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26S proteasome non-ATPase regulatory subunit 2 (26S proteasome regulatory subunit RPN1) (26S proteasome regulatory subunit S2) (26S proteasome subunit p97) (Protein 55.11) (Tumor necrosis factor type 1 receptor-associated protein 2)

 PSMD2_HUMAN             Reviewed;         908 AA.
Q13200; B4DX07; B4DXY1; E7EW34; E9PCS3; Q12932; Q15321; Q53XQ4;
Q96I12;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 3.
12-SEP-2018, entry version 191.
RecName: Full=26S proteasome non-ATPase regulatory subunit 2;
AltName: Full=26S proteasome regulatory subunit RPN1;
AltName: Full=26S proteasome regulatory subunit S2;
AltName: Full=26S proteasome subunit p97;
AltName: Full=Protein 55.11;
AltName: Full=Tumor necrosis factor type 1 receptor-associated protein 2;
Name=PSMD2; Synonyms=TRAP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 49-66; 81-85;
91-117; 138-145; 148-158; 182-193; 209-229; 438-441 AND 471-481.
TISSUE=Fibrosarcoma;
PubMed=8774743; DOI=10.1111/j.1432-1033.1996.0912u.x;
Tsurumi C., Shimizu Y., Saeki M., Kato S., DeMartino G.N.,
Slaughter C.A., Fujimuro M., Yokosawa H., Yamasaki M., Hendil K.B.,
Toh-e A., Tanahashi N., Tanaka K.;
"cDNA cloning and functional analysis of the p97 subunit of the 26S
proteasome, a polypeptide identical to the type-1 tumor-necrosis-
factor-receptor-associated protein-2/55.11.";
Eur. J. Biochem. 239:912-921(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-724.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
ASP-313.
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-724.
TISSUE=Lung, Muscle, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-908.
PubMed=9126987;
Dunbar J.D., Song H.Y., Guo D., Wu L.-W., Donner D.B.;
"Two-hybrid cloning of a gene encoding TNF receptor-associated protein
2, a protein that interacts with the intracellular domain of the type
1 TNF receptor: identity with subunit 2 of the 26S protease.";
J. Immunol. 158:4252-4259(1997).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-908.
TISSUE=Liver;
PubMed=7601280; DOI=10.1016/0014-5793(95)00534-G;
Boldin M.P., Mett I.L., Wallach D.;
"A protein related to a proteasomal subunit binds to the intracellular
domain of the p55 TNF receptor upstream to its 'death domain'.";
FEBS Lett. 367:39-44(1995).
[8]
FUNCTION.
PubMed=1317798; DOI=10.1111/j.1432-1033.1992.tb16961.x;
Kanayama H.O., Tamura T., Ugai S., Kagawa S., Tanahashi N.,
Yoshimura T., Tanaka K., Ichihara A.;
"Demonstration that a human 26S proteolytic complex consists of a
proteasome and multiple associated protein components and hydrolyzes
ATP and ubiquitin-ligated proteins by closely linked mechanisms.";
Eur. J. Biochem. 206:567-578(1992).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-24; SER-29 AND
TYR-194, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human
26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-361, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-24 AND SER-361,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-361, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-147 AND SER-361,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-361 AND SER-363,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
PubMed=27428775; DOI=10.1038/nsmb.3273;
Huang X., Luan B., Wu J., Shi Y.;
"An atomic structure of the human 26S proteasome.";
Nat. Struct. Mol. Biol. 23:778-785(2016).
[23]
STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), AND SUBUNIT.
PubMed=27342858; DOI=10.1073/pnas.1608050113;
Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
"Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
-!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
involved in the ATP-dependent degradation of ubiquitinated
proteins. This complex plays a key role in the maintenance of
protein homeostasis by removing misfolded or damaged proteins,
which could impair cellular functions, and by removing proteins
whose functions are no longer required. Therefore, the proteasome
participates in numerous cellular processes, including cell cycle
progression, apoptosis, or DNA damage repair.
