PSMD1_HUMAN
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 03-AUG-2022, entry version 202.
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};
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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 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 AlphaFoldDB; Q99460; -.
DR SMR; Q99460; -.
DR BioGRID; 111680; 323.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; Q99460; -.
DR DIP; DIP-27548N; -.
DR IntAct; Q99460; 90.
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; Q99460; -.
DR PeptideAtlas; Q99460; -.
DR PRIDE; Q99460; -.
DR ProteomicsDB; 78278; -. [Q99460-1]
DR ProteomicsDB; 78279; -. [Q99460-2]
DR Antibodypedia; 34412; 138 antibodies from 22 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 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; MIMVQQN; -.
DR OrthoDB; 235012at2759; -.
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-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q99460; -.
DR SIGNOR; Q99460; -.
DR BioGRID-ORCS; 5707; 782 hits in 1088 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 211 other tissues.
DR ExpressionAtlas; Q99460; baseline and differential.
DR Genevisible; Q99460; HS.
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; -; 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; IPR035266; PSMD1.
DR InterPro; IPR040623; RPN2_C.
DR PANTHER; PTHR10943:SF2; PTHR10943:SF2; 1.
DR Pfam; PF01851; PC_rep; 3.
DR Pfam; PF18004; RPN2_C; 1.
DR PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
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
