ID PSMD5_HUMAN Reviewed; 504 AA. AC Q16401; B4DZM8; Q15045; Q4VXG8; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 09-APR-2025, entry version 207. 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 75-96; RP 311-337 AND 431-449. RC TISSUE=Mammary cancer; RX PubMed=7559544; DOI=10.1074/jbc.270.40.23726; RA Deveraux Q., Jensen C., Rechsteiner M.; RT "Molecular cloning and expression of a 26 S protease subunit enriched in RT dileucine repeats."; RL J. Biol. Chem. 270:23726-23729(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=7584044; DOI=10.1093/dnares/1.5.223; RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., RA Kawarabayasi Y., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. II. The RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 1:223-229(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; 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 [7] RP PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [8] RP PROTEIN SEQUENCE OF 2-10, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (OCT-2004) to UniProtKB. RN [9] RP FUNCTION AS PROTEASOME CHAPERONE, SUBUNIT, AND INTERACTION WITH PSMC2. RX PubMed=19490896; DOI=10.1016/j.cell.2009.05.008; RA Kaneko T., Hamazaki J., Iemura S., Sasaki K., Furuyama K., Natsume T., RA Tanaka K., Murata S.; RT "Assembly pathway of the Mammalian proteasome base subcomplex is mediated RT by multiple specific chaperones."; RL Cell 137:914-925(2009). RN [10] RP INTERACTION WITH PSMC1; PSMC2; PSMD1 AND PSMD6. RX PubMed=19217412; DOI=10.1016/j.molcel.2009.01.010; RA Le Tallec B., Barrault M.B., Guerois R., Carre T., Peyroche A.; RT "Hsm3/S5b participates in the assembly pathway of the 19S regulatory RT particle of the proteasome."; RL Mol. Cell 33:389-399(2009). RN [11] RP FUNCTION AS PROTEASOME CHAPERONE, AND INTERACTION WITH PSMC2. RX PubMed=19412159; DOI=10.1038/nature08063; RA Roelofs J., Park S., Haas W., Tian G., McAllister F.E., Huo Y., Lee B.H., RA Zhang F., Shi Y., Gygi S.P., Finley D.; RT "Chaperone-mediated pathway of proteasome regulatory particle assembly."; RL Nature 459:861-865(2009). RN [12] 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., Buerckstuemmer T., RA 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 [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). 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. {ECO:0000269|PubMed:19412159, CC ECO:0000269|PubMed:19490896}. 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:19217412, ECO:0000269|PubMed:19412159, CC ECO:0000269|PubMed:19490896}. CC -!- INTERACTION: CC Q16401; Q9H0C5: BTBD1; NbExp=3; IntAct=EBI-752143, EBI-935503; CC Q16401; Q9BX70: BTBD2; NbExp=3; IntAct=EBI-752143, EBI-710091; CC Q16401; Q8WTX7: CASTOR1; NbExp=3; IntAct=EBI-752143, EBI-10276168; CC Q16401; P49821: NDUFV1; NbExp=3; IntAct=EBI-752143, EBI-748312; CC Q16401; P62191: PSMC1; NbExp=14; IntAct=EBI-752143, EBI-357598; CC Q16401; P35998: PSMC2; NbExp=25; IntAct=EBI-752143, EBI-359710; CC Q16401; Q12800: TFCP2; NbExp=3; IntAct=EBI-752143, EBI-717422; CC Q16401; O76024: WFS1; NbExp=3; IntAct=EBI-752143, EBI-720609; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q16401-1; Sequence=Displayed; CC Name=2; CC IsoId=Q16401-2; Sequence=VSP_045176; 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}. CC -!- CAUTION: Was initially identified as a genuine component of the 26S CC proteasome. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; S79862; AAB35397.1; -; mRNA. DR EMBL; D31889; BAA06687.1; -; mRNA. DR EMBL; AK303007; BAG64140.1; -; mRNA. DR EMBL; AL161911; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW87471.1; -; Genomic_DNA. DR EMBL; BC014478; AAH14478.1; -; mRNA. DR CCDS; CCDS59143.1; -. [Q16401-2] DR CCDS; CCDS6824.1; -. [Q16401-1] DR RefSeq; NP_001257356.1; NM_001270427.2. [Q16401-2] DR RefSeq; NP_005038.1; NM_005047.4. [Q16401-1] DR AlphaFoldDB; Q16401; -. DR SMR; Q16401; -. DR BioGRID; 111684; 136. DR CORUM; Q16401; -. DR IntAct; Q16401; 61. DR MINT; Q16401; -. DR STRING; 9606.ENSP00000210313; -. DR GlyGen; Q16401; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q16401; -. DR MetOSite; Q16401; -. DR PhosphoSitePlus; Q16401; -. DR SwissPalm; Q16401; -. DR BioMuta; PSMD5; -. DR DMDM; 3122657; -. DR CPTAC; CPTAC-428; -. DR CPTAC; CPTAC-429; -. DR jPOST; Q16401; -. DR MassIVE; Q16401; -. DR PaxDb; 9606-ENSP00000210313; -. DR PeptideAtlas; Q16401; -. DR ProteomicsDB; 5609; -. DR ProteomicsDB; 60870; -. [Q16401-1] DR Pumba; Q16401; -. DR TopDownProteomics; Q16401-1; -. [Q16401-1] DR Antibodypedia; 757; 248 antibodies from 28 providers. DR DNASU; 5711; -. DR Ensembl; ENST00000210313.8; ENSP00000210313.2; ENSG00000095261.14. [Q16401-1] DR Ensembl; ENST00000373904.5; ENSP00000363011.5; ENSG00000095261.14. [Q16401-2] DR GeneID; 5711; -. DR KEGG; hsa:5711; -. DR MANE-Select; ENST00000210313.8; ENSP00000210313.2; NM_005047.4; NP_005038.1. DR UCSC; uc004bko.5; human. [Q16401-1] DR AGR; HGNC:9563; -. DR CTD; 5711; -. DR DisGeNET; 5711; -. DR GeneCards; PSMD5; -. DR HGNC; HGNC:9563; PSMD5. DR HPA; ENSG00000095261; Low tissue specificity. DR MIM; 604452; gene. DR neXtProt; NX_Q16401; -. DR OpenTargets; ENSG00000095261; -. DR PharmGKB; PA33909; -. DR VEuPathDB; HostDB:ENSG00000095261; -. DR eggNOG; KOG4413; Eukaryota. DR GeneTree; ENSGT00390000013040; -. DR HOGENOM; CLU_043710_0_0_1; -. DR InParanoid; Q16401; -. DR OMA; WGQEYIS; -. DR OrthoDB; 10250600at2759; -. DR PhylomeDB; Q16401; -. DR TreeFam; TF106231; -. DR PathwayCommons; Q16401; -. DR Reactome; R-HSA-9907900; Proteasome assembly. DR SignaLink; Q16401; -. DR BioGRID-ORCS; 5711; 11 hits in 1165 CRISPR screens. DR ChiTaRS; PSMD5; human. DR GeneWiki; PSMD5; -. DR GenomeRNAi; 5711; -. DR Pharos; Q16401; Tbio. DR PRO; PR:Q16401; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q16401; protein. DR Bgee; ENSG00000095261; Expressed in hair follicle and 211 other cell types or tissues. DR ExpressionAtlas; Q16401; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB. DR GO; GO:0000502; C:proteasome complex; TAS:ProtInc. DR GO; GO:0070682; P:proteasome regulatory particle assembly; IDA:UniProtKB. DR FunFam; 1.25.10.10:FF:000208; 26S proteasome non-ATPase regulatory subunit 5; 1. DR FunFam; 1.25.10.10:FF:000261; 26S proteasome non-ATPase regulatory subunit 5; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR019538; PSMD5. DR PANTHER; PTHR13554:SF10; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 5; 1. DR PANTHER; PTHR13554; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 5-RELATED; 1. DR Pfam; PF10508; Proteasom_PSMB; 1. DR SUPFAM; SSF48371; ARM repeat; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Chaperone; Direct protein sequencing; KW Proteomics identification; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.8, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..504 FT /note="26S proteasome non-ATPase regulatory subunit 5" FT /id="PRO_0000173835" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.8, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT VAR_SEQ 145..187 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045176" FT VARIANT 21 FT /note="E -> G (in dbSNP:rs2297575)" FT /id="VAR_051556" FT VARIANT 72 FT /note="L -> H (in dbSNP:rs17282618)" FT /id="VAR_051557" SQ SEQUENCE 504 AA; 56196 MW; 30F31602DDF4EF89 CRC64; MAAQALALLR EVARLEAPLE ELRALHSVLQ AVPLNELRQQ AAELRLGPLF SLLNENHREK TTLCVSILER LLQAMEPVHV ARNLRVDLQR GLIHPDDSVK ILTLSQIGRI VENSDAVTEI LNNAELLKQI VYCIGGENLS VAKAAIKSLS RISLTQAGLE ALFESNLLDD LKSVMKTNDI VRYRVYELII EISSVSPESL NYCTTSGLVT QLLRELTGED VLVRATCIEM VTSLAYTHHG RQYLAQEGVI DQISNIIVGA DSDPFSSFYL PGFVKFFGNL AVMDSPQQIC ERYPIFVEKV FEMIESQDPT MIGVAVDTVG ILGSNVEGKQ VLQKTGTRFE RLLMRIGHQS KNAPVELKIR CLDAISSLLY LPPEQQTDDL LRMTESWFSS LSRDPLELFR GISSQPFPEL HCAALKVFTA IANQPWAQKL MFNSPGFVEY VVDRSVEHDK ASKDAKYELV KALANSKTIA EIFGNPNYLR LRTYLSEGPY YVKPVSTTAV EGAE //