{ECO:0000269|PubMed:1317798}.
-!- FUNCTION: Binds to the intracellular domain of tumor necrosis
factor type 1 receptor. The binding domain of TRAP1 and TRAP2
resides outside the death domain of TNFR1.
-!- SUBUNIT: Component of the 19S proteasome regulatory particle
complex. The 26S proteasome consists of a 20S core particle (CP)
and two 19S regulatory subunits (RP). The regulatory particle is
made of a lid composed of 9 subunits, a base containing 6 ATPases
and few additional components including PSMD2 (PubMed:27428775,
PubMed:27342858). Interacts with RPGRIP1L (By similarity).
{ECO:0000250|UniProtKB:Q8VDM4, ECO:0000269|PubMed:27342858,
ECO:0000269|PubMed:27428775}.
-!- INTERACTION:
Q53HB3:-; NbExp=2; IntAct=EBI-357648, EBI-9362707;
Q99933:BAG1; NbExp=7; IntAct=EBI-357648, EBI-1030678;
Q8AZK7:EBNA-LP (xeno); NbExp=2; IntAct=EBI-357648, EBI-1185167;
Q8K2C9:Hacd3 (xeno); NbExp=2; IntAct=EBI-357648, EBI-8329978;
P58340:MLF1; NbExp=2; IntAct=EBI-357648, EBI-721328;
P62191:PSMC1; NbExp=16; IntAct=EBI-357648, EBI-357598;
Q53XL8:PSMC1; NbExp=3; IntAct=EBI-357648, EBI-10242995;
P35998:PSMC2; NbExp=3; IntAct=EBI-357648, EBI-359710;
P62195:PSMC5; NbExp=9; IntAct=EBI-357648, EBI-357745;
P55036:PSMD4; NbExp=3; IntAct=EBI-357648, EBI-359318;
Q8WVY7:UBLCP1; NbExp=10; IntAct=EBI-357648, EBI-750011;
Q9Y5K5:UCHL5; NbExp=5; IntAct=EBI-357648, EBI-1051183;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q13200-1; Sequence=Displayed;
Name=2;
IsoId=Q13200-2; Sequence=VSP_055065;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q13200-3; Sequence=VSP_055066;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Found in skeletal muscle, liver, heart, brain,
kidney, pancreas, lung and placenta.
-!- SIMILARITY: Belongs to the proteasome subunit S2 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA87705.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; D78151; BAA11226.1; -; mRNA.
EMBL; BT009736; AAP88738.1; -; mRNA.
EMBL; AK301759; BAG63219.1; -; mRNA.
EMBL; AK302177; BAG63543.1; -; mRNA.
EMBL; AC078797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002368; AAH02368.1; -; mRNA.
EMBL; BC002997; AAH02997.1; -; mRNA.
EMBL; BC007897; AAH07897.1; -; mRNA.
EMBL; U12596; AAA87705.1; ALT_INIT; mRNA.
EMBL; X86446; CAA60167.1; -; mRNA.
CCDS; CCDS3258.1; -. [Q13200-1]
CCDS; CCDS63853.1; -. [Q13200-3]
CCDS; CCDS63854.1; -. [Q13200-2]
RefSeq; NP_001265637.1; NM_001278708.1. [Q13200-3]
RefSeq; NP_001265638.1; NM_001278709.1. [Q13200-2]
RefSeq; NP_002799.3; NM_002808.4. [Q13200-1]
UniGene; Hs.518464; -.
PDB; 5GJQ; EM; 4.50 A; Z=1-908.
PDB; 5GJR; EM; 3.50 A; AC/Z=1-908.
PDB; 5L4K; EM; 4.50 A; Z=1-908.
PDB; 5LN3; EM; 6.80 A; Z=1-908.
PDB; 5T0C; EM; 3.80 A; Af/Bf=1-908.
