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Q6PDW4

- Q6PDW4_RAT

UniProt

Q6PDW4 - Q6PDW4_RAT

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Protein

Proteasome subunit beta type

Gene

Psmb1

Organism
Rattus norvegicus (Rat)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at transcript 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

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteolysis involved in cellular protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine proteaseUniRule annotation

Enzyme and pathway databases

ReactomeiREACT_194781. Separation of Sister Chromatids.
REACT_196424. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_198391. Asymmetric localization of PCP proteins.
REACT_199194. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199197. ER-Phagosome pathway.
REACT_199247. Activation of NF-kappaB in B cells.
REACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_204983. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_206488. degradation of DVL.
REACT_206997. CDT1 association with the CDC6:ORC:origin complex.
REACT_211117. Orc1 removal from chromatin.
REACT_212486. CDK-mediated phosphorylation and removal of Cdc6.
REACT_220232. Regulation of ornithine decarboxylase (ODC).
REACT_227706. degradation of AXIN.
REACT_235738. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_236654. Hedgehog ligand biogenesis.
REACT_240793. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_244609. SCF-beta-TrCP mediated degradation of Emi1.
REACT_245329. APC/C:Cdc20 mediated degradation of Securin.
REACT_246662. SCF(Skp2)-mediated degradation of p27/p21.
REACT_247625. Ubiquitin-dependent degradation of Cyclin D1.
REACT_252335. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_255131. Hh ligand biogenesis disease.
REACT_257365. Degradation of beta-catenin by the destruction complex.
REACT_259430. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_269272. Degradation of GLI1 by the proteasome.
REACT_269753. GLI3 is processed to GLI3R by the proteasome.
REACT_270919. Degradation of GLI2 by the proteasome.

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: Chromosome 1

Organism-specific databases

RGDi621092. Psmb1.

Subcellular locationi

Cytoplasm UniRule annotationSAAS annotation. Nucleus UniRule annotationSAAS annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleus Source: UniProtKB-SubCell
  4. proteasome core complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

NucleusSAAS annotation, ProteasomeUniRule annotationImported

Expressioni

Gene expression databases

GenevestigatoriQ6PDW4.

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

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000075035.
HOVERGENiHBG000961.
KOiK02732.
OMAiQCRAGGA.
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 .
RefSeqi XP_006228043.1. XM_006227981.1.
UniGenei Rn.6016.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi T01.986.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000002037 ; ENSRNOP00000002037 ; ENSRNOG00000001488 .
GeneIDi 94198.
KEGGi rno:94198.

Organism-specific databases

CTDi 5689.
RGDi 621092. Psmb1.

Phylogenomic databases

GeneTreei ENSGT00550000075035.
HOVERGENi HBG000961.
KOi K02732.
OMAi QCRAGGA.
OrthoDBi EOG7WHHBB.
TreeFami TF106218.

Enzyme and pathway databases

Reactomei REACT_194781. Separation of Sister Chromatids.
REACT_196424. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_198391. Asymmetric localization of PCP proteins.
REACT_199194. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199197. ER-Phagosome pathway.
REACT_199247. Activation of NF-kappaB in B cells.
REACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_204983. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_206488. degradation of DVL.
REACT_206997. CDT1 association with the CDC6:ORC:origin complex.
REACT_211117. Orc1 removal from chromatin.
REACT_212486. CDK-mediated phosphorylation and removal of Cdc6.
REACT_220232. Regulation of ornithine decarboxylase (ODC).
REACT_227706. degradation of AXIN.
REACT_235738. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_236654. Hedgehog ligand biogenesis.
REACT_240793. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_244609. SCF-beta-TrCP mediated degradation of Emi1.
REACT_245329. APC/C:Cdc20 mediated degradation of Securin.
REACT_246662. SCF(Skp2)-mediated degradation of p27/p21.
REACT_247625. Ubiquitin-dependent degradation of Cyclin D1.
REACT_252335. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_255131. Hh ligand biogenesis disease.
REACT_257365. Degradation of beta-catenin by the destruction complex.
REACT_259430. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_269272. Degradation of GLI1 by the proteasome.
REACT_269753. GLI3 is processed to GLI3R by the proteasome.
REACT_270919. Degradation of GLI2 by the proteasome.

Miscellaneous databases

PROi Q6PDW4.

Gene expression databases

Genevestigatori Q6PDW4.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3