PSMD2_HUMAN
ID PSMD2_HUMAN Reviewed; 908 AA.
AC Q13200; B4DX07; B4DXY1; E7EW34; E9PCS3; Q12932; Q15321; Q53XQ4; Q96I12;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 3.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 2;
DE AltName: Full=26S proteasome regulatory subunit RPN1;
DE AltName: Full=26S proteasome regulatory subunit S2;
DE AltName: Full=26S proteasome subunit p97;
DE AltName: Full=Protein 55.11;
DE AltName: Full=Tumor necrosis factor type 1 receptor-associated protein 2;
GN Name=PSMD2; Synonyms=TRAP2;
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], AND PROTEIN SEQUENCE OF 49-66; 81-85; 91-117;
RP 138-145; 148-158; 182-193; 209-229; 438-441 AND 471-481.
RC TISSUE=Fibrosarcoma;
RX PubMed=8774743; DOI=10.1111/j.1432-1033.1996.0912u.x;
RA Tsurumi C., Shimizu Y., Saeki M., Kato S., DeMartino G.N., Slaughter C.A.,
RA Fujimuro M., Yokosawa H., Yamasaki M., Hendil K.B., Toh-e A., Tanahashi N.,
RA Tanaka K.;
RT "cDNA cloning and functional analysis of the p97 subunit of the 26S
RT proteasome, a polypeptide identical to the type-1 tumor-necrosis-factor-
RT receptor-associated protein-2/55.11.";
RL Eur. J. Biochem. 239:912-921(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-724.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP ASP-313.
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=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-724.
RC TISSUE=Lung, Muscle, and 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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-908.
RX PubMed=9126987;
RA Dunbar J.D., Song H.Y., Guo D., Wu L.-W., Donner D.B.;
RT "Two-hybrid cloning of a gene encoding TNF receptor-associated protein 2, a
RT protein that interacts with the intracellular domain of the type 1 TNF
RT receptor: identity with subunit 2 of the 26S protease.";
RL J. Immunol. 158:4252-4259(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-908.
RC TISSUE=Liver;
RX PubMed=7601280; DOI=10.1016/0014-5793(95)00534-g;
RA Boldin M.P., Mett I.L., Wallach D.;
RT "A protein related to a proteasomal subunit binds to the intracellular
RT domain of the p55 TNF receptor upstream to its 'death domain'.";
RL FEBS Lett. 367:39-44(1995).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-24; SER-29 AND
RP TYR-194, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP 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 [15]
RP IDENTIFICATION BY MASS 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-361, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-24 AND SER-361, AND
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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-361, 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-147 AND SER-361, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-361 AND SER-363, AND
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 [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [23]
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 [24]
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 -!- FUNCTION: Binds to the intracellular domain of tumor necrosis factor
CC type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside
CC the death domain of TNFR1.
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 PSMD2 (PubMed:27428775, PubMed:27342858).
CC Interacts with RPGRIP1L (By similarity). Interacts with CRY1 in a KDM8-
CC dependent manner (By similarity). {ECO:0000250|UniProtKB:Q8VDM4,
CC ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775}.
