Full text data of ANAPC5
ANAPC5
(APC5)
[Confidence: low (only semi-automatic identification from reviews)]
Anaphase-promoting complex subunit 5; APC5 (Cyclosome subunit 5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Anaphase-promoting complex subunit 5; APC5 (Cyclosome subunit 5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UJX4
ID APC5_HUMAN Reviewed; 755 AA.
AC Q9UJX4; E9PFB2; Q8N4H7; Q9BQD4;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-OCT-2003, sequence version 2.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Anaphase-promoting complex subunit 5;
DE Short=APC5;
DE AltName: Full=Cyclosome subunit 5;
GN Name=ANAPC5; Synonyms=APC5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBUNIT.
RX PubMed=9469815; DOI=10.1126/science.279.5354.1219;
RA Yu H., Peters J.-M., King R.W., Page A.M., Hieter P., Kirschner M.W.;
RT "Identification of a cullin homology region in a subunit of the
RT anaphase-promoting complex.";
RL Science 279:1219-1222(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Hepatoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Esophagus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Cervix, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION AT SER-195.
RX PubMed=14657031; DOI=10.1093/emboj/cdg627;
RA Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J.,
RA Peters J.-M.;
RT "Mitotic regulation of the human anaphase-promoting complex by
RT phosphorylation.";
RL EMBO J. 22:6598-6609(2003).
RN [7]
RP FUNCTION OF THE APC/C.
RX PubMed=18485873; DOI=10.1016/j.cell.2008.04.012;
RA Jin L., Williamson A., Banerjee S., Philipp I., Rape M.;
RT "Mechanism of ubiquitin-chain formation by the human anaphase-
RT promoting complex.";
RL Cell 133:653-665(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ELECTRON MICROSCOPY OF THE APC/C.
RX PubMed=16364912; DOI=10.1016/j.molcel.2005.11.008;
RA Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A.,
RA Engel A., Peters J.-M., Stark H.;
RT "Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a
RT cryo-electron microscopy model of vertebrate APC/C.";
RL Mol. Cell 20:867-879(2005).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-617.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC progression through mitosis and the G1 phase of the cell cycle.
CC The APC/C complex acts by mediating ubiquitination and subsequent
CC degradation of target proteins: it mainly mediates the formation
CC of 'Lys-11'-linked polyubiquitin chains and, to a lower extent,
CC the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin
CC chains.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: The APC/C is composed of at least 12 subunits.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UJX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJX4-2; Sequence=VSP_008466, VSP_008467, VSP_008468,
CC VSP_008469;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9UJX4-3; Sequence=VSP_044878, VSP_044879;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the APC5 family.
CC -!- SIMILARITY: Contains 4 TPR repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF191339; AAF05753.1; -; mRNA.
DR EMBL; AK025614; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX537687; CAD97812.1; -; mRNA.
DR EMBL; AC048337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001081; AAH01081.1; -; mRNA.
DR EMBL; BC001950; AAH01950.1; -; mRNA.
DR EMBL; BC006301; AAH06301.1; -; mRNA.
DR EMBL; BC034243; AAH34243.1; -; mRNA.
DR RefSeq; NP_001131031.1; NM_001137559.1.
DR RefSeq; NP_057321.2; NM_016237.4.
DR UniGene; Hs.7101; -.
DR ProteinModelPortal; Q9UJX4; -.
DR DIP; DIP-32945N; -.
DR IntAct; Q9UJX4; 28.
DR MINT; MINT-1391095; -.
DR STRING; 9606.ENSP00000261819; -.
DR PhosphoSite; Q9UJX4; -.
DR DMDM; 37537861; -.
DR PaxDb; Q9UJX4; -.
DR PeptideAtlas; Q9UJX4; -.
DR PRIDE; Q9UJX4; -.
DR Ensembl; ENST00000261819; ENSP00000261819; ENSG00000089053.
DR Ensembl; ENST00000344395; ENSP00000343787; ENSG00000089053.
DR Ensembl; ENST00000441917; ENSP00000415061; ENSG00000089053.
DR Ensembl; ENST00000536366; ENSP00000445310; ENSG00000089053.
DR Ensembl; ENST00000605884; ENSP00000475286; ENSG00000272204.
