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Protein

Anaphase-promoting complex subunit 4

Gene

ANAPC4

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
  • ubiquitin-protein transferase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciZFISH:ENSG00000053900-MONOMER.
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.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit 4
Short name:
APC4
Alternative name(s):
Cyclosome subunit 4
Gene namesi
Name:ANAPC4
Synonyms:APC4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:19990. ANAPC4.

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

Organism-specific databases

DisGeNETi29945.
OpenTargetsiENSG00000053900.
PharmGKBiPA134894250.

Polymorphism and mutation databases

BioMutaiANAPC4.
DMDMi205371737.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000645951 – 808Anaphase-promoting complex subunit 4Add BLAST808

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei469Phosphotyrosine1 Publication1
Modified residuei757PhosphoserineCombined sources1
Modified residuei758PhosphoserineCombined sources1
Modified residuei777PhosphoserineCombined sources1
Modified residuei779Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UJX5.
PaxDbiQ9UJX5.
PeptideAtlasiQ9UJX5.
PRIDEiQ9UJX5.

PTM databases

iPTMnetiQ9UJX5.
PhosphoSitePlusiQ9UJX5.

Expressioni

Gene expression databases

BgeeiENSG00000053900.
CleanExiHS_ANAPC4.
ExpressionAtlasiQ9UJX5. baseline and differential.
GenevisibleiQ9UJX5. HS.

Organism-specific databases

HPAiCAB032519.
HPA038395.
HPA038396.

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KIF18AQ8NI772EBI-2554854,EBI-355426
NEK2P519556EBI-2554854,EBI-633182

GO - Molecular functioni

  • protein phosphatase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi118982. 67 interactors.
DIPiDIP-56450N.
IntActiQ9UJX5. 33 interactors.
MINTiMINT-4787108.
STRINGi9606.ENSP00000318775.

Structurei

Secondary structure

1808
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 18Combined sources7
Beta strandi23 – 28Combined sources6
Beta strandi30 – 39Combined sources10
Beta strandi44 – 49Combined sources6
Helixi50 – 52Combined sources3
Beta strandi54 – 58Combined sources5
Beta strandi62 – 64Combined sources3
Beta strandi68 – 73Combined sources6
Beta strandi77 – 87Combined sources11
Beta strandi89 – 105Combined sources17
Beta strandi112 – 117Combined sources6
Turni120 – 122Combined sources3
Helixi133 – 136Combined sources4
Beta strandi155 – 160Combined sources6
Helixi162 – 169Combined sources8
Beta strandi174 – 179Combined sources6
Beta strandi183 – 189Combined sources7
Turni190 – 192Combined sources3
Beta strandi193 – 199Combined sources7
Beta strandi203 – 210Combined sources8
Beta strandi214 – 223Combined sources10
Beta strandi228 – 237Combined sources10
Helixi239 – 243Combined sources5
Helixi245 – 284Combined sources40
Turni320 – 324Combined sources5
Helixi327 – 350Combined sources24
Helixi352 – 370Combined sources19
Helixi373 – 376Combined sources4
Helixi383 – 426Combined sources44
Turni427 – 429Combined sources3
Helixi448 – 456Combined sources9
Helixi474 – 478Combined sources5
Helixi526 – 547Combined sources22
Beta strandi551 – 560Combined sources10
Turni561 – 563Combined sources3
Beta strandi573 – 578Combined sources6
Turni579 – 582Combined sources4
Beta strandi583 – 606Combined sources24
Beta strandi614 – 624Combined sources11
Beta strandi636 – 645Combined sources10
Beta strandi648 – 657Combined sources10
Turni659 – 661Combined sources3
Beta strandi664 – 670Combined sources7
Helixi671 – 673Combined sources3
Helixi679 – 682Combined sources4
Beta strandi702 – 707Combined sources6
Beta strandi709 – 713Combined sources5
Beta strandi721 – 724Combined sources4
Beta strandi726 – 728Combined sources3
Beta strandi730 – 734Combined sources5
Beta strandi738 – 745Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UI9electron microscopy3.60I1-808[»]
5A31electron microscopy4.30I1-808[»]
5BPWX-ray3.40A1-808[»]
5G04electron microscopy4.00I1-808[»]
5G05electron microscopy3.40I1-808[»]
5KHRelectron microscopy6.10I1-808[»]
5L9Uelectron microscopy6.40I1-808[»]
5LCWelectron microscopy4.00I1-808[»]
ProteinModelPortaliQ9UJX5.
SMRiQ9UJX5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the APC4 family.Curated

