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Protein

Proteasome subunit beta type

Gene

Psmb1

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.UniRule annotation

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine proteaseUniRule annotation

Enzyme and pathway databases

ReactomeiREACT_272498. APC/C:Cdc20 mediated degradation of Securin.
REACT_274511. Regulation of ornithine decarboxylase (ODC).
REACT_275019. Ubiquitin-dependent degradation of Cyclin D1.
REACT_277636. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_279869. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_280071. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_280715. GLI3 is processed to GLI3R by the proteasome.
REACT_287195. Degradation of GLI2 by the proteasome.
REACT_288207. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_289020. Degradation of beta-catenin by the destruction complex.
REACT_290448. Orc1 removal from chromatin.
REACT_295138. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_297906. Separation of Sister Chromatids.
REACT_305105. degradation of DVL.
REACT_309656. SCF-beta-TrCP mediated degradation of Emi1.
REACT_312094. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_317312. SCF(Skp2)-mediated degradation of p27/p21.
REACT_318052. Activation of NF-kappaB in B cells.
REACT_325005. CDT1 association with the CDC6:ORC:origin complex.
REACT_327126. Hedgehog 'on' state.
REACT_333644. Asymmetric localization of PCP proteins.
REACT_334373. degradation of AXIN.
REACT_336450. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_336611. Hedgehog ligand biogenesis.
REACT_338477. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_343414. ER-Phagosome pathway.
REACT_346077. CDK-mediated phosphorylation and removal of Cdc6.
REACT_349901. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_357442. Degradation of GLI1 by the proteasome.
REACT_359556. CLEC7A (Dectin-1) signaling.
REACT_361793. Dectin-1 mediated noncanonical NF-kB signaling.

Protein family/group databases

MEROPSiT01.986.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta typeUniRule annotation (EC:3.4.25.1UniRule annotation)
Gene namesi
Name:Psmb1Imported
ORF Names:rCG_22979Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi621092. Psmb1.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

NucleusSAAS annotation, ProteasomeUniRule annotationImported

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits.UniRule annotation

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002037.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000075035.
HOVERGENiHBG000961.
KOiK02732.
OMAiEHRFNPY.
OrthoDBiEOG7WHHBB.
TreeFamiTF106218.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6PDW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSTAAYRDP DRELVMGPQG SAGPVQMRFS PYAFNGGTVL AIAGEDFSIV
60 70 80 90 100
ASDTRLSEGF SIHTRDSPKC YKLTDKTVIG CSGFHGDCLT LTKIIEARLK
110 120 130 140 150
MYKHSNNKAM TTGAIAAMLS TILYSRRFFP YYVYNIIGGL DEEGKGAVYS
160 170 180 190 200
FDPVGSYQRD SFKAGGSASA MLQPLLDNQV GFKNMQNVEH VPLTLDRAMR
210 220 230 240
LVKDVFISAA ERDVYTGDAL RICIVTKEGI REETVPLRKD
Length:240
Mass (Da):26,407
Last modified:July 5, 2004 - v1
Checksum:iEF3C3CAA6D935954
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06002674 Genomic DNA. No translation available.
AABR06002675 Genomic DNA. No translation available.
BC058455 mRNA. Translation: AAH58455.1.
CH474033 Genomic DNA. Translation: EDL99819.1.
RefSeqiXP_006228043.1. XM_006227981.1.
UniGeneiRn.6016.

Genome annotation databases

EnsembliENSRNOT00000002037; ENSRNOP00000002037; ENSRNOG00000001488.
GeneIDi94198.
KEGGirno:94198.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06002674 Genomic DNA. No translation available.
AABR06002675 Genomic DNA. No translation available.
BC058455 mRNA. Translation: AAH58455.1.
CH474033 Genomic DNA. Translation: EDL99819.1.
RefSeqiXP_006228043.1. XM_006227981.1.
UniGeneiRn.6016.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002037.

Protein family/group databases

MEROPSiT01.986.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000002037; ENSRNOP00000002037; ENSRNOG00000001488.
GeneIDi94198.
KEGGirno:94198.

Organism-specific databases

CTDi5689.
RGDi621092. Psmb1.

Phylogenomic databases

GeneTreeiENSGT00550000075035.
HOVERGENiHBG000961.
KOiK02732.
OMAiEHRFNPY.
OrthoDBiEOG7WHHBB.
TreeFamiTF106218.

Enzyme and pathway databases

ReactomeiREACT_272498. APC/C:Cdc20 mediated degradation of Securin.
REACT_274511. Regulation of ornithine decarboxylase (ODC).
REACT_275019. Ubiquitin-dependent degradation of Cyclin D1.
REACT_277636. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_279869. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_280071. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_280715. GLI3 is processed to GLI3R by the proteasome.
REACT_287195. Degradation of GLI2 by the proteasome.
REACT_288207. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_289020. Degradation of beta-catenin by the destruction complex.
REACT_290448. Orc1 removal from chromatin.
REACT_295138. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_297906. Separation of Sister Chromatids.
REACT_305105. degradation of DVL.
REACT_309656. SCF-beta-TrCP mediated degradation of Emi1.
REACT_312094. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_317312. SCF(Skp2)-mediated degradation of p27/p21.
REACT_318052. Activation of NF-kappaB in B cells.
REACT_325005. CDT1 association with the CDC6:ORC:origin complex.
REACT_327126. Hedgehog 'on' state.
REACT_333644. Asymmetric localization of PCP proteins.
REACT_334373. degradation of AXIN.
REACT_336450. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_336611. Hedgehog ligand biogenesis.
REACT_338477. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_343414. ER-Phagosome pathway.
REACT_346077. CDK-mediated phosphorylation and removal of Cdc6.
REACT_349901. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_357442. Degradation of GLI1 by the proteasome.
REACT_359556. CLEC7A (Dectin-1) signaling.
REACT_361793. Dectin-1 mediated noncanonical NF-kB signaling.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary glandImported.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  5. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiQ6PDW4_RAT
AccessioniPrimary (citable) accession number: Q6PDW4
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: June 24, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.