Full text data of PSMB7
PSMB7
(Z)
[Confidence: high (present in two of the MS resources)]
Proteasome subunit beta type-7; 3.4.25.1 (Macropain chain Z; Multicatalytic endopeptidase complex chain Z; Proteasome subunit Z; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome subunit beta type-7; 3.4.25.1 (Macropain chain Z; Multicatalytic endopeptidase complex chain Z; Proteasome subunit Z; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00003217
IPI00003217 Proteasome subunit beta type 7 precursor 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
IPI00003217 Proteasome subunit beta type 7 precursor 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
Q99436
ID PSB7_HUMAN Reviewed; 277 AA.
AC Q99436; Q5TBG6; Q96AG8; Q9BWA7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1997, sequence version 1.
DT 22-JAN-2014, entry version 140.
DE RecName: Full=Proteasome subunit beta type-7;
DE EC=3.4.25.1;
DE AltName: Full=Macropain chain Z;
DE AltName: Full=Multicatalytic endopeptidase complex chain Z;
DE AltName: Full=Proteasome subunit Z;
DE Flags: Precursor;
GN Name=PSMB7; Synonyms=Z;
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=8666937; DOI=10.1084/jem.183.4.1807;
RA Hisamatsu H., Shimbara N., Saito Y., Kristensen P., Hendil K.B.,
RA Fujiwara T., Takahashi E., Tanahashi N., Tamura T., Ichihara A.,
RA Tanaka K.;
RT "Newly identified pair of proteasomal subunits regulated reciprocally
RT by interferon gamma.";
RL J. Exp. Med. 183:1807-1816(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-39.
RC TISSUE=Lung, Urinary bladder, and Uterus;
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 165-184 AND 259-277, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
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 [7]
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 [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RX PubMed=18549262; DOI=10.1021/pr8000892;
RA Rho J.H., Qin S., Wang J.Y., Roehrl M.H.;
RT "Proteomic expression analysis of surgical human colorectal cancer
RT tissues: up-regulation of PSB7, PRDX1, and SRP9 and hypoxic adaptation
RT in cancer.";
RL J. Proteome Res. 7:2959-2972(2008).
RN [9]
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 [10]
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).
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 unit is responsible of the 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. This subunit can be displaced by
CC the equivalent immune-specific subunit PSMB10. Interacts with HIV-
CC 1 TAT protein.
CC -!- INTERACTION:
CC P20618:PSMB1; NbExp=8; IntAct=EBI-603319, EBI-372273;
CC P28074:PSMB5; NbExp=7; IntAct=EBI-603319, EBI-357828;
CC P28065:PSMB9; NbExp=5; IntAct=EBI-603319, EBI-603300;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed at a low level in colonic mucosa.
CC Up-regulated in colorectal cancer tissues.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
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DR EMBL; D38048; BAA07238.1; -; mRNA.
DR EMBL; AL137846; CAI10873.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87582.1; -; Genomic_DNA.
DR EMBL; BC000509; AAH00509.1; -; mRNA.
DR EMBL; BC008414; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC017116; AAH17116.2; -; mRNA.
DR RefSeq; NP_002790.1; NM_002799.3.
DR UniGene; Hs.213470; -.
DR ProteinModelPortal; Q99436; -.
DR SMR; Q99436; 44-263.
DR IntAct; Q99436; 25.
DR MINT; MINT-1351242; -.
DR STRING; 9606.ENSP00000259457; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.011; -.
DR PhosphoSite; Q99436; -.
DR DMDM; 17380263; -.
DR PaxDb; Q99436; -.
DR PeptideAtlas; Q99436; -.
DR PRIDE; Q99436; -.
DR DNASU; 5695; -.
DR Ensembl; ENST00000259457; ENSP00000259457; ENSG00000136930.
DR GeneID; 5695; -.
DR KEGG; hsa:5695; -.
DR UCSC; uc004boj.4; human.
DR CTD; 5695; -.
DR GeneCards; GC09M127115; -.
DR HGNC; HGNC:9544; PSMB7.
DR HPA; HPA052408; -.
DR MIM; 604030; gene.
DR neXtProt; NX_Q99436; -.
DR PharmGKB; PA33889; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000182856; -.
DR HOVERGEN; HBG093416; -.
DR InParanoid; Q99436; -.
DR KO; K02739; -.
DR OMA; QIWCAGA; -.
DR OrthoDB; EOG7CRTQJ; -.
DR PhylomeDB; Q99436; -.
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; PSMB7; human.
DR GeneWiki; PSMB7; -.
DR GenomeRNAi; 5695; -.
DR NextBio; 22122; -.
DR PRO; PR:Q99436; -.
