Full text data of PSMD9
PSMD9
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
26S proteasome non-ATPase regulatory subunit 9 (26S proteasome regulatory subunit p27)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
26S proteasome non-ATPase regulatory subunit 9 (26S proteasome regulatory subunit p27)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O00233
ID PSMD9_HUMAN Reviewed; 223 AA.
AC O00233; B2RD35; G3V1Q6; Q9BQ42;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 3.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 9;
DE AltName: Full=26S proteasome regulatory subunit p27;
GN Name=PSMD9;
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] (ISOFORMS P27-S AND P27-L).
RX PubMed=9653651; DOI=10.1006/geno.1998.5301;
RA Watanabe T.K., Saito A., Suzuki M., Fujiwara T., Takahashi E.,
RA Slaughter C.A., DeMartino G.N., Hendil K.B., Chung C.H., Tanahashi N.,
RA Tanaka K.;
RT "cDNA cloning and characterization of a human proteasomal modulator
RT subunit, p27 (PSMD9).";
RL Genomics 50:241-250(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P27-L), AND VARIANT
RP ALA-17.
RC TISSUE=Hippocampus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
RP ALA-17.
RC TISSUE=Liver;
RX PubMed=16712791; DOI=10.1016/j.bbrc.2006.04.175;
RA Wang A.G., Yoon S.Y., Oh J.H., Jeon Y.J., Kim M., Kim J.M., Byun S.S.,
RA Yang J.O., Kim J.H., Kim D.G., Yeom Y.I., Yoo H.S., Kim Y.S.,
RA Kim N.S.;
RT "Identification of intrahepatic cholangiocarcinoma related genes by
RT comparison with normal liver tissues using expressed sequence tags.";
RL Biochem. Biophys. Res. Commun. 345:1022-1032(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [7]
RP FUNCTION AS PROTEASOME CHAPERONE, INTERACTION WITH PSMC3, AND SUBUNIT.
RX PubMed=19490896; DOI=10.1016/j.cell.2009.05.008;
RA Kaneko T., Hamazaki J., Iemura S., Sasaki K., Furuyama K., Natsume T.,
RA Tanaka K., Murata S.;
RT "Assembly pathway of the Mammalian proteasome base subcomplex is
RT mediated by multiple specific chaperones.";
RL Cell 137:914-925(2009).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-17, AND MASS SPECTROMETRY.
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).
CC -!- FUNCTION: Acts as a chaperone during the assembly of the 26S
CC proteasome, specifically of the base subcomplex of the PA700/19S
CC regulatory complex (RC). During the base subcomplex assembly is
CC part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as
CC modulator trimer complex; PSMD9 is released during the further
CC base assembly process.
CC -!- SUBUNIT: Interacts with PSMC3. Part of a transient complex
CC (modulator) containing PSMD9, PSMC6 and PSMC3 formed during the
CC assembly of the 26S proteasome.
CC -!- INTERACTION:
CC P17980:PSMC3; NbExp=4; IntAct=EBI-750973, EBI-359720;
CC P62333:PSMC6; NbExp=5; IntAct=EBI-750973, EBI-357669;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=p27-L;
CC IsoId=O00233-1; Sequence=Displayed;
CC Name=p27-S;
CC IsoId=O00233-2; Sequence=VSP_005300;
CC Name=3;
CC IsoId=O00233-3; Sequence=VSP_046004;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, highly
CC expressed in liver and kidney.
CC -!- SIMILARITY: Belongs to the proteasome subunit p27 family.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC -!- CAUTION: Was initially identified as a component of the 26S
CC proteasome.
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DR EMBL; AB003177; BAA19790.1; -; mRNA.
DR EMBL; AK315389; BAG37782.1; -; mRNA.
DR EMBL; CB111716; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC069503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW98296.1; -; Genomic_DNA.
DR EMBL; BC002383; AAH02383.1; -; mRNA.
DR EMBL; BC004184; AAH04184.1; -; mRNA.
DR EMBL; BC004213; AAH04213.1; -; mRNA.
DR RefSeq; NP_001248329.1; NM_001261400.1.
DR RefSeq; NP_002804.2; NM_002813.5.
DR UniGene; Hs.131151; -.
DR ProteinModelPortal; O00233; -.
DR SMR; O00233; 136-196.
DR IntAct; O00233; 7.
DR MINT; MINT-1435362; -.
DR STRING; 9606.ENSP00000261817; -.
DR PhosphoSite; O00233; -.
DR OGP; O00233; -.
DR PaxDb; O00233; -.
DR PRIDE; O00233; -.
DR DNASU; 5715; -.
DR Ensembl; ENST00000537407; ENSP00000445058; ENSG00000110801.
DR Ensembl; ENST00000541212; ENSP00000440485; ENSG00000110801.
DR GeneID; 5715; -.
DR KEGG; hsa:5715; -.
DR UCSC; uc001ubl.4; human.
DR CTD; 5715; -.
DR GeneCards; GC12P122326; -.
DR HGNC; HGNC:9567; PSMD9.
DR HPA; HPA040512; -.
DR HPA; HPA044220; -.
DR MIM; 603146; gene.
DR neXtProt; NX_O00233; -.
DR PharmGKB; PA33913; -.
DR eggNOG; COG0265; -.
DR HOGENOM; HOG000216665; -.
DR HOVERGEN; HBG001851; -.
DR InParanoid; O00233; -.
DR KO; K06693; -.
DR OMA; LLGCNIV; -.
DR PhylomeDB; O00233; -.
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 GeneWiki; PSMD9; -.
DR GenomeRNAi; 5715; -.
DR NextBio; 22202; -.
DR PRO; PR:O00233; -.
DR ArrayExpress; O00233; -.
DR Bgee; O00233; -.
DR CleanEx; HS_PSMD9; -.
DR Genevestigator; O00233; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005838; C:proteasome regulatory particle; NAS:UniProtKB.
DR GO; GO:0043425; F:bHLH transcription factor binding; ISS:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:BHF-UCL.
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:0046676; P:negative regulation of insulin secretion; ISS:BHF-UCL.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:BHF-UCL.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0070682; P:proteasome regulatory particle assembly; IMP:UniProtKB.
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:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR001478; PDZ.
DR Pfam; PF13180; PDZ_2; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Complete proteome; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 223 26S proteasome non-ATPase regulatory
FT subunit 9.
FT /FTId=PRO_0000173852.
FT DOMAIN 108 195 PDZ.
FT MOD_RES 129 129 Phosphoserine (By similarity).
FT VAR_SEQ 47 151 Missing (in isoform 3).
FT /FTId=VSP_046004.
FT VAR_SEQ 186 223 KPLNVTVIRRGEKHQLRLVPTRWAGKGLLGCNIIPLQR ->
FT ALAPTILLSVSMNLTTPGTSSRSP (in isoform p27-
FT S).
FT /FTId=VSP_005300.
FT VARIANT 17 17 V -> A (in dbSNP:rs2230681).
FT /FTId=VAR_009953.
FT VARIANT 74 74 T -> I (in dbSNP:rs2291116).
FT /FTId=VAR_057047.
FT VARIANT 134 134 R -> W (in dbSNP:rs1177573).
FT /FTId=VAR_057048.
FT VARIANT 197 197 E -> G (in dbSNP:rs14259).
FT /FTId=VAR_057049.
SQ SEQUENCE 223 AA; 24682 MW; 98B3A623323A8F37 CRC64;
MSDEEARQSG GSSQAGVVTV SDVQELMRRK EEIEAQIKAN YDVLESQKGI GMNEPLVDCE
GYPRSDVDLY QVRTARHNII CLQNDHKAVM KQVEEALHQL HARDKEKQAR DMAEAHKEAM
SRKLGQSESQ GPPRAFAKVN SISPGSPASI AGLQVDDEIV EFGSVNTQNF QSLHNIGSVV
QHSEGKPLNV TVIRRGEKHQ LRLVPTRWAG KGLLGCNIIP LQR
//
ID PSMD9_HUMAN Reviewed; 223 AA.
AC O00233; B2RD35; G3V1Q6; Q9BQ42;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 3.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 9;
DE AltName: Full=26S proteasome regulatory subunit p27;
GN Name=PSMD9;
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] (ISOFORMS P27-S AND P27-L).
RX PubMed=9653651; DOI=10.1006/geno.1998.5301;
RA Watanabe T.K., Saito A., Suzuki M., Fujiwara T., Takahashi E.,
RA Slaughter C.A., DeMartino G.N., Hendil K.B., Chung C.H., Tanahashi N.,
RA Tanaka K.;
RT "cDNA cloning and characterization of a human proteasomal modulator
RT subunit, p27 (PSMD9).";
RL Genomics 50:241-250(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P27-L), AND VARIANT
RP ALA-17.
RC TISSUE=Hippocampus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
RP ALA-17.
RC TISSUE=Liver;
RX PubMed=16712791; DOI=10.1016/j.bbrc.2006.04.175;
RA Wang A.G., Yoon S.Y., Oh J.H., Jeon Y.J., Kim M., Kim J.M., Byun S.S.,
RA Yang J.O., Kim J.H., Kim D.G., Yeom Y.I., Yoo H.S., Kim Y.S.,
RA Kim N.S.;
RT "Identification of intrahepatic cholangiocarcinoma related genes by
RT comparison with normal liver tissues using expressed sequence tags.";
RL Biochem. Biophys. Res. Commun. 345:1022-1032(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [7]
RP FUNCTION AS PROTEASOME CHAPERONE, INTERACTION WITH PSMC3, AND SUBUNIT.
RX PubMed=19490896; DOI=10.1016/j.cell.2009.05.008;
RA Kaneko T., Hamazaki J., Iemura S., Sasaki K., Furuyama K., Natsume T.,
RA Tanaka K., Murata S.;
RT "Assembly pathway of the Mammalian proteasome base subcomplex is
RT mediated by multiple specific chaperones.";
RL Cell 137:914-925(2009).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-17, AND MASS SPECTROMETRY.
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).
CC -!- FUNCTION: Acts as a chaperone during the assembly of the 26S
CC proteasome, specifically of the base subcomplex of the PA700/19S
CC regulatory complex (RC). During the base subcomplex assembly is
CC part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as
CC modulator trimer complex; PSMD9 is released during the further
CC base assembly process.
CC -!- SUBUNIT: Interacts with PSMC3. Part of a transient complex
CC (modulator) containing PSMD9, PSMC6 and PSMC3 formed during the
CC assembly of the 26S proteasome.
CC -!- INTERACTION:
CC P17980:PSMC3; NbExp=4; IntAct=EBI-750973, EBI-359720;
CC P62333:PSMC6; NbExp=5; IntAct=EBI-750973, EBI-357669;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=p27-L;
CC IsoId=O00233-1; Sequence=Displayed;
CC Name=p27-S;
CC IsoId=O00233-2; Sequence=VSP_005300;
CC Name=3;
CC IsoId=O00233-3; Sequence=VSP_046004;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, highly
CC expressed in liver and kidney.
CC -!- SIMILARITY: Belongs to the proteasome subunit p27 family.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC -!- CAUTION: Was initially identified as a component of the 26S
CC proteasome.
CC -----------------------------------------------------------------------
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DR EMBL; AB003177; BAA19790.1; -; mRNA.
DR EMBL; AK315389; BAG37782.1; -; mRNA.
DR EMBL; CB111716; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC069503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW98296.1; -; Genomic_DNA.
DR EMBL; BC002383; AAH02383.1; -; mRNA.
DR EMBL; BC004184; AAH04184.1; -; mRNA.
DR EMBL; BC004213; AAH04213.1; -; mRNA.
DR RefSeq; NP_001248329.1; NM_001261400.1.
DR RefSeq; NP_002804.2; NM_002813.5.
DR UniGene; Hs.131151; -.
DR ProteinModelPortal; O00233; -.
DR SMR; O00233; 136-196.
DR IntAct; O00233; 7.
DR MINT; MINT-1435362; -.
DR STRING; 9606.ENSP00000261817; -.
DR PhosphoSite; O00233; -.
DR OGP; O00233; -.
DR PaxDb; O00233; -.
DR PRIDE; O00233; -.
DR DNASU; 5715; -.
