Reviewed, UniProtKB/Swiss-Prot Q9H1A4 (APC1_HUMAN)

Names and origin

Protein names

Recommended name:
    Anaphase-promoting complex subunit 1
      Short name=APC1
Alternative name(s):
    Cyclosome subunit 1
    Testis-specific gene 24 protein
    Mitotic checkpoint regulator

Gene names

Name:	ANAPC1
Synonyms:	TSG24

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	1944 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.8
Pathway	Protein modification; protein ubiquitination.
Subunit structure	The APC/C is composed of at least 12 subunits.
Post-translational modification	Phosphorylated. Phosphorylation on Ser-355 occurs specifically during mitosis. Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14
Sequence similarities	Belongs to the APC1 family. Contains 4 PC repeats.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Domain	Repeat
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 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.8 Inferred from direct assay. Source: UniProtKB
Cellular component	anaphase-promoting complex Ref.15 Inferred from direct assay. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome nucleoplasm Inferred from Experiment. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1944	1944	Anaphase-promoting complex subunit 1		PRO_0000215871
Regions
	Repeat	1297 – 1325	29	PC 1
	Repeat	1366 – 1404	39	PC 2
	Repeat	1467 – 1501	35	PC 3
	Repeat	1520 – 1552	33	PC 4
Amino acid modifications
	Modified residue	51	1	Phosphoserine Ref.11
	Modified residue	60	1	Phosphoserine Ref.11 Ref.14
	Modified residue	65	1	Phosphothreonine Ref.11
	Modified residue	202	1	Phosphoserine Ref.4
	Modified residue	286	1	Phosphoserine Ref.4
	Modified residue	291	1	Phosphothreonine Ref.4 Ref.11
	Modified residue	341	1	Phosphoserine Ref.7 Ref.10 Ref.11
	Modified residue	355	1	Phosphoserine Ref.4 Ref.9 Ref.11
	Modified residue	362	1	Phosphoserine Ref.9 Ref.11
	Modified residue	373	1	Phosphoserine Ref.4
	Modified residue	377	1	Phosphoserine Ref.4 Ref.9 Ref.10
	Modified residue	537	1	Phosphothreonine Ref.4
	Modified residue	547	1	Phosphoserine Ref.10 Ref.11 Ref.14
	Modified residue	555	1	Phosphoserine Ref.10 Ref.14
	Modified residue	563	1	Phosphoserine Ref.11
	Modified residue	569	1	Phosphoserine Ref.9
	Modified residue	571	1	Phosphotyrosine Ref.4
	Modified residue	686	1	Phosphoserine Ref.6 Ref.10 Ref.11 Ref.14
	Modified residue	688	1	Phosphoserine Ref.4 Ref.5 Ref.6 Ref.10 Ref.11 Ref.14
	Modified residue	699	1	Phosphoserine Ref.13
	Modified residue	731	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	604	1	M → V in BAB14687. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9H1A4-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: E08B1FE3FC28917E	FASTA	1,944	216,500
