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Proteasome activator complex subunit 1 (11S regulator complex subunit alpha) (REG-alpha) (Activator of multicatalytic protease subunit 1) (Interferon gamma up-regulated I-5111 protein) (IGUP I-5111) (Proteasome activator 28 subunit alpha) (PA28a) (PA28alpha)

 PSME1_HUMAN             Reviewed;         249 AA.
Q06323; A6NJG9; H0YNE3; Q6IBM2; Q9UEF4;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-OCT-2017, entry version 174.
RecName: Full=Proteasome activator complex subunit 1;
AltName: Full=11S regulator complex subunit alpha;
Short=REG-alpha;
AltName: Full=Activator of multicatalytic protease subunit 1;
AltName: Full=Interferon gamma up-regulated I-5111 protein;
Short=IGUP I-5111;
AltName: Full=Proteasome activator 28 subunit alpha;
Short=PA28a;
Short=PA28alpha;
Name=PSME1; Synonyms=IFI5111;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lung fibroblast;
PubMed=8269930; DOI=10.1111/j.1432-1033.1993.tb18392.x;
Honore B., Leffers H., Madsen P., Celis J.E.;
"Interferon-gamma up-regulates a unique set of proteins in human
keratinocytes. Molecular cloning and expression of the cDNA encoding
the RGD-sequence-containing protein IGUP I-5111.";
Eur. J. Biochem. 218:421-430(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
TISSUE=Blood;
PubMed=8051173;
Realini C., Dubiel W., Pratt G., Ferrell K., Rechsteiner M.;
"Molecular cloning and expression of a gamma-interferon-inducible
activator of the multicatalytic protease.";
J. Biol. Chem. 269:20727-20732(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=10199920; DOI=10.1007/s002510050517;
McCusker D., Wilson M., Trowsdale J.;
"Organization of the genes encoding the human proteasome activators
PA28alpha and beta.";
Immunogenetics 49:438-445(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-118.
PubMed=9590240;
Kohda K., Ishibashi T., Shimbara N., Tanaka K., Matsuda Y.,
Kasahara M.;
"Characterization of the mouse PA28 activator complex gene family:
complete organizations of the three member genes and a physical map of
the approximately 150-kb region containing the alpha- and beta-subunit
genes.";
J. Immunol. 160:4923-4935(1998).
[11]
PROTEIN SEQUENCE OF 25-35; 191-197 AND 199-209.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[12]
SUBUNIT.
PubMed=9385652; DOI=10.1002/pro.5560061123;
Johnston S.C., Whitby F.G., Realini C., Rechsteiner M., Hill C.P.;
"The proteasome 11S regulator subunit REG alpha (PA28 alpha) is a
heptamer.";
Protein Sci. 6:2469-2473(1997).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human
26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[17]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=9403698; DOI=10.1038/37670;
Knowlton J.R., Johnston S.C., Whitby F.G., Realini C., Zhang Z.,
Rechsteiner M., Hill C.P.;
"Structure of the proteasome activator REGalpha (PA28alpha).";
Nature 390:639-643(1997).
-!- FUNCTION: Implicated in immunoproteasome assembly and required for
efficient antigen processing. The PA28 activator complex enhances
the generation of class I binding peptides by altering the
cleavage pattern of the proteasome.
-!- SUBUNIT: Heterodimer of PSME1 and PSME2, which forms a hexameric
ring. PSME1 can form homoheptamers. {ECO:0000269|PubMed:9385652}.
-!- INTERACTION:
Q9UL46:PSME2; NbExp=5; IntAct=EBI-712149, EBI-741630;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q06323-1; Sequence=Displayed;
Name=2;
IsoId=Q06323-2; Sequence=VSP_046880;
Note=Gene prediction based on EST data.;
Name=3;
IsoId=Q06323-3; Sequence=VSP_055166, VSP_055167;
Note=Gene prediction based on EST data.;
-!- INDUCTION: By IFNG/IFN-gamma.
-!- SIMILARITY: Belongs to the PA28 family. {ECO:0000305}.
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EMBL; L07633; AAA16521.1; -; mRNA.
EMBL; U10360; AAA53230.1; -; Genomic_DNA.
EMBL; AF078829; AAF02217.1; -; Genomic_DNA.
EMBL; BT019337; AAV38144.1; -; mRNA.
EMBL; AK312211; BAG35144.1; -; mRNA.
EMBL; CR456780; CAG33061.1; -; mRNA.
EMBL; AL136295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471078; EAW66105.1; -; Genomic_DNA.
EMBL; BC000352; AAH00352.1; -; mRNA.
EMBL; BC007503; AAH07503.1; -; mRNA.
EMBL; AB007137; BAA28836.1; -; Genomic_DNA.
CCDS; CCDS41930.1; -. [Q06323-2]
CCDS; CCDS61415.1; -. [Q06323-3]
CCDS; CCDS9612.1; -. [Q06323-1]
PIR; A54859; A54859.