DR Ensembl; ENST00000537407; ENSP00000445058; ENSG00000110801.
DR Ensembl; ENST00000541212; ENSP00000440485; ENSG00000110801.
DR GeneID; 5715; -.
DR KEGG; hsa:5715; -.
DR UCSC; uc001ubl.4; human.
DR CTD; 5715; -.
DR GeneCards; GC12P122326; -.
DR HGNC; HGNC:9567; PSMD9.
DR HPA; HPA040512; -.
DR HPA; HPA044220; -.
DR MIM; 603146; gene.
DR neXtProt; NX_O00233; -.
DR PharmGKB; PA33913; -.
DR eggNOG; COG0265; -.
DR HOGENOM; HOG000216665; -.
DR HOVERGEN; HBG001851; -.
DR InParanoid; O00233; -.
DR KO; K06693; -.
DR OMA; LLGCNIV; -.
DR PhylomeDB; O00233; -.
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 GeneWiki; PSMD9; -.
DR GenomeRNAi; 5715; -.
DR NextBio; 22202; -.
DR PRO; PR:O00233; -.
DR ArrayExpress; O00233; -.
DR Bgee; O00233; -.
DR CleanEx; HS_PSMD9; -.
DR Genevestigator; O00233; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005838; C:proteasome regulatory particle; NAS:UniProtKB.
DR GO; GO:0043425; F:bHLH transcription factor binding; ISS:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:BHF-UCL.
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:0046676; P:negative regulation of insulin secretion; ISS:BHF-UCL.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:BHF-UCL.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0070682; P:proteasome regulatory particle assembly; IMP:UniProtKB.
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:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR001478; PDZ.
DR Pfam; PF13180; PDZ_2; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Complete proteome; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 223 26S proteasome non-ATPase regulatory
FT subunit 9.
FT /FTId=PRO_0000173852.
FT DOMAIN 108 195 PDZ.
FT MOD_RES 129 129 Phosphoserine (By similarity).
FT VAR_SEQ 47 151 Missing (in isoform 3).
FT /FTId=VSP_046004.
FT VAR_SEQ 186 223 KPLNVTVIRRGEKHQLRLVPTRWAGKGLLGCNIIPLQR ->
FT ALAPTILLSVSMNLTTPGTSSRSP (in isoform p27-
FT S).
FT /FTId=VSP_005300.
FT VARIANT 17 17 V -> A (in dbSNP:rs2230681).
FT /FTId=VAR_009953.
FT VARIANT 74 74 T -> I (in dbSNP:rs2291116).
FT /FTId=VAR_057047.
FT VARIANT 134 134 R -> W (in dbSNP:rs1177573).
FT /FTId=VAR_057048.
FT VARIANT 197 197 E -> G (in dbSNP:rs14259).
FT /FTId=VAR_057049.
SQ SEQUENCE 223 AA; 24682 MW; 98B3A623323A8F37 CRC64;
MSDEEARQSG GSSQAGVVTV SDVQELMRRK EEIEAQIKAN YDVLESQKGI GMNEPLVDCE
GYPRSDVDLY QVRTARHNII CLQNDHKAVM KQVEEALHQL HARDKEKQAR DMAEAHKEAM
SRKLGQSESQ GPPRAFAKVN SISPGSPASI AGLQVDDEIV EFGSVNTQNF QSLHNIGSVV
QHSEGKPLNV TVIRRGEKHQ LRLVPTRWAG KGLLGCNIIP LQR
//
MIM
603146
*RECORD*
*FIELD* NO
603146
*FIELD* TI
*603146 PROTEASOME 26S SUBUNIT, NON-ATPase, 9; PSMD9
;;BRIDGE 1, RAT, HOMOLOG OF
*FIELD* TX
read moreThe 26S proteasome is a eukaryotic ATP-dependent protease that
selectively degrades intracellular target proteins that are modified by
the covalent attachment of ubiquitin. It is composed of a central
catalytic 20S proteasome, which consists of a family of small proteins,
and 2 large regulatory modules, named PA700, which consist of
approximately 20 heterogeneous proteins. A proteasomal modulator
complex, composed of p27, p42, and p50 subunits, stimulates the
association of the 20S proteasome with PA700 to form the active 26S
proteasome. Watanabe et al. (1998) cloned 2 distinct human brain cDNAs
encoding p27, or PSMD9. Compared with the longer cDNA, the shorter cDNA
has a 65-bp deletion near the 3-prime region that results in a new
in-frame termination codon farther downstream. The longer cDNA encodes a
deduced 209-amino acid protein with a calculated molecular mass of
22,764 Da. The shorter cDNA encodes a deduced 223-amino acid protein
with a calculated molecular mass of 24,652 Da. The longer PSMD9 protein
exhibits 36% sequence identity with an S. cerevisiae protein, which the
authors named NAS2 for 'non-ATPase subunit 2,' and 31.9% identity with a
C. elegans protein. Disruption of the yeast NAS2 gene did not affect
cell viability or proliferation. Watanabe et al. (1998) demonstrated
that the PSMD9 protein, along with the ATPase components TBP1 (PSMC3;
186852) and p42 (PSMC6; 602708), associated with both the modulator
complex and the 26S proteasome complex. Northern blot analysis detected
an approximately 1.3-kb PSMD9 transcript in all tissues examined, with
highest levels in liver and kidney.