DR ArrayExpress; Q99436; -.
DR Bgee; Q99436; -.
DR CleanEx; HS_PSMB7; -.
DR Genevestigator; Q99436; -.
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; IPR000243; Pept_T1A_subB.
DR InterPro; IPR024689; Proteasome_bsu_C.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR Pfam; PF12465; Pr_beta_C; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Hydrolase; Nucleus; Polymorphism; Protease;
KW Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1 43 Removed in mature form.
FT /FTId=PRO_0000026645.
FT CHAIN 44 277 Proteasome subunit beta type-7.
FT /FTId=PRO_0000026646.
FT ACT_SITE 44 44 Nucleophile (By similarity).
FT VARIANT 39 39 V -> A (in dbSNP:rs4574).
FT /FTId=VAR_013292.
SQ SEQUENCE 277 AA; 29965 MW; A610C949A0ACF1CE CRC64;
MAAVSVYAPP VGGFSFDNCR RNAVLEADFA KRGYKLPKVR KTGTTIAGVV YKDGIVLGAD
TRATEGMVVA DKNCSKIHFI SPNIYCCGAG TAADTDMTTQ LISSNLELHS LSTGRLPRVV
TANRMLKQML FRYQGYIGAA LVLGGVDVTG PHLYSIYPHG STDKLPYVTM GSGSLAAMAV
FEDKFRPDME EEEAKNLVSE AIAAGIFNDL GSGSNIDLCV ISKNKLDFLR PYTVPNKKGT
RLGRYRCEKG TTAVLTEKIT PLEIEVLEET VQTMDTS
//
ID PSB7_HUMAN Reviewed; 277 AA.
AC Q99436; Q5TBG6; Q96AG8; Q9BWA7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1997, sequence version 1.
DT 22-JAN-2014, entry version 140.
DE RecName: Full=Proteasome subunit beta type-7;
DE EC=3.4.25.1;
DE AltName: Full=Macropain chain Z;
DE AltName: Full=Multicatalytic endopeptidase complex chain Z;
DE AltName: Full=Proteasome subunit Z;
DE Flags: Precursor;
GN Name=PSMB7; Synonyms=Z;
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=8666937; DOI=10.1084/jem.183.4.1807;
RA Hisamatsu H., Shimbara N., Saito Y., Kristensen P., Hendil K.B.,
RA Fujiwara T., Takahashi E., Tanahashi N., Tamura T., Ichihara A.,
RA Tanaka K.;
RT "Newly identified pair of proteasomal subunits regulated reciprocally
RT by interferon gamma.";
RL J. Exp. Med. 183:1807-1816(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-39.
RC TISSUE=Lung, Urinary bladder, and Uterus;
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 165-184 AND 259-277, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
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 [7]
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 [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RX PubMed=18549262; DOI=10.1021/pr8000892;
RA Rho J.H., Qin S., Wang J.Y., Roehrl M.H.;
RT "Proteomic expression analysis of surgical human colorectal cancer
RT tissues: up-regulation of PSB7, PRDX1, and SRP9 and hypoxic adaptation
RT in cancer.";
RL J. Proteome Res. 7:2959-2972(2008).
RN [9]
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 [10]
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).
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 unit is responsible of the 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. This subunit can be displaced by
CC the equivalent immune-specific subunit PSMB10. Interacts with HIV-
CC 1 TAT protein.
CC -!- INTERACTION:
CC P20618:PSMB1; NbExp=8; IntAct=EBI-603319, EBI-372273;
CC P28074:PSMB5; NbExp=7; IntAct=EBI-603319, EBI-357828;
CC P28065:PSMB9; NbExp=5; IntAct=EBI-603319, EBI-603300;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed at a low level in colonic mucosa.
CC Up-regulated in colorectal cancer tissues.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
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DR EMBL; D38048; BAA07238.1; -; mRNA.
DR EMBL; AL137846; CAI10873.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87582.1; -; Genomic_DNA.
DR EMBL; BC000509; AAH00509.1; -; mRNA.
DR EMBL; BC008414; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC017116; AAH17116.2; -; mRNA.
DR RefSeq; NP_002790.1; NM_002799.3.
DR UniGene; Hs.213470; -.
DR ProteinModelPortal; Q99436; -.
DR SMR; Q99436; 44-263.
DR IntAct; Q99436; 25.
DR MINT; MINT-1351242; -.
DR STRING; 9606.ENSP00000259457; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.011; -.
DR PhosphoSite; Q99436; -.
DR DMDM; 17380263; -.
DR PaxDb; Q99436; -.
DR PeptideAtlas; Q99436; -.
DR PRIDE; Q99436; -.
