PSMD5_HUMAN
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 03-AUG-2022, entry version 192.
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=12; IntAct=EBI-752143, EBI-357598;
CC Q16401; P35998: PSMC2; NbExp=23; 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}.
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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_001270427.1. [Q16401-2]
DR RefSeq; NP_005038.1; NM_005047.3. [Q16401-1]
DR AlphaFoldDB; Q16401; -.
DR SMR; Q16401; -.
DR BioGRID; 111684; 119.
DR CORUM; Q16401; -.
DR IntAct; Q16401; 47.
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 BioMuta; PSMD5; -.
DR DMDM; 3122657; -.
DR CPTAC; CPTAC-428; -.
DR CPTAC; CPTAC-429; -.
DR EPD; Q16401; -.
DR jPOST; Q16401; -.
DR MassIVE; Q16401; -.
DR MaxQB; Q16401; -.
DR PaxDb; Q16401; -.
DR PeptideAtlas; Q16401; -.
DR PRIDE; Q16401; -.
DR ProteomicsDB; 5609; -.
DR ProteomicsDB; 60870; -. [Q16401-1]
DR TopDownProteomics; Q16401-1; -. [Q16401-1]
DR Antibodypedia; 757; 225 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 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; LVAREWC; -.
DR OrthoDB; 602046at2759; -.
DR PhylomeDB; Q16401; -.
DR TreeFam; TF106231; -.
DR PathwayCommons; Q16401; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q16401; -.
DR BioGRID-ORCS; 5711; 10 hits in 1078 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 209 other tissues.
DR ExpressionAtlas; Q16401; baseline and differential.
DR Genevisible; Q16401; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; 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 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; Alternative splicing; Chaperone; Direct protein sequencing;
KW 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
