PRS8_MOUSE
ID PRS8_MOUSE Reviewed; 406 AA.
AC P62196; O35051; P47210; P52915; P52916; Q3UL51; Q9CWN5;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=26S proteasome regulatory subunit 8;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT6;
DE AltName: Full=Proteasome 26S subunit ATPase 5;
DE AltName: Full=Proteasome subunit p45;
DE AltName: Full=p45/SUG;
DE Short=mSUG1;
GN Name=Psmc5; Synonyms=Sug1;
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 [MRNA], AND INTERACTION WITH NUCLEAR RECEPTORS.
RX PubMed=8598193;
RA Vom Baur E., Zechel C., Heery D., Heine M.J., Garnier J.-M., Vivat V.,
RA le Douarin B., Gronemeyer H., Chambon P., Losson R.;
RT "Differential ligand-dependent interactions between the AF-2 activating
RT domain of nuclear receptors and the putative transcriptional intermediary
RT factors mSUG1 and TIF1.";
RL EMBO J. 15:110-124(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and Muellerian duct;
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 [3]
RP IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX, AND ACETYLATION AT
RP ALA-2.
RX PubMed=16857966; DOI=10.1161/01.res.0000237386.98506.f7;
RA Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J.,
RA Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.;
RT "Mapping the murine cardiac 26S proteasome complexes.";
RL Circ. Res. 99:362-371(2006).
RN [4]
RP INTERACTION WITH PRPF19.
RX PubMed=17349974; DOI=10.1016/j.bbrc.2007.02.134;
RA Sihn C.R., Cho S.Y., Lee J.H., Lee T.R., Kim S.H.;
RT "Mouse homologue of yeast Prp19 interacts with mouse SUG1, the regulatory
RT subunit of 26S proteasome.";
RL Biochem. Biophys. Res. Commun. 356:175-180(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required. Therefore, the proteasome participates in numerous cellular
CC processes, including cell cycle progression, apoptosis, or DNA damage
CC repair. PSMC5 belongs to the heterohexameric ring of AAA (ATPases
CC associated with diverse cellular activities) proteins that unfolds
CC ubiquitinated target proteins that are concurrently translocated into a
CC proteolytic chamber and degraded into peptides.
CC {ECO:0000250|UniProtKB:P62195}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC regulatory subunits (RP) (By similarity). The regulatory particle is
CC made of a lid composed of 9 subunits, a base containing 6 ATPases
CC including PSMC5 and few additional components (By similarity).
CC Component of a complex with USP49 and RUVBL1 (By similarity). Interacts
CC with PRPF19 (PubMed:17349974). Interacts with TRIM5 (By similarity).
CC Interacts with NDC80 (By similarity). Interacts with PAAF1 (By
CC similarity). Interacts, in vitro, with the thyroid hormone receptor (in
CC a thyroid hormone T3-dependent manner) and with retinoid X receptor
CC (RXR) (PubMed:8598193). Interacts with ERCC6 (By similarity).
CC {ECO:0000250|UniProtKB:P62195, ECO:0000269|PubMed:17349974,
CC ECO:0000269|PubMed:8598193}.
CC -!- INTERACTION:
CC P62196; P19447: ERCC3; Xeno; NbExp=6; IntAct=EBI-357713, EBI-1183307;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62195}. Nucleus
CC {ECO:0000250|UniProtKB:P62195}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; Z54219; CAA90961.1; -; mRNA.
DR EMBL; AK010505; BAB26990.1; -; mRNA.
DR EMBL; AK135451; BAE22539.1; -; mRNA.
DR EMBL; AK145703; BAE26599.1; -; mRNA.
DR CCDS; CCDS25553.1; -.
DR PIR; S61923; S61923.
DR RefSeq; NP_032976.1; NM_008950.1.
DR AlphaFoldDB; P62196; -.
DR SMR; P62196; -.
DR BioGRID; 202430; 62.
DR DIP; DIP-35174N; -.
DR IntAct; P62196; 10.
DR MINT; P62196; -.