DR Ensembl; ENST00000605978; ENSP00000475940; ENSG00000272204.
DR Ensembl; ENST00000607064; ENSP00000475599; ENSG00000272204.
DR Ensembl; ENST00000607392; ENSP00000475271; ENSG00000272204.
DR GeneID; 51433; -.
DR KEGG; hsa:51433; -.
DR UCSC; uc001uah.3; human.
DR CTD; 51433; -.
DR GeneCards; GC12M121746; -.
DR HGNC; HGNC:15713; ANAPC5.
DR HPA; HPA039457; -.
DR MIM; 606948; gene.
DR neXtProt; NX_Q9UJX4; -.
DR PharmGKB; PA24788; -.
DR eggNOG; NOG320252; -.
DR HOGENOM; HOG000033988; -.
DR HOVERGEN; HBG001285; -.
DR InParanoid; Q9UJX4; -.
DR KO; K03352; -.
DR OMA; LYWRSSC; -.
DR OrthoDB; EOG7T7GSR; -.
DR PhylomeDB; Q9UJX4; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_120956; Cellular responses to stress.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_8017; APC-Cdc20 mediated degradation of Nek2A.
DR UniPathway; UPA00143; -.
DR ChiTaRS; ANAPC5; human.
DR GeneWiki; ANAPC5; -.
DR GenomeRNAi; 51433; -.
DR NextBio; 55001; -.
DR PRO; PR:Q9UJX4; -.
DR ArrayExpress; Q9UJX4; -.
DR Bgee; Q9UJX4; -.
DR CleanEx; HS_ANAPC5; -.
DR Genevestigator; Q9UJX4; -.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; TAS:ProtInc.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0000090; P:mitotic anaphase; TAS:ProtInc.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR026000; Apc5/TPR19_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR Pfam; PF12862; Apc5; 2.
DR PROSITE; PS50005; TPR; FALSE_NEG.
DR PROSITE; PS50293; TPR_REGION; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Complete proteome;
KW Mitosis; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation pathway.
FT CHAIN 1 755 Anaphase-promoting complex subunit 5.
FT /FTId=PRO_0000064597.
FT REPEAT 301 334 TPR 1.
FT REPEAT 522 555 TPR 2.
FT REPEAT 581 614 TPR 3.
FT REPEAT 678 711 TPR 4.
FT MOD_RES 195 195 Phosphoserine.
FT VAR_SEQ 1 121 Missing (in isoform 2).
FT /FTId=VSP_008466.
FT VAR_SEQ 1 99 Missing (in isoform 3).
FT /FTId=VSP_044878.
FT VAR_SEQ 122 131 TEPEVHKTSV -> MLSPCLSSYF (in isoform 2).
FT /FTId=VSP_008467.
FT VAR_SEQ 318 340 QQAELALQEAIRIAQESNDHVCL -> TSPPWEYSPLFNRE
FT LLLGRRQTS (in isoform 2).
FT /FTId=VSP_008468.
FT VAR_SEQ 341 755 Missing (in isoform 2).
FT /FTId=VSP_008469.
FT VAR_SEQ 375 387 Missing (in isoform 3).
FT /FTId=VSP_044879.
FT VARIANT 617 617 Q -> H (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035793.
FT CONFLICT 24 24 F -> L (in Ref. 1; AAF05753).
