Full text data of PSMD2
PSMD2
(TRAP2)
[Confidence: high (present in two of the MS resources)]
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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00012268
IPI00012268 26S proteasome non-ATPase regulatory subunit 5 Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00012268 26S proteasome non-ATPase regulatory subunit 5 Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q13200
ID PSMD2_HUMAN Reviewed; 908 AA.
AC Q13200; Q12932; Q15321; Q53XQ4; Q96I12;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JUL-1999, sequence version 3.
DT 22-JAN-2014, entry version 140.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 49-66; 81-85;
RP 91-117; 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.,
RA Slaughter C.A., Fujimuro M., Yokosawa H., Yamasaki M., Hendil K.B.,
RA Toh-e A., Tanahashi N., 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-
RT factor-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
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
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
RT 2, a protein that interacts with the intracellular domain of the type
RT 1 TNF receptor: identity with subunit 2 of the 26S protease.";
RL J. Immunol. 158:4252-4259(1997).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-24; SER-29 AND
RP TYR-194, AND MASS SPECTROMETRY.
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
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP SPECTROMETRY.
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
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP SPECTROMETRY.
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 [11]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-361, AND MASS
RP SPECTROMETRY.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-24 AND SER-361,
RP AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-361, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which
CC is involved in the ATP-dependent degradation of ubiquitinated
CC proteins.
CC -!- FUNCTION: Binds to the intracellular domain of tumor necrosis
CC factor type 1 receptor. The binding domain of TRAP1 and TRAP2
CC resides outside the death domain of TNFR1.
CC -!- INTERACTION:
CC P62191:PSMC1; NbExp=6; IntAct=EBI-357648, EBI-357598;
CC P62195:PSMC5; NbExp=9; IntAct=EBI-357648, EBI-357745;
CC Q9Y5K5:UCHL5; NbExp=5; IntAct=EBI-357648, EBI-1051183;
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.
CC -!- SIMILARITY: Contains 7 PC repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA87705.1; Type=Erroneous initiation;
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DR EMBL; D78151; BAA11226.1; -; mRNA.
DR EMBL; BT009736; AAP88738.1; -; mRNA.
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 RefSeq; NP_001265637.1; NM_001278708.1.
DR RefSeq; NP_001265638.1; NM_001278709.1.
DR RefSeq; NP_002799.3; NM_002808.4.
DR UniGene; Hs.518464; -.
DR ProteinModelPortal; Q13200; -.
DR IntAct; Q13200; 34.
DR MINT; MINT-1142723; -.
DR STRING; 9606.ENSP00000310129; -.
DR DrugBank; DB00188; Bortezomib.
DR PhosphoSite; Q13200; -.
DR DMDM; 6174930; -.
DR PaxDb; Q13200; -.
DR PeptideAtlas; Q13200; -.
DR PRIDE; Q13200; -.
DR DNASU; 5708; -.
DR Ensembl; ENST00000310118; ENSP00000310129; ENSG00000175166.
DR GeneID; 5708; -.
DR KEGG; hsa:5708; -.
DR UCSC; uc003fnn.1; human.
DR CTD; 5708; -.
DR GeneCards; GC03P184016; -.
DR HGNC; HGNC:9559; PSMD2.
DR HPA; HPA045192; -.
DR MIM; 606223; gene.
DR neXtProt; NX_Q13200; -.
DR PharmGKB; PA33905; -.
DR eggNOG; COG5110; -.
DR HOVERGEN; HBG001842; -.
DR InParanoid; Q13200; -.
DR KO; K03028; -.
DR OMA; IAQGLTH; -.
DR OrthoDB; EOG70KGNV; -.
DR PhylomeDB; Q13200; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSMD2; human.
DR GeneWiki; PSMD2; -.
DR GenomeRNAi; 5708; -.
DR NextBio; 22178; -.
DR PRO; PR:Q13200; -.
DR ArrayExpress; Q13200; -.
DR Bgee; Q13200; -.
DR CleanEx; HS_PSMD2; -.
DR Genevestigator; Q13200; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005838; C:proteasome regulatory particle; TAS:ProtInc.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein 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:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; 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:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR016643; 26S_Psome_Rpn1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR Pfam; PF01851; PC_rep; 2.
DR PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
DR SUPFAM; SSF48371; SSF48371; 4.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Direct protein sequencing;
KW Phosphoprotein; Polymorphism; Proteasome; Reference proteome; Repeat.
FT CHAIN 1 908 26S proteasome non-ATPase regulatory
FT subunit 2.
FT /FTId=PRO_0000173810.
FT REPEAT 409 442 PC 1.
FT REPEAT 443 479 PC 2.
FT REPEAT 480 514 PC 3.
FT REPEAT 517 551 PC 4.
FT REPEAT 560 589 PC 5.
