Full text data of PSMB2
PSMB2
[Confidence: high (present in two of the MS resources)]
Proteasome subunit beta type-2; 3.4.25.1 (Macropain subunit C7-I; Multicatalytic endopeptidase complex subunit C7-I; Proteasome component C7-I)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome subunit beta type-2; 3.4.25.1 (Macropain subunit C7-I; Multicatalytic endopeptidase complex subunit C7-I; Proteasome component C7-I)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00028006
IPI00028006 Proteasome subunit beta type 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
IPI00028006 Proteasome subunit beta type 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
P49721
ID PSB2_HUMAN Reviewed; 201 AA.
AC P49721; D3DPS0; P31145; Q9BWZ9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Proteasome subunit beta type-2;
DE EC=3.4.25.1;
DE AltName: Full=Macropain subunit C7-I;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C7-I;
DE AltName: Full=Proteasome component C7-I;
GN Name=PSMB2;
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].
RX PubMed=7918633; DOI=10.1016/0167-4781(94)90060-4;
RA Nothwang H.G., Tamura T., Tanaka K., Ichihara A.;
RT "Sequence analyses and inter-species comparisons of three novel human
RT proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine potential
RT proteolytic active-site residues.";
RL Biochim. Biophys. Acta 1219:361-368(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PROTEIN SEQUENCE OF 71-85 AND 171-181, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 172-177 AND 186-193.
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
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [9]
RP PROTEIN SEQUENCE OF 72-85.
RC TISSUE=Placenta;
RX PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
RA Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
RT "Human proteasome subunits from 2-dimensional gels identified by
RT partial sequencing.";
RL Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
RN [10]
RP INTERACTION WITH HIV-1 TAT.
RX PubMed=14550573; DOI=10.1016/S0014-5793(03)01025-1;
RA Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
RA Mayer R.J., Krueger E.;
RT "Human immunodeficiency virus-1 Tat protein interacts with distinct
RT proteasomal alpha and beta subunits.";
RL FEBS Lett. 553:200-204(2003).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP INDUCTION.
RX PubMed=19787249;
RA Wada T., Yamashita Y., Saga Y., Takahashi K., Koinuma K., Choi Y.L.,
RA Kaneda R., Fujiwara S., Soda M., Watanabe H., Kurashina K.,
RA Hatanaka H., Enomoto M., Takada S., Mano H., Suzuki M.;
RT "Screening for genetic abnormalities involved in ovarian
RT carcinogenesis using retroviral expression libraries.";
RL Int. J. Oncol. 35:973-976(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [15]
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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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: The proteasome is a multicatalytic proteinase complex
CC which is characterized by its ability to cleave peptides with Arg,
CC Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC activity. This subunit has a trypsin-like activity.
CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
CC specificity.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
CC two 19S regulatory subunits. The 20S proteasome core is composed
CC of 28 subunits that are arranged in four stacked rings, resulting
CC in a barrel-shaped structure. The two end rings are each formed by
CC seven alpha subunits, and the two central rings are each formed by
CC seven beta subunits. The catalytic chamber with the active sites
CC is on the inside of the barrel. Interacts with HIV-1 TAT protein.
CC -!- INTERACTION:
CC P49720:PSMB3; NbExp=4; IntAct=EBI-359335, EBI-603340;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- INDUCTION: Up-regulated in ovarian cancer cell lines.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
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DR EMBL; D26599; BAA05646.1; -; mRNA.
DR EMBL; CR456862; CAG33143.1; -; mRNA.
DR EMBL; BT007137; AAP35801.1; -; mRNA.
DR EMBL; AL354864; CAC36031.2; -; Genomic_DNA.
DR EMBL; AL157951; CAC36031.2; JOINED; Genomic_DNA.
DR EMBL; AL357035; CAC36031.2; JOINED; Genomic_DNA.
DR EMBL; AL357035; CAI22074.1; -; Genomic_DNA.
DR EMBL; AL354864; CAI22074.1; JOINED; Genomic_DNA.
