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Proteasome subunit beta type (EC 3.4.25.1)

 Q9VUJ1_DROME            Unreviewed;       272 AA.
Q9VUJ1;
01-MAY-2000, integrated into UniProtKB/TrEMBL.
01-MAY-2000, sequence version 1.
31-JAN-2018, entry version 154.
RecName: Full=Proteasome subunit beta type {ECO:0000256|RuleBase:RU004203};
EC=3.4.25.1 {ECO:0000256|RuleBase:RU004203};
Name=Prosbeta2 {ECO:0000313|EMBL:AAF49685.1,
ECO:0000313|FlyBase:FBgn0023174};
Synonyms=3329 {ECO:0000313|EMBL:AAF49685.1},
anon-EST:fe1E6 {ECO:0000313|EMBL:AAF49685.1},
anon-EST:fe1G6 {ECO:0000313|EMBL:AAF49685.1},
b2 {ECO:0000313|EMBL:AAF49685.1},
beta 2 {ECO:0000313|EMBL:AAF49685.1},
Beta-2 {ECO:0000313|EMBL:AAF49685.1},
beta-2 {ECO:0000313|EMBL:AAF49685.1},
beta2 {ECO:0000313|EMBL:AAF49685.1},
beta2_dm {ECO:0000313|EMBL:AAF49685.1},
Dmel\CG3329 {ECO:0000313|EMBL:AAF49685.1},
DTS-7 {ECO:0000313|EMBL:AAF49685.1},
DTS7 {ECO:0000313|EMBL:AAF49685.1},
Dts7 {ECO:0000313|EMBL:AAF49685.1},
l(3)DTS7 {ECO:0000313|EMBL:AAF49685.1},
Pros-beta-2 {ECO:0000313|FlyBase:FBgn0023174},
Prosbeta {ECO:0000313|EMBL:AAF49685.1},
prosbeta {ECO:0000313|EMBL:AAF49685.1},
Prosbeta 2 {ECO:0000313|EMBL:AAF49685.1},
PROSbeta2 {ECO:0000313|EMBL:AAF49685.1},
prosbeta2 {ECO:0000313|EMBL:AAF49685.1};
ORFNames=CG3329 {ECO:0000313|EMBL:AAF49685.1,
ECO:0000313|FlyBase:FBgn0023174},
Dmel_CG3329 {ECO:0000313|EMBL:AAF49685.1};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF49685.1, ECO:0000313|Proteomes:UP000000803};
[1] {ECO:0000313|EMBL:AAF49685.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L.,
Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J.,
Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2] {ECO:0000313|EMBL:AAK93400.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Berkeley {ECO:0000313|EMBL:AAK93400.1};
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.,
Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.,
Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J.,
Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K.,
Yu C., Lewis S.E., Rubin G.M., Celniker S.;
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:AAF49685.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537568;
Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
"Finishing a whole-genome shotgun: release 3 of the Drosophila
melanogaster euchromatic genome sequence.";
Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
[4] {ECO:0000313|EMBL:AAF49685.1, ECO:0000313|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5] {ECO:0000313|EMBL:AAF49685.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537573;
Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M.,
Ashburner M., Celniker S.E.;
"The transposable elements of the Drosophila melanogaster euchromatin:
a genomics perspective.";
Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
[6] {ECO:0000313|EMBL:AAF49685.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537574;
Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
Karpen G.H.;
"Heterochromatic sequences in a Drosophila whole-genome shotgun
assembly.";
Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
[7] {ECO:0000313|EMBL:AAF49685.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
Ashburner M., Anxolabehere D.;
"Combined evidence annotation of transposable elements in genome
sequences.";
PLoS Comput. Biol. 1:166-175(2005).
[8] {ECO:0000313|EMBL:AAF49685.1}
NUCLEOTIDE SEQUENCE.
O'Boyle S.T.;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[9] {ECO:0000313|EMBL:AAF49685.1}
NUCLEOTIDE SEQUENCE.
Berkeley Drosophila Genome Project;
Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E.,
Yu C., Rubin G.;
"Drosophila melanogaster release 4 sequence.";
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[10] {ECO:0000313|EMBL:AAF49685.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569856; DOI=10.1126/science.1139815;
Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
"The Release 5.1 annotation of Drosophila melanogaster
heterochromatin.";
Science 316:1586-1591(2007).
[11] {ECO:0000313|EMBL:AAF49685.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569867; DOI=10.1126/science.1139816;
Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
Dimitri P., Karpen G.H., Celniker S.E.;
"Sequence finishing and mapping of Drosophila melanogaster
heterochromatin.";
Science 316:1625-1628(2007).
[12] {ECO:0000313|EMBL:AAF49685.1}
NUCLEOTIDE SEQUENCE.
FlyBase;
Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity. {ECO:0000256|RuleBase:RU004203}.
-!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
two 19S regulatory subunits. {ECO:0000256|RuleBase:RU004203}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004203}.
Nucleus {ECO:0000256|RuleBase:RU004203,
ECO:0000256|SAAS:SAAS00551005}.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000256|RuleBase:RU004203}.
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EMBL; AE014296; AAF49685.1; -; Genomic_DNA.
EMBL; AY051976; AAK93400.1; -; mRNA.
RefSeq; NP_524076.2; NM_079352.4.
UniGene; Dm.4370; -.
SMR; Q9VUJ1; -.
IntAct; Q9VUJ1; 1.
MINT; MINT-291296; -.
