PSMD5_MOUSE
ID PSMD5_MOUSE Reviewed; 504 AA.
AC Q8BJY1; A2AUB0; Q3UFV2; Q5DU49; Q8BMA9; Q8VEE9;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 5;
DE AltName: Full=26S protease subunit S5 basic;
DE AltName: Full=26S proteasome subunit S5B;
GN Name=Psmd5; Synonyms=Kiaa0072;
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;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-504.
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX.
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 [7]
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: Acts as a chaperone during the assembly of the 26S
CC proteasome, specifically of the base subcomplex of the PA700/19S
CC regulatory complex (RC). In the initial step of the base subcomplex
CC assembly is part of an intermediate PSMD5:PSMC2:PSMC1:PSMD2 module
CC which probably assembles with a PSMD10:PSMC4:PSMC5:PAAF1 module
CC followed by dissociation of PSMD5 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PSMC1, PSMC2, PSMD1 and PSMD6. Part of
CC transient complex containing PSMD5, PSMC2, PSMC1 and PSMD2 formed
CC during the assembly of the 26S proteasome.
CC {ECO:0000269|PubMed:16857966}.
CC -!- DOMAIN: Rich in dileucine repeats, which have been implicated in
CC trafficking of a variety of transmembrane proteins.
CC -!- SIMILARITY: Belongs to the proteasome subunit S5B/HSM3 family.
CC {ECO:0000305}.
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DR EMBL; AK032992; BAC28117.1; -; mRNA.
DR EMBL; AK078419; BAC37265.1; -; mRNA.
DR EMBL; AK145587; BAE26526.1; -; mRNA.
DR EMBL; AK148284; BAE28457.1; -; mRNA.
DR EMBL; AL929068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08630.1; -; Genomic_DNA.
DR EMBL; BC019112; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK220321; BAD90393.1; -; mRNA.
DR CCDS; CCDS15953.1; -.
DR RefSeq; NP_542121.2; NM_080554.2.
DR AlphaFoldDB; Q8BJY1; -.
DR SMR; Q8BJY1; -.
DR BioGRID; 211865; 44.
DR IntAct; Q8BJY1; 2.
DR STRING; 10090.ENSMUSP00000028225; -.
DR iPTMnet; Q8BJY1; -.
DR PhosphoSitePlus; Q8BJY1; -.
DR SwissPalm; Q8BJY1; -.
DR EPD; Q8BJY1; -.
DR jPOST; Q8BJY1; -.
DR MaxQB; Q8BJY1; -.
DR PaxDb; Q8BJY1; -.
DR PeptideAtlas; Q8BJY1; -.
DR PRIDE; Q8BJY1; -.
DR ProteomicsDB; 291703; -.
DR Antibodypedia; 757; 225 antibodies from 28 providers.
DR DNASU; 66998; -.
DR Ensembl; ENSMUST00000028225; ENSMUSP00000028225; ENSMUSG00000026869.
DR GeneID; 66998; -.
DR KEGG; mmu:66998; -.
DR UCSC; uc008jje.1; mouse.
DR CTD; 5711; -.
DR MGI; MGI:1914248; Psmd5.
DR VEuPathDB; HostDB:ENSMUSG00000026869; -.
DR eggNOG; KOG4413; Eukaryota.
DR GeneTree; ENSGT00390000013040; -.
DR HOGENOM; CLU_043710_0_0_1; -.
DR InParanoid; Q8BJY1; -.
DR OMA; LVAREWC; -.
DR OrthoDB; 602046at2759; -.
DR PhylomeDB; Q8BJY1; -.
DR TreeFam; TF106231; -.
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; 66998; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Psmd5; mouse.
DR PRO; PR:Q8BJY1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BJY1; protein.
DR Bgee; ENSMUSG00000026869; Expressed in fetal liver hematopoietic progenitor cell and 267 other tissues.
DR ExpressionAtlas; Q8BJY1; baseline and differential.
DR Genevisible; Q8BJY1; MM.
DR GO; GO:0022624; C:proteasome accessory complex; IDA:UniProtKB.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; ISO:MGI.
DR GO; GO:0070682; P:proteasome regulatory particle assembly; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR019538; PSMD5.
DR PANTHER; PTHR13554; PTHR13554; 1.
DR Pfam; PF10508; Proteasom_PSMB; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16401"
FT CHAIN 2..504
FT /note="26S proteasome non-ATPase regulatory subunit 5"
FT /id="PRO_0000173837"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q16401"
FT CONFLICT 158
FT /note="G -> V (in Ref. 1; BAC37265)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="L -> P (in Ref. 4; BC019112)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="H -> L (in Ref. 5; BAD90393)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 55972 MW; 66D56A2BD43B895C CRC64;
MAAQAVSLLR EVARLEAPLE ELRALQSVVQ AVPLHELREQ AAELRLRPLF SLLNQNNREQ
TALCVSILER LLQAVEPIHL ARNLRLDLQR GLTHPDDSVK TLTLSQIGRI VENSEAVTEI
LNNAELLKQI VYCIGGENLS VAKAAIKSLS RISLTQAGLE ALFESNLLDD LKNVMKTNDV
VRYRVYELII DISSVSSESL NYCTTSGLVT QLLKELTGED VLVRATCIEM VTSLAYTHHG
RQYLAQEGVI DQISNIIVGA DSDPFSGFYL PGFVKFFGNL AVMDSPQQIC ERYPVFLEKV
FEMADSQDPT MIGVAVDTVG ILGSSVEGKQ VLQKTGTRFE RVLMRVGYQA KNASTELKIR
CLDAVSSLLY LSPEQQTDDF LGMTESWFSS MSRDSLELFR GISNQPFPEL HCAALKVFTA
IADQPWAQRL MFNSPGFVEF VMDRSVEHDK ASKDAKYELV KALANSKTVA EIFGNSNYLR
LRAYLSEGPY YVKPVATTAV EGAD
