Full text data of PSMB3
PSMB3
[Confidence: high (present in two of the MS resources)]
Proteasome subunit beta type-3; 3.4.25.1 (Proteasome chain 13; Proteasome component C10-II; Proteasome theta chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome subunit beta type-3; 3.4.25.1 (Proteasome chain 13; Proteasome component C10-II; Proteasome theta chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00028004
IPI00028004 Proteasome subunit beta type 3 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
IPI00028004 Proteasome subunit beta type 3 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
P49720
ID PSB3_HUMAN Reviewed; 205 AA.
AC P49720; P31147; Q0P6J7; Q96E27;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Proteasome subunit beta type-3;
DE EC=3.4.25.1;
DE AltName: Full=Proteasome chain 13;
DE AltName: Full=Proteasome component C10-II;
DE AltName: Full=Proteasome theta chain;
GN Name=PSMB3;
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], AND VARIANT LEU-34.
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].
RC TISSUE=Muscle;
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 [3]
RP PROTEIN SEQUENCE OF 2-15; 28-41; 49-66; 71-77; 100-115 AND 178-192,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2008) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 29-42; 50-67 AND 101-116, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 49-66 AND 99-111.
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 [6]
RP PROTEIN SEQUENCE OF 100-115.
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 [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 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 [9]
RP INDUCTION.
RX PubMed=18281682; DOI=10.1093/humrep/den024;
RA Martinez-Heredia J., de Mateo S., Vidal-Taboada J.M., Ballesca J.L.,
RA Oliva R.;
RT "Identification of proteomic differences in asthenozoospermic sperm
RT samples.";
RL Hum. Reprod. 23:783-791(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77, 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 [12]
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.
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 P49721:PSMB2; NbExp=4; IntAct=EBI-603340, EBI-359335;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- INDUCTION: Up-regulated in asthenozoospermic sperm.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D26598; BAA05645.1; -; mRNA.
DR EMBL; BC013008; AAH13008.1; -; mRNA.
DR PIR; S55041; S55041.
DR RefSeq; NP_002786.2; NM_002795.3.
DR UniGene; Hs.82793; -.
DR ProteinModelPortal; P49720; -.
DR SMR; P49720; 2-205.
DR IntAct; P49720; 21.
DR MINT; MINT-5001041; -.
DR STRING; 9606.ENSP00000225426; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.983; -.
DR PhosphoSite; P49720; -.
DR DMDM; 20532411; -.
DR OGP; P49720; -.
DR REPRODUCTION-2DPAGE; IPI00028004; -.
DR PaxDb; P49720; -.
DR PeptideAtlas; P49720; -.
DR PRIDE; P49720; -.
DR DNASU; 5691; -.
DR Ensembl; ENST00000225426; ENSP00000225426; ENSG00000108294.
DR GeneID; 5691; -.
DR KEGG; hsa:5691; -.
DR UCSC; uc002hqr.3; human.
DR CTD; 5691; -.
DR GeneCards; GC17P036909; -.
DR H-InvDB; HIX0030292; -.
DR HGNC; HGNC:9540; PSMB3.
DR MIM; 602176; gene.
DR neXtProt; NX_P49720; -.
DR PharmGKB; PA33885; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000090523; -.
DR HOVERGEN; HBG004446; -.
DR InParanoid; P49720; -.
DR KO; K02735; -.
DR OMA; MVSNLLY; -.
DR OrthoDB; EOG783MWB; -.
DR PhylomeDB; P49720; -.
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; PSMB3; human.
DR GeneWiki; PSMB3; -.
DR GenomeRNAi; 5691; -.
DR NextBio; 22106; -.
DR PRO; PR:P49720; -.
DR ArrayExpress; P49720; -.
DR Bgee; P49720; -.
DR CleanEx; HS_PSMB3; -.
DR Genevestigator; P49720; -.
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 Host-virus interaction; Hydrolase; Nucleus; Polymorphism; Protease;
KW Proteasome; Reference proteome; Threonine protease.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 205 Proteasome subunit beta type-3.
FT /FTId=PRO_0000148057.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 77 77 N6-acetyllysine.
FT VARIANT 34 34 M -> L (in dbSNP:rs4907).
FT /FTId=VAR_034415.
SQ SEQUENCE 205 AA; 22949 MW; 624972384C0112FD CRC64;
MSIMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY IGLAGLATDV
QTVAQRLKFR LNLYELKEGR QIKPYTLMSM VANLLYEKRF GPYYTEPVIA GLDPKTFKPF
ICSLDLIGCP MVTDDFVVSG TCAEQMYGMC ESLWEPNMDP DHLFETISQA MLNAVDRDAV
SGMGVIVHII EKDKITTRTL KARMD
//
ID PSB3_HUMAN Reviewed; 205 AA.
AC P49720; P31147; Q0P6J7; Q96E27;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Proteasome subunit beta type-3;
DE EC=3.4.25.1;
DE AltName: Full=Proteasome chain 13;
DE AltName: Full=Proteasome component C10-II;
DE AltName: Full=Proteasome theta chain;
GN Name=PSMB3;
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], AND VARIANT LEU-34.
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].
RC TISSUE=Muscle;
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 [3]
RP PROTEIN SEQUENCE OF 2-15; 28-41; 49-66; 71-77; 100-115 AND 178-192,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2008) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 29-42; 50-67 AND 101-116, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 49-66 AND 99-111.
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 [6]
RP PROTEIN SEQUENCE OF 100-115.
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 [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 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 [9]
RP INDUCTION.
RX PubMed=18281682; DOI=10.1093/humrep/den024;
RA Martinez-Heredia J., de Mateo S., Vidal-Taboada J.M., Ballesca J.L.,
RA Oliva R.;
RT "Identification of proteomic differences in asthenozoospermic sperm
RT samples.";
RL Hum. Reprod. 23:783-791(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77, 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 [12]
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.
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 P49721:PSMB2; NbExp=4; IntAct=EBI-603340, EBI-359335;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- INDUCTION: Up-regulated in asthenozoospermic sperm.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D26598; BAA05645.1; -; mRNA.
DR EMBL; BC013008; AAH13008.1; -; mRNA.
DR PIR; S55041; S55041.
DR RefSeq; NP_002786.2; NM_002795.3.
DR UniGene; Hs.82793; -.
DR ProteinModelPortal; P49720; -.
DR SMR; P49720; 2-205.
DR IntAct; P49720; 21.
DR MINT; MINT-5001041; -.
DR STRING; 9606.ENSP00000225426; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.983; -.
DR PhosphoSite; P49720; -.
DR DMDM; 20532411; -.
DR OGP; P49720; -.
DR REPRODUCTION-2DPAGE; IPI00028004; -.
DR PaxDb; P49720; -.
DR PeptideAtlas; P49720; -.
DR PRIDE; P49720; -.
DR DNASU; 5691; -.
DR Ensembl; ENST00000225426; ENSP00000225426; ENSG00000108294.
DR GeneID; 5691; -.
DR KEGG; hsa:5691; -.
DR UCSC; uc002hqr.3; human.
DR CTD; 5691; -.
DR GeneCards; GC17P036909; -.
DR H-InvDB; HIX0030292; -.
DR HGNC; HGNC:9540; PSMB3.
DR MIM; 602176; gene.
DR neXtProt; NX_P49720; -.
DR PharmGKB; PA33885; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000090523; -.
DR HOVERGEN; HBG004446; -.
DR InParanoid; P49720; -.
DR KO; K02735; -.
DR OMA; MVSNLLY; -.
DR OrthoDB; EOG783MWB; -.
DR PhylomeDB; P49720; -.
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; PSMB3; human.
DR GeneWiki; PSMB3; -.
DR GenomeRNAi; 5691; -.
DR NextBio; 22106; -.
DR PRO; PR:P49720; -.
DR ArrayExpress; P49720; -.
DR Bgee; P49720; -.
DR CleanEx; HS_PSMB3; -.
DR Genevestigator; P49720; -.
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 Host-virus interaction; Hydrolase; Nucleus; Polymorphism; Protease;
KW Proteasome; Reference proteome; Threonine protease.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 205 Proteasome subunit beta type-3.
FT /FTId=PRO_0000148057.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 77 77 N6-acetyllysine.
FT VARIANT 34 34 M -> L (in dbSNP:rs4907).
FT /FTId=VAR_034415.
SQ SEQUENCE 205 AA; 22949 MW; 624972384C0112FD CRC64;
MSIMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY IGLAGLATDV
QTVAQRLKFR LNLYELKEGR QIKPYTLMSM VANLLYEKRF GPYYTEPVIA GLDPKTFKPF
ICSLDLIGCP MVTDDFVVSG TCAEQMYGMC ESLWEPNMDP DHLFETISQA MLNAVDRDAV
SGMGVIVHII EKDKITTRTL KARMD
//
MIM
602176
*RECORD*
*FIELD* NO
602176
*FIELD* TI
*602176 PROTEASOME SUBUNIT, BETA-TYPE, 3; PSMB3
;;PROTEASOME SUBUNIT BETA-3
*FIELD* TX
read moreSee PSMB2 (602175). McCusker et al. (1997) mapped PSMB3 to 2q35 by
fluorescence in situ hybridization.
*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
dkim: 7/23/1998
mark: 12/12/1997
*RECORD*
*FIELD* NO
602176
*FIELD* TI
*602176 PROTEASOME SUBUNIT, BETA-TYPE, 3; PSMB3
;;PROTEASOME SUBUNIT BETA-3
*FIELD* TX
read moreSee PSMB2 (602175). McCusker et al. (1997) mapped PSMB3 to 2q35 by
fluorescence in situ hybridization.
*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
dkim: 7/23/1998
mark: 12/12/1997