STRING; 7227.FBpp0075382; -.
MEROPS; T01.A02; -.
PaxDb; Q9VUJ1; -.
EnsemblMetazoa; FBtr0075629; FBpp0075382; FBgn0023174.
GeneID; 39628; -.
KEGG; dme:Dmel_CG3329; -.
CTD; 39628; -.
FlyBase; FBgn0023174; Prosbeta2.
eggNOG; KOG0173; Eukaryota.
eggNOG; COG0638; LUCA.
GeneTree; ENSGT00510000046533; -.
KO; K02739; -.
OMA; DLCVIRK; -.
OrthoDB; EOG091G0E5S; -.
Reactome; R-DME-1169091; Activation of NF-kappaB in B cells.
Reactome; R-DME-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-DME-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-DME-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-DME-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-DME-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-DME-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-DME-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-DME-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-DME-202424; Downstream TCR signaling.
Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
Reactome; R-DME-209406; Degradation of NF-kappa-B inhibitor, CACT.
Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM.
Reactome; R-DME-216167; Nuclear CI is degraded.
Reactome; R-DME-2871837; FCERI mediated NF-kB activation.
Reactome; R-DME-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-DME-432395; Degradation of TIM.
Reactome; R-DME-432524; Degradation of PER.
Reactome; R-DME-446652; Interleukin-1 family signaling.
Reactome; R-DME-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-DME-4608870; Asymmetric localization of PCP proteins.
Reactome; R-DME-4641257; Degradation of AXIN.
Reactome; R-DME-4641258; Degradation of DVL.
Reactome; R-DME-5358346; Hedgehog ligand biogenesis.
Reactome; R-DME-538848; Degradation of CLK.
Reactome; R-DME-538864; Degradation of CRY.
Reactome; R-DME-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-DME-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-DME-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-DME-5658442; Regulation of RAS by GAPs.
Reactome; R-DME-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-DME-5689603; UCH proteinases.
Reactome; R-DME-5689880; Ub-specific processing proteases.
Reactome; R-DME-6798695; Neutrophil degranulation.
Reactome; R-DME-68949; Orc1 removal from chromatin.
Reactome; R-DME-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-DME-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-DME-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-DME-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-DME-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-DME-8948751; Regulation of PTEN stability and activity.
Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
GenomeRNAi; 39628; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0023174; -.
ExpressionAtlas; Q9VUJ1; differential.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000502; C:proteasome complex; IDA:FlyBase.
GO; GO:0005839; C:proteasome core complex; IDA:FlyBase.
GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:FlyBase.
GO; GO:0004175; F:endopeptidase activity; ISS:FlyBase.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:FlyBase.
GO; GO:0007623; P:circadian rhythm; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:FlyBase.
GO; GO:0008063; P:Toll signaling pathway; TAS:Reactome.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR000243; Pept_T1A_subB.
InterPro; IPR035216; Proteasome_beta7.
InterPro; IPR024689; Proteasome_bsu_C.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
PANTHER; PTHR11599:SF44; PTHR11599:SF44; 1.
Pfam; PF12465; Pr_beta_C; 1.
Pfam; PF00227; Proteasome; 1.
PRINTS; PR00141; PROTEASOME.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00854; PROTEASOME_BETA_1; 1.
PROSITE; PS51476; PROTEASOME_BETA_2; 1.
1: Evidence at protein level;
Complete proteome {ECO:0000313|Proteomes:UP000000803};
Cytoplasm {ECO:0000256|RuleBase:RU004203};
Hydrolase {ECO:0000256|RuleBase:RU004203};
Nucleus {ECO:0000256|RuleBase:RU004203,
ECO:0000256|SAAS:SAAS00039288};
Protease {ECO:0000256|RuleBase:RU004203};
Proteasome {ECO:0000256|RuleBase:RU004203,
ECO:0000313|EMBL:AAF49685.1};
Proteomics identification {ECO:0000213|PeptideAtlas:Q9VUJ1};
Reference proteome {ECO:0000313|Proteomes:UP000000803};
Threonine protease {ECO:0000256|RuleBase:RU004203}.
DOMAIN 231 263 Pr_beta_C. {ECO:0000259|Pfam:PF12465}.
SEQUENCE 272 AA; 29827 MW; 24461F336E215E77 CRC64;
MDLDNARDLP RAGFNFDNCK RNATLLNRGF KPPTTTKTGT TIVGIIYKDG VILGADTRAT
EGPIVSDKNC AKIHYLAKNI YCCGAGTAAD TEMTTDLISS QLELHRLQTD REVRVVAANT
MLKQMLFRYQ GHISAALVLG GVDKTGPHIY SIHPHGSSDK LPYATMGSGS LAAMTVFESR
WKPDLSEEEG KKLVRDAIAS GVFNDLGSGS NIDLCVIRKG SVEYLRNYEL ANKKGKRQLD
YRFKTGTSTV LHTNIKDLLV TERVQAVPME IS


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EIAAB32753 Lmp3,Low molecular mass protein 3,Macropain beta chain,Mouse,Multicatalytic endopeptidase complex beta chain,Mus musculus,Proteasome beta chain,Proteasome chain 3,Proteasome subunit beta type-4,Psmb4
EIAAB32741 Bos taurus,Bovine,Proteasome subunit beta type-10,Proteasome subunit beta-2i,PSMB10


 

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