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Database: UniProt
Entry: Q99460
LinkDB: Q99460
Original site: Q99460 
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   02-JUN-2021, entry version 198.
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   SMR; Q99460; -.
DR   BioGRID; 111680; 269.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; Q99460; -.
DR   DIP; DIP-27548N; -.
DR   IntAct; Q99460; 81.
DR   MINT; Q99460; -.
DR   STRING; 9606.ENSP00000309474; -.
DR   ChEMBL; CHEMBL2364701; -.
DR   DrugCentral; Q99460; -.
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; 132 antibodies.
DR   DNASU; 5707; -.
DR   Ensembl; ENST00000308696; ENSP00000309474; ENSG00000173692. [Q99460-1]
DR   Ensembl; ENST00000373635; ENSP00000362738; ENSG00000173692. [Q99460-2]
DR   Ensembl; ENST00000677230; ENSP00000503068; ENSG00000173692. [Q99460-1]
DR   GeneID; 5707; -.
DR   KEGG; hsa:5707; -.
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:ENSG00000173692.12; -.
DR   eggNOG; KOG2062; Eukaryota.
DR   GeneTree; ENSGT00940000153386; -.
DR   HOGENOM; CLU_002323_0_0_1; -.
DR   InParanoid; Q99460; -.
DR   OMA; TGNLNMA; -.
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-68827; CDT1 association with the CDC6:ORC:origin 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-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SIGNOR; Q99460; -.
DR   BioGRID-ORCS; 5707; 771 hits in 1000 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 and 252 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:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
DR   GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0036388; P:pre-replicative complex assembly; TAS:Reactome.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR   GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
DR   GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR   GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
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
//
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