DR EMBL; AL157951; CAI22074.1; JOINED; Genomic_DNA.
DR EMBL; AL157951; CAI23521.1; -; Genomic_DNA.
DR EMBL; AL354864; CAI23521.1; JOINED; Genomic_DNA.
DR EMBL; AL357035; CAI23521.1; JOINED; Genomic_DNA.
DR EMBL; CH471059; EAX07406.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07407.1; -; Genomic_DNA.
DR EMBL; BC101836; AAI01837.1; -; mRNA.
DR EMBL; BC105126; AAI05127.1; -; mRNA.
DR EMBL; BC107901; AAI07902.1; -; mRNA.
DR PIR; S55040; S55040.
DR RefSeq; NP_002785.1; NM_002794.4.
DR UniGene; Hs.471441; -.
DR ProteinModelPortal; P49721; -.
DR SMR; P49721; 1-199.
DR IntAct; P49721; 19.
DR MINT; MINT-1144735; -.
DR STRING; 9606.ENSP00000362334; -.
DR BindingDB; P49721; -.
DR ChEMBL; CHEMBL2364701; -.
DR DrugBank; DB00188; Bortezomib.
DR MEROPS; T01.984; -.
DR PhosphoSite; P49721; -.
DR DMDM; 1709762; -.
DR OGP; P49721; -.
DR REPRODUCTION-2DPAGE; IPI00028006; -.
DR REPRODUCTION-2DPAGE; P49721; -.
DR PaxDb; P49721; -.
DR PeptideAtlas; P49721; -.
DR PRIDE; P49721; -.
DR DNASU; 5690; -.
DR Ensembl; ENST00000373237; ENSP00000362334; ENSG00000126067.
DR GeneID; 5690; -.
DR KEGG; hsa:5690; -.
DR UCSC; uc001bzf.2; human.
DR CTD; 5690; -.
DR GeneCards; GC01M036042; -.
DR HGNC; HGNC:9539; PSMB2.
DR HPA; HPA026322; -.
DR HPA; HPA026324; -.
DR MIM; 602175; gene.
DR neXtProt; NX_P49721; -.
DR PharmGKB; PA33884; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000188743; -.
DR HOVERGEN; HBG000815; -.
DR KO; K02734; -.
DR OMA; HFVRGEL; -.
DR OrthoDB; EOG7N63NQ; -.
DR PhylomeDB; P49721; -.
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; PSMB2; human.
DR GeneWiki; PSMB2; -.
DR GenomeRNAi; 5690; -.
DR NextBio; 22102; -.
DR PRO; PR:P49721; -.
DR Bgee; P49721; -.
DR CleanEx; HS_PSMB2; -.
DR Genevestigator; P49721; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
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:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
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:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR Pfam; PF00227; Proteasome; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Hydrolase; Nucleus; Protease; Proteasome;
KW Reference proteome; Threonine protease.
FT CHAIN 1 201 Proteasome subunit beta type-2.
FT /FTId=PRO_0000148043.
FT MOD_RES 1 1 N-acetylmethionine.
SQ SEQUENCE 201 AA; 22836 MW; 04D085D7BAA76130 CRC64;
MEYLIGIQGP DYVLVASDRV AASNIVQMKD DHDKMFKMSE KILLLCVGEA GDTVQFAEYI
QKNVQLYKMR NGYELSPTAA ANFTRRNLAD CLRSRTPYHV NLLLAGYDEH EGPALYYMDY
LAALAKAPFA AHGYGAFLTL SILDRYYTPT ISRERAVELL RKCLEELQKR FILNLPTFSV
RIIDKNGIHD LDNISFPKQG S
//
ID PSB2_HUMAN Reviewed; 201 AA.
AC P49721; D3DPS0; P31145; Q9BWZ9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Proteasome subunit beta type-2;
DE EC=3.4.25.1;
DE AltName: Full=Macropain subunit C7-I;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C7-I;
DE AltName: Full=Proteasome component C7-I;
GN Name=PSMB2;
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].
