PSMD9_HUMAN
ID PSMD9_HUMAN Reviewed; 223 AA.
AC O00233; B2RD35; G3V1Q6; Q9BQ42;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 200.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT 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., 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., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., 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., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., 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., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 mediated
RT by multiple specific chaperones.";
RL Cell 137:914-925(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-17, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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 part of
CC an intermediate PSMD9:PSMC6:PSMC3 module, also known as modulator
CC trimer complex; PSMD9 is released during the further base assembly
CC process. {ECO:0000269|PubMed:19490896}.
CC -!- SUBUNIT: Interacts with PSMC3. Part of a transient complex (modulator)
CC containing PSMD9, PSMC6 and PSMC3 formed during the assembly of the 26S
CC proteasome. {ECO:0000269|PubMed:19490896}.
CC -!- INTERACTION:
CC O00233; Q9UHI8: ADAMTS1; NbExp=3; IntAct=EBI-750973, EBI-2511802;
CC O00233; O43865: AHCYL1; NbExp=3; IntAct=EBI-750973, EBI-2371423;
CC O00233; Q8N9N5: BANP; NbExp=3; IntAct=EBI-750973, EBI-744695;
CC O00233; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-750973, EBI-10171416;
CC O00233; Q5SZL2-5: CEP85L; NbExp=3; IntAct=EBI-750973, EBI-12344751;
CC O00233; P0DML2: CSH1; NbExp=5; IntAct=EBI-750973, EBI-13375302;
CC O00233; P09651-2: HNRNPA1; NbExp=5; IntAct=EBI-750973, EBI-352677;
CC O00233; P08887-2: IL6R; NbExp=3; IntAct=EBI-750973, EBI-16630231;
CC O00233; P03952: KLKB1; NbExp=3; IntAct=EBI-750973, EBI-10087153;
CC O00233; P06858: LPL; NbExp=3; IntAct=EBI-750973, EBI-715909;
CC O00233; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-750973, EBI-16439278;
CC O00233; Q9NZQ3: NCKIPSD; NbExp=4; IntAct=EBI-750973, EBI-745080;
CC O00233; P17980: PSMC3; NbExp=16; IntAct=EBI-750973, EBI-359720;
CC O00233; P62333: PSMC6; NbExp=15; IntAct=EBI-750973, EBI-357669;
CC O00233; P62263: RPS14; NbExp=3; IntAct=EBI-750973, EBI-352783;
CC O00233; P15923-1: TCF3; NbExp=2; IntAct=EBI-750973, EBI-769645;
CC O00233; Q12933: TRAF2; NbExp=3; IntAct=EBI-750973, EBI-355744;
CC O00233; Q9HCM9: TRIM39; NbExp=4; IntAct=EBI-750973, EBI-739510;
CC O00233; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-750973, EBI-5235829;
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 -!- TISSUE SPECIFICITY: Expressed in all tissues tested, highly expressed
CC in liver and kidney.
CC -!- SIMILARITY: Belongs to the proteasome subunit p27 family.
CC {ECO:0000305}.
CC -!- CAUTION: Was initially identified as a component of the 26S proteasome.
CC {ECO:0000305}.
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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 CCDS; CCDS58284.1; -. [O00233-3]
DR CCDS; CCDS9225.1; -. [O00233-1]
DR RefSeq; NP_001248329.1; NM_001261400.2. [O00233-3]
DR RefSeq; NP_002804.2; NM_002813.6. [O00233-1]
DR AlphaFoldDB; O00233; -.
DR SMR; O00233; -.
DR BioGRID; 111687; 141.
DR CORUM; O00233; -.
DR IntAct; O00233; 35.
DR MINT; O00233; -.
DR STRING; 9606.ENSP00000440485; -.
DR GlyGen; O00233; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00233; -.
DR MetOSite; O00233; -.
DR PhosphoSitePlus; O00233; -.
DR BioMuta; PSMD9; -.
DR OGP; O00233; -.
DR EPD; O00233; -.
DR jPOST; O00233; -.
DR MassIVE; O00233; -.
DR MaxQB; O00233; -.
DR PaxDb; O00233; -.