CC -!- INTERACTION:
CC Q13200; Q16186: ADRM1; NbExp=3; IntAct=EBI-357648, EBI-954387;
CC Q13200; Q99933: BAG1; NbExp=8; IntAct=EBI-357648, EBI-1030678;
CC Q13200; P27797: CALR; NbExp=3; IntAct=EBI-357648, EBI-1049597;
CC Q13200; P36957: DLST; NbExp=3; IntAct=EBI-357648, EBI-351007;
CC Q13200; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-357648, EBI-739467;
CC Q13200; P58340: MLF1; NbExp=2; IntAct=EBI-357648, EBI-721328;
CC Q13200; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-357648, EBI-1055945;
CC Q13200; P17612: PRKACA; NbExp=3; IntAct=EBI-357648, EBI-476586;
CC Q13200; P62191: PSMC1; NbExp=16; IntAct=EBI-357648, EBI-357598;
CC Q13200; Q53XL8: PSMC1; NbExp=3; IntAct=EBI-357648, EBI-10242995;
CC Q13200; P35998: PSMC2; NbExp=4; IntAct=EBI-357648, EBI-359710;
CC Q13200; P62195: PSMC5; NbExp=10; IntAct=EBI-357648, EBI-357745;
CC Q13200; P55036: PSMD4; NbExp=3; IntAct=EBI-357648, EBI-359318;
CC Q13200; P54725: RAD23A; NbExp=3; IntAct=EBI-357648, EBI-746453;
CC Q13200; P50454: SERPINH1; NbExp=4; IntAct=EBI-357648, EBI-350723;
CC Q13200; Q13148: TARDBP; NbExp=3; IntAct=EBI-357648, EBI-372899;
CC Q13200; Q6DHY5: TBC1D3G; NbExp=3; IntAct=EBI-357648, EBI-13092532;
CC Q13200; P37173: TGFBR2; NbExp=3; IntAct=EBI-357648, EBI-296151;
CC Q13200; Q8WVY7: UBLCP1; NbExp=13; IntAct=EBI-357648, EBI-750011;
CC Q13200; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-357648, EBI-947187;
CC Q13200; Q9Y5K5: UCHL5; NbExp=5; IntAct=EBI-357648, EBI-1051183;
CC Q13200; Q9Y2B5: VPS9D1; NbExp=3; IntAct=EBI-357648, EBI-9031083;
CC Q13200; O15060: ZBTB39; NbExp=3; IntAct=EBI-357648, EBI-9995672;
CC Q13200; Q53HB3; NbExp=2; IntAct=EBI-357648, EBI-9362707;
CC Q13200; Q8AZK7: EBNA-LP; Xeno; NbExp=2; IntAct=EBI-357648, EBI-1185167;
CC Q13200; Q8K2C9: Hacd3; Xeno; NbExp=2; IntAct=EBI-357648, EBI-8329978;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q13200-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13200-2; Sequence=VSP_055065;
CC Name=3;
CC IsoId=Q13200-3; Sequence=VSP_055066;
CC -!- TISSUE SPECIFICITY: Found in skeletal muscle, liver, heart, brain,
CC kidney, pancreas, lung and placenta.
CC -!- SIMILARITY: Belongs to the proteasome subunit S2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA87705.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D78151; BAA11226.1; -; mRNA.
DR EMBL; BT009736; AAP88738.1; -; mRNA.
DR EMBL; AK301759; BAG63219.1; -; mRNA.
DR EMBL; AK302177; BAG63543.1; -; mRNA.
DR EMBL; AC078797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002368; AAH02368.1; -; mRNA.
DR EMBL; BC002997; AAH02997.1; -; mRNA.
DR EMBL; BC007897; AAH07897.1; -; mRNA.
DR EMBL; U12596; AAA87705.1; ALT_INIT; mRNA.
DR EMBL; X86446; CAA60167.1; -; mRNA.
DR CCDS; CCDS3258.1; -. [Q13200-1]
DR CCDS; CCDS63853.1; -. [Q13200-3]
DR CCDS; CCDS63854.1; -. [Q13200-2]
DR RefSeq; NP_001265637.1; NM_001278708.1. [Q13200-3]
DR RefSeq; NP_001265638.1; NM_001278709.1. [Q13200-2]
DR RefSeq; NP_002799.3; NM_002808.4. [Q13200-1]
DR PDB; 5GJQ; EM; 4.50 A; Z=1-908.
DR PDB; 5GJR; EM; 3.50 A; AC/Z=1-908.
DR PDB; 5L4K; EM; 4.50 A; Z=1-908.
DR PDB; 5LN3; EM; 6.80 A; Z=1-908.
DR PDB; 5T0C; EM; 3.80 A; Af/Bf=1-908.
DR PDB; 5T0G; EM; 4.40 A; f=164-908.
DR PDB; 5T0H; EM; 6.80 A; f=164-908.
