Full text data of PSME2
PSME2
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Proteasome activator complex subunit 2 (11S regulator complex subunit beta; REG-beta; Activator of multicatalytic protease subunit 2; Proteasome activator 28 subunit beta; PA28b; PA28beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome activator complex subunit 2 (11S regulator complex subunit beta; REG-beta; Activator of multicatalytic protease subunit 2; Proteasome activator 28 subunit beta; PA28b; PA28beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00384051
IPI00384051 Proteasome activator complex subunit 2 Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00384051 Proteasome activator complex subunit 2 Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q9UL46
ID PSME2_HUMAN Reviewed; 239 AA.
AC Q9UL46; Q15129;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 4.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Proteasome activator complex subunit 2;
DE AltName: Full=11S regulator complex subunit beta;
DE Short=REG-beta;
DE AltName: Full=Activator of multicatalytic protease subunit 2;
DE AltName: Full=Proteasome activator 28 subunit beta;
DE Short=PA28b;
DE Short=PA28beta;
GN Name=PSME2;
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 [GENOMIC DNA], AND VARIANT PRO-89.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-89.
RX PubMed=7789512; DOI=10.1016/0014-5793(95)00492-R;
RA Ahn J.Y., Tanahashi N., Akiyama K., Hisamatsu H., Noda C., Tanaka K.,
RA Chung C.H., Shibmara N., Willy P.J., Mott J.D., Slaughter C.A.,
RA DeMartino G.N.;
RT "Primary structures of two homologous subunits of PA28, a gamma-
RT interferon-inducible protein activator of the 20S proteasome.";
RL FEBS Lett. 366:37-42(1995).
RN [3]
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.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA 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.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-89.
RC TISSUE=Liver, Pancreas, and Placenta;
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 [5]
RP PROTEIN SEQUENCE OF 2-61; 91-115; 132-145; 155-171; 181-226 AND
RP 232-239, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [6]
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
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Implicated in immunoproteasome assembly and required for
CC efficient antigen processing. The PA28 activator complex enhances
CC the generation of class I binding peptides by altering the
CC cleavage pattern of the proteasome.
CC -!- SUBUNIT: Heterodimer of PSME1 and PSME2, which forms a hexameric
CC ring.
CC -!- INDUCTION: By IFNG/IFN-gamma.
CC -!- SIMILARITY: Belongs to the PA28 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF079558; AAF02218.1; -; Genomic_DNA.
DR EMBL; D45248; BAA08205.1; -; mRNA.
DR EMBL; AL136295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004368; AAH04368.1; -; mRNA.
DR EMBL; BC019885; AAH19885.1; -; mRNA.
DR EMBL; BC072025; AAH72025.1; -; mRNA.
DR PIR; I53518; I53518.
DR RefSeq; NP_002809.2; NM_002818.2.
DR UniGene; Hs.434081; -.
DR UniGene; Hs.512410; -.
DR ProteinModelPortal; Q9UL46; -.
DR SMR; Q9UL46; 7-66, 97-232.
DR IntAct; Q9UL46; 13.
DR MINT; MINT-1478095; -.
DR STRING; 9606.ENSP00000216802; -.
DR PhosphoSite; Q9UL46; -.
DR DMDM; 296453017; -.
DR OGP; Q9UL46; -.
DR REPRODUCTION-2DPAGE; IPI00384051; -.
DR PaxDb; Q9UL46; -.
DR PRIDE; Q9UL46; -.
DR DNASU; 5721; -.
DR Ensembl; ENST00000216802; ENSP00000216802; ENSG00000100911.
DR GeneID; 5721; -.
DR KEGG; hsa:5721; -.
DR UCSC; uc001wmj.3; human.
DR CTD; 5721; -.
DR GeneCards; GC14M024612; -.
DR HGNC; HGNC:9569; PSME2.
DR MIM; 602161; gene.
DR neXtProt; NX_Q9UL46; -.
DR PharmGKB; PA33915; -.
DR eggNOG; NOG280316; -.
DR HOGENOM; HOG000282822; -.
DR HOVERGEN; HBG053745; -.
DR KO; K06697; -.
DR OMA; DGFQTNI; -.
DR PhylomeDB; Q9UL46; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSME2; human.
DR GeneWiki; PSME2; -.
DR GenomeRNAi; 5721; -.
DR NextBio; 22238; -.
DR PRO; PR:Q9UL46; -.
DR ArrayExpress; Q9UL46; -.
DR Bgee; Q9UL46; -.
DR CleanEx; HS_PSME2; -.
DR Genevestigator; Q9UL46; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0008537; C:proteasome activator complex; IEA:InterPro.