RefSeq; NP_001268457.1; NM_001281528.1. [Q06323-3]
RefSeq; NP_006254.1; NM_006263.3. [Q06323-1]
UniGene; Hs.75348; -.
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.
PDBsum; 1AVO; -.
ProteinModelPortal; Q06323; -.
SMR; Q06323; -.
BioGrid; 111692; 79.
CORUM; Q06323; -.
IntAct; Q06323; 26.
MINT; MINT-5002728; -.
STRING; 9606.ENSP00000372155; -.
iPTMnet; Q06323; -.
PhosphoSitePlus; Q06323; -.
SwissPalm; Q06323; -.
DMDM; 1170519; -.
DOSAC-COBS-2DPAGE; Q06323; -.
OGP; Q06323; -.
SWISS-2DPAGE; Q06323; -.
EPD; Q06323; -.
PaxDb; Q06323; -.
PeptideAtlas; Q06323; -.
PRIDE; Q06323; -.
TopDownProteomics; Q06323-1; -. [Q06323-1]
DNASU; 5720; -.
Ensembl; ENST00000206451; ENSP00000206451; ENSG00000092010. [Q06323-1]
Ensembl; ENST00000382708; ENSP00000372155; ENSG00000092010. [Q06323-2]
Ensembl; ENST00000561435; ENSP00000453976; ENSG00000092010. [Q06323-3]
GeneID; 5720; -.
KEGG; hsa:5720; -.
UCSC; uc001wmg.4; human. [Q06323-1]
CTD; 5720; -.
DisGeNET; 5720; -.
EuPathDB; HostDB:ENSG00000092010.14; -.
GeneCards; PSME1; -.
HGNC; HGNC:9568; PSME1.
HPA; HPA006632; -.
MIM; 600654; gene.
neXtProt; NX_Q06323; -.
OpenTargets; ENSG00000092010; -.
PharmGKB; PA33914; -.
eggNOG; KOG4470; Eukaryota.
eggNOG; ENOG410XQVX; LUCA.
GeneTree; ENSGT00510000046374; -.
HOGENOM; HOG000282822; -.
HOVERGEN; HBG053745; -.
InParanoid; Q06323; -.
KO; K06696; -.
OMA; TQISKYY; -.
OrthoDB; EOG091G0GX7; -.
PhylomeDB; Q06323; -.
TreeFam; TF106236; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; PSME1; human.
EvolutionaryTrace; Q06323; -.
GeneWiki; PSME1; -.
GenomeRNAi; 5720; -.
PRO; PR:Q06323; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000092010; -.
CleanEx; HS_PSME1; -.
ExpressionAtlas; Q06323; baseline and differential.
Genevisible; Q06323; HS.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0008537; C:proteasome activator complex; IEA:InterPro.
GO; GO:0000502; C:proteasome complex; TAS:ProtInc.
GO; GO:0061133; F:endopeptidase activator activity; IBA:GO_Central.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0010950; P:positive regulation of endopeptidase activity; IBA:GO_Central.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IBA:GO_Central.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
Gene3D; 1.20.120.180; -; 1.
Gene3D; 1.20.5.120; -; 1.
InterPro; IPR003186; PA28_C.
InterPro; IPR036997; PA28_C_sf.
InterPro; IPR036996; PA28_N_sf.
InterPro; IPR009077; Proteasome_activ_PA28.
InterPro; IPR003185; Proteasome_activ_PA28_N.
InterPro; IPR036252; Proteasome_activ_sf.
PANTHER; PTHR10660; PTHR10660; 1.
Pfam; PF02251; PA28_alpha; 1.
Pfam; PF02252; PA28_beta; 1.
SUPFAM; SSF47216; SSF47216; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Polymorphism; Proteasome;
Reference proteome.
CHAIN 1 249 Proteasome activator complex subunit 1.
/FTId=PRO_0000161779.
VAR_SEQ 224 249 AVLYDIILKNFEKLKKPRGETKGMIY -> VRRQGQGRGGQ
RQLSQATHSLTLQARG (in isoform 2).
{ECO:0000305}.
/FTId=VSP_046880.
VAR_SEQ 224 233 AVLYDIILKN -> VRRLCYMTSS (in isoform 3).
{ECO:0000305}.
/FTId=VSP_055166.
VAR_SEQ 234 249 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_055167.
VARIANT 55 55 S -> N (in dbSNP:rs1803830).
/FTId=VAR_011993.
VARIANT 244 244 T -> K (in dbSNP:rs14930).
/FTId=VAR_011994.
HELIX 8 30 {ECO:0000244|PDB:1AVO}.
HELIX 32 45 {ECO:0000244|PDB:1AVO}.
HELIX 47 49 {ECO:0000244|PDB:1AVO}.
HELIX 108 137 {ECO:0000244|PDB:1AVO}.
HELIX 148 190 {ECO:0000244|PDB:1AVO}.
HELIX 196 232 {ECO:0000244|PDB:1AVO}.
HELIX 234 238 {ECO:0000244|PDB:1AVO}.
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


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