FT REPEAT 692 723 PC 6.
FT REPEAT 742 757 PC 7.
FT COMPBIAS 623 641 Glu/Lys-rich.
FT MOD_RES 1 1 N-acetylmethionine (By similarity).
FT MOD_RES 16 16 Phosphoserine.
FT MOD_RES 24 24 Phosphothreonine.
FT MOD_RES 29 29 Phosphoserine.
FT MOD_RES 194 194 Phosphotyrosine.
FT MOD_RES 361 361 Phosphoserine.
FT VARIANT 176 176 A -> T (in dbSNP:rs11545172).
FT /FTId=VAR_051554.
FT VARIANT 313 313 E -> D (in dbSNP:rs11545169).
FT /FTId=VAR_051555.
FT VARIANT 724 724 N -> Y (in dbSNP:rs17856236).
FT /FTId=VAR_067451.
FT CONFLICT 10 10 P -> R (in Ref. 5; CAA60167).
FT CONFLICT 21 21 P -> S (in Ref. 4).
FT CONFLICT 32 32 E -> G (in Ref. 4).
FT CONFLICT 43 43 Q -> L (in Ref. 4).
FT CONFLICT 57 57 E -> V (in Ref. 4).
FT CONFLICT 60 60 V -> A (in Ref. 1; BAA11226).
FT CONFLICT 226 226 Y -> S (in Ref. 4; AAA87705).
FT CONFLICT 260 260 S -> T (in Ref. 5; CAA60167).
FT CONFLICT 281 283 IFT -> SS (in Ref. 4; AAA87705).
FT CONFLICT 415 415 G -> A (in Ref. 1; BAA11226).
FT CONFLICT 731 731 M -> MGM (in Ref. 4).
FT CONFLICT 900 908 LRKNPNYDL -> FGRTPIMISK (in Ref. 3 and
FT 5).
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
//
ID PSMD2_HUMAN Reviewed; 908 AA.
AC Q13200; Q12932; Q15321; Q53XQ4; Q96I12;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JUL-1999, sequence version 3.
DT 22-JAN-2014, entry version 140.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 49-66; 81-85;
RP 91-117; 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.,
RA Slaughter C.A., Fujimuro M., Yokosawa H., Yamasaki M., Hendil K.B.,
RA Toh-e A., Tanahashi N., 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-
RT factor-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
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
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
RT 2, a protein that interacts with the intracellular domain of the type
RT 1 TNF receptor: identity with subunit 2 of the 26S protease.";
RL J. Immunol. 158:4252-4259(1997).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-24; SER-29 AND
RP TYR-194, AND MASS SPECTROMETRY.
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
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP SPECTROMETRY.
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
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP SPECTROMETRY.
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 [11]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-361, AND MASS
RP SPECTROMETRY.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-24 AND SER-361,
RP AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-361, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which
CC is involved in the ATP-dependent degradation of ubiquitinated
CC proteins.
CC -!- FUNCTION: Binds to the intracellular domain of tumor necrosis
CC factor type 1 receptor. The binding domain of TRAP1 and TRAP2
CC resides outside the death domain of TNFR1.
CC -!- INTERACTION:
CC P62191:PSMC1; NbExp=6; IntAct=EBI-357648, EBI-357598;
CC P62195:PSMC5; NbExp=9; IntAct=EBI-357648, EBI-357745;
CC Q9Y5K5:UCHL5; NbExp=5; IntAct=EBI-357648, EBI-1051183;
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.
CC -!- SIMILARITY: Contains 7 PC repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA87705.1; Type=Erroneous initiation;
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DR EMBL; D78151; BAA11226.1; -; mRNA.
DR EMBL; BT009736; AAP88738.1; -; mRNA.
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 RefSeq; NP_001265637.1; NM_001278708.1.
DR RefSeq; NP_001265638.1; NM_001278709.1.
DR RefSeq; NP_002799.3; NM_002808.4.
DR UniGene; Hs.518464; -.
DR ProteinModelPortal; Q13200; -.
DR IntAct; Q13200; 34.
DR MINT; MINT-1142723; -.
DR STRING; 9606.ENSP00000310129; -.
DR DrugBank; DB00188; Bortezomib.
DR PhosphoSite; Q13200; -.
DR DMDM; 6174930; -.
DR PaxDb; Q13200; -.
DR PeptideAtlas; Q13200; -.
DR PRIDE; Q13200; -.
DR DNASU; 5708; -.
DR Ensembl; ENST00000310118; ENSP00000310129; ENSG00000175166.
DR GeneID; 5708; -.
DR KEGG; hsa:5708; -.
DR UCSC; uc003fnn.1; human.
DR CTD; 5708; -.
DR GeneCards; GC03P184016; -.
DR HGNC; HGNC:9559; PSMD2.
DR HPA; HPA045192; -.
