Full text data of PSMB1
PSMB1
(PSC5)
[Confidence: high (present in two of the MS resources)]
Proteasome subunit beta type-1; 3.4.25.1 (Macropain subunit C5; Multicatalytic endopeptidase complex subunit C5; Proteasome component C5; Proteasome gamma chain; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome subunit beta type-1; 3.4.25.1 (Macropain subunit C5; Multicatalytic endopeptidase complex subunit C5; Proteasome component C5; Proteasome gamma chain; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00025019
IPI00025019 Proteasome subunit beta type 1 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
IPI00025019 Proteasome subunit beta type 1 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
P20618
ID PSB1_HUMAN Reviewed; 241 AA.
AC P20618; B5BU76; Q9BWA8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1992, sequence version 2.
DT 22-JAN-2014, entry version 152.
DE RecName: Full=Proteasome subunit beta type-1;
DE EC=3.4.25.1;
DE AltName: Full=Macropain subunit C5;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C5;
DE AltName: Full=Proteasome component C5;
DE AltName: Full=Proteasome gamma chain;
DE Flags: Precursor;
GN Name=PSMB1; Synonyms=PSC5;
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=2025653; DOI=10.1016/0167-4781(91)90090-9;
RA Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H.,
RA Tanaka K., Ichihara A.;
RT "Molecular cloning and sequence analysis of cDNAs for five major
RT subunits of human proteasomes (multi-catalytic proteinase
RT complexes).";
RL Biochim. Biophys. Acta 1089:95-102(1991).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-11.
RC TISSUE=Brain, and Lung;
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 [6]
RP PROTEIN SEQUENCE OF 29-52.
RX PubMed=2306472; DOI=10.1016/0167-4838(90)90165-C;
RA Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N.,
RA Slaughter C.A.;
RT "Relationships among the subunits of the high molecular weight
RT proteinase, macropain (proteasome).";
RL Biochim. Biophys. Acta 1037:178-185(1990).
RN [7]
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 [8]
RP INTERACTION WITH SERPINB2.
RX PubMed=14732874; DOI=10.1093/abbs/36.1.42;
RA Fan J., Zhang Y.Q., Li P., Hou M., Tan L., Wang X., Zhu Y.S.;
RT "Interaction of plasminogen activator inhibitor-2 and proteasome
RT subunit, beta type 1.";
RL Acta Biochim. Biophys. Sin. 36:42-46(2004).
RN [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
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 [12]
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.
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 SERPINB2. Interacts
CC with HIV-1 TAT protein.
CC -!- INTERACTION:
CC P28074:PSMB5; NbExp=3; IntAct=EBI-372273, EBI-357828;
CC Q99436:PSMB7; NbExp=8; IntAct=EBI-372273, EBI-603319;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
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DR EMBL; D00761; BAA00658.1; -; mRNA.
DR EMBL; BT019720; AAV38525.1; -; mRNA.
DR EMBL; AB451312; BAG70126.1; -; mRNA.
DR EMBL; AB451442; BAG70256.1; -; mRNA.
DR EMBL; AL031259; CAA20287.1; -; Genomic_DNA.
DR EMBL; BC000508; AAH00508.1; -; mRNA.
DR EMBL; BC020807; AAH20807.1; -; mRNA.
DR PIR; S15973; SNHUC5.
DR RefSeq; NP_002784.1; NM_002793.3.
DR UniGene; Hs.352768; -.
DR ProteinModelPortal; P20618; -.
DR SMR; P20618; 29-241.
DR IntAct; P20618; 21.
DR MINT; MINT-3009312; -.
DR STRING; 9606.ENSP00000262193; -.
DR BindingDB; P20618; -.
DR ChEMBL; CHEMBL4208; -.
DR DrugBank; DB00188; Bortezomib.
DR MEROPS; T01.986; -.
DR PhosphoSite; P20618; -.
DR DMDM; 130853; -.
DR REPRODUCTION-2DPAGE; IPI00025019; -.
DR UCD-2DPAGE; P20618; -.
DR PaxDb; P20618; -.
DR PeptideAtlas; P20618; -.
DR PRIDE; P20618; -.
DR DNASU; 5689; -.
DR Ensembl; ENST00000262193; ENSP00000262193; ENSG00000008018.