E12 and E47 (see TCF3; 147141), members of the ubiquitous E2A protein
family, function with basic helix-loop-helix (bHLH) proteins to bind and
transactivate promoters via conserved sequence elements known as E
boxes. By yeast 2-hybrid screening of a rat insulinoma cell cDNA library
using the bHLH domain-containing C terminus of E12 as bait, Thomas et
al. (1999) obtained a cDNA encoding rat Bridge-1. Sequence analysis
predicted that the 222-amino acid Bridge-1 protein shares 98% amino acid
similarity with human PSMD9 over the first 184 amino acids but diverges
in the C terminus Bridge-1 contains a PDZ-like domain from amino acids
138 to 178, forming 3 beta sheets and 2 alpha helices. SDS-PAGE analysis
showed that Bridge-1 is expressed as a 28-kD protein, close to the
deduced value of 25 kD. Using Bridge-1 cDNA as probe, Northern blot
analysis detected a 1.0-kb transcript in all rat and human tissues
tested, with highest expression in pancreas, testis, kidney, and liver.
Immunocytochemistry assessment demonstrated predominant nuclear
localization of Bridge-1, with lower levels in cytoplasm.
Immunoprecipitation analysis determined that anti-Bridge-1
coimmunoprecipitates E12 or E12 and E47 through their C-terminal bHLH
domains, but only in the presence of the PDZ domain of Bridge-1. CAT
assays indicated that Bridge-1 together with E12 or E47 coactivates
insulin (176730) promoter elements.
By fluorescence in situ hybridization, Watanabe et al. (1998) mapped the
PMSD9 gene to 12q24.2-q24.3.
*FIELD* RF
1. Thomas, M. K.; Yao, K.-M.; Tenser, M. S.; Wong, G. G.; Habener,
J. F.: Bridge-1, a novel PDZ-domain coactivator of E2A-mediated regulation
of insulin gene transcription. Molec. Cell. Biol. 19: 8492-8504,
1999.
2. Watanabe, T. K.; Saito, A.; Suzuki, M.; Fujiwara, T.; Takahashi,
E.; Slaughter, C. A.; DeMartino, G. N.; Hendil, K. B.; Chung, C. H.;
Tanahashi, N.; Tanaka, K.: cDNA cloning and characterization of a
human proteasomal modulator subunit, p27 (PSMD9). Genomics 50: 241-250,
1998.