PDB; 5T0G; EM; 4.40 A; f=164-908.
PDB; 5T0H; EM; 6.80 A; f=164-908.
PDB; 5T0I; EM; 8.00 A; f=164-908.
PDB; 5T0J; EM; 8.00 A; f=164-908.
PDB; 5VHF; EM; 5.70 A; f=6-853.
PDB; 5VHH; EM; 6.10 A; f=6-853.
PDB; 5VHI; EM; 6.80 A; f=6-853.
PDB; 5VHJ; EM; 8.50 A; f=70-853.
PDB; 5VHM; EM; 8.30 A; f=6-853.
PDB; 5VHN; EM; 7.30 A; f=6-853.
PDB; 5VHO; EM; 8.30 A; f=6-853.
PDB; 5VHP; EM; 7.90 A; f=70-853.
PDB; 5VHQ; EM; 8.90 A; f=6-853.
PDB; 5VHR; EM; 7.70 A; f=6-853.
PDB; 5VHS; EM; 8.80 A; f=70-853.
PDBsum; 5GJQ; -.
PDBsum; 5GJR; -.
PDBsum; 5L4K; -.
PDBsum; 5LN3; -.
PDBsum; 5T0C; -.
PDBsum; 5T0G; -.
PDBsum; 5T0H; -.
PDBsum; 5T0I; -.
PDBsum; 5T0J; -.
PDBsum; 5VHF; -.
PDBsum; 5VHH; -.
PDBsum; 5VHI; -.
PDBsum; 5VHJ; -.
PDBsum; 5VHM; -.
PDBsum; 5VHN; -.
PDBsum; 5VHO; -.
PDBsum; 5VHP; -.
PDBsum; 5VHQ; -.
PDBsum; 5VHR; -.
PDBsum; 5VHS; -.
ProteinModelPortal; Q13200; -.
SMR; Q13200; -.
BioGrid; 111681; 186.
CORUM; Q13200; -.
DIP; DIP-38204N; -.
IntAct; Q13200; 158.
MINT; Q13200; -.
STRING; 9606.ENSP00000310129; -.
ChEMBL; CHEMBL2364701; -.
MoonDB; Q13200; Predicted.
iPTMnet; Q13200; -.
PhosphoSitePlus; Q13200; -.
SwissPalm; Q13200; -.
BioMuta; PSMD2; -.
DMDM; 6174930; -.
EPD; Q13200; -.
MaxQB; Q13200; -.
PaxDb; Q13200; -.
PeptideAtlas; Q13200; -.
PRIDE; Q13200; -.
ProteomicsDB; 59219; -.
DNASU; 5708; -.
Ensembl; ENST00000310118; ENSP00000310129; ENSG00000175166. [Q13200-1]
Ensembl; ENST00000435761; ENSP00000402618; ENSG00000175166. [Q13200-2]
Ensembl; ENST00000439383; ENSP00000416028; ENSG00000175166. [Q13200-3]
GeneID; 5708; -.
KEGG; hsa:5708; -.
UCSC; uc003fnn.3; human. [Q13200-1]
CTD; 5708; -.
DisGeNET; 5708; -.
EuPathDB; HostDB:ENSG00000175166.16; -.
GeneCards; PSMD2; -.
HGNC; HGNC:9559; PSMD2.
HPA; HPA045192; -.
MIM; 606223; gene.
neXtProt; NX_Q13200; -.
OpenTargets; ENSG00000175166; -.
PharmGKB; PA33905; -.
eggNOG; KOG2005; Eukaryota.
eggNOG; COG5110; LUCA.
GeneTree; ENSGT00550000074983; -.
HOGENOM; HOG000176022; -.
HOVERGEN; HBG001842; -.
InParanoid; Q13200; -.
KO; K03028; -.
OMA; MVDICAY; -.
OrthoDB; EOG091G04TC; -.
PhylomeDB; Q13200; -.
