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Protein

Proteasome subunit beta type

Gene

Psmb3

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 2 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.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta typeUniRule annotation (EC:3.4.25.1UniRule annotation)
Gene namesi
Name:Psmb3Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi61875. Psmb3.

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation
  • Nucleus UniRule annotationSAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

NucleusSAAS annotation, ProteasomeUniRule annotation

PTM / Processingi

Proteomic databases

PRIDEiF1LNN1.

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.ENSRNOP00000017377.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074820.
OMAiGCLNFAK.
OrthoDBiEOG783MWB.
TreeFamiTF106216.

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.

F1LNN1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY
60 70 80 90 100
IGLAGLATDV QTVAQRLKFR LNLYELKEGR QIKPYTLMSM VANLLYEKRF
110 120 130 140 150
GPYYTEPVIA GLDPKTFKPF ICSLDLIGCP MVTDDFVVSG TCSEQMYGMC
160 170 180 190 200
ESLWEPNMEP EHLFETISTP MLNAVDRDAV SGMGVIVHII EKDKITTRTL

KARMD
Length:205
Mass (Da):22,978
Last modified:April 3, 2013 - v2
Checksum:i4AFB18442D3F36DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06065478 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENSRNOT00000017377; ENSRNOP00000017377; ENSRNOG00000012938.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06065478 Genomic DNA. No translation available.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017377.

Proteomic databases

PRIDEiF1LNN1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017377; ENSRNOP00000017377; ENSRNOG00000012938.

Organism-specific databases

RGDi61875. Psmb3.

Phylogenomic databases

GeneTreeiENSGT00550000074820.
OMAiGCLNFAK.
OrthoDBiEOG783MWB.
TreeFamiTF106216.

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.

Miscellaneous databases

NextBioi35575862.

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. "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.
  2. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiF1LNN1_RAT
AccessioniPrimary (citable) accession number: F1LNN1
Entry historyi
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: April 3, 2013
Last modified: June 24, 2015
This is version 31 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

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.