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Q9UJX6 (ANC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Anaphase-promoting complex subunit 2

Short name=APC2
Alternative name(s):
Cyclosome subunit 2
Gene names
Name:ANAPC2
Synonyms:APC2, KIAA1406
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length822 AA.
Sequence statusComplete.
Protein existenceEvidence 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. 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. Ref.6 Ref.9

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with NEUROD2 By similarity. The APC/C is composed of at least 12 subunits. Interacts through the cullin domain with ANAPC11 and with UBCH10. Ref.1 Ref.6

Sequence similarities

Belongs to the cullin family.

Sequence caution

The sequence AAH09487.2 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Differentiation
Mitosis
Neurogenesis
Ubl conjugation pathway
   Coding sequence diversityAlternative splicing
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

cyclin catabolic process

Traceable author statement Ref.1. Source: ProtInc

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic 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 axon extension

Inferred from electronic annotation. Source: Ensembl

positive regulation of dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of synapse maturation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of synaptic plasticity

Inferred from sequence or structural similarity. Source: UniProtKB

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.9. Source: UniProtKB

regulation of cyclin-dependent protein serine/threonine kinase activity

Traceable author statement Ref.1. Source: ProtInc

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

ubiquitin-dependent protein catabolic process

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentanaphase-promoting complex

Inferred from direct assay Ref.15. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionubiquitin-protein transferase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UJX6-1)

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: Q9UJX6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     350-352: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 822822Anaphase-promoting complex subunit 2
PRO_0000119811

Amino acid modifications

Modified residue2181Phosphoserine Ref.8 Ref.10 Ref.11
Modified residue3141Phosphoserine Ref.7 Ref.10
Modified residue4701Phosphoserine Ref.11 Ref.13
Modified residue5341Phosphoserine Ref.7 Ref.11
Modified residue8101Phosphotyrosine By similarity

Natural variations

Alternative sequence350 – 3523Missing in isoform 2.
VSP_008463

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 94A2B1D015805573

FASTA82293,828
        10         20         30         40         50         60 
MAAAVVVAEG DSDSRPGQEL LVAWNTVSTG LVPPAALGLV SSRTSGAVPP KEEELRAAVE 

        70         80         90        100        110        120 
VLRGHGLHSV LEEWFVEVLQ NDLQANISPE FWNAISQCEN SADEPQCLLL LLDAFGLLES 

       130        140        150        160        170        180 
RLDPYLRSLE LLEKWTRLGL LMGTGAQGLR EEVHTMLRGV LFFSTPRTFQ EMIQRLYGCF 

       190        200        210        220        230        240 
LRVYMQSKRK GEGGTDPELE GELDSRYARR RYYRLLQSPL CAGCSSDKQQ CWCRQALEQF 

       250        260        270        280        290        300 
HQLSQVLHRL SLLERVSAEA VTTTLHQVTR ERMEDRCRGE YERSFLREFH KWIERVVGWL 

       310        320        330        340        350        360 
GKVFLQDGPA RPASPEAGNT LRRWRCHVQR FFYRIYASLR IEELFSIVRD FPDSRPAIED 

       370        380        390        400        410        420 
LKYCLERTDQ RQQLLVSLKA ALETRLLHPG VNTCDIITLY ISAIKALRVL DPSMVILEVA 

       430        440        450        460        470        480 
CEPIRRYLRT REDTVRQIVA GLTGDSDGTG DLAVELSKTD PASLETGQDS EDDSGEPEDW 

       490        500        510        520        530        540 
VPDPVDADPG KSSSKRRSSD IISLLVSIYG SKDLFINEYR SLLADRLLHQ FSFSPEREIR 

       550        560        570        580        590        600 
NVELLKLRFG EAPMHFCEVM LKDMADSRRI NANIREEDEK RPAEEQPPFG VYAVILSSEF 

       610        620        630        640        650        660 
WPPFKDEKLE VPEDIRAALE AYCKKYEQLK AMRTLSWKHT LGLVTMDVEL ADRTLSVAVT 

       670        680        690        700        710        720 
PVQAVILLYF QDQASWTLEE LSKAVKMPVA LLRRRMSVWL QQGVLREEPP GTFSVIEEER 

       730        740        750        760        770        780 
PQDRDNMVLI DSDDESDSGM ASQADQKEEE LLLFWTYIQA MLTNLESLSL DRIYNMLRMF 

       790        800        810        820 
VVTGPALAEI DLQELQGYLQ KKVRDQQLVY SAGVYRLPKN CS 

« Hide

Isoform 2 [UniParc].

Checksum: E3FC0627ECE9C324
Show »

FASTA81993,469

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 243-822 (ISOFORM 2).
Tissue: Brain, Cervix and Ovary.
[4]"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-822 (ISOFORM 1).
Tissue: Brain.
[5]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[6]"APC2 cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex."
Tang Z., Li B., Bharadwaj R., Zhu H., Oezkan E., Hakala K., Deisenhofer J., Yu H.
Mol. Biol. Cell 12:3839-3851(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ANAPC11 AND UBCH10.
[7]"Mitotic regulation of the human anaphase-promoting complex by phosphorylation."
Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J., Peters J.-M.
EMBO J. 22:6598-6609(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-314 AND SER-534.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218 AND SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-470 AND SER-534, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS7033.1. [Q9UJX6-1]
RefSeqNP_037498.1. NM_013366.3. [Q9UJX6-1]
UniGeneHs.533262.

3D structure databases

ProteinModelPortalQ9UJX6.
SMRQ9UJX6. Positions 508-696.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118937. 51 interactions.
DIPDIP-32957N.
IntActQ9UJX6. 20 interactions.
MINTMINT-1196367.
STRING9606.ENSP00000314004.

PTM databases

PhosphoSiteQ9UJX6.

Polymorphism databases

DMDM37537863.

Proteomic databases

MaxQBQ9UJX6.
PaxDbQ9UJX6.
PRIDEQ9UJX6.

Protocols and materials databases

DNASU29882.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323927; ENSP00000314004; ENSG00000176248. [Q9UJX6-1]
GeneID29882.
KEGGhsa:29882.
UCSCuc004clq.1. human. [Q9UJX6-2]
uc004clr.1. human. [Q9UJX6-1]

Organism-specific databases

CTD29882.
GeneCardsGC09M140069.
HGNCHGNC:19989. ANAPC2.
HPACAB018692.
MIM606946. gene.
neXtProtNX_Q9UJX6.
PharmGKBPA134884359.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5647.
HOGENOMHOG000033936.
HOVERGENHBG045327.
InParanoidQ9UJX6.
KOK03349.
OMAELLVAWN.
OrthoDBEOG76MK7Q.
PhylomeDBQ9UJX6.
TreeFamTF105442.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
SignaLinkQ9UJX6.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9UJX6.
BgeeQ9UJX6.
CleanExHS_ANAPC2.
HS_APC2.
GenevestigatorQ9UJX6.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR014786. APC_su2_C.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF08672. APC2. 1 hit.
PF00888. Cullin. 1 hit.
[Graphical view]
SMARTSM01013. APC2. 1 hit.
SM00182. CULLIN. 1 hit.
[Graphical view]
SUPFAMSSF75632. SSF75632. 1 hit.
PROSITEPS50069. CULLIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiANAPC2.
GenomeRNAi29882.
NextBio52411.
PROQ9UJX6.
SOURCESearch...

Entry information

Entry nameANC2_HUMAN
AccessionPrimary (citable) accession number: Q9UJX6
Secondary accession number(s): Q5VSG1 expand/collapse secondary AC list , Q96DG5, Q96GG4, Q9P2E1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM