PSME1_HUMAN
ID PSME1_HUMAN Reviewed; 249 AA.
AC Q06323; A6NJG9; H0YNE3; Q6IBM2; Q9UEF4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Proteasome activator complex subunit 1;
DE AltName: Full=11S regulator complex subunit alpha;
DE Short=REG-alpha;
DE AltName: Full=Activator of multicatalytic protease subunit 1;
DE AltName: Full=Interferon gamma up-regulated I-5111 protein;
DE Short=IGUP I-5111;
DE AltName: Full=Proteasome activator 28 subunit alpha;
DE Short=PA28a;
DE Short=PA28alpha;
GN Name=PSME1; Synonyms=IFI5111;
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] (ISOFORM 1).
RC TISSUE=Lung fibroblast;
RX PubMed=8269930; DOI=10.1111/j.1432-1033.1993.tb18392.x;
RA Honore B., Leffers H., Madsen P., Celis J.E.;
RT "Interferon-gamma up-regulates a unique set of proteins in human
RT keratinocytes. Molecular cloning and expression of the cDNA encoding the
RT RGD-sequence-containing protein IGUP I-5111.";
RL Eur. J. Biochem. 218:421-430(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Blood;
RX PubMed=8051173; DOI=10.1016/s0021-9258(17)32052-5;
RA Realini C., Dubiel W., Pratt G., Ferrell K., Rechsteiner M.;
RT "Molecular cloning and expression of a gamma-interferon-inducible activator
RT of the multicatalytic protease.";
RL J. Biol. Chem. 269:20727-20732(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=10199920; DOI=10.1007/s002510050517;
RA McCusker D., Wilson M., Trowsdale J.;
RT "Organization of the genes encoding the human proteasome activators
RT PA28alpha and beta.";
RL Immunogenetics 49:438-445(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [8]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-118.
RX PubMed=9590240;
RA Kohda K., Ishibashi T., Shimbara N., Tanaka K., Matsuda Y., Kasahara M.;
RT "Characterization of the mouse PA28 activator complex gene family: complete
RT organizations of the three member genes and a physical map of the
RT approximately 150-kb region containing the alpha- and beta-subunit genes.";
RL J. Immunol. 160:4923-4935(1998).
RN [11]
RP PROTEIN SEQUENCE OF 25-35; 191-197 AND 199-209.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [12]
RP SUBUNIT.
RX PubMed=9385652; DOI=10.1002/pro.5560061123;
RA Johnston S.C., Whitby F.G., Realini C., Rechsteiner M., Hill C.P.;
RT "The proteasome 11S regulator subunit REG alpha (PA28 alpha) is a
RT heptamer.";
RL Protein Sci. 6:2469-2473(1997).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human 26S
RT proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=9403698; DOI=10.1038/37670;
RA Knowlton J.R., Johnston S.C., Whitby F.G., Realini C., Zhang Z.,
RA Rechsteiner M., Hill C.P.;
RT "Structure of the proteasome activator REGalpha (PA28alpha).";
RL Nature 390:639-643(1997).
CC -!- FUNCTION: Implicated in immunoproteasome assembly and required for
CC efficient antigen processing. The PA28 activator complex enhances the
CC generation of class I binding peptides by altering the cleavage pattern
CC of the proteasome.
CC -!- SUBUNIT: Heterodimer of PSME1 and PSME2, which forms a hexameric ring.
CC PSME1 can form homoheptamers. {ECO:0000269|PubMed:9385652}.
CC -!- INTERACTION:
CC Q06323; P22607: FGFR3; NbExp=3; IntAct=EBI-712149, EBI-348399;
CC Q06323; Q14957: GRIN2C; NbExp=3; IntAct=EBI-712149, EBI-8285963;
CC Q06323; P06396: GSN; NbExp=3; IntAct=EBI-712149, EBI-351506;
CC Q06323; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-712149, EBI-1055254;
CC Q06323; Q9UL46: PSME2; NbExp=6; IntAct=EBI-712149, EBI-741630;
CC Q06323; Q5JTV8: TOR1AIP1; NbExp=3; IntAct=EBI-712149, EBI-2559665;
CC Q06323; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-712149, EBI-741480;
CC Q06323; Q9Y649; NbExp=3; IntAct=EBI-712149, EBI-25900580;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q06323-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q06323-2; Sequence=VSP_046880;
CC Name=3;
CC IsoId=Q06323-3; Sequence=VSP_055166, VSP_055167;
CC -!- INDUCTION: By IFNG/IFN-gamma.
