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Q9UJX4 (APC5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 5

Short name=APC5
Alternative name(s):
Cyclosome subunit 5
Gene names
Name:ANAPC5
Synonyms:APC5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length755 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. Ref.7

Pathway

Protein modification; protein ubiquitination.

Subunit structure

The APC/C is composed of at least 12 subunits. Ref.1

Sequence similarities

Belongs to the APC5 family.

Contains 4 TPR repeats.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
Ubl conjugation pathway
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
TPR repeat
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement Ref.1. Source: ProtInc

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic anaphase

Traceable author statement Ref.1. Source: ProtInc

mitotic cell cycle

Traceable author statement. Source: Reactome

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 ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein K11-linked ubiquitination

Inferred from direct assay Ref.7. Source: UniProtKB

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.10. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21241890. Source: BHF-UCL

   Molecular_functionprotein phosphatase binding

Inferred from physical interaction PubMed 21241890. Source: BHF-UCL

ubiquitin-protein ligase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 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.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9UJX4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-99: Missing.
     375-387: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 755755Anaphase-promoting complex subunit 5
PRO_0000064597

Regions

Repeat301 – 33434TPR 1
Repeat522 – 55534TPR 2
Repeat581 – 61434TPR 3
Repeat678 – 71134TPR 4

Amino acid modifications

Modified residue1951Phosphoserine Ref.6

Natural variations

Alternative sequence1 – 121121Missing in isoform 2.
VSP_008466
Alternative sequence1 – 9999Missing in isoform 3.
VSP_044878
Alternative sequence122 – 13110TEPEVHKTSV → MLSPCLSSYF in isoform 2.
VSP_008467
Alternative sequence318 – 34023QQAEL…DHVCL → TSPPWEYSPLFNRELLLGRR QTS in isoform 2.
VSP_008468
Alternative sequence341 – 755415Missing in isoform 2.
VSP_008469
Alternative sequence375 – 38713Missing in isoform 3.
VSP_044879
Natural variant6171Q → H in a breast cancer sample; somatic mutation. Ref.11
VAR_035793

Experimental info

Sequence conflict241F → L in AAF05753. Ref.1

Sequences

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

Last modified October 3, 2003. Version 2.
Checksum: 174F68EAB44760EB

FASTA75585,077
        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 

« Hide

Isoform 2 [UniParc].

Checksum: E74D54AFF6C8744E
Show »

FASTA21925,147
Isoform 3 [UniParc].

Checksum: 6245611F5812F7CC
Show »

FASTA64372,526

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]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Hepatoma.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Esophagus.
[4]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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).
Tissue: Brain, Cervix and Lung.
[6]"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-195.
[7]"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.
[8]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"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].
[10]"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.
[11]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-617.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF191339 mRNA. Translation: AAF05753.1.
AK025614 mRNA. No translation available.
BX537687 mRNA. Translation: CAD97812.1.
AC048337 Genomic DNA. No translation available.
AC069209 Genomic DNA. No translation available.
BC001081 mRNA. Translation: AAH01081.1.
BC001950 mRNA. Translation: AAH01950.1.
BC006301 mRNA. Translation: AAH06301.1.
BC034243 mRNA. Translation: AAH34243.1.
RefSeqNP_001131031.1. NM_001137559.1.
NP_057321.2. NM_016237.4.
UniGeneHs.7101.

3D structure databases

ProteinModelPortalQ9UJX4.
SMRQ9UJX4. Positions 472-498, 545-608, 618-648.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119537. 53 interactions.
DIPDIP-32945N.
IntActQ9UJX4. 28 interactions.
MINTMINT-1391095.
STRING9606.ENSP00000261819.

PTM databases

PhosphoSiteQ9UJX4.

Polymorphism databases

DMDM37537861.

Proteomic databases

PaxDbQ9UJX4.
PeptideAtlasQ9UJX4.
PRIDEQ9UJX4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261819; ENSP00000261819; ENSG00000089053. [Q9UJX4-1]
ENST00000344395; ENSP00000343787; ENSG00000089053. [Q9UJX4-3]
ENST00000441917; ENSP00000415061; ENSG00000089053. [Q9UJX4-3]
ENST00000536366; ENSP00000445310; ENSG00000089053. [Q9UJX4-2]
ENST00000605884; ENSP00000475286; ENSG00000272204. [Q9UJX4-3]
ENST00000605978; ENSP00000475940; ENSG00000272204. [Q9UJX4-3]
ENST00000607064; ENSP00000475599; ENSG00000272204. [Q9UJX4-1]
ENST00000607392; ENSP00000475271; ENSG00000272204. [Q9UJX4-2]
GeneID51433.
KEGGhsa:51433.
UCSCuc001uag.3. human. [Q9UJX4-1]
uc001uah.3. human.

Organism-specific databases

CTD51433.
GeneCardsGC12M121746.
HGNCHGNC:15713. ANAPC5.
HPAHPA039457.
MIM606948. gene.
neXtProtNX_Q9UJX4.
PharmGKBPA24788.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320252.
HOGENOMHOG000033988.
HOVERGENHBG001285.
InParanoidQ9UJX4.
KOK03352.
OMALYWRSSC.
OrthoDBEOG7T7GSR.
PhylomeDBQ9UJX4.
TreeFamTF105444.

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.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9UJX4.
BgeeQ9UJX4.
CleanExHS_ANAPC5.
GenevestigatorQ9UJX4.

Family and domain databases

Gene3D1.25.40.10. 4 hits.
InterProIPR026000. Apc5/TPR19_dom.
IPR011990. TPR-like_helical.
[Graphical view]
PfamPF12862. Apc5. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSANAPC5. human.
GeneWikiANAPC5.
GenomeRNAi51433.
NextBio55001.
PROQ9UJX4.
SOURCESearch...

Entry information

Entry nameAPC5_HUMAN
AccessionPrimary (citable) accession number: Q9UJX4
Secondary accession number(s): E9PFB2, Q8N4H7, Q9BQD4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: April 16, 2014
This is version 123 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM