ID PSMD1_HUMAN Reviewed; 953 AA. AC Q99460; B8ZZH9; Q24JU0; Q53TI2; Q6GMU5; Q6P2P4; Q6PJM7; Q6PKG9; Q86VU1; AC Q8IV79; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 31-AUG-2004, sequence version 2. DT 27-MAR-2024, entry version 211. DE RecName: Full=26S proteasome non-ATPase regulatory subunit 1; DE AltName: Full=26S proteasome regulatory subunit RPN2; DE AltName: Full=26S proteasome regulatory subunit S1; DE AltName: Full=26S proteasome subunit p112; GN Name=PSMD1; 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). RX PubMed=8816993; DOI=10.1091/mbc.7.6.853; RA Yokota K., Kagawa S., Shimizu Y., Akioka H., Tsurumi C., Noda C., RA Fujimuro M., Yokosawa H., Fujiwara T., Takahashi E., Ohba M., Yamasaki M., RA DeMartino G.N., Slaughter C.A., Toh-e A., Tanaka K.; RT "cDNA cloning of p112, the largest regulatory subunit of the human 26s RT proteasome, and functional analysis of its yeast homologue, sen3p."; RL Mol. Biol. Cell 7:853-870(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Cervix, Liver, Lymph, Placenta, Testis, and Uterus; 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 [4] RP FUNCTION. RX PubMed=1317798; DOI=10.1111/j.1432-1033.1992.tb16961.x; RA Kanayama H.O., Tamura T., Ugai S., Kagawa S., Tanahashi N., Yoshimura T., RA Tanaka K., Ichihara A.; RT "Demonstration that a human 26S proteolytic complex consists of a RT proteasome and multiple associated protein components and hydrolyzes ATP RT and ubiquitin-ligated proteins by closely linked mechanisms."; RL Eur. J. Biochem. 206:567-578(1992). RN [5] RP INTERACTION WITH ADRM1. RX PubMed=16990800; DOI=10.1038/sj.emboj.7601338; RA Hamazaki J., Iemura S., Natsume T., Yashiroda H., Tanaka K., Murata S.; RT "A novel proteasome-interacting protein recruits the deubiquitinating RT enzyme UCH37 to 26S proteasomes."; RL EMBO J. 25:4524-4536(2006). RN [6] RP INTERACTION WITH ADRM1. RX PubMed=16906146; DOI=10.1038/ncb1460; RA Yao T., Song L., Xu W., DeMartino G.N., Florens L., Swanson S.K., RA Washburn M.P., Conaway R.C., Conaway J.W., Cohen R.E.; RT "Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme RT by Adrm1."; RL Nat. Cell Biol. 8:994-1002(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273; SER-290; THR-311 AND RP SER-315, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17323924; DOI=10.1021/bi061994u; RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.; RT "Mass spectrometric characterization of the affinity-purified human 26S RT proteasome complex."; RL Biochemistry 46:3553-3565(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273; THR-311; SER-315; RP THR-830 AND SER-834, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] 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). RN [18] RP INTERACTION WITH ZFAND1. RX PubMed=29804830; DOI=10.1016/j.molcel.2018.04.021; RA Turakhiya A., Meyer S.R., Marincola G., Boehm S., Vanselow J.T., RA Schlosser A., Hofmann K., Buchberger A.; RT "ZFAND1 recruits p97 and the 26S proteasome to promote the clearance of RT arsenite-induced stress granules."; RL Mol. Cell 70:906-919(2018). RN [19] RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT. RX PubMed=27428775; DOI=10.1038/nsmb.3273; RA Huang X., Luan B., Wu J., Shi Y.; RT "An atomic structure of the human 26S proteasome."; RL Nat. Struct. Mol. Biol. 23:778-785(2016). RN [20] RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), AND SUBUNIT. RX PubMed=27342858; DOI=10.1073/pnas.1608050113; RA Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G., RA Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.; RT "Structure of the human 26S proteasome at a resolution of 3.9 Aa."; RL Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016). 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. {ECO:0000269|PubMed:1317798}. 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). The regulatory particle is made of a lid CC composed of 9 subunits, a base containing 6 ATPases and few additional CC components including PSMD1 (PubMed:27428775, PubMed:27342858). CC Interacts with ADRM1 (PubMed:16990800, PubMed:16906146). Interacts with CC ZFAND1 (PubMed:29804830). {ECO:0000269|PubMed:16906146, CC ECO:0000269|PubMed:16990800, ECO:0000269|PubMed:27342858, CC ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:29804830}. CC -!- INTERACTION: CC Q99460; Q16186: ADRM1; NbExp=5; IntAct=EBI-357874, EBI-954387; CC Q99460-1; Q9JKV1: Adrm1; Xeno; NbExp=2; IntAct=EBI-15703973, EBI-8762776; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q99460-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99460-2; Sequence=VSP_011475; CC -!- SIMILARITY: Belongs to the proteasome subunit S1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH01053.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAH14013.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAH39845.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAH47897.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAH64398.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAH73833.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={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; D44466; BAA07918.1; -; mRNA. DR EMBL; AC009407; AAX93127.1; -; Genomic_DNA. DR EMBL; BC001053; AAH01053.1; ALT_SEQ; mRNA. DR EMBL; BC014013; AAH14013.1; ALT_SEQ; mRNA. DR EMBL; BC039845; AAH39845.1; ALT_SEQ; mRNA. DR EMBL; BC047897; AAH47897.1; ALT_SEQ; mRNA. DR EMBL; BC064398; AAH64398.1; ALT_SEQ; mRNA. DR EMBL; BC073833; AAH73833.1; ALT_SEQ; mRNA. DR EMBL; BC094720; AAH94720.1; -; mRNA. DR EMBL; BC112344; AAI12345.1; -; mRNA. DR EMBL; BC114434; AAI14435.1; -; mRNA. DR CCDS; CCDS2482.1; -. [Q99460-1] DR CCDS; CCDS54436.1; -. [Q99460-2] DR RefSeq; NP_001177966.1; NM_001191037.1. [Q99460-2] DR RefSeq; NP_002798.2; NM_002807.3. [Q99460-1] DR PDB; 5GJQ; EM; 4.50 A; N=1-953. DR PDB; 5GJR; EM; 3.50 A; 1/N=1-953. DR PDB; 5L4K; EM; 4.50 A; N=1-953. DR PDB; 5LN3; EM; 6.80 A; N=1-953. DR PDB; 5M32; EM; 3.80 A; i=1-953. DR PDB; 5T0C; EM; 3.80 A; AU/BU=1-953. DR PDB; 5T0G; EM; 4.40 A; U=1-953. DR PDB; 5T0H; EM; 6.80 A; U=1-953. DR PDB; 5T0I; EM; 8.00 A; U=1-953. DR PDB; 5T0J; EM; 8.00 A; U=1-953. DR PDB; 5V1Y; X-ray; 1.42 A; E/F=940-953. DR PDB; 5V1Z; X-ray; 2.00 A; E/F=932-953. DR PDB; 5VFP; EM; 4.20 A; U=7-917. DR PDB; 5VFQ; EM; 4.20 A; U=7-917. DR PDB; 5VFR; EM; 4.90 A; U=7-917. DR PDB; 5VFS; EM; 3.60 A; U=7-917. DR PDB; 5VFT; EM; 7.00 A; U=7-917. DR PDB; 5VFU; EM; 5.80 A; U=7-917. DR PDB; 5VGZ; EM; 3.70 A; U=1-935. DR PDB; 5VHF; EM; 5.70 A; U=95-935. DR PDB; 5VHH; EM; 6.10 A; U=1-935. DR PDB; 5VHI; EM; 6.80 A; U=1-935. DR PDB; 5VHS; EM; 8.80 A; U=1-935. DR PDB; 6CO4; NMR; -; B=940-953. DR PDB; 6MSB; EM; 3.00 A; U=1-953. DR PDB; 6MSD; EM; 3.20 A; U=1-953. DR PDB; 6MSE; EM; 3.30 A; C=142-210. DR PDB; 6MSG; EM; 3.50 A; U=1-953. DR PDB; 6MSH; EM; 3.60 A; U=1-953. DR PDB; 6MSJ; EM; 3.30 A; U=1-953. DR PDB; 6MSK; EM; 3.20 A; U=1-953. DR PDB; 6OI4; X-ray; 1.76 A; E/F=940-952. DR PDB; 6UYI; NMR; -; B=940-953. DR PDB; 6UYJ; NMR; -; B=940-953. DR PDB; 6WJD; EM; 4.80 A; U=1-953. DR PDB; 6WJN; EM; 5.70 A; U=7-917. DR PDB; 7QXN; EM; 3.70 A; U=1-953. DR PDB; 7QXP; EM; 3.60 A; U=1-953. DR PDB; 7QXU; EM; 4.30 A; U=1-953. DR PDB; 7QXW; EM; 4.10 A; U=1-953. DR PDB; 7QXX; EM; 4.40 A; U=1-953. DR PDB; 7QY7; EM; 4.70 A; U=1-953. DR PDB; 7QYA; EM; 4.80 A; U=1-953. DR PDB; 7QYB; EM; 4.10 A; U=1-953. DR PDB; 7W37; EM; 3.00 A; U=1-953. DR PDB; 7W38; EM; 3.10 A; U=1-953. DR PDB; 7W39; EM; 3.20 A; U=1-953. DR PDB; 7W3A; EM; 3.50 A; U=1-953. DR PDB; 7W3B; EM; 3.60 A; U=1-953. DR PDB; 7W3C; EM; 3.40 A; U=1-953. DR PDB; 7W3F; EM; 3.30 A; U=1-953. DR PDB; 7W3G; EM; 3.20 A; U=1-953. DR PDB; 7W3H; EM; 3.20 A; U=1-953. DR PDB; 7W3I; EM; 3.50 A; U=1-953. DR PDB; 7W3J; EM; 3.50 A; U=1-953. DR PDB; 7W3K; EM; 3.60 A; U=1-953. DR PDB; 7W3M; EM; 3.50 A; U=1-953. DR PDB; 8CVT; EM; 3.00 A; U=1-953. DR PDBsum; 5GJQ; -. DR PDBsum; 5GJR; -. DR PDBsum; 5L4K; -. DR PDBsum; 5LN3; -. DR PDBsum; 5M32; -. DR PDBsum; 5T0C; -. DR PDBsum; 5T0G; -. DR PDBsum; 5T0H; -. DR PDBsum; 5T0I; -. DR PDBsum; 5T0J; -. DR PDBsum; 5V1Y; -. DR PDBsum; 5V1Z; -. DR PDBsum; 5VFP; -. DR PDBsum; 5VFQ; -. DR PDBsum; 5VFR; -. DR PDBsum; 5VFS; -. DR PDBsum; 5VFT; -. DR PDBsum; 5VFU; -. DR PDBsum; 5VGZ; -. DR PDBsum; 5VHF; -. DR PDBsum; 5VHH; -. DR PDBsum; 5VHI; -. DR PDBsum; 5VHS; -. DR PDBsum; 6CO4; -. DR PDBsum; 6MSB; -. DR PDBsum; 6MSD; -. DR PDBsum; 6MSE; -. DR PDBsum; 6MSG; -. DR PDBsum; 6MSH; -. DR PDBsum; 6MSJ; -. DR PDBsum; 6MSK; -. DR PDBsum; 6OI4; -. DR PDBsum; 6UYI; -. DR PDBsum; 6UYJ; -. DR PDBsum; 6WJD; -. DR PDBsum; 6WJN; -. DR PDBsum; 7QXN; -. DR PDBsum; 7QXP; -. DR PDBsum; 7QXU; -. DR PDBsum; 7QXW; -. DR PDBsum; 7QXX; -. DR PDBsum; 7QY7; -. DR PDBsum; 7QYA; -. DR PDBsum; 7QYB; -. DR PDBsum; 7W37; -. DR PDBsum; 7W38; -. DR PDBsum; 7W39; -. DR PDBsum; 7W3A; -. DR PDBsum; 7W3B; -. DR PDBsum; 7W3C; -. DR PDBsum; 7W3F; -. DR PDBsum; 7W3G; -. DR PDBsum; 7W3H; -. DR PDBsum; 7W3I; -. DR PDBsum; 7W3J; -. DR PDBsum; 7W3K; -. DR PDBsum; 7W3M; -. DR PDBsum; 8CVT; -. DR AlphaFoldDB; Q99460; -. DR EMDB; EMD-14201; -. DR EMDB; EMD-14202; -. DR EMDB; EMD-14203; -. DR EMDB; EMD-14204; -. DR EMDB; EMD-14205; -. DR EMDB; EMD-14209; -. DR EMDB; EMD-14210; -. DR EMDB; EMD-14211; -. DR EMDB; EMD-8672; -. DR EMDB; EMD-8674; -. DR EMDB; EMD-8675; -. DR EMDB; EMD-8676; -. DR EMDB; EMD-8684; -. DR SMR; Q99460; -. DR BioGRID; 111680; 434. DR ComplexPortal; CPX-5993; 26S Proteasome complex. DR CORUM; Q99460; -. DR DIP; DIP-27548N; -. DR IntAct; Q99460; 95. DR MINT; Q99460; -. DR STRING; 9606.ENSP00000309474; -. DR ChEMBL; CHEMBL2364701; -. DR DrugCentral; Q99460; -. DR GlyGen; Q99460; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q99460; -. DR MetOSite; Q99460; -. DR PhosphoSitePlus; Q99460; -. DR SwissPalm; Q99460; -. DR BioMuta; PSMD1; -. DR DMDM; 51704332; -. DR CPTAC; CPTAC-119; -. DR CPTAC; CPTAC-120; -. DR EPD; Q99460; -. DR jPOST; Q99460; -. DR MassIVE; Q99460; -. DR MaxQB; Q99460; -. DR PaxDb; 9606-ENSP00000309474; -. DR PeptideAtlas; Q99460; -. DR ProteomicsDB; 78278; -. [Q99460-1] DR ProteomicsDB; 78279; -. [Q99460-2] DR Pumba; Q99460; -. DR Antibodypedia; 34412; 157 antibodies from 23 providers. DR DNASU; 5707; -. DR Ensembl; ENST00000308696.11; ENSP00000309474.6; ENSG00000173692.14. [Q99460-1] DR Ensembl; ENST00000373635.9; ENSP00000362738.4; ENSG00000173692.14. [Q99460-2] DR Ensembl; ENST00000677230.1; ENSP00000503068.1; ENSG00000173692.14. [Q99460-1] DR GeneID; 5707; -. DR KEGG; hsa:5707; -. DR MANE-Select; ENST00000308696.11; ENSP00000309474.6; NM_002807.4; NP_002798.2. DR UCSC; uc002vrm.3; human. [Q99460-1] DR AGR; HGNC:9554; -. DR CTD; 5707; -. DR DisGeNET; 5707; -. DR GeneCards; PSMD1; -. DR HGNC; HGNC:9554; PSMD1. DR HPA; ENSG00000173692; Low tissue specificity. DR MIM; 617842; gene. DR neXtProt; NX_Q99460; -. DR OpenTargets; ENSG00000173692; -. DR PharmGKB; PA33899; -. DR VEuPathDB; HostDB:ENSG00000173692; -. DR eggNOG; KOG2062; Eukaryota. DR GeneTree; ENSGT00940000153386; -. DR HOGENOM; CLU_002323_0_0_1; -. DR InParanoid; Q99460; -. DR OMA; IMFGRQE; -. DR OrthoDB; 151732at2759; -. DR PhylomeDB; Q99460; -. DR TreeFam; TF105742; -. DR BRENDA; 5.6.1.5; 2681. DR PathwayCommons; Q99460; -. 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-6798695; Neutrophil degranulation. 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-9824272; Somitogenesis. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q99460; -. DR SIGNOR; Q99460; -. DR BioGRID-ORCS; 5707; 811 hits in 1166 CRISPR screens. DR ChiTaRS; PSMD1; human. DR GeneWiki; PSMD1; -. DR GenomeRNAi; 5707; -. DR Pharos; Q99460; Tbio. DR PRO; PR:Q99460; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q99460; Protein. DR Bgee; ENSG00000173692; Expressed in tendon of biceps brachii and 213 other cell types or tissues. DR ExpressionAtlas; Q99460; baseline and differential. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB. DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB. DR GO; GO:0005838; C:proteasome regulatory particle; TAS:ProtInc. DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central. DR GO; GO:0034515; C:proteasome storage granule; IBA:GO_Central. DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ARUK-UCL. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR016642; 26S_Psome_Rpn2. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR002015; Proteasome/cyclosome_rpt. DR InterPro; IPR048570; PSMD1_RPN2_N. DR InterPro; IPR040623; RPN2_C. DR PANTHER; PTHR10943; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT; 1. DR PANTHER; PTHR10943:SF2; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 1; 1. DR Pfam; PF13646; HEAT_2; 1. DR Pfam; PF01851; PC_rep; 4. DR Pfam; PF18004; RPN2_C; 1. DR Pfam; PF21505; RPN2_N; 1. DR PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR Genevisible; Q99460; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Phosphoprotein; KW Proteasome; Reference proteome; Repeat. FT CHAIN 1..953 FT /note="26S proteasome non-ATPase regulatory subunit 1" FT /id="PRO_0000173801" FT REPEAT 403..436 FT /note="PC 1" FT REPEAT 441..474 FT /note="PC 2" FT REPEAT 476..510 FT /note="PC 3" FT REPEAT 511..545 FT /note="PC 4" FT REPEAT 547..580 FT /note="PC 5" FT REPEAT 581..616 FT /note="PC 6" FT REPEAT 617..649 FT /note="PC 7" FT REPEAT 651..685 FT /note="PC 8" FT REPEAT 686..726 FT /note="PC 9" FT REPEAT 729..761 FT /note="PC 10" FT REGION 279..318 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 839..881 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 930..953 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 839..874 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 939..953 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT MOD_RES 273 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17323924, FT ECO:0007744|PubMed:23186163" FT MOD_RES 290 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17323924" FT MOD_RES 310 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 311 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17323924, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 315 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17323924, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 720 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q3TXS7" FT MOD_RES 830 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 834 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 797..827 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_011475" FT CONFLICT 85 FT /note="G -> R (in Ref. 1; BAA07918)" FT /evidence="ECO:0000305" FT CONFLICT 616 FT /note="R -> S (in Ref. 1; BAA07918)" FT /evidence="ECO:0000305" SQ SEQUENCE 953 AA; 105836 MW; B8682146082D21FA CRC64; MITSAAGIIS LLDEDEPQLK EFALHKLNAV VNDFWAEISE SVDKIEVLYE DEGFRSRQFA ALVASKVFYH LGAFEESLNY ALGAGDLFNV NDNSEYVETI IAKCIDHYTK QCVENADLPE GEKKPIDQRL EGIVNKMFQR CLDDHKYKQA IGIALETRRL DVFEKTILES NDVPGMLAYS LKLCMSLMQN KQFRNKVLRV LVKIYMNLEK PDFINVCQCL IFLDDPQAVS DILEKLVKED NLLMAYQICF DLYESASQQF LSSVIQNLRT VGTPIASVPG STNTGTVPGS EKDSDSMETE EKTSSAFVGK TPEASPEPKD QTLKMIKILS GEMAIELHLQ FLIRNNNTDL MILKNTKDAV RNSVCHTATV IANSFMHCGT TSDQFLRDNL EWLARATNWA KFTATASLGV IHKGHEKEAL QLMATYLPKD TSPGSAYQEG GGLYALGLIH ANHGGDIIDY LLNQLKNASN DIVRHGGSLG LGLAAMGTAR QDVYDLLKTN LYQDDAVTGE AAGLALGLVM LGSKNAQAIE DMVGYAQETQ HEKILRGLAV GIALVMYGRM EEADALIESL CRDKDPILRR SGMYTVAMAY CGSGNNKAIR RLLHVAVSDV NDDVRRAAVE SLGFILFRTP EQCPSVVSLL SESYNPHVRY GAAMALGICC AGTGNKEAIN LLEPMTNDPV NYVRQGALIA SALIMIQQTE ITCPKVNQFR QLYSKVINDK HDDVMAKFGA ILAQGILDAG GHNVTISLQS RTGHTHMPSV VGVLVFTQFW FWFPLSHFLS LAYTPTCVIG LNKDLKMPKV QYKSNCKPST FAYPAPLEVP KEKEKEKVST AVLSITAKAK KKEKEKEKKE EEKMEVDEAE KKEEKEKKKE PEPNFQLLDN PARVMPAQLK VLTMPETCRY QPFKPLSIGG IIILKDTSED IEELVEPVAA HGPKIEEEEQ EPEPPEPFEY IDD //