DR GeneID; 5689; -.
DR KEGG; hsa:5689; -.
DR UCSC; uc003qxr.3; human.
DR CTD; 5689; -.
DR GeneCards; GC06M170844; -.
DR HGNC; HGNC:9537; PSMB1.
DR HPA; CAB033911; -.
DR HPA; HPA029635; -.
DR HPA; HPA029637; -.
DR MIM; 602017; gene.
DR neXtProt; NX_P20618; -.
DR PharmGKB; PA33882; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091081; -.
DR HOVERGEN; HBG000961; -.
DR InParanoid; P20618; -.
DR KO; K02732; -.
DR OMA; QCRAGGA; -.
DR OrthoDB; EOG7WHHBB; -.
DR PhylomeDB; P20618; -.
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; PSMB1; human.
DR GeneWiki; PSMB1; -.
DR GenomeRNAi; 5689; -.
DR NextBio; 22098; -.
DR PRO; PR:P20618; -.
DR Bgee; P20618; -.
DR CleanEx; HS_PSMB1; -.
DR Genevestigator; P20618; -.
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: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 Glycoprotein; Host-virus interaction; Hydrolase; Nucleus;
KW Phosphoprotein; Polymorphism; Protease; Proteasome;
KW Reference proteome; Threonine protease.
FT PROPEP 1 28
FT /FTId=PRO_0000259623.
FT CHAIN 29 241 Proteasome subunit beta type-1.
FT /FTId=PRO_0000148030.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 150 150 Phosphotyrosine (By similarity).
FT MOD_RES 204 204 N6-acetyllysine.
FT CARBOHYD 58 58 O-linked (GlcNAc) (By similarity).
FT CARBOHYD 209 209 O-linked (GlcNAc) (By similarity).
FT VARIANT 11 11 P -> A (in dbSNP:rs12717).
FT /FTId=VAR_051547.
FT VARIANT 208 208 I -> N (in dbSNP:rs10541).
FT /FTId=VAR_051548.
SQ SEQUENCE 241 AA; 26489 MW; AE8FC42799F39157 CRC64;
MLSSTAMYSA PGRDLGMEPH RAAGPLQLRF SPYVFNGGTI LAIAGEDFAI VASDTRLSEG
FSIHTRDSPK CYKLTDKTVI GCSGFHGDCL TLTKIIEARL KMYKHSNNKA MTTGAIAAML
STILYSRRFF PYYVYNIIGG LDEEGKGAVY SFDPVGSYQR DSFKAGGSAS AMLQPLLDNQ
VGFKNMQNVE HVPLSLDRAM RLVKDVFISA AERDVYTGDA LRICIVTKEG IREETVSLRK
D
//
ID PSB1_HUMAN Reviewed; 241 AA.
AC P20618; B5BU76; Q9BWA8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1992, sequence version 2.
DT 22-JAN-2014, entry version 152.
DE RecName: Full=Proteasome subunit beta type-1;
DE EC=3.4.25.1;
DE AltName: Full=Macropain subunit C5;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C5;
DE AltName: Full=Proteasome component C5;
DE AltName: Full=Proteasome gamma chain;
DE Flags: Precursor;
GN Name=PSMB1; Synonyms=PSC5;
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=2025653; DOI=10.1016/0167-4781(91)90090-9;
RA Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H.,
RA Tanaka K., Ichihara A.;
RT "Molecular cloning and sequence analysis of cDNAs for five major
RT subunits of human proteasomes (multi-catalytic proteinase
RT complexes).";
RL Biochim. Biophys. Acta 1089:95-102(1991).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-11.
RC TISSUE=Brain, and Lung;
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 [6]
RP PROTEIN SEQUENCE OF 29-52.
RX PubMed=2306472; DOI=10.1016/0167-4838(90)90165-C;
RA Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N.,
RA Slaughter C.A.;
RT "Relationships among the subunits of the high molecular weight
RT proteinase, macropain (proteasome).";
RL Biochim. Biophys. Acta 1037:178-185(1990).
RN [7]
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 [8]
RP INTERACTION WITH SERPINB2.
RX PubMed=14732874; DOI=10.1093/abbs/36.1.42;
RA Fan J., Zhang Y.Q., Li P., Hou M., Tan L., Wang X., Zhu Y.S.;
RT "Interaction of plasminogen activator inhibitor-2 and proteasome
RT subunit, beta type 1.";
RL Acta Biochim. Biophys. Sin. 36:42-46(2004).