CC -!- SIMILARITY: Belongs to the PA28 family. {ECO:0000305}.
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DR EMBL; L07633; AAA16521.1; -; mRNA.
DR EMBL; U10360; AAA53230.1; -; Genomic_DNA.
DR EMBL; AF078829; AAF02217.1; -; Genomic_DNA.
DR EMBL; BT019337; AAV38144.1; -; mRNA.
DR EMBL; AK312211; BAG35144.1; -; mRNA.
DR EMBL; CR456780; CAG33061.1; -; mRNA.
DR EMBL; AL136295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66105.1; -; Genomic_DNA.
DR EMBL; BC000352; AAH00352.1; -; mRNA.
DR EMBL; BC007503; AAH07503.1; -; mRNA.
DR EMBL; AB007137; BAA28836.1; -; Genomic_DNA.
DR CCDS; CCDS41930.1; -. [Q06323-2]
DR CCDS; CCDS61415.1; -. [Q06323-3]
DR CCDS; CCDS9612.1; -. [Q06323-1]
DR PIR; A54859; A54859.
DR RefSeq; NP_001268457.1; NM_001281528.1. [Q06323-3]
DR RefSeq; NP_006254.1; NM_006263.3. [Q06323-1]
DR PDB; 1AVO; X-ray; 2.80 A; A/C/E/G/I/K/M=4-63, B/D/F/H/J/L/N=104-242.
DR PDB; 7DR6; EM; 4.10 A; B/C/E/G=1-249.
DR PDB; 7DRW; EM; 4.20 A; I/J/L/N/Q/a/e/i=1-249.
DR PDBsum; 1AVO; -.
DR PDBsum; 7DR6; -.
DR PDBsum; 7DRW; -.
DR AlphaFoldDB; Q06323; -.
DR SMR; Q06323; -.
DR BioGRID; 111692; 152.
DR CORUM; Q06323; -.
DR IntAct; Q06323; 60.
DR MINT; Q06323; -.
DR STRING; 9606.ENSP00000372155; -.
DR ChEMBL; CHEMBL4295804; -.
DR DrugBank; DB09130; Copper.
DR GlyGen; Q06323; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q06323; -.
DR MetOSite; Q06323; -.
DR PhosphoSitePlus; Q06323; -.
DR SwissPalm; Q06323; -.
DR BioMuta; PSME1; -.
DR DMDM; 1170519; -.
DR DOSAC-COBS-2DPAGE; Q06323; -.
DR OGP; Q06323; -.
DR SWISS-2DPAGE; Q06323; -.
DR CPTAC; CPTAC-121; -.
DR CPTAC; CPTAC-122; -.
DR EPD; Q06323; -.
DR jPOST; Q06323; -.
DR MassIVE; Q06323; -.
DR MaxQB; Q06323; -.
DR PaxDb; Q06323; -.
DR PeptideAtlas; Q06323; -.
DR PRIDE; Q06323; -.
DR ProteomicsDB; 1336; -.
DR ProteomicsDB; 40533; -.
DR ProteomicsDB; 58431; -. [Q06323-1]
DR TopDownProteomics; Q06323-1; -. [Q06323-1]
DR Antibodypedia; 1712; 322 antibodies from 38 providers.
DR DNASU; 5720; -.
DR Ensembl; ENST00000206451.11; ENSP00000206451.6; ENSG00000092010.15. [Q06323-1]
DR Ensembl; ENST00000382708.7; ENSP00000372155.3; ENSG00000092010.15. [Q06323-2]
DR Ensembl; ENST00000561435.5; ENSP00000453976.1; ENSG00000092010.15. [Q06323-3]
DR Ensembl; ENST00000643169.1; ENSP00000493882.1; ENSG00000284916.2. [Q06323-3]
DR Ensembl; ENST00000645537.2; ENSP00000495095.1; ENSG00000284916.2. [Q06323-1]
DR Ensembl; ENST00000646132.1; ENSP00000496083.1; ENSG00000284916.2. [Q06323-2]
DR GeneID; 5720; -.
DR KEGG; hsa:5720; -.
DR MANE-Select; ENST00000206451.11; ENSP00000206451.6; NM_006263.4; NP_006254.1.
DR UCSC; uc001wmg.4; human. [Q06323-1]
DR CTD; 5720; -.