RX PubMed=7918633; DOI=10.1016/0167-4781(94)90060-4;
RA Nothwang H.G., Tamura T., Tanaka K., Ichihara A.;
RT "Sequence analyses and inter-species comparisons of three novel human
RT proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine potential
RT proteolytic active-site residues.";
RL Biochim. Biophys. Acta 1219:361-368(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PROTEIN SEQUENCE OF 71-85 AND 171-181, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 172-177 AND 186-193.
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
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [9]
RP PROTEIN SEQUENCE OF 72-85.
RC TISSUE=Placenta;
RX PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
RA Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
RT "Human proteasome subunits from 2-dimensional gels identified by
RT partial sequencing.";
RL Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
RN [10]
RP INTERACTION WITH HIV-1 TAT.
RX PubMed=14550573; DOI=10.1016/S0014-5793(03)01025-1;
RA Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
RA Mayer R.J., Krueger E.;
RT "Human immunodeficiency virus-1 Tat protein interacts with distinct
RT proteasomal alpha and beta subunits.";
RL FEBS Lett. 553:200-204(2003).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP INDUCTION.
RX PubMed=19787249;
RA Wada T., Yamashita Y., Saga Y., Takahashi K., Koinuma K., Choi Y.L.,
RA Kaneda R., Fujiwara S., Soda M., Watanabe H., Kurashina K.,
RA Hatanaka H., Enomoto M., Takada S., Mano H., Suzuki M.;
RT "Screening for genetic abnormalities involved in ovarian
RT carcinogenesis using retroviral expression libraries.";
RL Int. J. Oncol. 35:973-976(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [15]
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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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: The proteasome is a multicatalytic proteinase complex
CC which is characterized by its ability to cleave peptides with Arg,
CC Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC activity. This subunit has a trypsin-like activity.
CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
CC specificity.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
CC two 19S regulatory subunits. The 20S proteasome core is composed
CC of 28 subunits that are arranged in four stacked rings, resulting
CC in a barrel-shaped structure. The two end rings are each formed by
CC seven alpha subunits, and the two central rings are each formed by
CC seven beta subunits. The catalytic chamber with the active sites
CC is on the inside of the barrel. Interacts with HIV-1 TAT protein.
CC -!- INTERACTION:
CC P49720:PSMB3; NbExp=4; IntAct=EBI-359335, EBI-603340;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- INDUCTION: Up-regulated in ovarian cancer cell lines.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
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DR EMBL; D26599; BAA05646.1; -; mRNA.
DR EMBL; CR456862; CAG33143.1; -; mRNA.
DR EMBL; BT007137; AAP35801.1; -; mRNA.
DR EMBL; AL354864; CAC36031.2; -; Genomic_DNA.
DR EMBL; AL157951; CAC36031.2; JOINED; Genomic_DNA.
DR EMBL; AL357035; CAC36031.2; JOINED; Genomic_DNA.
DR EMBL; AL357035; CAI22074.1; -; Genomic_DNA.
DR EMBL; AL354864; CAI22074.1; JOINED; Genomic_DNA.
DR EMBL; AL157951; CAI22074.1; JOINED; Genomic_DNA.
DR EMBL; AL157951; CAI23521.1; -; Genomic_DNA.
DR EMBL; AL354864; CAI23521.1; JOINED; Genomic_DNA.
DR EMBL; AL357035; CAI23521.1; JOINED; Genomic_DNA.
DR EMBL; CH471059; EAX07406.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07407.1; -; Genomic_DNA.
DR EMBL; BC101836; AAI01837.1; -; mRNA.
DR EMBL; BC105126; AAI05127.1; -; mRNA.
DR EMBL; BC107901; AAI07902.1; -; mRNA.
DR PIR; S55040; S55040.
DR RefSeq; NP_002785.1; NM_002794.4.
DR UniGene; Hs.471441; -.
DR ProteinModelPortal; P49721; -.
DR SMR; P49721; 1-199.
