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APC10_MOUSE
ID   APC10_MOUSE             Reviewed;         185 AA.
AC   Q8K2H6; Q9CW24;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Anaphase-promoting complex subunit 10;
DE            Short=APC10;
DE   AltName: Full=Cyclosome subunit 10;
GN   Name=Anapc10; Synonyms=Apc10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH PIWIL1.
RX   PubMed=23328397; DOI=10.1016/j.devcel.2012.12.006;
RA   Zhao S., Gou L.T., Zhang M., Zu L.D., Hua M.M., Hua Y., Shi H.J., Li Y.,
RA   Li J., Li D., Wang E.D., Liu M.F.;
RT   "piRNA-triggered MIWI ubiquitination and removal by APC/C in late
RT   spermatogenesis.";
RL   Dev. Cell 24:13-25(2013).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-169, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
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. The
CC       APC/C complex acts by mediating ubiquitination and subsequent
CC       degradation of target proteins: it mainly mediates the formation of
CC       'Lys-11'-linked polyubiquitin chains and, to a lower extent, the
CC       formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By
CC       similarity). {ECO:0000250|UniProtKB:Q9UM13}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: The mammalian APC/C is composed at least of 14 distinct
CC       subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6,
CC       ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and
CC       ANAPC16 that assemble into a complex of at least 19 chains with a
CC       combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1
CC       and FBXO5. The C-terminus of APC10 binds to CDC27/APC3 (By similarity).
CC       Interacts with PIWIL1; interaction only takes place when PIWIL1 binds
CC       piRNA (PubMed:23328397). {ECO:0000250|UniProtKB:Q9UM13,
CC       ECO:0000269|PubMed:23328397}.
CC   -!- SIMILARITY: Belongs to the APC10 family. {ECO:0000305}.
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DR   EMBL; AK005303; BAB23942.1; -; mRNA.
DR   EMBL; AK041373; BAC30921.1; -; mRNA.
DR   EMBL; BC031460; AAH31460.1; -; mRNA.
DR   CCDS; CCDS22439.1; -.
DR   RefSeq; NP_081180.1; NM_026904.2.
DR   RefSeq; XP_006531402.1; XM_006531339.3.
DR   RefSeq; XP_006531403.1; XM_006531340.3.
DR   RefSeq; XP_006531406.1; XM_006531343.3.
DR   AlphaFoldDB; Q8K2H6; -.
DR   SMR; Q8K2H6; -.
DR   BioGRID; 213166; 1.
DR   CORUM; Q8K2H6; -.
DR   IntAct; Q8K2H6; 2.
DR   MINT; Q8K2H6; -.
DR   STRING; 10090.ENSMUSP00000048244; -.
DR   iPTMnet; Q8K2H6; -.
DR   PhosphoSitePlus; Q8K2H6; -.
DR   EPD; Q8K2H6; -.
DR   MaxQB; Q8K2H6; -.
DR   PaxDb; Q8K2H6; -.
DR   PeptideAtlas; Q8K2H6; -.
DR   PRIDE; Q8K2H6; -.
DR   ProteomicsDB; 296367; -.
DR   Antibodypedia; 7474; 238 antibodies from 31 providers.
DR   DNASU; 68999; -.
DR   Ensembl; ENSMUST00000048147; ENSMUSP00000048244; ENSMUSG00000036977.
DR   Ensembl; ENSMUST00000210812; ENSMUSP00000148220; ENSMUSG00000036977.
DR   GeneID; 68999; -.
DR   KEGG; mmu:68999; -.
DR   UCSC; uc009miv.1; mouse.
DR   CTD; 10393; -.
DR   MGI; MGI:1916249; Anapc10.
DR   VEuPathDB; HostDB:ENSMUSG00000036977; -.
DR   eggNOG; KOG3437; Eukaryota.
DR   GeneTree; ENSGT00390000013722; -.
DR   HOGENOM; CLU_039415_3_0_1; -.
DR   InParanoid; Q8K2H6; -.
DR   OMA; FITIEFP; -.
DR   OrthoDB; 1588694at2759; -.
DR   PhylomeDB; Q8K2H6; -.
DR   TreeFam; TF105446; -.
DR   Reactome; R-MMU-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR   Reactome; R-MMU-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-MMU-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR   Reactome; R-MMU-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR   Reactome; R-MMU-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR   Reactome; R-MMU-176412; Phosphorylation of the APC/C.
DR   Reactome; R-MMU-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR   Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 68999; 22 hits in 73 CRISPR screens.
DR   ChiTaRS; Anapc10; mouse.
DR   PRO; PR:Q8K2H6; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8K2H6; protein.
DR   Bgee; ENSMUSG00000036977; Expressed in manus and 224 other tissues.
DR   Genevisible; Q8K2H6; MM.
DR   GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR   CDD; cd08366; APC10; 1.
DR   InterPro; IPR016901; APC10/Doc1.
DR   InterPro; IPR004939; APC_su10/DOC_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   PANTHER; PTHR12936; PTHR12936; 1.
DR   Pfam; PF03256; ANAPC10; 1.
DR   PIRSF; PIRSF028841; APC10_sub; 1.
DR   SMART; SM01337; APC10; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   PROSITE; PS51284; DOC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Cell division; Mitosis; Reference proteome;
KW   Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM13"
FT   CHAIN           2..185
FT                   /note="Anaphase-promoting complex subunit 10"
FT                   /id="PRO_0000174012"
FT   DOMAIN          2..185
FT                   /note="DOC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM13"
FT   MOD_RES         169
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
SQ   SEQUENCE   185 AA;  21266 MW;  9C198C42541A7C31 CRC64;
     MTTPNKTPPG ADPKQLERTA TVREIGSQAV WSLSSCKPGF GVDQLRDDNL ETYWQSDGSQ
     PHLVNIQFRR KTTVKTLCIY ADYKSDESYT PSKISVRVGN NFHNLQEIRQ LELVEPSGWI
     HVPLTDNHKK PTRTFMIQIA VLANHQNGRD THMRQIKIYT PVEESSIGKF PRCTTIDFMM
     YRSIR
 
 
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