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F1LNN1

- F1LNN1_RAT

UniProt

F1LNN1 - F1LNN1_RAT

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Protein

Proteasome subunit beta type

Gene

Psmb3

Organism
Rattus norvegicus (Rat)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

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.

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: Chromosome 10

Organism-specific databases

RGDi61875. Psmb3.

Subcellular locationi

Cytoplasm UniRule annotationSAAS annotation. Nucleus UniRule annotationSAAS annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  3. proteasome core complex Source: InterPro
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

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074820.
OMAiMDLIGCP.
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

ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi F1LNN1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000017377 ; ENSRNOP00000017377 ; ENSRNOG00000012938 .

Organism-specific databases

RGDi 61875. Psmb3.

Phylogenomic databases

GeneTreei ENSGT00550000074820.
OMAi MDLIGCP.
OrthoDBi EOG783MWB.
TreeFami TF106216.

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

NextBioi 35575862.

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. "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: November 26, 2014
This is version 26 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, Reference proteomeImported

External Data

Dasty 3