DR IntAct; P49721; 19.
DR MINT; MINT-1144735; -.
DR STRING; 9606.ENSP00000362334; -.
DR BindingDB; P49721; -.
DR ChEMBL; CHEMBL2364701; -.
DR DrugBank; DB00188; Bortezomib.
DR MEROPS; T01.984; -.
DR PhosphoSite; P49721; -.
DR DMDM; 1709762; -.
DR OGP; P49721; -.
DR REPRODUCTION-2DPAGE; IPI00028006; -.
DR REPRODUCTION-2DPAGE; P49721; -.
DR PaxDb; P49721; -.
DR PeptideAtlas; P49721; -.
DR PRIDE; P49721; -.
DR DNASU; 5690; -.
DR Ensembl; ENST00000373237; ENSP00000362334; ENSG00000126067.
DR GeneID; 5690; -.
DR KEGG; hsa:5690; -.
DR UCSC; uc001bzf.2; human.
DR CTD; 5690; -.
DR GeneCards; GC01M036042; -.
DR HGNC; HGNC:9539; PSMB2.
DR HPA; HPA026322; -.
DR HPA; HPA026324; -.
DR MIM; 602175; gene.
DR neXtProt; NX_P49721; -.
DR PharmGKB; PA33884; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000188743; -.
DR HOVERGEN; HBG000815; -.
DR KO; K02734; -.
DR OMA; HFVRGEL; -.
DR OrthoDB; EOG7N63NQ; -.
DR PhylomeDB; P49721; -.
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; PSMB2; human.
DR GeneWiki; PSMB2; -.
DR GenomeRNAi; 5690; -.
DR NextBio; 22102; -.
DR PRO; PR:P49721; -.
DR Bgee; P49721; -.
DR CleanEx; HS_PSMB2; -.
DR Genevestigator; P49721; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
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:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
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:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR Pfam; PF00227; Proteasome; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Hydrolase; Nucleus; Protease; Proteasome;
KW Reference proteome; Threonine protease.
FT CHAIN 1 201 Proteasome subunit beta type-2.
FT /FTId=PRO_0000148043.
FT MOD_RES 1 1 N-acetylmethionine.
SQ SEQUENCE 201 AA; 22836 MW; 04D085D7BAA76130 CRC64;
MEYLIGIQGP DYVLVASDRV AASNIVQMKD DHDKMFKMSE KILLLCVGEA GDTVQFAEYI
QKNVQLYKMR NGYELSPTAA ANFTRRNLAD CLRSRTPYHV NLLLAGYDEH EGPALYYMDY
LAALAKAPFA AHGYGAFLTL SILDRYYTPT ISRERAVELL RKCLEELQKR FILNLPTFSV
RIIDKNGIHD LDNISFPKQG S
//
MIM
602175
*RECORD*
*FIELD* NO
602175
*FIELD* TI
*602175 PROTEASOME SUBUNIT, BETA-TYPE, 2; PSMB2
;;PROTEASOME SUBUNIT BETA-4
*FIELD* TX
read moreThe proteasome is responsible for degradation of short lived and
misfolded cytosolic and nuclear proteins in the cell. It consists of a
complex of proteins that form a 20S core particle in both prokaryotes
and eukaryotes. The 20S proteasome is composed of 7 alpha and 7 beta
subunits that dimerize to form an alpha(7)beta(7)beta(7)alpha(7)
structure. Subunits are designated alpha or beta depending on their
homology to the Thermoplasma acidophilus proteasome in which the beta
subunits are catalytically active. The 20S core complex associates with
regulatory proteins that function as proteasome activators in vivo. One
pathway of activation uses a 19S complex that is involved in the
ubiquitin (191339) pathway of protein breakdown. The PA28 complex is an
alternative proteasome activator that does not employ the use of
ubiquitin. The complex is composed of 2 homologous subunits called alpha
and beta, which form a hexameric ring. PA28 appears to be involved in
the presentation of endogenous antigens by MHC class I molecules. The
PA28 complex is expressed constitutively in antigen-presenting cells,
and its expression is upregulated by interferon gamma (147570). Many of
the genes involved in class I antigen presentation are encoded within
the MHC, including the 2 proteasome subunits PSMB9 (177045), also known
as LMP2, and PSMB8 (177046), also known as LMP7. McCusker et al. (1997)
completed the mapping of the human proteasome beta-type genes: by
fluorescence in situ hybridization they mapped the PSMB2 gene to 1p34.2,
the PSMB3 gene (602176) to 2q35, and the PSMB4 gene (602177) to 1q21.