SQ SEQUENCE 755 AA; 85077 MW; 174F68EAB44760EB CRC64;
MASVHESLYF NPMMTNGVVH ANVFGIKDWV TPYKIAVLVL LNEMSRTGEG AVSLMERRRL
NQLLLPLLQG PDITLSKLYK LIEESCPQLA NSVQIRIKLM AEGELKDMEQ FFDDLSDSFS
GTEPEVHKTS VVGLFLRHMI LAYSKLSFSQ VFKLYTALQQ YFQNGEKKTV EDADMELTSR
DEGERKMEKE ELDVSVREEE VSCSGPLSQK QAEFFLSQQA SLLKNDETKA LTPASLQKEL
NNLLKFNPDF AEAHYLSYLN NLRVQDVFSS THSLLHYFDR LILTGAESKS NGEEGYGRSL
RYAALNLAAL HCRFGHYQQA ELALQEAIRI AQESNDHVCL QHCLSWLYVL GQKRSDSYVL
LEHSVKKAVH FGLPYLASLG IQSLVQQRAF AGKTANKLMD ALKDSDLLHW KHSLSELIDI
SIAQKTAIWR LYGRSTMALQ QAQMLLSMNS LEAVNAGVQQ NNTESFAVAL CHLAELHAEQ
GCFAAASEVL KHLKERFPPN SQHAQLWMLC DQKIQFDRAM NDGKYHLADS LVTGITALNS
IEGVYRKAVV LQAQNQMSEA HKLLQKLLVH CQKLKNTEMV ISVLLSVAEL YWRSSSPTIA
LPMLLQALAL SKEYRLQYLA SETVLNLAFA QLILGIPEQA LSLLHMAIEP ILADGAILDK
GRAMFLVAKC QVASAASYDQ PKKAEALEAA IENLNEAKNY FAKVDCKERI RDVVYFQARL
YHTLGKTQER NRCAMLFRQL HQELPSHGVP LINHL
//
ID APC5_HUMAN Reviewed; 755 AA.
AC Q9UJX4; E9PFB2; Q8N4H7; Q9BQD4;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-OCT-2003, sequence version 2.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Anaphase-promoting complex subunit 5;
DE Short=APC5;
DE AltName: Full=Cyclosome subunit 5;
GN Name=ANAPC5; Synonyms=APC5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBUNIT.
RX PubMed=9469815; DOI=10.1126/science.279.5354.1219;
RA Yu H., Peters J.-M., King R.W., Page A.M., Hieter P., Kirschner M.W.;
RT "Identification of a cullin homology region in a subunit of the
RT anaphase-promoting complex.";
RL Science 279:1219-1222(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Hepatoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Esophagus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Cervix, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION AT SER-195.
RX PubMed=14657031; DOI=10.1093/emboj/cdg627;
RA Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J.,
RA Peters J.-M.;
RT "Mitotic regulation of the human anaphase-promoting complex by
RT phosphorylation.";
RL EMBO J. 22:6598-6609(2003).
RN [7]
RP FUNCTION OF THE APC/C.
RX PubMed=18485873; DOI=10.1016/j.cell.2008.04.012;
RA Jin L., Williamson A., Banerjee S., Philipp I., Rape M.;
RT "Mechanism of ubiquitin-chain formation by the human anaphase-
RT promoting complex.";
RL Cell 133:653-665(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ELECTRON MICROSCOPY OF THE APC/C.
RX PubMed=16364912; DOI=10.1016/j.molcel.2005.11.008;
RA Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A.,
RA Engel A., Peters J.-M., Stark H.;
RT "Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a
RT cryo-electron microscopy model of vertebrate APC/C.";
RL Mol. Cell 20:867-879(2005).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-617.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC progression through mitosis and the G1 phase of the cell cycle.
CC The APC/C complex acts by mediating ubiquitination and subsequent
CC degradation of target proteins: it mainly mediates the formation
CC of 'Lys-11'-linked polyubiquitin chains and, to a lower extent,
CC the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin
CC chains.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: The APC/C is composed of at least 12 subunits.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UJX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJX4-2; Sequence=VSP_008466, VSP_008467, VSP_008468,
CC VSP_008469;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9UJX4-3; Sequence=VSP_044878, VSP_044879;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the APC5 family.
CC -!- SIMILARITY: Contains 4 TPR repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF191339; AAF05753.1; -; mRNA.
DR EMBL; AK025614; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX537687; CAD97812.1; -; mRNA.
DR EMBL; AC048337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001081; AAH01081.1; -; mRNA.
DR EMBL; BC001950; AAH01950.1; -; mRNA.
DR EMBL; BC006301; AAH06301.1; -; mRNA.
DR EMBL; BC034243; AAH34243.1; -; mRNA.
DR RefSeq; NP_001131031.1; NM_001137559.1.
DR RefSeq; NP_057321.2; NM_016237.4.
DR UniGene; Hs.7101; -.
DR ProteinModelPortal; Q9UJX4; -.
DR DIP; DIP-32945N; -.