RN [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
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 [12]
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.
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 SERPINB2. Interacts
CC with HIV-1 TAT protein.
CC -!- INTERACTION:
CC P28074:PSMB5; NbExp=3; IntAct=EBI-372273, EBI-357828;
CC Q99436:PSMB7; NbExp=8; IntAct=EBI-372273, EBI-603319;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
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DR EMBL; D00761; BAA00658.1; -; mRNA.
DR EMBL; BT019720; AAV38525.1; -; mRNA.
DR EMBL; AB451312; BAG70126.1; -; mRNA.
DR EMBL; AB451442; BAG70256.1; -; mRNA.
DR EMBL; AL031259; CAA20287.1; -; Genomic_DNA.
DR EMBL; BC000508; AAH00508.1; -; mRNA.
DR EMBL; BC020807; AAH20807.1; -; mRNA.
DR PIR; S15973; SNHUC5.
DR RefSeq; NP_002784.1; NM_002793.3.
DR UniGene; Hs.352768; -.
DR ProteinModelPortal; P20618; -.
DR SMR; P20618; 29-241.
DR IntAct; P20618; 21.
DR MINT; MINT-3009312; -.
DR STRING; 9606.ENSP00000262193; -.
DR BindingDB; P20618; -.
DR ChEMBL; CHEMBL4208; -.
DR DrugBank; DB00188; Bortezomib.
DR MEROPS; T01.986; -.
DR PhosphoSite; P20618; -.
DR DMDM; 130853; -.
DR REPRODUCTION-2DPAGE; IPI00025019; -.
DR UCD-2DPAGE; P20618; -.
DR PaxDb; P20618; -.
DR PeptideAtlas; P20618; -.
DR PRIDE; P20618; -.
DR DNASU; 5689; -.
DR Ensembl; ENST00000262193; ENSP00000262193; ENSG00000008018.
DR GeneID; 5689; -.
DR KEGG; hsa:5689; -.
DR UCSC; uc003qxr.3; human.
DR CTD; 5689; -.
DR GeneCards; GC06M170844; -.
DR HGNC; HGNC:9537; PSMB1.
DR HPA; CAB033911; -.
DR HPA; HPA029635; -.
DR HPA; HPA029637; -.
DR MIM; 602017; gene.
DR neXtProt; NX_P20618; -.
DR PharmGKB; PA33882; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091081; -.
DR HOVERGEN; HBG000961; -.
DR InParanoid; P20618; -.
DR KO; K02732; -.
DR OMA; QCRAGGA; -.
DR OrthoDB; EOG7WHHBB; -.
DR PhylomeDB; P20618; -.
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; PSMB1; human.
DR GeneWiki; PSMB1; -.
DR GenomeRNAi; 5689; -.
DR NextBio; 22098; -.
DR PRO; PR:P20618; -.
DR Bgee; P20618; -.
DR CleanEx; HS_PSMB1; -.
DR Genevestigator; P20618; -.
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: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 Glycoprotein; Host-virus interaction; Hydrolase; Nucleus;
KW Phosphoprotein; Polymorphism; Protease; Proteasome;
KW Reference proteome; Threonine protease.
FT PROPEP 1 28
FT /FTId=PRO_0000259623.
FT CHAIN 29 241 Proteasome subunit beta type-1.
FT /FTId=PRO_0000148030.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 150 150 Phosphotyrosine (By similarity).
FT MOD_RES 204 204 N6-acetyllysine.
FT CARBOHYD 58 58 O-linked (GlcNAc) (By similarity).
FT CARBOHYD 209 209 O-linked (GlcNAc) (By similarity).
FT VARIANT 11 11 P -> A (in dbSNP:rs12717).
FT /FTId=VAR_051547.
FT VARIANT 208 208 I -> N (in dbSNP:rs10541).
FT /FTId=VAR_051548.
