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Protein

Anaphase-promoting complex subunit 4

Gene

ANAPC4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

  • anaphase-promoting complex-dependent catabolic process Source: GO_Central
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • positive regulation of mitotic metaphase/anaphase transition Source: GO_Central
  • protein K11-linked ubiquitination Source: UniProtKB

Keywordsi

Biological processCell 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-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SIGNORiQ9UJX5
UniPathwayi
UPA00143

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

EuPathDBiHostDB:ENSG00000053900.10
HGNCiHGNC:19990 ANAPC4
MIMi606947 gene
neXtProtiNX_Q9UJX5

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi33D → K: Impairs UBE2S-mediated polyubiquitination, decreasing substrate affinity. Does not affect UBE2C-mediated multiubiquitination. 1 Publication1

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
Cross-linki772Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei777PhosphoserineCombined sources1
Modified residuei779Phosphoserine1 Publication1
Cross-linki798Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9UJX5
PaxDbiQ9UJX5
PeptideAtlasiQ9UJX5
PRIDEiQ9UJX5
ProteomicsDBi84686
84687 [Q9UJX5-2]

PTM databases

iPTMnetiQ9UJX5
PhosphoSitePlusiQ9UJX5

Expressioni

Gene expression databases

BgeeiENSG00000053900 Expressed in 206 organ(s), highest expression level in endometrium
CleanExiHS_ANAPC4
ExpressionAtlasiQ9UJX5 baseline and differential
GenevisibleiQ9UJX5 HS

Organism-specific databases

HPAiCAB032519
HPA038395
HPA038396

Interactioni

Subunit structurei

The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5 (PubMed:25043029, PubMed:27259151, PubMed:9469815, PubMed:26083744). In the context of the APC/C complex, directly interacts with UBE2S (PubMed:27259151).4 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi118982, 75 interactors
CORUMiQ9UJX5
DIPiDIP-56450N
IntActiQ9UJX5, 40 interactors
MINTiQ9UJX5
STRINGi9606.ENSP00000318775

Structurei

Secondary structure

1808
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
OMAiTKYANSQ
OrthoDBiEOG091G02AJ
PhylomeDBiQ9UJX5
TreeFamiTF105443

Family and domain databases

Gene3Di2.130.10.10, 1 hit
InterProiView protein in InterPro
IPR024789 APC4
IPR024790 APC4_long_dom
IPR017169 APC4_metazoa
IPR024977 Apc4_WD40_dom
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR036322 WD40_repeat_dom_sf
PANTHERiPTHR13260 PTHR13260, 1 hit
PfamiView protein in Pfam
PF12896 ANAPC4, 1 hit
PF12894 ANAPC4_WD40, 1 hit
PIRSFiPIRSF037303 APC4, 1 hit
SUPFAMiSSF50978 SSF50978, 1 hit

Sequences (3+)i

Sequence statusi: Complete.

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

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6RAP6D6RAP6_HUMAN
Anaphase-promoting complex subunit ...
ANAPC4
162Annotation score:
D6RFM7D6RFM7_HUMAN
Anaphase-promoting complex subunit ...
ANAPC4
83Annotation score:

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 dbSNP:rs34811474Ensembl.1
Natural variantiVAR_054045800E → G. Corresponds to variant dbSNP:rs11550697Ensembl.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

Similar proteinsi

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[»]
5KHUelectron microscopy4.80I1-808[»]
5L9Telectron microscopy6.40I1-808[»]
5L9Uelectron microscopy6.40I1-808[»]
5LCWelectron microscopy4.00I1-808[»]
ProteinModelPortaliQ9UJX5
SMRiQ9UJX5
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118982, 75 interactors
CORUMiQ9UJX5
DIPiDIP-56450N
IntActiQ9UJX5, 40 interactors
MINTiQ9UJX5
STRINGi9606.ENSP00000318775

PTM databases

iPTMnetiQ9UJX5
PhosphoSitePlusiQ9UJX5

Polymorphism and mutation databases

BioMutaiANAPC4
DMDMi205371737

Proteomic databases

EPDiQ9UJX5
PaxDbiQ9UJX5
PeptideAtlasiQ9UJX5
PRIDEiQ9UJX5
ProteomicsDBi84686
84687 [Q9UJX5-2]

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
EuPathDBiHostDB:ENSG00000053900.10
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
OMAiTKYANSQ
OrthoDBiEOG091G02AJ
PhylomeDBiQ9UJX5
TreeFamiTF105443

Enzyme and pathway databases

UniPathwayi
UPA00143

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-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SIGNORiQ9UJX5

Miscellaneous databases

ChiTaRSiANAPC4 human
GeneWikiiANAPC4
GenomeRNAii29945
PROiPR:Q9UJX5
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000053900 Expressed in 206 organ(s), highest expression level in endometrium
CleanExiHS_ANAPC4
ExpressionAtlasiQ9UJX5 baseline and differential
GenevisibleiQ9UJX5 HS

Family and domain databases

Gene3Di2.130.10.10, 1 hit
InterProiView protein in InterPro
IPR024789 APC4
IPR024790 APC4_long_dom
IPR017169 APC4_metazoa
IPR024977 Apc4_WD40_dom
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR036322 WD40_repeat_dom_sf
PANTHERiPTHR13260 PTHR13260, 1 hit
PfamiView protein in Pfam
PF12896 ANAPC4, 1 hit
PF12894 ANAPC4_WD40, 1 hit
PIRSFiPIRSF037303 APC4, 1 hit
SUPFAMiSSF50978 SSF50978, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiAPC4_HUMAN
AccessioniPrimary (citable) accession number: Q9UJX5
Secondary accession number(s): A8K8H1
, E9PCR4, Q6PCC6, Q9NSH6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: September 2, 2008
Last modified: November 7, 2018
This is version 157 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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