DR GO; GO:0000502; C:proteasome complex; TAS:ProtInc.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.20.120.180; -; 1.
DR Gene3D; 1.20.5.120; -; 1.
DR InterPro; IPR009077; Proteasome_activ_pa28.
DR InterPro; IPR003186; Proteasome_activ_pa28_C.
DR InterPro; IPR003185; Proteasome_activ_pa28_N.
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 Acetylation; Complete proteome; Direct protein sequencing;
KW Phosphoprotein; Polymorphism; Proteasome; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 239 Proteasome activator complex subunit 2.
FT /FTId=PRO_0000161785.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 10 10 Phosphoserine.
FT VARIANT 89 89 H -> P (in dbSNP:rs7146672).
FT /FTId=VAR_063111.
FT CONFLICT 229 229 N -> T (in Ref. 2; BAA08205).
SQ SEQUENCE 239 AA; 27402 MW; 98A30D83B3F93A91 CRC64;
MAKPCGVRLS GEARKQVEVF RQNLFQEAEE FLYRFLPQKI IYLNQLLQED SLNVADLTSL
RAPLDIPIPD PPPKDDEMET DKQEKKEVHK CGFLPGNEKV LSLLALVKPE VWTLKEKCIL
VITWIQHLIP KIEDGNDFGV AIQEKVLERV NAVKTKVEAF QTTISKYFSE RGDAVAKASK
ETHVMDYRAL VHERDEAAYG ELRAMVLDLR AFYAELYHII SSNLEKIVNP KGEEKPSMY
//
ID PSME2_HUMAN Reviewed; 239 AA.
AC Q9UL46; Q15129;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 4.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Proteasome activator complex subunit 2;
DE AltName: Full=11S regulator complex subunit beta;
DE Short=REG-beta;
DE AltName: Full=Activator of multicatalytic protease subunit 2;
DE AltName: Full=Proteasome activator 28 subunit beta;
DE Short=PA28b;
DE Short=PA28beta;
GN Name=PSME2;
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 [GENOMIC DNA], AND VARIANT PRO-89.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-89.
RX PubMed=7789512; DOI=10.1016/0014-5793(95)00492-R;
RA Ahn J.Y., Tanahashi N., Akiyama K., Hisamatsu H., Noda C., Tanaka K.,
RA Chung C.H., Shibmara N., Willy P.J., Mott J.D., Slaughter C.A.,
RA DeMartino G.N.;
RT "Primary structures of two homologous subunits of PA28, a gamma-
RT interferon-inducible protein activator of the 20S proteasome.";
RL FEBS Lett. 366:37-42(1995).
RN [3]
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.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA 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.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-89.
RC TISSUE=Liver, Pancreas, and Placenta;
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 [5]
RP PROTEIN SEQUENCE OF 2-61; 91-115; 132-145; 155-171; 181-226 AND
RP 232-239, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [6]
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
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Implicated in immunoproteasome assembly and required for
CC efficient antigen processing. The PA28 activator complex enhances
CC the generation of class I binding peptides by altering the
CC cleavage pattern of the proteasome.
CC -!- SUBUNIT: Heterodimer of PSME1 and PSME2, which forms a hexameric
CC ring.
CC -!- INDUCTION: By IFNG/IFN-gamma.
CC -!- SIMILARITY: Belongs to the PA28 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF079558; AAF02218.1; -; Genomic_DNA.
DR EMBL; D45248; BAA08205.1; -; mRNA.
DR EMBL; AL136295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004368; AAH04368.1; -; mRNA.
DR EMBL; BC019885; AAH19885.1; -; mRNA.
DR EMBL; BC072025; AAH72025.1; -; mRNA.
DR PIR; I53518; I53518.
DR RefSeq; NP_002809.2; NM_002818.2.
DR UniGene; Hs.434081; -.
DR UniGene; Hs.512410; -.
DR ProteinModelPortal; Q9UL46; -.
DR SMR; Q9UL46; 7-66, 97-232.
DR IntAct; Q9UL46; 13.
DR MINT; MINT-1478095; -.
DR STRING; 9606.ENSP00000216802; -.
DR PhosphoSite; Q9UL46; -.
DR DMDM; 296453017; -.
DR OGP; Q9UL46; -.
DR REPRODUCTION-2DPAGE; IPI00384051; -.
DR PaxDb; Q9UL46; -.
DR PRIDE; Q9UL46; -.
DR DNASU; 5721; -.
DR Ensembl; ENST00000216802; ENSP00000216802; ENSG00000100911.
DR GeneID; 5721; -.
DR KEGG; hsa:5721; -.
DR UCSC; uc001wmj.3; human.
DR CTD; 5721; -.
DR GeneCards; GC14M024612; -.