DR MIM; 606223; gene.
DR neXtProt; NX_Q13200; -.
DR PharmGKB; PA33905; -.
DR eggNOG; COG5110; -.
DR HOVERGEN; HBG001842; -.
DR InParanoid; Q13200; -.
DR KO; K03028; -.
DR OMA; IAQGLTH; -.
DR OrthoDB; EOG70KGNV; -.
DR PhylomeDB; Q13200; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSMD2; human.
DR GeneWiki; PSMD2; -.
DR GenomeRNAi; 5708; -.
DR NextBio; 22178; -.
DR PRO; PR:Q13200; -.
DR ArrayExpress; Q13200; -.
DR Bgee; Q13200; -.
DR CleanEx; HS_PSMD2; -.
DR Genevestigator; Q13200; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005838; C:proteasome regulatory particle; TAS:ProtInc.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein 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:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; 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:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR016643; 26S_Psome_Rpn1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR Pfam; PF01851; PC_rep; 2.
DR PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
DR SUPFAM; SSF48371; SSF48371; 4.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Direct protein sequencing;
KW Phosphoprotein; Polymorphism; Proteasome; Reference proteome; Repeat.
FT CHAIN 1 908 26S proteasome non-ATPase regulatory
FT subunit 2.
FT /FTId=PRO_0000173810.
FT REPEAT 409 442 PC 1.
FT REPEAT 443 479 PC 2.
FT REPEAT 480 514 PC 3.
FT REPEAT 517 551 PC 4.
FT REPEAT 560 589 PC 5.
FT REPEAT 692 723 PC 6.
FT REPEAT 742 757 PC 7.
FT COMPBIAS 623 641 Glu/Lys-rich.
FT MOD_RES 1 1 N-acetylmethionine (By similarity).
FT MOD_RES 16 16 Phosphoserine.
FT MOD_RES 24 24 Phosphothreonine.
FT MOD_RES 29 29 Phosphoserine.
FT MOD_RES 194 194 Phosphotyrosine.
FT MOD_RES 361 361 Phosphoserine.
FT VARIANT 176 176 A -> T (in dbSNP:rs11545172).
FT /FTId=VAR_051554.
FT VARIANT 313 313 E -> D (in dbSNP:rs11545169).
FT /FTId=VAR_051555.
FT VARIANT 724 724 N -> Y (in dbSNP:rs17856236).
FT /FTId=VAR_067451.
FT CONFLICT 10 10 P -> R (in Ref. 5; CAA60167).
FT CONFLICT 21 21 P -> S (in Ref. 4).
FT CONFLICT 32 32 E -> G (in Ref. 4).
FT CONFLICT 43 43 Q -> L (in Ref. 4).
FT CONFLICT 57 57 E -> V (in Ref. 4).
FT CONFLICT 60 60 V -> A (in Ref. 1; BAA11226).
FT CONFLICT 226 226 Y -> S (in Ref. 4; AAA87705).
FT CONFLICT 260 260 S -> T (in Ref. 5; CAA60167).
FT CONFLICT 281 283 IFT -> SS (in Ref. 4; AAA87705).
FT CONFLICT 415 415 G -> A (in Ref. 1; BAA11226).
FT CONFLICT 731 731 M -> MGM (in Ref. 4).
FT CONFLICT 900 908 LRKNPNYDL -> FGRTPIMISK (in Ref. 3 and
FT 5).
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
//
MIM
606223
*RECORD*
*FIELD* NO
606223
*FIELD* TI
*606223 PROTEASOME 26S SUBUNIT, NON-ATPASE, 2; PSMD2
;;PROTEASOME 26S, SUBUNIT 2; S2;;
read moreTUMOR NECROSIS FACTOR RECEPTOR-ASSOCIATED PROTEIN 2; TRAP2;;
TNFR-ASSOCIATED PROTEIN 2
*FIELD* TX
The 26S proteasome is a multisubunit protein complex involved in the
degradation of constitutively short-lived proteins, regulatory proteins,
and abnormal and malfolded proteins. It is composed of a 700-kD 20S
proteasome catalytic core proteinase (e.g., PSMA3; 176843) and PA700
regulatory modules. The PA700 subunits are divided into a family of
ATPases (e.g., PSMC6; 602708) and a family of non-ATPases (e.g., PSMD9;
603146).
