc]. Checksum: 2F7914F35CCFC4A5	FASTA	537	60,002
	10 20 30 40 50 60 MDPGDAAILE SSLRILYRLF ESVLPPLPAA LQSRMNVIDH VRDMAAAGLH SNVRLLSSLL 70 80 90 100 110 120 LTMSNNNPEL FSPPQKYQLL VYHADSLFHD KEYRNAVSKY TMALQQKKAL SKTSKVRPST 130 140 150 160 170 180 GNSASTPQSQ CLPSEIEVKY KMAECYTMLK QDKDAIAILD GIPSRQRTPK INMMLANLYK 190 200 210 220 230 240 KAGQERPSVT SYKEVLRQCP LALDAILGLL SLSVKGAEVA SMTMNVIQTV PNLDWLSVWI 250 260 270 280 290 300 KAYAFVHTGD NSRAISTICS LEKKSLLRDN VDLLGSLADL YFRAGDNKNS VLKFEQAQML 310 320 330 340 350 360 DPYLIKGMDV YGYLLAREGR LEDVENLGCR LFNISDQHAE PWVVSGCHSF YSKRYSRALY 370 380 390 400 410 420 LGAKAIQLNS NSVQALLLKG AALRNMGRVQ EAIIHFREAI RLAPCRLDCY EGLIECYLAS 430 440 450 460 470 480 NSIREAMVMA NNVYKTLGAN AQTLTLLATV CLEDPVTQEK AKTLLDKALT QRPDYIKAVV 490 500 510 520 530 KKAELLSREQ KYEDGIALLR NALANQSDCV LHRILGDFLV AVNEYQEAMD QYSIALR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a cullin homology region in a subunit of the anaphase-promoting complex." Yu H., Peters J.-M., King R.W., Page A.M., Hieter P., Kirschner M.W. Science 279:1219-1222(1998) [PubMed: 9469815] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 34-599 (ISOFORM 1), SUBUNIT.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-599 (ISOFORM 1). Tissue: Ovary and Skin.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 316-599 (ISOFORM 2). Tissue: Testis.
[4]	"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.
[5]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]	"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.
[7]	"Crystal structure of the N-terminal domain of anaphase-promoting complex subunit 7." Han D., Kim K., Kim Y., Kang Y., Lee J.Y., Kim Y. J. Biol. Chem. 284:15137-15146(2009) [PubMed: 19091741] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 35-181, HOMODIMERIZATION, MUTAGENESIS OF LEU-56 AND LEU-60.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF191340 mRNA. Translation: AAF05754.1.
BC002941 mRNA. Translation: AAH02941.2.
BC009498 mRNA. Translation: AAH09498.2.
BC017316 mRNA. Translation: AAH17316.2. Sequence problems.
AL137586 mRNA. Translation: CAB70828.1.

IPI

IPI00008248.
IPI00915282.

PIR

T46297.

RefSeq

NP_001131136.1. NM_001137664.1.
NP_057322.2. NM_016238.2.

UniGene

Hs.719935.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FFL	X-ray	2.50	A/B/C/D	35-181	[»]

ProteinModelPortal

Q9UJX3.

SMR

Q9UJX3. Positions 35-180, 244-558.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39765N.

IntAct

Q9UJX3. 20 interactions.

STRING

Q9UJX3.

PTM databases

PhosphoSite

Q9UJX3.

Polymorphism databases

DMDM

294862527.

Proteomic databases

PeptideAtlas

Q9UJX3.

PRIDE

Q9UJX3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000354390; ENSP00000346363; ENSG00000196510.
ENST00000455511; ENSP00000394394; ENSG00000196510.

GeneID

51434.

KEGG

hsa:51434.

NMPDR

fig|9606.3.peg.8242.

Organism-specific databases

CTD

51434.

GeneCards

GC12M110810.

H-InvDB

HIX0019976.

HGNC

HGNC:17380. ANAPC7.

HPA

CAB009567.

MIM

606949. gene.

neXtProt

NX_Q9UJX3.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000005482.

HOGENOM

HBG505401.

HOVERGEN

HBG050529.

InParanoid

Q9UJX3.

OMA

QSIPNLD.

OrthoDB

EOG4FR0RB.

PhylomeDB

Q9UJX3.

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_6900. Immune System.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.

Gene expression databases

ArrayExpress

Q9UJX3.

Bgee

Q9UJX3.

CleanEx

HS_ANAPC7.

Genevestigator

Q9UJX3.

GermOnline

ENSG00000196510. Homo sapiens.

Family and domain databases

InterPro

IPR013026. TPR-contain.
IPR011990. TPR-like_helical.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]

Gene3D

G3DSA:1.25.40.10. TPR-like_helical. 3 hits.

KO

K03354.

Pfam

PF07719. TPR_2. 1 hit.
[Graphical view]

SMART

SM00028. TPR. 4 hits.
[Graphical view]

PROSITE

PS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

55005.

SOURCE

Search...

Entry information

Entry name

APC7_HUMAN

Accession

Primary (citable) accession number: Q9UJX3
Secondary accession number(s): Q96AC4 , Q96GF4, Q9BU24, Q9NT16

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	April 20, 2010
Last modified:	January 25, 2012
This is version 108 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.