DR DNASU; 5695; -.
DR Ensembl; ENST00000259457; ENSP00000259457; ENSG00000136930.
DR GeneID; 5695; -.
DR KEGG; hsa:5695; -.
DR UCSC; uc004boj.4; human.
DR CTD; 5695; -.
DR GeneCards; GC09M127115; -.
DR HGNC; HGNC:9544; PSMB7.
DR HPA; HPA052408; -.
DR MIM; 604030; gene.
DR neXtProt; NX_Q99436; -.
DR PharmGKB; PA33889; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000182856; -.
DR HOVERGEN; HBG093416; -.
DR InParanoid; Q99436; -.
DR KO; K02739; -.
DR OMA; QIWCAGA; -.
DR OrthoDB; EOG7CRTQJ; -.
DR PhylomeDB; Q99436; -.
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; PSMB7; human.
DR GeneWiki; PSMB7; -.
DR GenomeRNAi; 5695; -.
DR NextBio; 22122; -.
DR PRO; PR:Q99436; -.
DR ArrayExpress; Q99436; -.
DR Bgee; Q99436; -.
DR CleanEx; HS_PSMB7; -.
DR Genevestigator; Q99436; -.
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; IPR000243; Pept_T1A_subB.
DR InterPro; IPR024689; Proteasome_bsu_C.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR Pfam; PF12465; Pr_beta_C; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Hydrolase; Nucleus; Polymorphism; Protease;
KW Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1 43 Removed in mature form.
FT /FTId=PRO_0000026645.
FT CHAIN 44 277 Proteasome subunit beta type-7.
FT /FTId=PRO_0000026646.
FT ACT_SITE 44 44 Nucleophile (By similarity).
FT VARIANT 39 39 V -> A (in dbSNP:rs4574).
FT /FTId=VAR_013292.
SQ SEQUENCE 277 AA; 29965 MW; A610C949A0ACF1CE CRC64;
MAAVSVYAPP VGGFSFDNCR RNAVLEADFA KRGYKLPKVR KTGTTIAGVV YKDGIVLGAD
TRATEGMVVA DKNCSKIHFI SPNIYCCGAG TAADTDMTTQ LISSNLELHS LSTGRLPRVV
TANRMLKQML FRYQGYIGAA LVLGGVDVTG PHLYSIYPHG STDKLPYVTM GSGSLAAMAV
FEDKFRPDME EEEAKNLVSE AIAAGIFNDL GSGSNIDLCV ISKNKLDFLR PYTVPNKKGT
RLGRYRCEKG TTAVLTEKIT PLEIEVLEET VQTMDTS
//
MIM
604030
*RECORD*
*FIELD* NO
604030
*FIELD* TI
*604030 PROTEASOME SUBUNIT, BETA-TYPE, 7; PSMB7
;;PROTEASOME SUBUNIT Z;;
PROTEASOME SUBUNIT BETA-2
read more*FIELD* TX
The 20S (700-kD) proteasome, which contains multiple peptidase
activities, is one component of the 26S (2000-kD) complex, which
degrades ubiquitinated proteins. The 20S proteasome is composed of alpha
and proteolytic beta subunits. See PSMB2 (602175). One important
function of the proteasome in higher vertebrates is to generate the
peptides presented on MHC-class 1 molecules to circulating lymphocytes.
The cytokine gamma-interferon (IFNG; 147570), which stimulates antigen
presentation, alters proteasome subunit composition and functional
activity. Upon IFNG treatment, the beta subunits X (600306) and Y
(600307) are replaced by subunits LMP7 (177046) and LMP2 (177045),
respectively. The changes in peptidase activity are due to the
incorporation of the LMP subunits (Coux et al. (1996)).
Hisamatsu et al. (1996) determined that a third pair of proteasome
subunits, Z and MECL1 (176847), are expressed reciprocally in response
to IFNG treatment. Z is downregulated, while MECL1 is markedly induced,
suggesting that Z can be replaced by MECL1 in the proteasomal complex.
By screening a HepG2 cell line library with a probe based on the partial
amino acid sequence of the Z protein, the authors isolated cDNAs
encoding Z. Sequence analysis revealed that the predicted 277-amino acid
Z protein is a beta subunit. Z shares 58% and 55% protein sequence
identity with MECL1 and PUP1, a S. cerevisiae proteasomal subunit,
respectively. Both Z and MECL1 are proteolytically processed to generate
a mature protein with an N-terminal threonine residue that is required
for activity.
Coux et al. (1996) stated that the IFNG-induced beta subunits MECL1,
LMP7, and LMP2, likely alter peptidase activity because they contain
distinct active sites. Thus the proteasomes from IFNG-treated cells
should generate more peptides with hydrophobic or basic C termini, like
the vast majority of peptides presented on MHC class I molecules.