CLONING
Using a yeast 2-hybrid screen of a HeLa cDNA library with the
intracellular death domain of the p55 tumor necrosis factor receptor
(TNFRSF1A; 191190) as bait, Boldin et al. (1995) isolated a cDNA
encoding PSMD2, which they designated 55.11. Binding analysis indicated
that the 900-amino acid 55.11 protein binds to C-terminally truncated
p55 lacking the death domain. Northern blot analysis revealed expression
of an approximately 3.0-kb transcript in HeLa, leukemic T-cell, and
hepatic carcinoma cell lines. Recombinant 55.11 was expressed as an
84-kD protein. Sequence analysis predicted that 55.11 has a KEKE motif
and shares homology with the yeast Sen3 protein, a component of the 26S
proteasome regulatory complex. Boldin et al. (1995) proposed that given
the rapidity with which TNF binding decreases after the inhibition of
protein synthesis, TNFR has a short half-life consistent with
proteasomal degradation of the molecule.
By biochemical purification of a 97-kD PA700 subunit from bovine red
cells, peptide sequence analysis, and database searching, Tsurumi et al.
(1996) obtained a cDNA encoding PSMD2, which they termed p97. The
deduced 908-amino acid protein contains a KEKE motif, a hydrophilic
region rich in alternately positively charged (lys) and negatively
charged (glu) amino acids. Northern blot analysis detected ubiquitous
expression of a 3.0-kb transcript, with highest levels in heart and
skeletal muscle. Complementation analysis indicated that PSMD2 is a
functional homolog of Nas1 in yeast.
Using a yeast 2-hybrid screen with the intracellular domain of TNFR1 as
bait, Dunbar et al. (1997) cloned and characterized a partial cDNA
encoding PSMD2, which they called TRAP2.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PSMD2
gene to chromosome 3 (TMAP RH65279).
*FIELD* RF
1. 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.
2. 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. Immun. 158:
4252-4259, 1997.
3. 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. Europ.
J. Biochem. 239: 912-921, 1996.
*FIELD* CD
Paul J. Converse: 8/24/2001
*FIELD* ED
mgross: 11/10/2009
terry: 11/3/2009
mgross: 8/24/2001
*RECORD*
*FIELD* NO
606223
*FIELD* TI
*606223 PROTEASOME 26S SUBUNIT, NON-ATPASE, 2; PSMD2
;;PROTEASOME 26S, SUBUNIT 2; S2;;
read moreTUMOR NECROSIS FACTOR RECEPTOR-ASSOCIATED PROTEIN 2; TRAP2;;
TNFR-ASSOCIATED PROTEIN 2
*FIELD* TX
The 26S proteasome is a multisubunit protein complex involved in the
degradation of constitutively short-lived proteins, regulatory proteins,
and abnormal and malfolded proteins. It is composed of a 700-kD 20S
proteasome catalytic core proteinase (e.g., PSMA3; 176843) and PA700
regulatory modules. The PA700 subunits are divided into a family of
ATPases (e.g., PSMC6; 602708) and a family of non-ATPases (e.g., PSMD9;
603146).
CLONING
Using a yeast 2-hybrid screen of a HeLa cDNA library with the
intracellular death domain of the p55 tumor necrosis factor receptor
(TNFRSF1A; 191190) as bait, Boldin et al. (1995) isolated a cDNA
encoding PSMD2, which they designated 55.11. Binding analysis indicated
that the 900-amino acid 55.11 protein binds to C-terminally truncated
p55 lacking the death domain. Northern blot analysis revealed expression
of an approximately 3.0-kb transcript in HeLa, leukemic T-cell, and
hepatic carcinoma cell lines. Recombinant 55.11 was expressed as an
84-kD protein. Sequence analysis predicted that 55.11 has a KEKE motif
and shares homology with the yeast Sen3 protein, a component of the 26S
proteasome regulatory complex. Boldin et al. (1995) proposed that given
the rapidity with which TNF binding decreases after the inhibition of
protein synthesis, TNFR has a short half-life consistent with
proteasomal degradation of the molecule.
By biochemical purification of a 97-kD PA700 subunit from bovine red
cells, peptide sequence analysis, and database searching, Tsurumi et al.
(1996) obtained a cDNA encoding PSMD2, which they termed p97. The
deduced 908-amino acid protein contains a KEKE motif, a hydrophilic
region rich in alternately positively charged (lys) and negatively
charged (glu) amino acids. Northern blot analysis detected ubiquitous
expression of a 3.0-kb transcript, with highest levels in heart and
skeletal muscle. Complementation analysis indicated that PSMD2 is a
functional homolog of Nas1 in yeast.
Using a yeast 2-hybrid screen with the intracellular domain of TNFR1 as
bait, Dunbar et al. (1997) cloned and characterized a partial cDNA
encoding PSMD2, which they called TRAP2.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PSMD2
gene to chromosome 3 (TMAP RH65279).
*FIELD* RF
1. 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.
2. 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. Immun. 158:
4252-4259, 1997.
3. 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. Europ.
J. Biochem. 239: 912-921, 1996.
*FIELD* CD
Paul J. Converse: 8/24/2001
*FIELD* ED
mgross: 11/10/2009
terry: 11/3/2009
mgross: 8/24/2001