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Protein

Anaphase-promoting complex subunit 7

Gene

ANAPC7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.1 Publication

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 - Molecular functioni

  • protein phosphatase binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiQ9UJX3.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit 7
Short name:
APC7
Alternative name(s):
Cyclosome subunit 7
Gene namesi
Name:ANAPC7
Synonyms:APC7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:17380. ANAPC7.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: UniProtKB
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • nucleus Source: BHF-UCL
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561L → R: Loss of homodimerization; when associated with K-60. 1 Publication
Mutagenesisi60 – 601L → K: Loss of homodimerization; when associated with R-56. 1 Publication

Organism-specific databases

PharmGKBiPA134901290.

Polymorphism and mutation databases

BioMutaiANAPC7.
DMDMi294862527.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 599599Anaphase-promoting complex subunit 7PRO_0000106261Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei263 – 2631N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9UJX3.
MaxQBiQ9UJX3.
PaxDbiQ9UJX3.
PeptideAtlasiQ9UJX3.
PRIDEiQ9UJX3.
TopDownProteomicsiQ9UJX3-2. [Q9UJX3-2]

PTM databases

iPTMnetiQ9UJX3.
PhosphoSiteiQ9UJX3.

Expressioni

Gene expression databases

BgeeiQ9UJX3.
CleanExiHS_ANAPC7.
ExpressionAtlasiQ9UJX3. baseline and differential.
GenevisibleiQ9UJX3. HS.

Organism-specific databases

HPAiCAB009567.
HPA043915.

Interactioni

Subunit structurei

V-shaped homodimer. 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.2 Publications

GO - Molecular functioni

  • protein phosphatase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi119538. 74 interactions.
DIPiDIP-39765N.
IntActiQ9UJX3. 32 interactions.
MINTiMINT-3081296.
STRINGi9606.ENSP00000394394.

Structurei

Secondary structure

1
599
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 4610Combined sources
Helixi50 – 6617Combined sources
Helixi73 – 8917Combined sources
Helixi93 – 10816Combined sources
Helixi135 – 14814Combined sources
Helixi152 – 1609Combined sources
Helixi164 – 1663Combined sources
Helixi169 – 17810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FFLX-ray2.50A/B/C/D35-181[»]
4UI9electron microscopy3.60X/Y35-599[»]
5A31electron microscopy4.30X/Y1-599[»]
5G04electron microscopy4.00X/Y1-599[»]
5G05electron microscopy3.40X/Y1-599[»]
ProteinModelPortaliQ9UJX3.
SMRiQ9UJX3. Positions 36-552.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UJX3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati135 – 16834TPR 1Add
BLAST
Repeati203 – 23634TPR 2Add
BLAST
Repeati237 – 27034TPR 3Add
BLAST
Repeati271 – 30434TPR 4Add
BLAST
Repeati373 – 40634TPR 5Add
BLAST
Repeati407 – 44034TPR 6Add
BLAST
Repeati441 – 47535TPR 7Add
BLAST
Repeati476 – 50833TPR 8Add
BLAST
Repeati509 – 54234TPR 9Add
BLAST
Repeati543 – 56523TPR 10Add
BLAST

Sequence similaritiesi

Belongs to the APC7 family.Curated
Contains 10 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG1174. Eukaryota.
ENOG410XS2B. LUCA.
GeneTreeiENSGT00390000005482.
HOGENOMiHOG000007393.
HOVERGENiHBG050529.
InParanoidiQ9UJX3.
KOiK03354.
OMAiSIPNLDW.
OrthoDBiEOG71VSS4.
PhylomeDBiQ9UJX3.
TreeFamiTF105445.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 5 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 4 hits.
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UJX3-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDPGDAAILE SSLRILYRLF ESVLPPLPAA LQSRMNVIDH VRDMAAAGLH
60 70 80 90 100
SNVRLLSSLL LTMSNNNPEL FSPPQKYQLL VYHADSLFHD KEYRNAVSKY
110 120 130 140 150
TMALQQKKAL SKTSKVRPST GNSASTPQSQ CLPSEIEVKY KMAECYTMLK
160 170 180 190 200
QDKDAIAILD GIPSRQRTPK INMMLANLYK KAGQERPSVT SYKEVLRQCP
210 220 230 240 250
LALDAILGLL SLSVKGAEVA SMTMNVIQTV PNLDWLSVWI KAYAFVHTGD
260 270 280 290 300
NSRAISTICS LEKKSLLRDN VDLLGSLADL YFRAGDNKNS VLKFEQAQML
310 320 330 340 350
DPYLIKGMDV YGYLLAREGR LEDVENLGCR LFNISDQHAE PWVVSGCHSF
360 370 380 390 400
YSKRYSRALY LGAKAIQLNS NSVQALLLKG AALRNMGRVQ EAIIHFREAI
410 420 430 440 450
RLAPCRLDCY EGLIECYLAS NSIREAMVMA NNVYKTLGAN AQTLTLLATV
460 470 480 490 500
CLEDPVTQEK AKTLLDKALT QRPDYIKAVV KKAELLSREQ KYEDGIALLR
510 520 530 540 550
NALANQSDCV LHRILGDFLV AVNEYQEAMD QYSIALSLDP NDQKSLEGMQ
560 570 580 590
KMEKEESPTD ATQEEDVDDM EGSGEEGDLE GSDSEAAQWA DQEQWFGMQ
Length:599
Mass (Da):66,855
Last modified:April 20, 2010 - v4
Checksum:iD187A1D9DA41DE2C
GO
Isoform 2 (identifier: Q9UJX3-2) [UniParc]FASTAAdd to basket