DR HGNC; HGNC:9569; PSME2.
DR MIM; 602161; gene.
DR neXtProt; NX_Q9UL46; -.
DR PharmGKB; PA33915; -.
DR eggNOG; NOG280316; -.
DR HOGENOM; HOG000282822; -.
DR HOVERGEN; HBG053745; -.
DR KO; K06697; -.
DR OMA; DGFQTNI; -.
DR PhylomeDB; Q9UL46; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSME2; human.
DR GeneWiki; PSME2; -.
DR GenomeRNAi; 5721; -.
DR NextBio; 22238; -.
DR PRO; PR:Q9UL46; -.
DR ArrayExpress; Q9UL46; -.
DR Bgee; Q9UL46; -.
DR CleanEx; HS_PSME2; -.
DR Genevestigator; Q9UL46; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0008537; C:proteasome activator complex; IEA:InterPro.
DR GO; GO:0000502; C:proteasome complex; TAS:ProtInc.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.20.120.180; -; 1.
DR Gene3D; 1.20.5.120; -; 1.
DR InterPro; IPR009077; Proteasome_activ_pa28.
DR InterPro; IPR003186; Proteasome_activ_pa28_C.
DR InterPro; IPR003185; Proteasome_activ_pa28_N.
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 Acetylation; Complete proteome; Direct protein sequencing;
KW Phosphoprotein; Polymorphism; Proteasome; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 239 Proteasome activator complex subunit 2.
FT /FTId=PRO_0000161785.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 10 10 Phosphoserine.
FT VARIANT 89 89 H -> P (in dbSNP:rs7146672).
FT /FTId=VAR_063111.
FT CONFLICT 229 229 N -> T (in Ref. 2; BAA08205).
SQ SEQUENCE 239 AA; 27402 MW; 98A30D83B3F93A91 CRC64;
MAKPCGVRLS GEARKQVEVF RQNLFQEAEE FLYRFLPQKI IYLNQLLQED SLNVADLTSL
RAPLDIPIPD PPPKDDEMET DKQEKKEVHK CGFLPGNEKV LSLLALVKPE VWTLKEKCIL
VITWIQHLIP KIEDGNDFGV AIQEKVLERV NAVKTKVEAF QTTISKYFSE RGDAVAKASK
ETHVMDYRAL VHERDEAAYG ELRAMVLDLR AFYAELYHII SSNLEKIVNP KGEEKPSMY
//
MIM
602161
*RECORD*
*FIELD* NO
602161
*FIELD* TI
*602161 PROTEASOME ACTIVATOR SUBUNIT 2; PSME2
;;PROTEASOME ACTIVATOR 28-BETA;;
PA28-BETA; PA28B;;
read moreMCP ACTIVATOR, 31-KD SUBUNIT
*FIELD* TX
See PSME1 (600654) for further discussion of this gene family.
Ahn et al. (1995) reported the sequence of the human PA28-beta (PSME2)
gene and those of rat PA28-alpha (PSME1) and -beta. McCusker et al.
(1999) sequenced the PSME1 and PSME2 genes. They found that each gene
comprises 11 exons, consistent with gene duplication during vertebrate
evolution. The intron/exon organization of the genes was highly
conserved, the major difference being the absence of the exon encoding
the lysine and glutamic acid-rich KEKE motif in the gene product of the
PSME2 gene.
McCusker et al. (1997) used fluorescence in situ hybridization to show
that PSME1 and PSME2 lie within 30 to 40 kb of each other on band
14q11.2.
In vitro, PA28 binds and activates proteasomes. Preckel et al. (1999)
demonstrated that mice with a disrupted Pa28b gene lack Pa28a (Psme1)
and Pa28b polypeptides, demonstrating that Pa28 functions as a
heterooligomer in vivo. Processing of antigenic epitopes derived from
exogenous or endogenous antigens is altered in Pa28 -/- mice. Cytotoxic
T-lymphocyte responses are impaired and assembly of immunoproteasomes is
greatly inhibited in mice lacking Pa28. These results showed that PA28
is necessary for immunoproteasome assembly and is required for efficient
antigen processing, thus demonstrating the importance of PA28-mediated
proteasome function in immune responses.
*FIELD* RF
1. Ahn, J. Y.; Tanahashi, N.; Akiyama, K.; Hisamatsu, H.; Noda, C.;
Tanaka, K.; Chung, C. H.; Shibmara, N.; Willy, P. J.; Mott, J. D.;
Slaughter, C. A.; DeMartino, G. N.: Primary structures of two homologous
subunits of PA28, a gamma-interferon-inducible protein activator of
the 2OS proteasome. FEBS Lett. 366: 37-42, 1995.