They also showed that the genes encoding the alpha (600654) and beta
(602161) subunits of the PA28 complex are closely linked on 14q11.2,
within 1 Mb of the beta proteasome locus PSMB5 (600306). Thus, with the
exception of the genes encoding the PSMB9 and PSMB8 subunits, the beta
genes are not closely linked in the human genome. PSMB2 and PSMB4 map to
regions of chromosome 1 that are proposed to be paralogous to regions of
the human genome where other beta proteasome genes map: chromosome 6,
containing the major histocompatibility complex, and chromosome 9.
*FIELD* RF
1. 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.
*FIELD* CD
Victor A. McKusick: 12/12/1997
*FIELD* ED
mgross: 06/25/2007
carol: 5/12/2004
dkim: 7/23/1998
mark: 12/12/1997
*RECORD*
*FIELD* NO
602175
*FIELD* TI
*602175 PROTEASOME SUBUNIT, BETA-TYPE, 2; PSMB2
;;PROTEASOME SUBUNIT BETA-4
*FIELD* TX
read moreThe proteasome is responsible for degradation of short lived and
misfolded cytosolic and nuclear proteins in the cell. It consists of a
complex of proteins that form a 20S core particle in both prokaryotes
and eukaryotes. The 20S proteasome is composed of 7 alpha and 7 beta
subunits that dimerize to form an alpha(7)beta(7)beta(7)alpha(7)
structure. Subunits are designated alpha or beta depending on their
homology to the Thermoplasma acidophilus proteasome in which the beta
subunits are catalytically active. The 20S core complex associates with
regulatory proteins that function as proteasome activators in vivo. One
pathway of activation uses a 19S complex that is involved in the
ubiquitin (191339) pathway of protein breakdown. The PA28 complex is an
alternative proteasome activator that does not employ the use of
ubiquitin. The complex is composed of 2 homologous subunits called alpha
and beta, which form a hexameric ring. PA28 appears to be involved in
the presentation of endogenous antigens by MHC class I molecules. The
PA28 complex is expressed constitutively in antigen-presenting cells,
and its expression is upregulated by interferon gamma (147570). Many of
the genes involved in class I antigen presentation are encoded within
the MHC, including the 2 proteasome subunits PSMB9 (177045), also known
as LMP2, and PSMB8 (177046), also known as LMP7. McCusker et al. (1997)
completed the mapping of the human proteasome beta-type genes: by
fluorescence in situ hybridization they mapped the PSMB2 gene to 1p34.2,
the PSMB3 gene (602176) to 2q35, and the PSMB4 gene (602177) to 1q21.
They also showed that the genes encoding the alpha (600654) and beta
(602161) subunits of the PA28 complex are closely linked on 14q11.2,
within 1 Mb of the beta proteasome locus PSMB5 (600306). Thus, with the
exception of the genes encoding the PSMB9 and PSMB8 subunits, the beta
genes are not closely linked in the human genome. PSMB2 and PSMB4 map to
regions of chromosome 1 that are proposed to be paralogous to regions of
the human genome where other beta proteasome genes map: chromosome 6,
containing the major histocompatibility complex, and chromosome 9.
*FIELD* RF
1. 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.
*FIELD* CD
Victor A. McKusick: 12/12/1997
*FIELD* ED
mgross: 06/25/2007
carol: 5/12/2004
dkim: 7/23/1998
mark: 12/12/1997