Phylogenomic databases

eggNOGiKOG4640. Eukaryota.
ENOG410XPXK. LUCA.
GeneTreeiENSGT00390000004612.
HOGENOMiHOG000033987.
HOVERGENiHBG044815.
InParanoidiQ9UJX5.
KOiK03351.
OMAiMSCIVER.
OrthoDBiEOG091G02AJ.
PhylomeDBiQ9UJX5.
TreeFamiTF105443.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR024789. APC4.
IPR024790. APC4_long_dom.
IPR017169. APC4_metazoa.
IPR024977. Apc4_WD40_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR13260. PTHR13260. 1 hit.
PfamiPF12896. ANAPC4. 1 hit.
PF12894. ANAPC4_WD40. 1 hit.
[Graphical view]
PIRSFiPIRSF037303. APC4. 1 hit.
SUPFAMiSSF50978. SSF50978. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UJX5-1) [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
MLRFPTCFPS FRVVGEKQLP QEIIFLVWSP KRDLIALANT AGEVLLHRLA
60 70 80 90 100
SFHRVWSFPP NENTGKEVTC LAWRPDGKLL AFALADTKKI VLCDVEKPES
110 120 130 140 150
LHSFSVEAPV SCMHWMEVTV ESSVLTSFYN AEDESNLLLP KLPTLPKNYS
160 170 180 190 200
NTSKIFSEEN SDEIIKLLGD VRLNILVLGG SSGFIELYAY GMFKIARVTG
210 220 230 240 250
IAGTCLALCL SSDLKSLSVV TEVSTNGASE VSYFQLETNL LYSFLPEVTR
260 270 280 290 300
MARKFTHISA LLQYINLSLT CMCEAWEEIL MQMDSRLTKF VQEKNTTTSV
310 320 330 340 350
QDEFMHLLLW GKASAELQTL LMNQLTVKGL KKLGQSIESS YSSIQKLVIS
360 370 380 390 400
HLQSGSESLL YHLSELKGMA SWKQKYEPLG LDAAGIEEAI TAVGSFILKA
410 420 430 440 450
NELLQVIDSS MKNFKAFFRW LYVAMLRMTE DHVLPELNKM TQKDITFVAE
460 470 480 490 500
FLTEHFNEAP DLYNRKGKYF NVERVGQYLK DEDDDLVSPP NTEGNQWYDF
510 520 530 540 550
LQNSSHLKES PLLFPYYPRK SLHFVKRRME NIIDQCLQKP ADVIGKSMNQ
560 570 580 590 600
AICIPLYRDT RSEDSTRRLF KFPFLWNNKT SNLHYLLFTI LEDSLYKMCI
610 620 630 640 650
LRRHTDISQS VSNGLIAIKF GSFTYATTEK VRRSIYSCLD AQFYDDETVT
660 670 680 690 700
VVLKDTVGRE GRDRLLVQLP LSLVYNSEDS AEYQFTGTYS TRLDEQCSAI
710 720 730 740 750
PTRTMHFEKH WRLLESMKAQ YVAGNGFRKV SCVLSSNLRH VRVFEMDIDD
760 770 780 790 800
EWELDESSDE EEEASNKPVK IKEEVLSESE AENQQAGAAA LAPEIVIKVE

KLDPELDS
Length:808
Mass (Da):92,116
Last modified:September 2, 2008 - v2
Checksum:i80362CC8D8B2063F
GO
Isoform 2 (identifier: Q9UJX5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     542-551: DVIGKSMNQA → VSLKEMHVFV
     552-808: Missing.

Note: No experimental confirmation available.
Show »
Length:551
Mass (Da):62,639
Checksum:i16829B75DE9987DF
GO
Isoform 3 (identifier: Q9UJX5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     439-439: K → KV

Note: No experimental confirmation available.
Show »
Length:809
Mass (Da):92,216
Checksum:iDD0B4899C6501E09
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti286R → C in AAF05752 (PubMed:9469815).Curated1
Sequence conflicti293 – 295EKN → GKD in AAF05752 (PubMed:9469815).Curated3
Sequence conflicti756E → G in AAH59383 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035792155I → V in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_054044465R → Q.Corresponds to variant rs34811474dbSNPEnsembl.1
Natural variantiVAR_054045800E → G.Corresponds to variant rs11550697dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_056708439K → KV in isoform 3. Curated1
Alternative sequenceiVSP_008464542 – 551DVIGKSMNQA → VSLKEMHVFV in isoform 2. 1 Publication10
Alternative sequenceiVSP_008465552 – 808Missing in isoform 2. 1 PublicationAdd BLAST257

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191338 mRNA. Translation: AAF05752.1.
AK292336 mRNA. Translation: BAF85025.1.
CH471069 Genomic DNA. Translation: EAW92839.1.
BC059383 mRNA. Translation: AAH59383.1.
AL353932 mRNA. Translation: CAB89245.1.
CCDSiCCDS3434.1. [Q9UJX5-1]
CCDS68684.1. [Q9UJX5-3]
PIRiT48682.
RefSeqiNP_001273685.1. NM_001286756.1. [Q9UJX5-3]
NP_037499.2. NM_013367.2. [Q9UJX5-1]
UniGeneiHs.152173.

Genome annotation databases

EnsembliENST00000315368; ENSP00000318775; ENSG00000053900. [Q9UJX5-1]
ENST00000510092; ENSP00000426654; ENSG00000053900. [Q9UJX5-3]
GeneIDi29945.
KEGGihsa:29945.
UCSCiuc003gro.4. human. [Q9UJX5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191338 mRNA. Translation: AAF05752.1.
AK292336 mRNA. Translation: BAF85025.1.
CH471069 Genomic DNA. Translation: EAW92839.1.
BC059383 mRNA. Translation: AAH59383.1.
AL353932 mRNA. Translation: CAB89245.1.
CCDSiCCDS3434.1. [Q9UJX5-1]
CCDS68684.1. [Q9UJX5-3]
PIRiT48682.
RefSeqiNP_001273685.1. NM_001286756.1. [Q9UJX5-3]
NP_037499.2. NM_013367.2. [Q9UJX5-1]
UniGeneiHs.152173.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UI9electron microscopy3.60I1-808[»]
5A31electron microscopy4.30I1-808[»]
5BPWX-ray3.40A1-808[»]
5G04electron microscopy4.00I1-808[»]
5G05electron microscopy3.40I1-808[»]
5KHRelectron microscopy6.10I1-808[»]
5L9Uelectron microscopy6.40I1-808[»]
5LCWelectron microscopy4.00I1-808[»]
ProteinModelPortaliQ9UJX5.
SMRiQ9UJX5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118982. 67 interactors.
DIPiDIP-56450N.
IntActiQ9UJX5. 33 interactors.
MINTiMINT-4787108.
STRINGi9606.ENSP00000318775.

PTM databases

iPTMnetiQ9UJX5.
PhosphoSitePlusiQ9UJX5.

Polymorphism and mutation databases

BioMutaiANAPC4.
DMDMi205371737.

Proteomic databases

EPDiQ9UJX5.
PaxDbiQ9UJX5.
PeptideAtlasiQ9UJX5.
PRIDEiQ9UJX5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000315368; ENSP00000318775; ENSG00000053900. [Q9UJX5-1]
ENST00000510092; ENSP00000426654; ENSG00000053900. [Q9UJX5-3]
GeneIDi29945.
KEGGihsa:29945.
UCSCiuc003gro.4. human. [Q9UJX5-1]

Organism-specific databases

CTDi29945.
DisGeNETi29945.
GeneCardsiANAPC4.
HGNCiHGNC:19990. ANAPC4.
HPAiCAB032519.
HPA038395.
HPA038396.
MIMi606947. gene.
neXtProtiNX_Q9UJX5.
OpenTargetsiENSG00000053900.
PharmGKBiPA134894250.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4640. Eukaryota.
ENOG410XPXK. LUCA.
GeneTreeiENSGT00390000004612.
HOGENOMiHOG000033987.
HOVERGENiHBG044815.
InParanoidiQ9UJX5.
KOiK03351.
OMAiMSCIVER.
OrthoDBiEOG091G02AJ.
PhylomeDBiQ9UJX5.
TreeFamiTF105443.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000053900-MONOMER.
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.

Miscellaneous databases

ChiTaRSiANAPC4. human.
GeneWikiiANAPC4.
GenomeRNAii29945.
PROiQ9UJX5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000053900.
CleanExiHS_ANAPC4.
ExpressionAtlasiQ9UJX5. baseline and differential.
GenevisibleiQ9UJX5. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR024789. APC4.
IPR024790. APC4_long_dom.
IPR017169. APC4_metazoa.
IPR024977. Apc4_WD40_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR13260. PTHR13260. 1 hit.
PfamiPF12896. ANAPC4. 1 hit.
PF12894. ANAPC4_WD40. 1 hit.
[Graphical view]
PIRSFiPIRSF037303. APC4. 1 hit.
SUPFAMiSSF50978. SSF50978. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiAPC4_HUMAN
AccessioniPrimary (citable) accession number: Q9UJX5
Secondary accession number(s): A8K8H1
, E9PCR4, Q6PCC6, Q9NSH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: September 2, 2008
Last modified: November 30, 2016
This is version 139 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.