Reviewed, UniProtKB/Swiss-Prot Q9UJX4 (APC5_HUMAN)

Names and origin

Protein names

Recommended name:
    Anaphase-promoting complex subunit 5
      Short name=APC5
Alternative name(s):
    Cyclosome subunit 5

Gene names

Name:	ANAPC5
Synonyms:	APC5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	755 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 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	The APC/C is composed of at least 11 subunits.
Sequence similarities	Belongs to the APC5 family. Contains 4 TPR repeats.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat TPR repeat
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	G2/M transition of mitotic cell cycle Ref.1 Traceable author statement. Source: ProtInc anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome mitotic anaphase Ref.1 Traceable author statement. Source: ProtInc 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
Cellular component	anaphase-promoting complex Ref.1 Traceable author statement. Source: ProtInc cytosol Inferred from Experiment. Source: Reactome nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	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: Q9UJX4-1)

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: Q9UJX4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-121: Missing.
     122-131: TEPEVHKTSV → MLSPCLSSYF
     318-340: QQAELALQEAIRIAQESNDHVCL → TSPPWEYSPLFNRELLLGRRQTS
     341-755: Missing.

Notes: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 755	755	Anaphase-promoting complex subunit 5
Regions
	Repeat	301 – 334	34	TPR 1
	Repeat	522 – 555	34	TPR 2
	Repeat	581 – 614	34	TPR 3
	Repeat	678 – 711	34	TPR 4
Amino acid modifications
	Modified residue	195	1	Phosphoserine
	Modified residue	217	1	Phosphoserine
Natural variations
	Alternative sequence	1 – 121	121	Missing in isoform 2.
	Alternative sequence	122 – 131	10	TEPEVHKTSV → MLSPCLSSYF in isoform 2.
	Alternative sequence	318 – 340	23	QQAEL…DHVCL → TSPPWEYSPLFNRELLLGRR QTS in isoform 2.
	Alternative sequence	341 – 755	415	Missing in isoform 2.
	Natural variant	617	1	Q → H in a breast cancer sample; somatic mutation.
Experimental info
	Sequence conflict	24	1	F → L in AAF05753. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 3, 2003. Version 2. Checksum: 174F68EAB44760EB	FASTA	755	85,077
	10 20 30 40 50 60 MASVHESLYF NPMMTNGVVH ANVFGIKDWV TPYKIAVLVL LNEMSRTGEG AVSLMERRRL 70 80 90 100 110 120 NQLLLPLLQG PDITLSKLYK LIEESCPQLA NSVQIRIKLM AEGELKDMEQ FFDDLSDSFS 130 140 150 160 170 180 GTEPEVHKTS VVGLFLRHMI LAYSKLSFSQ VFKLYTALQQ YFQNGEKKTV EDADMELTSR 190 200 210 220 230 240 DEGERKMEKE ELDVSVREEE VSCSGPLSQK QAEFFLSQQA SLLKNDETKA LTPASLQKEL 250 260 270 280 290 300 NNLLKFNPDF AEAHYLSYLN NLRVQDVFSS THSLLHYFDR LILTGAESKS NGEEGYGRSL 310 320 330 340 350 360 RYAALNLAAL HCRFGHYQQA ELALQEAIRI AQESNDHVCL QHCLSWLYVL GQKRSDSYVL 370 380 390 400 410 420 LEHSVKKAVH FGLPYLASLG IQSLVQQRAF AGKTANKLMD ALKDSDLLHW KHSLSELIDI 430 440 450 460 470 480 SIAQKTAIWR LYGRSTMALQ QAQMLLSMNS LEAVNAGVQQ NNTESFAVAL CHLAELHAEQ 490 500 510 520 530 540 GCFAAASEVL KHLKERFPPN SQHAQLWMLC DQKIQFDRAM NDGKYHLADS LVTGITALNS 550 560 570 580 590 600 IEGVYRKAVV LQAQNQMSEA HKLLQKLLVH CQKLKNTEMV ISVLLSVAEL YWRSSSPTIA 610 620 630 640 650 660 LPMLLQALAL SKEYRLQYLA SETVLNLAFA QLILGIPEQA LSLLHMAIEP ILADGAILDK 670 680 690 700 710 720 GRAMFLVAKC QVASAASYDQ PKKAEALEAA IENLNEAKNY FAKVDCKERI RDVVYFQARL 730 740 750 YHTLGKTQER NRCAMLFRQL HQELPSHGVP LINHL
	Isoform 2 [UniParc]. Checksum: E74D54AFF6C8744E		219	25,147
	10 20 30 40 50 60 MLSPCLSSYF VGLFLRHMIL AYSKLSFSQV FKLYTALQQY FQNGEKKTVE DADMELTSRD 70 80 90 100 110 120 EGERKMEKEE LDVSVREEEV SCSGPLSQKQ AEFFLSQQAS LLKNDETKAL TPASLQKELN 130 140 150 160 170 180 NLLKFNPDFA EAHYLSYLNN LRVQDVFSST HSLLHYFDRL ILTGAESKSN GEEGYGRSLR 190 200 210 YAALNLAALH CRFGHYTSPP WEYSPLFNRE LLLGRRQTS

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]	The German cDNA consortium Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Oesophagus.
[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). Tissue: Brain, Cervix and Lung.
[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-195.
[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-217, MASS SPECTROMETRY. Tissue: Epithelium.
[6]	"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.
[7]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-617.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF191339 mRNA. Translation: AAF05753.1. BX537687 mRNA. Translation: CAD97812.1. BC001081 mRNA. Translation: AAH01081.1. BC001950 mRNA. Translation: AAH01950.1. BC006301 mRNA. Translation: AAH06301.1. BC034243 mRNA. Translation: AAH34243.1.
RefSeq	NP_057321.2.
UniGene	Hs.7101
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UJX4.
PTM databases
PhosphoSite	Q9UJX4.
Proteomic databases
PeptideAtlas	Q9UJX4.
Genome annotation databases
Ensembl	ENSG00000089053. Homo sapiens. [Contig view]
GeneID	51433.
KEGG	hsa:51433.
Organism-specific databases
H-InvDB	HIX0011080. HIX0042238.
HGNC	HGNC:15713. ANAPC5.
MIM	606948. gene.
PharmGKB	PA24788.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	Q9UJX4.
HOVERGEN	Q9UJX4.
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	Q9UJX4.
CleanEx	HS_ANAPC5.
GermOnline	ENSG00000089053. Homo sapiens.
Family and domain databases
InterPro	IPR011990. TPR-like_helical. IPR013026. TPR_region. [Graphical view]
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 1 hit.
PROSITE	PS50005. TPR. False negative. PS50293. TPR_REGION. False negative. [Graphical view]
ProDom	Q9UJX4. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

APC5_HUMAN

Accession

Primary (citable) accession number: Q9UJX4
Secondary accession number(s): Q8N4H7, Q9BQD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	October 3, 2003
Last modified:	July 22, 2008
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)