DR IntAct; Q9UJX4; 28.
DR MINT; MINT-1391095; -.
DR STRING; 9606.ENSP00000261819; -.
DR PhosphoSite; Q9UJX4; -.
DR DMDM; 37537861; -.
DR PaxDb; Q9UJX4; -.
DR PeptideAtlas; Q9UJX4; -.
DR PRIDE; Q9UJX4; -.
DR Ensembl; ENST00000261819; ENSP00000261819; ENSG00000089053.
DR Ensembl; ENST00000344395; ENSP00000343787; ENSG00000089053.
DR Ensembl; ENST00000441917; ENSP00000415061; ENSG00000089053.
DR Ensembl; ENST00000536366; ENSP00000445310; ENSG00000089053.
DR Ensembl; ENST00000605884; ENSP00000475286; ENSG00000272204.
DR Ensembl; ENST00000605978; ENSP00000475940; ENSG00000272204.
DR Ensembl; ENST00000607064; ENSP00000475599; ENSG00000272204.
DR Ensembl; ENST00000607392; ENSP00000475271; ENSG00000272204.
DR GeneID; 51433; -.
DR KEGG; hsa:51433; -.
DR UCSC; uc001uah.3; human.
DR CTD; 51433; -.
DR GeneCards; GC12M121746; -.
DR HGNC; HGNC:15713; ANAPC5.
DR HPA; HPA039457; -.
DR MIM; 606948; gene.
DR neXtProt; NX_Q9UJX4; -.
DR PharmGKB; PA24788; -.
DR eggNOG; NOG320252; -.
DR HOGENOM; HOG000033988; -.
DR HOVERGEN; HBG001285; -.
DR InParanoid; Q9UJX4; -.
DR KO; K03352; -.
DR OMA; LYWRSSC; -.
DR OrthoDB; EOG7T7GSR; -.
DR PhylomeDB; Q9UJX4; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_120956; Cellular responses to stress.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_8017; APC-Cdc20 mediated degradation of Nek2A.
DR UniPathway; UPA00143; -.
DR ChiTaRS; ANAPC5; human.
DR GeneWiki; ANAPC5; -.
DR GenomeRNAi; 51433; -.
DR NextBio; 55001; -.
DR PRO; PR:Q9UJX4; -.
DR ArrayExpress; Q9UJX4; -.
DR Bgee; Q9UJX4; -.
DR CleanEx; HS_ANAPC5; -.
DR Genevestigator; Q9UJX4; -.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; TAS:ProtInc.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0000090; P:mitotic anaphase; TAS:ProtInc.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR026000; Apc5/TPR19_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR Pfam; PF12862; Apc5; 2.
DR PROSITE; PS50005; TPR; FALSE_NEG.
DR PROSITE; PS50293; TPR_REGION; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Complete proteome;
KW Mitosis; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation pathway.
FT CHAIN 1 755 Anaphase-promoting complex subunit 5.
FT /FTId=PRO_0000064597.
FT REPEAT 301 334 TPR 1.
FT REPEAT 522 555 TPR 2.
FT REPEAT 581 614 TPR 3.
FT REPEAT 678 711 TPR 4.
FT MOD_RES 195 195 Phosphoserine.
FT VAR_SEQ 1 121 Missing (in isoform 2).
FT /FTId=VSP_008466.
FT VAR_SEQ 1 99 Missing (in isoform 3).
FT /FTId=VSP_044878.
FT VAR_SEQ 122 131 TEPEVHKTSV -> MLSPCLSSYF (in isoform 2).
FT /FTId=VSP_008467.
FT VAR_SEQ 318 340 QQAELALQEAIRIAQESNDHVCL -> TSPPWEYSPLFNRE
FT LLLGRRQTS (in isoform 2).
FT /FTId=VSP_008468.
FT VAR_SEQ 341 755 Missing (in isoform 2).
FT /FTId=VSP_008469.
FT VAR_SEQ 375 387 Missing (in isoform 3).
FT /FTId=VSP_044879.
FT VARIANT 617 617 Q -> H (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035793.
FT CONFLICT 24 24 F -> L (in Ref. 1; AAF05753).
