Reviewed, UniProtKB/Swiss-Prot Q9UJX6 (ANC2_HUMAN)

Names and origin

Protein names

Recommended name:
    Anaphase-promoting complex subunit 2
      Short name=APC2
Alternative name(s):
    Cyclosome subunit 2

Gene names

Name:	ANAPC2
Synonyms:	APC2, KIAA1406

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	822 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Ref.6
Pathway	Protein modification; protein ubiquitination.
Subunit structure	The APC/C is composed of at least 12 subunits. Interacts through the cullin domain with ANAPC11 and with UBCH10.
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 process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Coding sequence diversity	Alternative splicing
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW cyclin catabolic process Ref.1 Traceable author statement. Source: ProtInc mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome protein K11-linked ubiquitination Ref.10 Inferred from direct assay. Source: UniProtKB regulation of cyclin-dependent protein kinase activity Ref.1 Traceable author statement. Source: ProtInc
Cellular component	anaphase-promoting complex Ref.16 Inferred from direct assay. Source: UniProtKB cullin-RING ubiquitin ligase complex Inferred from electronic annotation. Source: InterPro cytosol Inferred from Experiment. Source: Reactome nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	ubiquitin protein ligase binding Inferred from electronic annotation. Source: InterPro ubiquitin-protein ligase activity Ref.1 Traceable author statement. 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 822	822	Anaphase-promoting complex subunit 2		PRO_0000119811
Amino acid modifications
	Modified residue	218	1	Phosphoserine Ref.8 Ref.11 Ref.12
	Modified residue	314	1	Phosphoserine Ref.11 Ref.7 Ref.9
	Modified residue	470	1	Phosphoserine Ref.12
	Modified residue	534	1	Phosphoserine Ref.11 Ref.12 Ref.7
	Modified residue	810	1	Phosphotyrosine By similarity
Natural variations
	Alternative sequence	350 – 352	3	Missing in isoform 2.		VSP_008463

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 94A2B1D015805573	FASTA	822	93,828
	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
	Isoform 2. Checksum: E3FC0627ECE9C324	FASTA	819	93,469
	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 SRPAIEDLKY 370 380 390 400 410 420 CLERTDQRQQ LLVSLKAALE TRLLHPGVNT CDIITLYISA IKALRVLDPS MVILEVACEP 430 440 450 460 470 480 IRRYLRTRED TVRQIVAGLT GDSDGTGDLA VELSKTDPAS LETGQDSEDD SGEPEDWVPD 490 500 510 520 530 540 PVDADPGKSS SKRRSSDIIS LLVSIYGSKD LFINEYRSLL ADRLLHQFSF SPEREIRNVE 550 560 570 580 590 600 LLKLRFGEAP MHFCEVMLKD MADSRRINAN IREEDEKRPA EEQPPFGVYA VILSSEFWPP 610 620 630 640 650 660 FKDEKLEVPE DIRAALEAYC KKYEQLKAMR TLSWKHTLGL VTMDVELADR TLSVAVTPVQ 670 680 690 700 710 720 AVILLYFQDQ ASWTLEELSK AVKMPVALLR RRMSVWLQQG VLREEPPGTF SVIEEERPQD 730 740 750 760 770 780 RDNMVLIDSD DESDSGMASQ ADQKEEELLL FWTYIQAMLT NLESLSLDRI YNMLRMFVVT 790 800 810 GPALAEIDLQ ELQGYLQKKV RDQQLVYSAG VYRLPKNCS

References

	« Hide 'large scale' referencesShow '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: 9469815] [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. , 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: 15164053] [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: 15489334] [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: 10718198] [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: 12168954] [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: 11739784] [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: 14657031] [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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, MASS SPECTROMETRY.
[10]	"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: 18485873] [Abstract] Cited for: FUNCTION OF THE APC/C.
[11]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-314 AND SER-534, MASS SPECTROMETRY.
[12]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-470 AND SER-534, MASS SPECTROMETRY.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY.
[15]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, MASS SPECTROMETRY. Tissue: T-cell.
[16]	"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: 16364912] [Abstract] Cited for: ELECTRON MICROSCOPY OF THE APC/C.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00002549. IPI00375832.
RefSeq	NP_037498.1.
UniGene	Hs.533262
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UJX6. 5 interactions.
STRING	Q9UJX6.
PTM databases
PhosphoSite	Q9UJX6.
Proteomic databases
PRIDE	Q9UJX6.
Genome annotation databases
Ensembl	ENST00000323927; ENSP00000314004; ENSG00000176248; Homo sapiens. [Genome view]
GeneID	29882.
KEGG	hsa:29882.
UCSC	uc004clq.1. human. uc004clr.1. human.
Organism-specific databases
CTD	29882.
GeneCards	GC09M139189.
H-InvDB	HIX0018699.
HGNC	HGNC:19989. ANAPC2.
HPA	CAB018692.
MIM	606946. gene.
PharmGKB	PA134884359.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG356979.
HOVERGEN	Q9UJX6.
InParanoid	Q9UJX6.
OMA	EEPPGTF.
OrthoDB	EOG94TRVD.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_8017. APC-Cdc20 mediated degradation of Nek2A. REACT_9035. APC/C:Cdh1-mediated degradation of Skp2.
Gene expression databases
ArrayExpress	Q9UJX6.
Bgee	Q9UJX6.
CleanEx	HS_ANAPC2. HS_APC2.
Genevestigator	Q9UJX6.
GermOnline	ENSG00000176248. Homo sapiens.
Family and domain databases
InterPro	IPR014786. APC2. IPR016158. Cullin_homology. IPR001373. Cullin_N. IPR011991. Wing_hlx_DNA_bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
Pfam	PF08672. APC2. 1 hit. PF00888. Cullin. 1 hit. [Graphical view]
SMART	SM00182. CULLIN. 1 hit. [Graphical view]
PROSITE	PS01256. CULLIN_1. False negative. PS50069. CULLIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	52411.
SOURCE	Search...

Entry information

Entry name

ANC2_HUMAN

Accession

Primary (citable) accession number: Q9UJX6
Secondary accession number(s): Q5VSG1 , Q96DG5, Q96GG4, Q9P2E1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	May 1, 2000
Last modified:	December 15, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.