DR PDB; 5T0I; EM; 8.00 A; f=164-908.
DR PDB; 5T0J; EM; 8.00 A; f=164-908.
DR PDB; 5VFP; EM; 4.20 A; f=1-908.
DR PDB; 5VFQ; EM; 4.20 A; f=1-908.
DR PDB; 5VFR; EM; 4.90 A; f=1-908.
DR PDB; 5VFS; EM; 3.60 A; f=6-853.
DR PDB; 5VFT; EM; 7.00 A; f=1-908.
DR PDB; 5VFU; EM; 5.80 A; f=1-908.
DR PDB; 5VHF; EM; 5.70 A; f=6-853.
DR PDB; 5VHH; EM; 6.10 A; f=6-853.
DR PDB; 5VHI; EM; 6.80 A; f=6-853.
DR PDB; 5VHJ; EM; 8.50 A; f=70-853.
DR PDB; 5VHM; EM; 8.30 A; f=6-853.
DR PDB; 5VHN; EM; 7.30 A; f=6-853.
DR PDB; 5VHO; EM; 8.30 A; f=6-853.
DR PDB; 5VHP; EM; 7.90 A; f=70-853.
DR PDB; 5VHQ; EM; 8.90 A; f=6-853.
DR PDB; 5VHR; EM; 7.70 A; f=6-853.
DR PDB; 5VHS; EM; 8.80 A; f=70-853.
DR PDB; 6MSB; EM; 3.00 A; f=1-908.
DR PDB; 6MSD; EM; 3.20 A; f=1-908.
DR PDB; 6MSG; EM; 3.50 A; f=1-892.
DR PDB; 6MSH; EM; 3.60 A; f=1-892.
DR PDB; 6MSJ; EM; 3.30 A; f=1-892.
DR PDB; 6MSK; EM; 3.20 A; f=1-892.
DR PDB; 6WJD; EM; 4.80 A; f=1-908.
DR PDB; 6WJN; EM; 5.70 A; f=1-908.
DR PDBsum; 5GJQ; -.
DR PDBsum; 5GJR; -.
DR PDBsum; 5L4K; -.
DR PDBsum; 5LN3; -.
DR PDBsum; 5T0C; -.
DR PDBsum; 5T0G; -.
DR PDBsum; 5T0H; -.
DR PDBsum; 5T0I; -.
DR PDBsum; 5T0J; -.
DR PDBsum; 5VFP; -.
DR PDBsum; 5VFQ; -.
DR PDBsum; 5VFR; -.
DR PDBsum; 5VFS; -.
DR PDBsum; 5VFT; -.
DR PDBsum; 5VFU; -.
DR PDBsum; 5VHF; -.
DR PDBsum; 5VHH; -.
DR PDBsum; 5VHI; -.
DR PDBsum; 5VHJ; -.
DR PDBsum; 5VHM; -.
DR PDBsum; 5VHN; -.
DR PDBsum; 5VHO; -.
DR PDBsum; 5VHP; -.
DR PDBsum; 5VHQ; -.
DR PDBsum; 5VHR; -.
DR PDBsum; 5VHS; -.
DR PDBsum; 6MSB; -.
DR PDBsum; 6MSD; -.
DR PDBsum; 6MSG; -.
DR PDBsum; 6MSH; -.
DR PDBsum; 6MSJ; -.
DR PDBsum; 6MSK; -.
DR PDBsum; 6WJD; -.
DR PDBsum; 6WJN; -.
DR AlphaFoldDB; Q13200; -.
DR SMR; Q13200; -.
DR BioGRID; 111681; 321.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; Q13200; -.
DR DIP; DIP-38204N; -.
DR IntAct; Q13200; 201.
DR MINT; Q13200; -.
DR STRING; 9606.ENSP00000310129; -.
DR ChEMBL; CHEMBL2364701; -.
DR MoonDB; Q13200; Predicted.
DR GlyGen; Q13200; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13200; -.
DR MetOSite; Q13200; -.
