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Protein

Anaphase-promoting complex subunit 2

Gene

ANAPC2

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

Functioni

Together with the RING-H2 protein ANAPC11, constitutes the catalytic 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. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 drives presynaptic differentiation.2 Publications

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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Differentiation, Mitosis, Neurogenesis, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciZFISH:ENSG00000176248-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.
SignaLinkiQ9UJX6.
SIGNORiQ9UJX6.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit 2
Short name:
APC2
Alternative name(s):
Cyclosome subunit 2
Gene namesi
Name:ANAPC2
Synonyms:APC2, KIAA1406
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:19989. ANAPC2.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

DisGeNETi29882.
OpenTargetsiENSG00000176248.
PharmGKBiPA134884359.

Polymorphism and mutation databases

BioMutaiANAPC2.
DMDMi37537863.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001198111 – 822Anaphase-promoting complex subunit 2Add BLAST822

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei218PhosphoserineCombined sources1
Modified residuei314PhosphoserineCombined sources1 Publication1
Modified residuei470PhosphoserineCombined sources1
Modified residuei534PhosphoserineCombined sources1 Publication1
Modified residuei697PhosphoserineBy similarity1
Modified residuei810PhosphotyrosineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UJX6.
PaxDbiQ9UJX6.
PeptideAtlasiQ9UJX6.
PRIDEiQ9UJX6.
TopDownProteomicsiQ9UJX6-2. [Q9UJX6-2]

PTM databases

iPTMnetiQ9UJX6.
PhosphoSitePlusiQ9UJX6.

Expressioni

Gene expression databases

BgeeiENSG00000176248.
CleanExiHS_ANAPC2.
HS_APC2.
GenevisibleiQ9UJX6. HS.

Organism-specific databases

HPAiCAB018692.

Interactioni

Subunit structurei

Interacts with NEUROD2 (By similarity). 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. Interacts through the cullin domain with ANAPC11 and with UBCH10.By similarity3 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi118937. 59 interactors.
DIPiDIP-32957N.
IntActiQ9UJX6. 25 interactors.
MINTiMINT-1196367.
STRINGi9606.ENSP00000314004.

Structurei

Secondary structure

1822
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi748 – 765Combined sources18
Helixi770 – 780Combined sources11
Helixi792 – 804Combined sources13
Beta strandi807 – 811Combined sources5
Beta strandi814 – 816Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UI9electron microscopy3.60N1-822[»]
4YIIX-ray1.80A735-822[»]
5A31electron microscopy4.30N74-818[»]
5G04electron microscopy4.00N1-822[»]
5G05electron microscopy3.40N1-822[»]
5KHRelectron microscopy6.10N1-822[»]
5L9Uelectron microscopy6.40N1-822[»]
5LCWelectron microscopy4.00N1-822[»]
ProteinModelPortaliQ9UJX6.
SMRiQ9UJX6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni502 – 700Cullin homology1 PublicationAdd BLAST199

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2165. Eukaryota.
ENOG410XRBY. LUCA.
GeneTreeiENSGT00390000016127.
HOGENOMiHOG000033936.
HOVERGENiHBG045327.
InParanoidiQ9UJX6.
KOiK03349.
OMAiSMVVDIY.
OrthoDBiEOG091G07N8.
PhylomeDBiQ9UJX6.
TreeFamiTF105442.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR014786. APC_su2_C.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08672. ANAPC2. 1 hit.
PF00888. Cullin. 1 hit.
[Graphical view]
SMARTiSM01013. APC2. 1 hit.
SM00182. CULLIN. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEiPS50069. CULLIN_2. 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: Q9UJX6-1) [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
MAAAVVVAEG DSDSRPGQEL LVAWNTVSTG LVPPAALGLV SSRTSGAVPP
60 70 80 90 100
KEEELRAAVE VLRGHGLHSV LEEWFVEVLQ NDLQANISPE FWNAISQCEN
110 120 130 140 150
SADEPQCLLL LLDAFGLLES RLDPYLRSLE LLEKWTRLGL LMGTGAQGLR
160 170 180 190 200
EEVHTMLRGV LFFSTPRTFQ EMIQRLYGCF LRVYMQSKRK GEGGTDPELE
210 220 230 240 250
GELDSRYARR RYYRLLQSPL CAGCSSDKQQ CWCRQALEQF HQLSQVLHRL
260 270 280 290 300
SLLERVSAEA VTTTLHQVTR ERMEDRCRGE YERSFLREFH KWIERVVGWL
310 320 330 340 350
GKVFLQDGPA RPASPEAGNT LRRWRCHVQR FFYRIYASLR IEELFSIVRD
360 370 380 390 400
FPDSRPAIED LKYCLERTDQ RQQLLVSLKA ALETRLLHPG VNTCDIITLY
410 420 430 440 450
ISAIKALRVL DPSMVILEVA CEPIRRYLRT REDTVRQIVA GLTGDSDGTG
460 470 480 490 500
DLAVELSKTD PASLETGQDS EDDSGEPEDW VPDPVDADPG KSSSKRRSSD
510 520 530 540 550
IISLLVSIYG SKDLFINEYR SLLADRLLHQ FSFSPEREIR NVELLKLRFG
560 570 580 590 600
EAPMHFCEVM LKDMADSRRI NANIREEDEK RPAEEQPPFG VYAVILSSEF
610 620 630 640 650
WPPFKDEKLE VPEDIRAALE AYCKKYEQLK AMRTLSWKHT LGLVTMDVEL
660 670 680 690 700
ADRTLSVAVT PVQAVILLYF QDQASWTLEE LSKAVKMPVA LLRRRMSVWL
710 720 730 740 750
QQGVLREEPP GTFSVIEEER PQDRDNMVLI DSDDESDSGM ASQADQKEEE
760 770 780 790 800
LLLFWTYIQA MLTNLESLSL DRIYNMLRMF VVTGPALAEI DLQELQGYLQ
810 820
KKVRDQQLVY SAGVYRLPKN CS
Length:822
Mass (Da):93,828
Last modified:May 1, 2000 - v1
Checksum:i94A2B1D015805573
GO
Isoform 2 (identifier: Q9UJX6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     350-352: Missing.