	10 20 30 40 50 60 MSNFYEERTT MIAARDLQEF VPFGRDHCKH HPNALNLQLR QLQPASELWS SDGAAGLVGS 70 80 90 100 110 120 LQEVTIHEKQ KESWQLRKGV SEIGEDVDYD EELYVAGNMV IWSKGSKSQA LAVYKAFTVD 130 140 150 160 170 180 SPVQQALWCD FIISQDKSEK AYSSNEVEKC ICILQSSCIN MHSIEGKDYI ASLPFQVANV 190 200 210 220 230 240 WPTKYGLLFE RSASSHEVPP GSPREPLPTM FSMLHPLDEI TPLVCKSGSL FGSSRVQYVV 250 260 270 280 290 300 DHAMKIVFLN TDPSIVMTYD AVQNVHSVWT LRRVKSEEEN VVLKFSEQGG TPQNVATSSS 310 320 330 340 350 360 LTAHLRSLSK GDSPVTSPFQ NYSSIHSQSR STSSPSLHSR SPSISNMAAL SRAHSPALGV 370 380 390 400 410 420 HSFSGVQRFN ISSHNQSPKR HSISHSPNSN SNGSFLAPET EPIVPELCID HLWTETITNI 430 440 450 460 470 480 REKNSQASKV FITSDLCGQK FLCFLVESQL QLRCVKFQES NDKTQLIFGS VTNIPAKDAA 490 500 510 520 530 540 PVEKIDTMLV LEGSGNLVLY TGVVRVGKVF IPGLPAPSLT MSNTMPRPST PLDGVSTPKP 550 560 570 580 590 600 LSKLLGSLDE VVLLSPVPEL RDSSKLHDSL YNEDCTFQQL GTYIHSIRDP VHNRVTLELS 610 620 630 640 650 660 NGSMVRITIP EIATSELVQT CLQAIKFILP KEIAVQMLVK WYNVHSAPGG PSYHSEWNLF 670 680 690 700 710 720 VTCLMNMMGY NTDRLAWTRN FDFEGSLSPV IAPKKARPSE TGSDDDWEYL LNSDYHQNVE 730 740 750 760 770 780 SHLLNRSLCL SPSEASQMKD EDFSQNLSLD SSTLLFTHIP AIFFVLHLVY EELKLNTLMG 790 800 810 820 830 840 EGICSLVELL VQLARDLKLG PYVDHYYRDY PTLVRTTGQV CTIDPGQTGF MHHPSFFTSE 850 860 870 880 890 900 PPSIYQWVSS CLKGEGMPPY PYLPGICERS RLVVLSIALY ILGDESLVSD ESSQYLTRIT 910 920 930 940 950 960 IAPQKLQVEQ EENRFSFRHS TSVSSLAERL VVWMTNVGFT LRDLETLPFG IALPIRDAIY 970 980 990 1000 1010 1020 HCREQPASDW PEAVCLLIGR QDLSKQACEG NLPKGKSVLS SDVPSGTETE EEDDGMNDMN 1030 1040 1050 1060 1070 1080 HEVMSLIWSE DLRVQDVRRL LQSAHPVRVN VVQYPELSDH EFIEEKENRL LQLCQRTMAL 1090 1100 1110 1120 1130 1140 PVGRGMFTLF SYHPVPTEPL PIPKLNLTGR APPRNTTVDL NSGNIDVPPN MTSWASFHNG 1150 1160 1170 1180 1190 1200 VAAGLKIAPA SQIDSAWIVY NKPKHAELAN EYAGFLMALG LNGHLTKLAT LNIHDYLTKG 1210 1220 1230 1240 1250 1260 HEMTSIGLLL GVSAAKLGTM DMSITRLLSI HIPALLPPTS TELDVPHNVQ VAAVVGIGLV 1270 1280 1290 1300 1310 1320 YQGTAHRHTA EVLLAEIGRP PGPEMEYCTD RESYSLAAGL ALGMVCLGHG SNLIGMSDLN 1330 1340 1350 1360 1370 1380 VPEQLYQYMV GGHRRFQTGM HREKHKSPSY QIKEGDTINV DVTCPGATLA LAMIYLKTNN 1390 1400 1410 1420 1430 1440 RSIADWLRAP DTMYLLDFVK PEFLLLRTLA RCLILWDDIL PNSKWVDSNV PQIIRENSIS 1450 1460 1470 1480 1490 1500 LSEIELPCSE DLNLETLSQA HVYIIAGACL SLGFRFAGSE NLSAFNCLHK FAKDFMTYLS 1510 1520 1530 1540 1550 1560 APNASVTGPH NLETCLSVVL LSLAMVMAGS GNLKVLQLCR FLHMKTGGEM NYGFHLAHHM 1570 1580 1590 1600 1610 1620 ALGLLFLGGG RYSLSTSNSS IAALLCALYP HFPAHSTDNR YHLQALRHLY VLAAEPRLLV 1630 1640 1650 1660 1670 1680 PVDVDTNTPC YALLEVTYKG TQWYEQTKEE LMAPTLLPEL HLLKQIKVKG PRYWELLIDL 1690 1700 1710 1720 1730 1740 SKGTQHLKSI LSKDGVLYVK LRAGQLSYKE DPMGWQSLLA QTVANRNSEA RAFKPETISA 1750 1760 1770 1780 1790 1800 FTSDPALLSF AEYFCKPTVN MGQKQEILDL FSSVLYECVT QETPEMLPAY IAMDQAIRRL 1810 1820 1830 1840 1850 1860 GRREMSETSE LWQIKLVLEF FSSRSHQERL QNHPKRGLFM NSEFLPVVKC TIDNTLDQWL 1870 1880 1890 1900 1910 1920 QVGGDMCVHA YLSGQPLEES QLSMLACFLV YHSVPAPQHL PPIGLEGSTS FAELLFKFKQ 1930 1940 LKMPVRALLR LAPLLLGNPQ PMVM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterisation of the human APC1, the largest subunit of the anaphase-promoting complex." Joergensen P.M., Graeslund S., Betz R., Stahl S., Larsson C., Hoeoeg C. Gene 262:51-59(2001) [PubMed: 11179667] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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]. Tissue: Colon and Ovary.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 510-1944. Tissue: Placenta.