DR PhosphoSitePlus; Q13200; -.
DR SwissPalm; Q13200; -.
DR BioMuta; PSMD2; -.
DR DMDM; 6174930; -.
DR CPTAC; CPTAC-261; -.
DR EPD; Q13200; -.
DR jPOST; Q13200; -.
DR MassIVE; Q13200; -.
DR MaxQB; Q13200; -.
DR PaxDb; Q13200; -.
DR PeptideAtlas; Q13200; -.
DR PRIDE; Q13200; -.
DR ProteomicsDB; 18762; -.
DR ProteomicsDB; 19502; -.
DR ProteomicsDB; 59219; -. [Q13200-1]
DR Antibodypedia; 33807; 606 antibodies from 36 providers.
DR DNASU; 5708; -.
DR Ensembl; ENST00000310118.9; ENSP00000310129.4; ENSG00000175166.17. [Q13200-1]
DR Ensembl; ENST00000435761.5; ENSP00000402618.1; ENSG00000175166.17. [Q13200-2]
DR Ensembl; ENST00000439383.5; ENSP00000416028.1; ENSG00000175166.17. [Q13200-3]
DR GeneID; 5708; -.
DR KEGG; hsa:5708; -.
DR MANE-Select; ENST00000310118.9; ENSP00000310129.4; NM_002808.5; NP_002799.3.
DR UCSC; uc003fnn.3; human. [Q13200-1]
DR CTD; 5708; -.
DR DisGeNET; 5708; -.
DR GeneCards; PSMD2; -.
DR HGNC; HGNC:9559; PSMD2.
DR HPA; ENSG00000175166; Tissue enhanced (skeletal).
DR MIM; 606223; gene.
DR neXtProt; NX_Q13200; -.
DR OpenTargets; ENSG00000175166; -.
DR PharmGKB; PA33905; -.
DR VEuPathDB; HostDB:ENSG00000175166; -.
DR eggNOG; KOG2005; Eukaryota.
DR GeneTree; ENSGT00940000153386; -.
DR HOGENOM; CLU_008705_1_0_1; -.
DR InParanoid; Q13200; -.
DR OMA; KTVYKHM; -.
DR OrthoDB; 229956at2759; -.
DR PhylomeDB; Q13200; -.
DR TreeFam; TF105739; -.
DR PathwayCommons; Q13200; -.
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; Q13200; -.
DR SIGNOR; Q13200; -.
DR BioGRID-ORCS; 5708; 768 hits in 1087 CRISPR screens.
DR ChiTaRS; PSMD2; human.
DR GeneWiki; PSMD2; -.
DR GenomeRNAi; 5708; -.
DR Pharos; Q13200; Tbio.
DR PRO; PR:Q13200; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q13200; protein.
DR Bgee; ENSG00000175166; Expressed in secondary oocyte and 206 other tissues.
DR ExpressionAtlas; Q13200; baseline and differential.
DR Genevisible; Q13200; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; 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:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
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; IPR016643; 26S_Psome_Rpn1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR041433; RPN1_C.
DR InterPro; IPR040892; RPN1_N.
DR PANTHER; PTHR10943:SF11; PTHR10943:SF11; 1.
DR Pfam; PF01851; PC_rep; 2.
DR Pfam; PF18051; RPN1_C; 1.
DR Pfam; PF17781; RPN1_RPN2_N; 1.
DR PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Phosphoprotein; Proteasome; Reference proteome; Repeat.