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

Show »
Length:537
Mass (Da):60,002
Checksum:i2F7914F35CCFC4A5
GO

Sequence cautioni

The sequence AAH17316.2 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841Q → R in AAF05754 (PubMed:9469815).Curated
Sequence conflicti302 – 3021P → L in AAF05754 (PubMed:9469815).Curated
Sequence conflicti537 – 5371S → R in CAB70828 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei537 – 59963SLDPN…WFGMQ → R in isoform 2. 1 PublicationVSP_039043Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44971.1. [Q9UJX3-2]
CCDS9145.2. [Q9UJX3-1]
PIRiT46297.
RefSeqiNP_001131136.1. NM_001137664.1. [Q9UJX3-2]
NP_057322.2. NM_016238.2. [Q9UJX3-1]
UniGeneiHs.719935.

Genome annotation databases

EnsembliENST00000450008; ENSP00000402314; ENSG00000196510. [Q9UJX3-2]
ENST00000455511; ENSP00000394394; ENSG00000196510. [Q9UJX3-1]
GeneIDi51434.
KEGGihsa:51434.
UCSCiuc001tqo.2. human. [Q9UJX3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44971.1. [Q9UJX3-2]
CCDS9145.2. [Q9UJX3-1]
PIRiT46297.
RefSeqiNP_001131136.1. NM_001137664.1. [Q9UJX3-2]
NP_057322.2. NM_016238.2. [Q9UJX3-1]
UniGeneiHs.719935.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FFLX-ray2.50A/B/C/D35-181[»]
4UI9electron microscopy3.60X/Y35-599[»]
5A31electron microscopy4.30X/Y1-599[»]
5G04electron microscopy4.00X/Y1-599[»]
5G05electron microscopy3.40X/Y1-599[»]
ProteinModelPortaliQ9UJX3.
SMRiQ9UJX3. Positions 36-552.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119538. 74 interactions.
DIPiDIP-39765N.
IntActiQ9UJX3. 32 interactions.
MINTiMINT-3081296.
STRINGi9606.ENSP00000394394.

PTM databases

iPTMnetiQ9UJX3.
PhosphoSiteiQ9UJX3.

Polymorphism and mutation databases

BioMutaiANAPC7.
DMDMi294862527.

Proteomic databases

EPDiQ9UJX3.
MaxQBiQ9UJX3.
PaxDbiQ9UJX3.
PeptideAtlasiQ9UJX3.
PRIDEiQ9UJX3.
TopDownProteomicsiQ9UJX3-2. [Q9UJX3-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000450008; ENSP00000402314; ENSG00000196510. [Q9UJX3-2]
ENST00000455511; ENSP00000394394; ENSG00000196510. [Q9UJX3-1]
GeneIDi51434.
KEGGihsa:51434.
UCSCiuc001tqo.2. human. [Q9UJX3-1]

Organism-specific databases

CTDi51434.
GeneCardsiANAPC7.
HGNCiHGNC:17380. ANAPC7.
HPAiCAB009567.
HPA043915.
MIMi606949. gene.
neXtProtiNX_Q9UJX3.
PharmGKBiPA134901290.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1174. Eukaryota.
ENOG410XS2B. LUCA.
GeneTreeiENSGT00390000005482.
HOGENOMiHOG000007393.
HOVERGENiHBG050529.
InParanoidiQ9UJX3.
KOiK03354.
OMAiSIPNLDW.
OrthoDBiEOG71VSS4.
PhylomeDBiQ9UJX3.
TreeFamiTF105445.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiQ9UJX3.

Miscellaneous databases

ChiTaRSiANAPC7. human.
EvolutionaryTraceiQ9UJX3.
GeneWikiiANAPC7.
GenomeRNAii51434.
PROiQ9UJX3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UJX3.
CleanExiHS_ANAPC7.
ExpressionAtlasiQ9UJX3. baseline and differential.
GenevisibleiQ9UJX3. HS.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 5 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 4 hits.
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-599 (ISOFORM 1).
    Tissue: Ovary and Skin.
  3. 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] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE APC/C.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  9. "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] [Europe PMC] [Abstract]
    Cited for: ELECTRON MICROSCOPY OF THE APC/C.
  10. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 35-181, HOMODIMERIZATION, TPR REPEATS, MUTAGENESIS OF LEU-56 AND LEU-60.
  11. "Molecular architecture and mechanism of the anaphase-promoting complex."
    Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.
    Nature 513:388-393(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE APC/C, SUBUNIT.

Entry informationi

Entry nameiAPC7_HUMAN
AccessioniPrimary (citable) accession number: Q9UJX3
Secondary accession number(s): Q96AC4
, Q96GF4, Q9BU24, Q9NT16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: April 20, 2010
Last modified: July 6, 2016
This is version 154 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-35 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.