SQ SEQUENCE 241 AA; 26489 MW; AE8FC42799F39157 CRC64;
MLSSTAMYSA PGRDLGMEPH RAAGPLQLRF SPYVFNGGTI LAIAGEDFAI VASDTRLSEG
FSIHTRDSPK CYKLTDKTVI GCSGFHGDCL TLTKIIEARL KMYKHSNNKA MTTGAIAAML
STILYSRRFF PYYVYNIIGG LDEEGKGAVY SFDPVGSYQR DSFKAGGSAS AMLQPLLDNQ
VGFKNMQNVE HVPLSLDRAM RLVKDVFISA AERDVYTGDA LRICIVTKEG IREETVSLRK
D
//
MIM
602017
*RECORD*
*FIELD* NO
602017
*FIELD* TI
*602017 PROTEASOME SUBUNIT, BETA-TYPE, 1; PSMB1
;;PROTEASOMAL SUBUNIT C5; HC5;;
PROTEASOME SUBUNIT BETA-6
read more*FIELD* TX
CLONING
Tamura et al. (1994) isolated 2 human proteasome genes encoding the
alpha-type HC3 (PSMA2; 176842) and the beta-type HC5 subunits. Analysis
of their promoter sequences revealed the absence of TATA and CAAT
elements and the existence of 2 or 3 GC boxes that function coordinately
as promoters of the 2 genes. Differences in the exon/intron
organizations of these genes, however, suggested that they diverged at
an early stage of evolution.
MAPPING
Trachtulec et al. (1997) mapped the human PSMB1 gene to a region of
chromosome 6q27 syntenic with the proximal part of mouse chromosome 17,
where the mouse homolog maps. In both human and mouse PSMB1 is tightly
linked to the TATA-binding protein gene (TBP; 600075). The 2 genes are
transcribed in the opposite orientation in both species.
GENE FAMILY
The TATA-binding protein (TBP) is a factor required for the
transcription of all classes of eukaryotic genes. The human TBP and
mouse Tbp are single-copy genes; in Drosophila TATA-binding protein
genes, the housekeeping Tbp and the developmentally regulated Trf, map
to opposite arms of the second chromosome. Trachtulec et al. (1997)
demonstrated in the mouse that the Tbp gene resides next to the
proteasomal subunit C5-encoding gene (Psmb1). The genes are located on
mouse chromosome 17 in the t complex within the 'Hybrid sterility 1'
(Hst1) region. They also demonstrated that the homologous human genes,
TBP and PSMB1, are tightly linked on chromosome 6q27 in a region
syntenic with the proximal part of mouse chromosome 17. The TATA-binding
protein and proteasomal subunit C5 genes are also linked on chromosome
III of C. elegans, and together they are linked to other genes whose
homologs map to human chromosome 6 and mouse chromosome 17. In
Drosophila, the 2 housekeeping TATA-binding protein genes map close to 2
other genes with homologs in the mammalian major histocompatibility
complex. Thus, Trachtulec et al. (1997) concluded that there exists
conserved synteny of unrelated genes between mammals and invertebrates.
See PSMB2 (602175) for further discussion of this gene family.
HISTORY
Okumura et al. (1995) mapped the PSMB1 gene to chromosome 7p13-p12 by
fluorescence in situ hybridization.
*FIELD* RF
1. Okumura, K.; Nogami, M.; Taguchi, H.; Hisamatsu, H.; Tanaka, K.
: The genes for the alpha-type HC3 (PMSA2) and beta-type HC5 (PMSB1)
subunits of human proteasomes map to chromosomes 6q27 and 7p12-p13
by fluorescence in situ hybridization. Genomics 27: 377-379, 1995.
2. Tamura, T.; Osaka, F.; Kawamura, Y.; Higuti, T.; Ishida, N.; Nothwang,
H.-G.; Tsurumi, C.; Tanaka, K.; Ichihara, A.: Isolation and characterization
of alpha-type HC3 and beta-type HC5 subunit genes of human proteasomes. J.
Molec. Biol. 244: 117-124, 1994.
3. Trachtulec, Z.; Hamvas, R. M. J.; Forejt, J.; Lehrach, H. R.; Vincek,
V.; Klein, J.: Linkage of TATA-binding protein and proteasome subunit
C5 genes in mice and humans reveals synteny conserved between mammals
and invertebrates. Genomics 44: 1-7, 1997.