DR PeptideAtlas; O00233; -.
DR PRIDE; O00233; -.
DR ProteomicsDB; 32407; -.
DR ProteomicsDB; 47799; -. [O00233-1]
DR ProteomicsDB; 47800; -. [O00233-2]
DR TopDownProteomics; O00233-1; -. [O00233-1]
DR Antibodypedia; 31601; 296 antibodies from 29 providers.
DR DNASU; 5715; -.
DR Ensembl; ENST00000537407.5; ENSP00000445058.1; ENSG00000110801.14. [O00233-2]
DR Ensembl; ENST00000541212.6; ENSP00000440485.1; ENSG00000110801.14. [O00233-1]
DR Ensembl; ENST00000542602.1; ENSP00000443772.1; ENSG00000110801.14. [O00233-3]
DR GeneID; 5715; -.
DR KEGG; hsa:5715; -.
DR MANE-Select; ENST00000541212.6; ENSP00000440485.1; NM_002813.7; NP_002804.2.
DR UCSC; uc001ubl.5; human. [O00233-1]
DR CTD; 5715; -.
DR DisGeNET; 5715; -.
DR GeneCards; PSMD9; -.
DR HGNC; HGNC:9567; PSMD9.
DR HPA; ENSG00000110801; Low tissue specificity.
DR MIM; 603146; gene.
DR neXtProt; NX_O00233; -.
DR OpenTargets; ENSG00000110801; -.
DR PharmGKB; PA33913; -.
DR VEuPathDB; HostDB:ENSG00000110801; -.
DR eggNOG; KOG3129; Eukaryota.
DR GeneTree; ENSGT00390000004147; -.
DR HOGENOM; CLU_073146_3_0_1; -.
DR InParanoid; O00233; -.
DR OMA; GCNIVPL; -.
DR OrthoDB; 1405146at2759; -.
DR PhylomeDB; O00233; -.
DR TreeFam; TF105995; -.
DR PathwayCommons; O00233; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; O00233; -.
DR BioGRID-ORCS; 5715; 74 hits in 1078 CRISPR screens.
DR ChiTaRS; PSMD9; human.
DR GeneWiki; PSMD9; -.
DR GenomeRNAi; 5715; -.
DR Pharos; O00233; Tbio.
DR PRO; PR:O00233; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O00233; protein.
DR Bgee; ENSG00000110801; Expressed in stromal cell of endometrium and 104 other tissues.
DR ExpressionAtlas; O00233; baseline and differential.
DR Genevisible; O00233; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
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:0046676; P:negative regulation of insulin secretion; ISS:BHF-UCL.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR GO; GO:0070682; P:proteasome regulatory particle assembly; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; NAS:UniProtKB.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR040815; Nas2_N.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR035269; PSMD9.
DR PANTHER; PTHR12651; PTHR12651; 1.
DR Pfam; PF18265; Nas2_N; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Phosphoprotein; Reference proteome.
FT CHAIN 1..223
FT /note="26S proteasome non-ATPase regulatory subunit 9"
FT /id="PRO_0000173852"
FT DOMAIN 108..195
FT /note="PDZ"
FT REGION 103..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CR00"
FT VAR_SEQ 47..151
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16712791"
FT /id="VSP_046004"
FT VAR_SEQ 186..223
FT /note="KPLNVTVIRRGEKHQLRLVPTRWAGKGLLGCNIIPLQR -> ALAPTILLSV
FT SMNLTTPGTSSRSP (in isoform p27-S)"
FT /evidence="ECO:0000303|PubMed:9653651"
FT /id="VSP_005300"
FT VARIANT 17
FT /note="V -> A (in dbSNP:rs2230681)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:16712791, ECO:0007744|PubMed:21269460"
FT /id="VAR_009953"
FT VARIANT 74
FT /note="T -> I (in dbSNP:rs2291116)"
FT /id="VAR_057047"
FT VARIANT 134
FT /note="R -> W (in dbSNP:rs1177573)"
FT /id="VAR_057048"
FT VARIANT 197
FT /note="E -> G (in dbSNP:rs14259)"
FT /id="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