SQ SEQUENCE 755 AA; 85077 MW; 174F68EAB44760EB CRC64;
MASVHESLYF NPMMTNGVVH ANVFGIKDWV TPYKIAVLVL LNEMSRTGEG AVSLMERRRL
NQLLLPLLQG PDITLSKLYK LIEESCPQLA NSVQIRIKLM AEGELKDMEQ FFDDLSDSFS
GTEPEVHKTS VVGLFLRHMI LAYSKLSFSQ VFKLYTALQQ YFQNGEKKTV EDADMELTSR
DEGERKMEKE ELDVSVREEE VSCSGPLSQK QAEFFLSQQA SLLKNDETKA LTPASLQKEL
NNLLKFNPDF AEAHYLSYLN NLRVQDVFSS THSLLHYFDR LILTGAESKS NGEEGYGRSL
RYAALNLAAL HCRFGHYQQA ELALQEAIRI AQESNDHVCL QHCLSWLYVL GQKRSDSYVL
LEHSVKKAVH FGLPYLASLG IQSLVQQRAF AGKTANKLMD ALKDSDLLHW KHSLSELIDI
SIAQKTAIWR LYGRSTMALQ QAQMLLSMNS LEAVNAGVQQ NNTESFAVAL CHLAELHAEQ
GCFAAASEVL KHLKERFPPN SQHAQLWMLC DQKIQFDRAM NDGKYHLADS LVTGITALNS
IEGVYRKAVV LQAQNQMSEA HKLLQKLLVH CQKLKNTEMV ISVLLSVAEL YWRSSSPTIA
LPMLLQALAL SKEYRLQYLA SETVLNLAFA QLILGIPEQA LSLLHMAIEP ILADGAILDK
GRAMFLVAKC QVASAASYDQ PKKAEALEAA IENLNEAKNY FAKVDCKERI RDVVYFQARL
YHTLGKTQER NRCAMLFRQL HQELPSHGVP LINHL
//
MIM
606948
*RECORD*
*FIELD* NO
606948
*FIELD* TI
*606948 ANAPHASE-PROMOTING COMPLEX, SUBUNIT 5; ANAPC5
;;APC5
*FIELD* TX
DESCRIPTION
read more
ANAPC5 is a subunit of the anaphase-promoting complex (APC), which
functions at the metaphase-to-anaphase transition of the cell cycle and
is regulated by spindle checkpoint proteins. The APC is an E3 ubiquitin
ligase that targets cell cycle regulatory proteins for degradation by
the proteasome, thereby allowing progression through the cell cycle
(summary by Jorgensen et al., 2001).
CLONING
By searching an EST database using frog APC peptide sequences, Yu et al.
(1998) obtained full-length cDNAs encoding APC2 (606946), APC4 (606947),
APC5, and APC7 (606949). The deduced 755-amino acid APC5 protein is
similar to a putative essential yeast protein. Yu et al. (1998) stated
that the APC is highly conserved from yeast to human.
GENE FUNCTION
Turnell et al. (2005) showed that 2 APC/cyclosome (APC/C) components,
APC5 and APC7, interact directly with the coactivators CBP (600140) and
p300 (602700) through protein-protein interaction domains that are
evolutionarily conserved in adenovirus E1A. This interaction stimulates
intrinsic CBP/p300 acetyltransferase activity and potentiates
CBP/p300-dependent transcription. Turnell et al. (2005) also showed that
APC5 and APC7 suppress E1A-mediated transformation in a
CBP/p300-dependent manner, indicating that these components of the APC/C
may be targeted during cellular transformation. Furthermore, Turnell et
al. (2005) established that CBP is required for APC/C function;
specifically, gene ablation of CBP by RNA-mediated interference markedly
reduces the E3 ubiquitin ligase activity of the APC/C and the
progression of cells through mitosis. Taken together, Turnell et al.
(2005) concluded that their results define discrete roles for the
APC/C-CBP/p300 complexes in growth regulation.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the ANAPC5
gene to chromosome 12 (TMAP WI-13062).
*FIELD* RF
1. Jorgensen, P. M.; Graslund, S.; Betz, R.; Stahl, S.; Larsson, C.;
Hoog, C.: Characterisation of the human APC1, the largest subunit
of the anaphase-promoting complex. Gene 262: 51-59, 2001.