DR STRING; 10090.ENSMUSP00000021049; -.
DR iPTMnet; P62196; -.
DR PhosphoSitePlus; P62196; -.
DR SwissPalm; P62196; -.
DR REPRODUCTION-2DPAGE; IPI00135640; -.
DR REPRODUCTION-2DPAGE; P62196; -.
DR CPTAC; non-CPTAC-3857; -.
DR EPD; P62196; -.
DR jPOST; P62196; -.
DR MaxQB; P62196; -.
DR PaxDb; P62196; -.
DR PeptideAtlas; P62196; -.
DR PRIDE; P62196; -.
DR ProteomicsDB; 291682; -.
DR Antibodypedia; 18742; 313 antibodies from 35 providers.
DR DNASU; 19184; -.
DR Ensembl; ENSMUST00000021049; ENSMUSP00000021049; ENSMUSG00000020708.
DR GeneID; 19184; -.
DR KEGG; mmu:19184; -.
DR UCSC; uc007lyn.1; mouse.
DR CTD; 5705; -.
DR MGI; MGI:105047; Psmc5.
DR VEuPathDB; HostDB:ENSMUSG00000020708; -.
DR eggNOG; KOG0728; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR HOGENOM; CLU_000688_2_0_1; -.
DR InParanoid; P62196; -.
DR OMA; TANCRVA; -.
DR OrthoDB; 571919at2759; -.
DR PhylomeDB; P62196; -.
DR BRENDA; 5.6.1.5; 3474.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
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-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 19184; 25 hits in 72 CRISPR screens.
DR PRO; PR:P62196; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P62196; protein.
DR Bgee; ENSMUSG00000020708; Expressed in otic placode and 263 other tissues.
DR ExpressionAtlas; P62196; baseline and differential.
DR Genevisible; P62196; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0031597; C:cytosolic proteasome complex; ISO:MGI.
DR GO; GO:0016234; C:inclusion body; ISO:MGI.
DR GO; GO:0031595; C:nuclear proteasome complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0022624; C:proteasome accessory complex; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; ISS:UniProtKB.
DR GO; GO:0005838; C:proteasome regulatory particle; IDA:MGI.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0140296; F:general transcription initiation factor binding; ISS:UniProtKB.
DR GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; ISO:MGI.
DR GO; GO:0031531; F:thyrotropin-releasing hormone receptor binding; ISS:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0090261; P:positive regulation of inclusion body assembly; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005937; 26S_Psome_P45-like.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:16857966"
FT CHAIN 2..406
FT /note="26S proteasome regulatory subunit 8"
FT /id="PRO_0000084722"
FT REGION 186..406
FT /note="May mediate interaction with PRPF9"
FT /evidence="ECO:0000269|PubMed:17349974"
FT BINDING 190..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:16857966"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62195"
FT MOD_RES 222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62195"
FT CONFLICT 375
FT /note="R -> G (in Ref. 2; BAB26990)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 45626 MW; 29C6410C4A85A7F7 CRC64;
MALDGPEQME LEEGKAGSGL RQYYLSKIEE LQLIVNDKSQ NLRRLQAQRN ELNAKVRLLR
EELQLLQEQG SYVGEVVRAM DKKKVLVKVH PEGKFVVDVD KNIDINDVTP NCRVALRNDS
YTLHKILPNK VDPLVSLMMV EKVPDSTYEM IGGLDKQIKE IKEVIELPVK HPELFEALGI
AQPKGVLLYG PPGTGKTLLA RAVAHHTDCT FIRVSGSELV QKFIGEGARM VRELFVMARE
HAPSIIFMDE IDSIGSSRLE GGSGGDSEVQ RTMLELLNQL DGFEATKNIK VIMATNRIDI
LDSALLRPGR IDRKIEFPPP NEEARLDILK IHSRKMNLTR GINLRKIAEL MPGASGAEVK
GVCTEAGMYA LRERRVHVTQ EDFEMAVAKV MQKDSEKNMS IKKLWK