FT CHAIN 1..908
FT /note="26S proteasome non-ATPase regulatory subunit 2"
FT /id="PRO_0000173810"
FT REPEAT 409..442
FT /note="PC 1"
FT REPEAT 443..479
FT /note="PC 2"
FT REPEAT 480..514
FT /note="PC 3"
FT REPEAT 517..551
FT /note="PC 4"
FT REPEAT 560..589
FT /note="PC 5"
FT REPEAT 692..723
FT /note="PC 6"
FT REPEAT 742..757
FT /note="PC 7"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDM4"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17323924, ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17323924,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17323924"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 194
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17323924"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 551
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDM4"
FT VAR_SEQ 1..163
FT /note="MEEGGRDKAPVQPQQSPAAAPGGTDEKPSGKERRDAGDKDKEQELSEEDKQL
FT QDELEMLVERLGEKDTSLYRPALEELRRQIRSSTTSMTSVPKPLKFLRPHYGKLKEIYE
FT NMAPGENKRFAADIISVLAMTMSGERECLKYRLVGSQEELASWGHEYVRHLA -> MSM
FT S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055065"
FT VAR_SEQ 1..130
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055066"
FT VARIANT 176
FT /note="A -> T (in dbSNP:rs11545172)"
FT /id="VAR_051554"
FT VARIANT 313
FT /note="E -> D (in dbSNP:rs11545169)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_051555"
FT VARIANT 724
FT /note="N -> Y (in dbSNP:rs17856236)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_067451"
FT CONFLICT 10
FT /note="P -> R (in Ref. 7; CAA60167)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="P -> S (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="E -> G (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="Q -> L (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="E -> V (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="V -> A (in Ref. 1; BAA11226)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="Y -> S (in Ref. 6; AAA87705)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="S -> T (in Ref. 7; CAA60167)"
FT /evidence="ECO:0000305"
FT CONFLICT 281..283
FT /note="IFT -> SS (in Ref. 6; AAA87705)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="G -> A (in Ref. 1; BAA11226)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="M -> MGM (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 776
FT /note="L -> P (in Ref. 3; BAG63219)"
FT /evidence="ECO:0000305"
FT CONFLICT 900..908
FT /note="LRKNPNYDL -> FGRTPIMISK (in Ref. 5 and 7)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 908 AA; 100200 MW; FAD71E7B26101BE3 CRC64;
MEEGGRDKAP VQPQQSPAAA PGGTDEKPSG KERRDAGDKD KEQELSEEDK QLQDELEMLV
ERLGEKDTSL YRPALEELRR QIRSSTTSMT SVPKPLKFLR PHYGKLKEIY ENMAPGENKR
FAADIISVLA MTMSGERECL KYRLVGSQEE LASWGHEYVR HLAGEVAKEW QELDDAEKVQ
REPLLTLVKE IVPYNMAHNA EHEACDLLME IEQVDMLEKD IDENAYAKVC LYLTSCVNYV
PEPENSALLR CALGVFRKFS RFPEALRLAL MLNDMELVED IFTSCKDVVV QKQMAFMLGR
HGVFLELSED VEEYEDLTEI MSNVQLNSNF LALARELDIM EPKVPDDIYK THLENNRFGG
SGSQVDSARM NLASSFVNGF VNAAFGQDKL LTDDGNKWLY KNKDHGMLSA AASLGMILLW
DVDGGLTQID KYLYSSEDYI KSGALLACGI VNSGVRNECD PALALLSDYV LHNSNTMRLG
SIFGLGLAYA GSNREDVLTL LLPVMGDSKS SMEVAGVTAL ACGMIAVGSC NGDVTSTILQ
TIMEKSETEL KDTYARWLPL GLGLNHLGKG EAIEAILAAL EVVSEPFRSF ANTLVDVCAY
AGSGNVLKVQ QLLHICSEHF DSKEKEEDKD KKEKKDKDKK EAPADMGAHQ GVAVLGIALI
AMGEEIGAEM ALRTFGHLLR YGEPTLRRAV PLALALISVS NPRLNILDTL SKFSHDADPE
VSYNSIFAMG MVGSGTNNAR LAAMLRQLAQ YHAKDPNNLF MVRLAQGLTH LGKGTLTLCP
YHSDRQLMSQ VAVAGLLTVL VSFLDVRNII LGKSHYVLYG LVAAMQPRML VTFDEELRPL
PVSVRVGQAV DVVGQAGKPK TITGFQTHTT PVLLAHGERA ELATEEFLPV TPILEGFVIL
RKNPNYDL