*FIELD* CD
Victor A. McKusick: 9/26/1997
*FIELD* ED
terry: 11/24/2010
terry: 10/15/2010
alopez: 3/15/2010
mgross: 6/25/2007
alopez: 11/20/1998
dkim: 7/23/1998
alopez: 7/16/1998
alopez: 3/18/1998
mark: 12/12/1997
mark: 9/26/1997
*RECORD*
*FIELD* NO
602017
*FIELD* TI
*602017 PROTEASOME SUBUNIT, BETA-TYPE, 1; PSMB1
;;PROTEASOMAL SUBUNIT C5; HC5;;
PROTEASOME SUBUNIT BETA-6
read more*FIELD* TX
CLONING
Tamura et al. (1994) isolated 2 human proteasome genes encoding the
alpha-type HC3 (PSMA2; 176842) and the beta-type HC5 subunits. Analysis
of their promoter sequences revealed the absence of TATA and CAAT
elements and the existence of 2 or 3 GC boxes that function coordinately
as promoters of the 2 genes. Differences in the exon/intron
organizations of these genes, however, suggested that they diverged at
an early stage of evolution.
MAPPING
Trachtulec et al. (1997) mapped the human PSMB1 gene to a region of
chromosome 6q27 syntenic with the proximal part of mouse chromosome 17,
where the mouse homolog maps. In both human and mouse PSMB1 is tightly
linked to the TATA-binding protein gene (TBP; 600075). The 2 genes are
transcribed in the opposite orientation in both species.
GENE FAMILY
The TATA-binding protein (TBP) is a factor required for the
transcription of all classes of eukaryotic genes. The human TBP and
mouse Tbp are single-copy genes; in Drosophila TATA-binding protein
genes, the housekeeping Tbp and the developmentally regulated Trf, map
to opposite arms of the second chromosome. Trachtulec et al. (1997)
demonstrated in the mouse that the Tbp gene resides next to the
proteasomal subunit C5-encoding gene (Psmb1). The genes are located on
mouse chromosome 17 in the t complex within the 'Hybrid sterility 1'
(Hst1) region. They also demonstrated that the homologous human genes,
TBP and PSMB1, are tightly linked on chromosome 6q27 in a region
syntenic with the proximal part of mouse chromosome 17. The TATA-binding
protein and proteasomal subunit C5 genes are also linked on chromosome
III of C. elegans, and together they are linked to other genes whose
homologs map to human chromosome 6 and mouse chromosome 17. In
Drosophila, the 2 housekeeping TATA-binding protein genes map close to 2
other genes with homologs in the mammalian major histocompatibility
complex. Thus, Trachtulec et al. (1997) concluded that there exists
conserved synteny of unrelated genes between mammals and invertebrates.
See PSMB2 (602175) for further discussion of this gene family.
HISTORY
Okumura et al. (1995) mapped the PSMB1 gene to chromosome 7p13-p12 by
fluorescence in situ hybridization.
*FIELD* RF
1. Okumura, K.; Nogami, M.; Taguchi, H.; Hisamatsu, H.; Tanaka, K.
: The genes for the alpha-type HC3 (PMSA2) and beta-type HC5 (PMSB1)
subunits of human proteasomes map to chromosomes 6q27 and 7p12-p13
by fluorescence in situ hybridization. Genomics 27: 377-379, 1995.
2. Tamura, T.; Osaka, F.; Kawamura, Y.; Higuti, T.; Ishida, N.; Nothwang,
H.-G.; Tsurumi, C.; Tanaka, K.; Ichihara, A.: Isolation and characterization
of alpha-type HC3 and beta-type HC5 subunit genes of human proteasomes. J.
Molec. Biol. 244: 117-124, 1994.
3. Trachtulec, Z.; Hamvas, R. M. J.; Forejt, J.; Lehrach, H. R.; Vincek,
V.; Klein, J.: Linkage of TATA-binding protein and proteasome subunit
C5 genes in mice and humans reveals synteny conserved between mammals
and invertebrates. Genomics 44: 1-7, 1997.
*FIELD* CD
Victor A. McKusick: 9/26/1997
*FIELD* ED
terry: 11/24/2010
terry: 10/15/2010
alopez: 3/15/2010
mgross: 6/25/2007
alopez: 11/20/1998
dkim: 7/23/1998
alopez: 7/16/1998
alopez: 3/18/1998
mark: 12/12/1997
mark: 9/26/1997