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Database: UniProt
Entry: Q13200
LinkDB: Q13200
Original site: Q13200 
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   02-JUN-2021, entry version 211.
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=12; 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   SMR; Q13200; -.
DR   BioGRID; 111681; 284.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; Q13200; -.
DR   DIP; DIP-38204N; -.
DR   IntAct; Q13200; 195.
DR   MINT; Q13200; -.
DR   STRING; 9606.ENSP00000310129; -.
DR   ChEMBL; CHEMBL2364701; -.
DR   MoonDB; Q13200; Predicted.
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; 555 antibodies.
DR   DNASU; 5708; -.
DR   Ensembl; ENST00000310118; ENSP00000310129; ENSG00000175166. [Q13200-1]
DR   Ensembl; ENST00000435761; ENSP00000402618; ENSG00000175166. [Q13200-2]
DR   Ensembl; ENST00000439383; ENSP00000416028; ENSG00000175166. [Q13200-3]
DR   GeneID; 5708; -.
DR   KEGG; hsa:5708; -.
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:ENSG00000175166.16; -.
DR   eggNOG; KOG2005; Eukaryota.
DR   GeneTree; ENSGT00940000153386; -.
DR   HOGENOM; CLU_008705_1_0_1; -.
DR   InParanoid; Q13200; -.
DR   OMA; MVDICAY; -.
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-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; Q13200; -.
DR   BioGRID-ORCS; 5708; 756 hits in 1000 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 testis and 244 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: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; 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
//
DBGET integrated database retrieval system