*FIELD* CN
Paul J. Converse - updated: 7/20/2000
*FIELD* CD
Sheryl A. Jankowski: 10/14/1998
*FIELD* ED
alopez: 02/07/2005
mgross: 7/20/2000
psherman: 10/15/1998
*RECORD*
*FIELD* NO
603146
*FIELD* TI
*603146 PROTEASOME 26S SUBUNIT, NON-ATPase, 9; PSMD9
;;BRIDGE 1, RAT, HOMOLOG OF
*FIELD* TX
read moreThe 26S proteasome is a eukaryotic ATP-dependent protease that
selectively degrades intracellular target proteins that are modified by
the covalent attachment of ubiquitin. It is composed of a central
catalytic 20S proteasome, which consists of a family of small proteins,
and 2 large regulatory modules, named PA700, which consist of
approximately 20 heterogeneous proteins. A proteasomal modulator
complex, composed of p27, p42, and p50 subunits, stimulates the
association of the 20S proteasome with PA700 to form the active 26S
proteasome. Watanabe et al. (1998) cloned 2 distinct human brain cDNAs
encoding p27, or PSMD9. Compared with the longer cDNA, the shorter cDNA
has a 65-bp deletion near the 3-prime region that results in a new
in-frame termination codon farther downstream. The longer cDNA encodes a
deduced 209-amino acid protein with a calculated molecular mass of
22,764 Da. The shorter cDNA encodes a deduced 223-amino acid protein
with a calculated molecular mass of 24,652 Da. The longer PSMD9 protein
exhibits 36% sequence identity with an S. cerevisiae protein, which the
authors named NAS2 for 'non-ATPase subunit 2,' and 31.9% identity with a
C. elegans protein. Disruption of the yeast NAS2 gene did not affect
cell viability or proliferation. Watanabe et al. (1998) demonstrated
that the PSMD9 protein, along with the ATPase components TBP1 (PSMC3;
186852) and p42 (PSMC6; 602708), associated with both the modulator
complex and the 26S proteasome complex. Northern blot analysis detected
an approximately 1.3-kb PSMD9 transcript in all tissues examined, with
highest levels in liver and kidney.
E12 and E47 (see TCF3; 147141), members of the ubiquitous E2A protein
family, function with basic helix-loop-helix (bHLH) proteins to bind and
transactivate promoters via conserved sequence elements known as E
boxes. By yeast 2-hybrid screening of a rat insulinoma cell cDNA library
using the bHLH domain-containing C terminus of E12 as bait, Thomas et
al. (1999) obtained a cDNA encoding rat Bridge-1. Sequence analysis
predicted that the 222-amino acid Bridge-1 protein shares 98% amino acid
similarity with human PSMD9 over the first 184 amino acids but diverges
in the C terminus Bridge-1 contains a PDZ-like domain from amino acids
138 to 178, forming 3 beta sheets and 2 alpha helices. SDS-PAGE analysis
showed that Bridge-1 is expressed as a 28-kD protein, close to the
deduced value of 25 kD. Using Bridge-1 cDNA as probe, Northern blot
analysis detected a 1.0-kb transcript in all rat and human tissues
tested, with highest expression in pancreas, testis, kidney, and liver.
Immunocytochemistry assessment demonstrated predominant nuclear
localization of Bridge-1, with lower levels in cytoplasm.
Immunoprecipitation analysis determined that anti-Bridge-1
coimmunoprecipitates E12 or E12 and E47 through their C-terminal bHLH
domains, but only in the presence of the PDZ domain of Bridge-1. CAT
assays indicated that Bridge-1 together with E12 or E47 coactivates
insulin (176730) promoter elements.
By fluorescence in situ hybridization, Watanabe et al. (1998) mapped the
PMSD9 gene to 12q24.2-q24.3.
*FIELD* RF
1. Thomas, M. K.; Yao, K.-M.; Tenser, M. S.; Wong, G. G.; Habener,
J. F.: Bridge-1, a novel PDZ-domain coactivator of E2A-mediated regulation
of insulin gene transcription. Molec. Cell. Biol. 19: 8492-8504,
1999.
2. Watanabe, T. K.; Saito, A.; Suzuki, M.; Fujiwara, T.; Takahashi,
E.; Slaughter, C. A.; DeMartino, G. N.; Hendil, K. B.; Chung, C. H.;
Tanahashi, N.; Tanaka, K.: cDNA cloning and characterization of a
human proteasomal modulator subunit, p27 (PSMD9). Genomics 50: 241-250,
1998.
*FIELD* CN
Paul J. Converse - updated: 7/20/2000
*FIELD* CD
Sheryl A. Jankowski: 10/14/1998
*FIELD* ED
alopez: 02/07/2005
mgross: 7/20/2000
psherman: 10/15/1998