[4]	"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-202; SER-286; THR-291; SER-355; SER-373; SER-377; THR-537; TYR-571 AND SER-688.
[5]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688 AND SER-731, MASS SPECTROMETRY. Tissue: Epithelium.
[6]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686 AND SER-688, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"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-341, MASS SPECTROMETRY.
[8]	"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.
[9]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355; SER-362; SER-377 AND SER-569, MASS SPECTROMETRY.
[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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341; SER-377; SER-547; SER-555; SER-686 AND SER-688, MASS SPECTROMETRY.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-60; THR-65; THR-291; SER-341; SER-355; SER-362; SER-547; SER-563; SER-686 AND SER-688, MASS SPECTROMETRY.
[12]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]	"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-699, MASS SPECTROMETRY.
[14]	"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-60; SER-547; SER-555; SER-686 AND SER-688, MASS SPECTROMETRY. Tissue: T-cell.
[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: 16364912] [Abstract] Cited for: ELECTRON MICROSCOPY OF THE APC/C.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ278357 mRNA. Translation: CAC19484.1. BC005089 mRNA. Translation: AAH05089.1. BC104902 mRNA. Translation: AAI04903.1. BC104904 mRNA. Translation: AAI04905.1. AK023807 mRNA. Translation: BAB14687.1.
IPI	IPI00033907.
RefSeq	NP_073153.1.
UniGene	Hs.436527
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9H1A4.
PTM databases
PhosphoSite	Q9H1A4.
Proteomic databases
PRIDE	Q9H1A4.
Genome annotation databases
Ensembl	ENST00000341068; ENSP00000339109; ENSG00000153107; Homo sapiens. [Genome view]
GeneID	64682.
KEGG	hsa:64682.
UCSC	uc002thi.1. human.
Organism-specific databases
CTD	64682.
GeneCards	GC02M112242. GC02M112243. GC02M112244. GC02M112245.
H-InvDB	HIX0002242. HIX0002372. HIX0030600. HIX0030607. HIX0057085. HIX0057215.
HGNC	HGNC:19988. ANAPC1.
MIM	608473. gene.
PharmGKB	PA134907013.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08377.
HOGENOM	HBG356022.
HOVERGEN	Q9H1A4.
InParanoid	Q9H1A4.
OMA	WTRNFDF.
PhylomeDB	Q9H1A4.
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	Q9H1A4.
Bgee	Q9H1A4.
CleanEx	HS_ANAPC1.
Genevestigator	Q9H1A4.
GermOnline	ENSG00000153107. Homo sapiens.
Family and domain databases
ProtoNet	Search...
Other Resources
NextBio	66605.
SOURCE	Search...

Entry information

Entry name

APC1_HUMAN

Accession

Primary (citable) accession number: Q9H1A4
Secondary accession number(s): Q2M3H8, Q9BSE6, Q9H8D0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	March 1, 2001
Last modified:	January 19, 2010
This is version 76 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.