2. Turnell, A. S.; Stewart, G. S.; Grand, R. J. A.; Rookes, S. M.;
Martin, A.; Yamano, H.; Elledge, S. J.; Gallimore, P. H.: The APC/C
and CBP/p300 cooperate to regulate transcription and cell-cycle progression. Nature 438:
690-695, 2005.
3. Yu, H.; Peters, J.-M.; King, R. W.; Page, A. M.; Hieter, P.; Kirschner,
M. W.: Identification of a cullin homology region in a subunit of
the anaphase-promoting complex. Science 279: 1219-1222, 1998.
*FIELD* CN
Ada Hamosh - updated: 1/30/2006
*FIELD* CD
Paul J. Converse: 5/16/2002
*FIELD* ED
carol: 12/30/2011
alopez: 2/1/2006
terry: 1/30/2006
mgross: 5/16/2002
*RECORD*
*FIELD* NO
606948
*FIELD* TI
*606948 ANAPHASE-PROMOTING COMPLEX, SUBUNIT 5; ANAPC5
;;APC5
*FIELD* TX
DESCRIPTION
read more
ANAPC5 is a subunit of the anaphase-promoting complex (APC), which
functions at the metaphase-to-anaphase transition of the cell cycle and
is regulated by spindle checkpoint proteins. The APC is an E3 ubiquitin
ligase that targets cell cycle regulatory proteins for degradation by
the proteasome, thereby allowing progression through the cell cycle
(summary by Jorgensen et al., 2001).
CLONING
By searching an EST database using frog APC peptide sequences, Yu et al.
(1998) obtained full-length cDNAs encoding APC2 (606946), APC4 (606947),
APC5, and APC7 (606949). The deduced 755-amino acid APC5 protein is
similar to a putative essential yeast protein. Yu et al. (1998) stated
that the APC is highly conserved from yeast to human.
GENE FUNCTION
Turnell et al. (2005) showed that 2 APC/cyclosome (APC/C) components,
APC5 and APC7, interact directly with the coactivators CBP (600140) and
p300 (602700) through protein-protein interaction domains that are
evolutionarily conserved in adenovirus E1A. This interaction stimulates
intrinsic CBP/p300 acetyltransferase activity and potentiates
CBP/p300-dependent transcription. Turnell et al. (2005) also showed that
APC5 and APC7 suppress E1A-mediated transformation in a
CBP/p300-dependent manner, indicating that these components of the APC/C
may be targeted during cellular transformation. Furthermore, Turnell et
al. (2005) established that CBP is required for APC/C function;
specifically, gene ablation of CBP by RNA-mediated interference markedly
reduces the E3 ubiquitin ligase activity of the APC/C and the
progression of cells through mitosis. Taken together, Turnell et al.
(2005) concluded that their results define discrete roles for the
APC/C-CBP/p300 complexes in growth regulation.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the ANAPC5
gene to chromosome 12 (TMAP WI-13062).
*FIELD* RF
1. Jorgensen, P. M.; Graslund, S.; Betz, R.; Stahl, S.; Larsson, C.;
Hoog, C.: Characterisation of the human APC1, the largest subunit
of the anaphase-promoting complex. Gene 262: 51-59, 2001.
2. Turnell, A. S.; Stewart, G. S.; Grand, R. J. A.; Rookes, S. M.;
Martin, A.; Yamano, H.; Elledge, S. J.; Gallimore, P. H.: The APC/C
and CBP/p300 cooperate to regulate transcription and cell-cycle progression. Nature 438:
690-695, 2005.
3. Yu, H.; Peters, J.-M.; King, R. W.; Page, A. M.; Hieter, P.; Kirschner,
M. W.: Identification of a cullin homology region in a subunit of
the anaphase-promoting complex. Science 279: 1219-1222, 1998.
*FIELD* CN
Ada Hamosh - updated: 1/30/2006
*FIELD* CD
Paul J. Converse: 5/16/2002
*FIELD* ED
carol: 12/30/2011
alopez: 2/1/2006
terry: 1/30/2006
mgross: 5/16/2002