DR DisGeNET; 5720; -.
DR GeneCards; PSME1; -.
DR HGNC; HGNC:9568; PSME1.
DR HPA; ENSG00000092010; Low tissue specificity.
DR MIM; 600654; gene.
DR neXtProt; NX_Q06323; -.
DR OpenTargets; ENSG00000092010; -.
DR PharmGKB; PA33914; -.
DR VEuPathDB; HostDB:ENSG00000092010; -.
DR eggNOG; KOG4470; Eukaryota.
DR GeneTree; ENSGT00950000183098; -.
DR HOGENOM; CLU_062515_0_0_1; -.
DR InParanoid; Q06323; -.
DR OMA; GPIYSNE; -.
DR PhylomeDB; Q06323; -.
DR TreeFam; TF106236; -.
DR PathwayCommons; Q06323; -.
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; Q06323; -.
DR BioGRID-ORCS; 5720; 311 hits in 1086 CRISPR screens.
DR ChiTaRS; PSME1; human.
DR EvolutionaryTrace; Q06323; -.
DR GeneWiki; PSME1; -.
DR GenomeRNAi; 5720; -.
DR Pharos; Q06323; Tbio.
DR PRO; PR:Q06323; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q06323; protein.
DR Bgee; ENSG00000092010; Expressed in granulocyte and 99 other tissues.
DR ExpressionAtlas; Q06323; baseline and differential.
DR Genevisible; Q06323; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0008537; C:proteasome activator complex; IEA:InterPro.
DR GO; GO:0000502; C:proteasome complex; TAS:ProtInc.
DR GO; GO:0061133; F:endopeptidase activator activity; IBA:GO_Central.
DR GO; GO:0019884; P:antigen processing and presentation of exogenous antigen; IEA:Ensembl.
DR GO; GO:0010950; P:positive regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.20.120.180; -; 1.
DR Gene3D; 1.20.5.120; -; 1.
DR InterPro; IPR003186; PA28_C.
DR InterPro; IPR036997; PA28_C_sf.
DR InterPro; IPR036996; PA28_N_sf.
DR InterPro; IPR009077; Proteasome_activ_PA28.
DR InterPro; IPR003185; Proteasome_activ_PA28_N.
DR InterPro; IPR036252; Proteasome_activ_sf.
DR PANTHER; PTHR10660; PTHR10660; 1.
DR Pfam; PF02251; PA28_alpha; 1.
DR Pfam; PF02252; PA28_beta; 1.
DR SUPFAM; SSF47216; SSF47216; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing; Proteasome;
KW Reference proteome.
FT CHAIN 1..249
FT /note="Proteasome activator complex subunit 1"
FT /id="PRO_0000161779"
FT REGION 60..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 224..249
FT /note="AVLYDIILKNFEKLKKPRGETKGMIY -> VRRQGQGRGGQRQLSQATHSLT
FT LQARG (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046880"
FT VAR_SEQ 224..233
FT /note="AVLYDIILKN -> VRRLCYMTSS (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_055166"
FT VAR_SEQ 234..249
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_055167"
FT VARIANT 55
FT /note="S -> N (in dbSNP:rs1803830)"
FT /id="VAR_011993"
FT VARIANT 244
FT /note="T -> K (in dbSNP:rs14930)"
FT /id="VAR_011994"
FT HELIX 8..30
FT /evidence="ECO:0007829|PDB:1AVO"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:1AVO"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1AVO"
FT HELIX 108..137
FT /evidence="ECO:0007829|PDB:1AVO"
FT HELIX 148..190
FT /evidence="ECO:0007829|PDB:1AVO"
FT HELIX 196..232
FT /evidence="ECO:0007829|PDB:1AVO"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:1AVO"
SQ SEQUENCE 249 AA; 28723 MW; 5E27727E5A0B0AAB CRC64;
MAMLRVQPEA QAKVDVFRED LCTKTENLLG SYFPKKISEL DAFLKEPALN EANLSNLKAP
LDIPVPDPVK EKEKEERKKQ QEKEDKDEKK KGEDEDKGPP CGPVNCNEKI VVLLQRLKPE
IKDVIEQLNL VTTWLQLQIP RIEDGNNFGV AVQEKVFELM TSLHTKLEGF HTQISKYFSE
RGDAVTKAAK QPHVGDYRQL VHELDEAEYR DIRLMVMEIR NAYAVLYDII LKNFEKLKKP
RGETKGMIY