Hisamatsu et al. (1996) proposed that 20S particles containing MECL1,
LMP7, and LMP2 be designated immunoproteasomes to emphasize their role
in immunologic processing of endogenous antigens.
By fluorescence in situ hybridization, Hisamatsu et al. (1996) mapped
the Z gene to 9q34.11-q34.12.
*FIELD* RF
1. Coux, O.; Tanaka, K.; Goldberg, A. L.: Structure and functions
of the 20S and 26S proteasomes. Ann. Rev. Biochem. 65: 801-847,
1996.
2. Hisamatsu, H.; Shimbara, N.; Saito, Y.; Kristensen, P.; Hendil,
K. B.; Fujiwara, T.; Takahashi, E.; Tanahashi, N.; Tamura, T.; Ichihara,
A.; Tanaka, K.: Newly identified pair of proteasomal subunits regulated
reciprocally by interferon gamma. J. Exp. Med. 183: 1807-1816, 1996.
*FIELD* CD
Rebekah S. Rasooly: 7/19/1999
*FIELD* ED
mgross: 06/25/2007
cwells: 7/25/2002
terry: 7/24/2002
alopez: 7/19/1999
*RECORD*
*FIELD* NO
604030
*FIELD* TI
*604030 PROTEASOME SUBUNIT, BETA-TYPE, 7; PSMB7
;;PROTEASOME SUBUNIT Z;;
PROTEASOME SUBUNIT BETA-2
read more*FIELD* TX
The 20S (700-kD) proteasome, which contains multiple peptidase
activities, is one component of the 26S (2000-kD) complex, which
degrades ubiquitinated proteins. The 20S proteasome is composed of alpha
and proteolytic beta subunits. See PSMB2 (602175). One important
function of the proteasome in higher vertebrates is to generate the
peptides presented on MHC-class 1 molecules to circulating lymphocytes.
The cytokine gamma-interferon (IFNG; 147570), which stimulates antigen
presentation, alters proteasome subunit composition and functional
activity. Upon IFNG treatment, the beta subunits X (600306) and Y
(600307) are replaced by subunits LMP7 (177046) and LMP2 (177045),
respectively. The changes in peptidase activity are due to the
incorporation of the LMP subunits (Coux et al. (1996)).
Hisamatsu et al. (1996) determined that a third pair of proteasome
subunits, Z and MECL1 (176847), are expressed reciprocally in response
to IFNG treatment. Z is downregulated, while MECL1 is markedly induced,
suggesting that Z can be replaced by MECL1 in the proteasomal complex.
By screening a HepG2 cell line library with a probe based on the partial
amino acid sequence of the Z protein, the authors isolated cDNAs
encoding Z. Sequence analysis revealed that the predicted 277-amino acid
Z protein is a beta subunit. Z shares 58% and 55% protein sequence
identity with MECL1 and PUP1, a S. cerevisiae proteasomal subunit,
respectively. Both Z and MECL1 are proteolytically processed to generate
a mature protein with an N-terminal threonine residue that is required
for activity.
Coux et al. (1996) stated that the IFNG-induced beta subunits MECL1,
LMP7, and LMP2, likely alter peptidase activity because they contain
distinct active sites. Thus the proteasomes from IFNG-treated cells
should generate more peptides with hydrophobic or basic C termini, like
the vast majority of peptides presented on MHC class I molecules.
Hisamatsu et al. (1996) proposed that 20S particles containing MECL1,
LMP7, and LMP2 be designated immunoproteasomes to emphasize their role
in immunologic processing of endogenous antigens.
By fluorescence in situ hybridization, Hisamatsu et al. (1996) mapped
the Z gene to 9q34.11-q34.12.
*FIELD* RF
1. Coux, O.; Tanaka, K.; Goldberg, A. L.: Structure and functions
of the 20S and 26S proteasomes. Ann. Rev. Biochem. 65: 801-847,
1996.
2. Hisamatsu, H.; Shimbara, N.; Saito, Y.; Kristensen, P.; Hendil,
K. B.; Fujiwara, T.; Takahashi, E.; Tanahashi, N.; Tamura, T.; Ichihara,
A.; Tanaka, K.: Newly identified pair of proteasomal subunits regulated
reciprocally by interferon gamma. J. Exp. Med. 183: 1807-1816, 1996.
*FIELD* CD
Rebekah S. Rasooly: 7/19/1999
*FIELD* ED
mgross: 06/25/2007
cwells: 7/25/2002
terry: 7/24/2002
alopez: 7/19/1999