Note: No experimental confirmation available.
Show »
Length:819
Mass (Da):93,469
Checksum:iE3FC0627ECE9C324
GO

Sequence cautioni

The sequence AAH09487 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_008463350 – 352Missing in isoform 2. 1 Publication3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191337 mRNA. Translation: AAF05751.1.
AL929554 Genomic DNA. Translation: CAH72881.1.
BC032503 mRNA. Translation: AAH32503.1.
BC001579 mRNA. Translation: AAH01579.1.
BC009487 mRNA. Translation: AAH09487.2. Sequence problems.
AB037827 mRNA. Translation: BAA92644.1.
CCDSiCCDS7033.1. [Q9UJX6-1]
RefSeqiNP_037498.1. NM_013366.3. [Q9UJX6-1]
UniGeneiHs.533262.

Genome annotation databases

EnsembliENST00000323927; ENSP00000314004; ENSG00000176248. [Q9UJX6-1]
GeneIDi29882.
KEGGihsa:29882.
UCSCiuc004clr.2. human. [Q9UJX6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191337 mRNA. Translation: AAF05751.1.
AL929554 Genomic DNA. Translation: CAH72881.1.
BC032503 mRNA. Translation: AAH32503.1.
BC001579 mRNA. Translation: AAH01579.1.
BC009487 mRNA. Translation: AAH09487.2. Sequence problems.
AB037827 mRNA. Translation: BAA92644.1.
CCDSiCCDS7033.1. [Q9UJX6-1]
RefSeqiNP_037498.1. NM_013366.3. [Q9UJX6-1]
UniGeneiHs.533262.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UI9electron microscopy3.60N1-822[»]
4YIIX-ray1.80A735-822[»]
5A31electron microscopy4.30N74-818[»]
5G04electron microscopy4.00N1-822[»]
5G05electron microscopy3.40N1-822[»]
5KHRelectron microscopy6.10N1-822[»]
5L9Uelectron microscopy6.40N1-822[»]
5LCWelectron microscopy4.00N1-822[»]
ProteinModelPortaliQ9UJX6.
SMRiQ9UJX6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118937. 59 interactors.
DIPiDIP-32957N.
IntActiQ9UJX6. 25 interactors.
MINTiMINT-1196367.
STRINGi9606.ENSP00000314004.

PTM databases

iPTMnetiQ9UJX6.
PhosphoSitePlusiQ9UJX6.

Polymorphism and mutation databases

BioMutaiANAPC2.
DMDMi37537863.

Proteomic databases

EPDiQ9UJX6.
PaxDbiQ9UJX6.
PeptideAtlasiQ9UJX6.
PRIDEiQ9UJX6.
TopDownProteomicsiQ9UJX6-2. [Q9UJX6-2]

Protocols and materials databases

DNASUi29882.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323927; ENSP00000314004; ENSG00000176248. [Q9UJX6-1]
GeneIDi29882.
KEGGihsa:29882.
UCSCiuc004clr.2. human. [Q9UJX6-1]

Organism-specific databases

CTDi29882.
DisGeNETi29882.
GeneCardsiANAPC2.
HGNCiHGNC:19989. ANAPC2.
HPAiCAB018692.
MIMi606946. gene.
neXtProtiNX_Q9UJX6.
OpenTargetsiENSG00000176248.
PharmGKBiPA134884359.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2165. Eukaryota.
ENOG410XRBY. LUCA.
GeneTreeiENSGT00390000016127.
HOGENOMiHOG000033936.
HOVERGENiHBG045327.
InParanoidiQ9UJX6.
KOiK03349.
OMAiSMVVDIY.
OrthoDBiEOG091G07N8.
PhylomeDBiQ9UJX6.
TreeFamiTF105442.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000176248-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.
SignaLinkiQ9UJX6.
SIGNORiQ9UJX6.

Miscellaneous databases

ChiTaRSiANAPC2. human.
GeneWikiiANAPC2.
GenomeRNAii29882.
PROiQ9UJX6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000176248.
CleanExiHS_ANAPC2.
HS_APC2.
GenevisibleiQ9UJX6. HS.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR014786. APC_su2_C.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08672. ANAPC2. 1 hit.
PF00888. Cullin. 1 hit.
[Graphical view]
SMARTiSM01013. APC2. 1 hit.
SM00182. CULLIN. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEiPS50069. CULLIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANC2_HUMAN
AccessioniPrimary (citable) accession number: Q9UJX6
Secondary accession number(s): Q5VSG1
, Q96DG5, Q96GG4, Q9P2E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 154 of the entry and version 1 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 9
    Human chromosome 9: 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.