2. McCusker, D.; Jones, T.; Sheer, D.; Trowsdale, J.: Genetic relationships
of the genes encoding the human proteasome beta subunits and the proteasome
PA28 complex. Genomics 45: 362-367, 1997.
3. McCusker, D.; Wilson, M.; Trowsdale, J.: Organization of the genes
encoding the human proteasome activators PA28-alpha and beta. Immunogenetics 49:
438-445, 1999.
4. Preckel, T.; Fung-Leung, W.-P.; Cai, Z.; Vitiello, A.; Salter-Cid,
L.; Winqvist, O.; Wolfe, T. G.; Von Herrath, M.; Angulo, A.; Ghazal,
P.; Lee, J.-D.; Fourie, A. M.; Wu, Y.; Pang, J.; Ngo, K.; Peterson,
P. A.; Fruh, K.; Yang, Y.: Impaired immunoproteasome assembly and
immune responses in PA28 -/- mice. Science 286: 2162-2165, 1999.
*FIELD* CD
Victor A. McKusick: 12/10/1997
*FIELD* ED
terry: 03/21/2001
alopez: 12/9/1999
jlewis: 6/17/1999
dholmes: 1/23/1998
mark: 12/10/1997
*RECORD*
*FIELD* NO
602161
*FIELD* TI
*602161 PROTEASOME ACTIVATOR SUBUNIT 2; PSME2
;;PROTEASOME ACTIVATOR 28-BETA;;
PA28-BETA; PA28B;;
read moreMCP ACTIVATOR, 31-KD SUBUNIT
*FIELD* TX
See PSME1 (600654) for further discussion of this gene family.
Ahn et al. (1995) reported the sequence of the human PA28-beta (PSME2)
gene and those of rat PA28-alpha (PSME1) and -beta. McCusker et al.
(1999) sequenced the PSME1 and PSME2 genes. They found that each gene
comprises 11 exons, consistent with gene duplication during vertebrate
evolution. The intron/exon organization of the genes was highly
conserved, the major difference being the absence of the exon encoding
the lysine and glutamic acid-rich KEKE motif in the gene product of the
PSME2 gene.
McCusker et al. (1997) used fluorescence in situ hybridization to show
that PSME1 and PSME2 lie within 30 to 40 kb of each other on band
14q11.2.
In vitro, PA28 binds and activates proteasomes. Preckel et al. (1999)
demonstrated that mice with a disrupted Pa28b gene lack Pa28a (Psme1)
and Pa28b polypeptides, demonstrating that Pa28 functions as a
heterooligomer in vivo. Processing of antigenic epitopes derived from
exogenous or endogenous antigens is altered in Pa28 -/- mice. Cytotoxic
T-lymphocyte responses are impaired and assembly of immunoproteasomes is
greatly inhibited in mice lacking Pa28. These results showed that PA28
is necessary for immunoproteasome assembly and is required for efficient
antigen processing, thus demonstrating the importance of PA28-mediated
proteasome function in immune responses.
*FIELD* RF
1. Ahn, J. Y.; Tanahashi, N.; Akiyama, K.; Hisamatsu, H.; Noda, C.;
Tanaka, K.; Chung, C. H.; Shibmara, N.; Willy, P. J.; Mott, J. D.;
Slaughter, C. A.; DeMartino, G. N.: Primary structures of two homologous
subunits of PA28, a gamma-interferon-inducible protein activator of
the 2OS proteasome. FEBS Lett. 366: 37-42, 1995.
2. McCusker, D.; Jones, T.; Sheer, D.; Trowsdale, J.: Genetic relationships
of the genes encoding the human proteasome beta subunits and the proteasome
PA28 complex. Genomics 45: 362-367, 1997.
3. McCusker, D.; Wilson, M.; Trowsdale, J.: Organization of the genes
encoding the human proteasome activators PA28-alpha and beta. Immunogenetics 49:
438-445, 1999.
4. Preckel, T.; Fung-Leung, W.-P.; Cai, Z.; Vitiello, A.; Salter-Cid,
L.; Winqvist, O.; Wolfe, T. G.; Von Herrath, M.; Angulo, A.; Ghazal,
P.; Lee, J.-D.; Fourie, A. M.; Wu, Y.; Pang, J.; Ngo, K.; Peterson,
P. A.; Fruh, K.; Yang, Y.: Impaired immunoproteasome assembly and
immune responses in PA28 -/- mice. Science 286: 2162-2165, 1999.
*FIELD* CD
Victor A. McKusick: 12/10/1997
*FIELD* ED
terry: 03/21/2001
alopez: 12/9/1999
jlewis: 6/17/1999
dholmes: 1/23/1998
mark: 12/10/1997