TreeFam; TF105739; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; PSMD2; human.
GeneWiki; PSMD2; -.
GenomeRNAi; 5708; -.
PRO; PR:Q13200; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000175166; Expressed in 231 organ(s), highest expression level in testis.
CleanEx; HS_PSMD2; -.
ExpressionAtlas; Q13200; baseline and differential.
Genevisible; Q13200; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0005838; C:proteasome regulatory particle; TAS:ProtInc.
GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
GO; GO:0034515; C:proteasome storage granule; IBA:GO_Central.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR016643; 26S_Psome_Rpn1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002015; Proteasome/cyclosome_rpt.
PANTHER; PTHR10943:SF1; PTHR10943:SF1; 1.
Pfam; PF01851; PC_rep; 2.
PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
SUPFAM; SSF48371; SSF48371; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Phosphoprotein; Polymorphism; Proteasome;
Reference proteome; Repeat.
CHAIN 1 908 26S proteasome non-ATPase regulatory
subunit 2.
/FTId=PRO_0000173810.
REPEAT 409 442 PC 1.
REPEAT 443 479 PC 2.
REPEAT 480 514 PC 3.
REPEAT 517 551 PC 4.
REPEAT 560 589 PC 5.
REPEAT 692 723 PC 6.
REPEAT 742 757 PC 7.
COMPBIAS 623 641 Glu/Lys-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q8VDM4}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17323924,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 24 24 Phosphothreonine.
{ECO:0000244|PubMed:17323924,
ECO:0000244|PubMed:20068231}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:17323924}.
MOD_RES 147 147 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 194 194 Phosphotyrosine.
{ECO:0000244|PubMed:17323924}.
MOD_RES 361 361 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 551 551 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDM4}.
VAR_SEQ 1 163 MEEGGRDKAPVQPQQSPAAAPGGTDEKPSGKERRDAGDKDK
EQELSEEDKQLQDELEMLVERLGEKDTSLYRPALEELRRQI
RSSTTSMTSVPKPLKFLRPHYGKLKEIYENMAPGENKRFAA
DIISVLAMTMSGERECLKYRLVGSQEELASWGHEYVRHLA
-> MSMS (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055065.
VAR_SEQ 1 130 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055066.
VARIANT 176 176 A -> T (in dbSNP:rs11545172).
/FTId=VAR_051554.
VARIANT 313 313 E -> D (in dbSNP:rs11545169).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_051555.
VARIANT 724 724 N -> Y (in dbSNP:rs17856236).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2}.
/FTId=VAR_067451.
CONFLICT 10 10 P -> R (in Ref. 7; CAA60167).
{ECO:0000305}.
CONFLICT 21 21 P -> S (in Ref. 6). {ECO:0000305}.
CONFLICT 32 32 E -> G (in Ref. 6). {ECO:0000305}.
CONFLICT 43 43 Q -> L (in Ref. 6). {ECO:0000305}.
CONFLICT 57 57 E -> V (in Ref. 6). {ECO:0000305}.
CONFLICT 60 60 V -> A (in Ref. 1; BAA11226).
{ECO:0000305}.
CONFLICT 226 226 Y -> S (in Ref. 6; AAA87705).
{ECO:0000305}.
CONFLICT 260 260 S -> T (in Ref. 7; CAA60167).
{ECO:0000305}.
CONFLICT 281 283 IFT -> SS (in Ref. 6; AAA87705).
{ECO:0000305}.
CONFLICT 415 415 G -> A (in Ref. 1; BAA11226).
{ECO:0000305}.
CONFLICT 731 731 M -> MGM (in Ref. 6). {ECO:0000305}.
CONFLICT 776 776 L -> P (in Ref. 3; BAG63219).
{ECO:0000305}.
CONFLICT 900 908 LRKNPNYDL -> FGRTPIMISK (in Ref. 5 and
7). {ECO:0000305}.
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


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