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Protein

Proteasome subunit beta type-6

Gene

Psmb6

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei34 – 341NucleophileBy similarity

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 protease

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

MEROPSiT01.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-6 (EC:3.4.25.1)
Alternative name(s):
Macropain delta chain
Multicatalytic endopeptidase complex delta chain
Proteasome chain 5
Proteasome delta chain
Proteasome subunit Y
Gene namesi
Name:Psmb6
Synonyms:Psmb6l
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10, UP000002494: Chromosome 2

Organism-specific databases

RGDi61881. Psmb6.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  3. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Propeptidei2 – 3332Removed in mature form1 PublicationPRO_0000026617Add
BLAST
Chaini34 – 238205Proteasome subunit beta type-6PRO_0000026618Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation, Zymogen

Proteomic databases

PaxDbiP28073.
PRIDEiP28073.

2D gel databases

World-2DPAGE0004:P28073.

Expressioni

Gene expression databases

GenevestigatoriP28073.

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. The catalytic chamber with the active sites is on the inside of the barrel. This subunit can be displaced by the equivalent immune-specific subunit PSMB9.

Protein-protein interaction databases

BioGridi248287. 1 interaction.
IntActiP28073. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP28073.
SMRiP28073. Positions 34-235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00510000046484.
HOGENOMiHOG000091079.
HOVERGENiHBG000123.
InParanoidiP28073.
KOiK02738.
OMAiMESHKEN.
OrthoDBiEOG79GT80.
PhylomeDBiP28073.
TreeFamiTF106221.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28073-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAALAVRGA VSAPAFGPEA LTPDWENREV STGTTIMAVQ FDGGVVLGAD
60 70 80 90 100
SRTTTGSYIA NRVTDKLTPI HDHIFCCRSG SAADTQAVAD AVTYQLGFHS
110 120 130 140 150
IELNEPPLVH TAASLFKEMC YRYREDLMAG IIIAGWDPQE GGQVYSVPMG
160 170 180 190 200
GMMVRQSFAI GGSGSSYIYG YVDATYREGM TKDECLQFTA NALALAMERD
210 220 230
GSSGGVIRLA AIQQSGVERQ VLLGDQIPKV TISTLPPP
Length:238
Mass (Da):25,290
Last modified:December 20, 2005 - v3
Checksum:i4B051AF11D78E49B
GO

Sequence cautioni

The sequence BAA01586.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC058451 mRNA. Translation: AAH58451.1.
AABR03076595 Genomic DNA. No translation available.
D10754 mRNA. Translation: BAA01586.1. Different initiation.
BN000325 mRNA. Translation: CAE48380.1.
PIRiJX0228.
S09086.
RefSeqiNP_476440.2. NM_057099.3.
UniGeneiRn.8118.

Genome annotation databases

EnsembliENSRNOT00000026507; ENSRNOP00000026507; ENSRNOG00000019551.
GeneIDi29666.
KEGGirno:29666.
UCSCiRGD:61881. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC058451 mRNA. Translation: AAH58451.1.
AABR03076595 Genomic DNA. No translation available.
D10754 mRNA. Translation: BAA01586.1. Different initiation.
BN000325 mRNA. Translation: CAE48380.1.
PIRiJX0228.
S09086.
RefSeqiNP_476440.2. NM_057099.3.
UniGeneiRn.8118.

3D structure databases

ProteinModelPortaliP28073.
SMRiP28073. Positions 34-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248287. 1 interaction.
IntActiP28073. 1 interaction.

Protein family/group databases

MEROPSiT01.010.

2D gel databases

World-2DPAGE0004:P28073.

Proteomic databases

PaxDbiP28073.
PRIDEiP28073.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026507; ENSRNOP00000026507; ENSRNOG00000019551.
GeneIDi29666.
KEGGirno:29666.
UCSCiRGD:61881. rat.

Organism-specific databases

CTDi5694.
RGDi61881. Psmb6.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00510000046484.
HOGENOMiHOG000091079.
HOVERGENiHBG000123.
InParanoidiP28073.
KOiK02738.
OMAiMESHKEN.
OrthoDBiEOG79GT80.
PhylomeDBiP28073.
TreeFamiTF106221.

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.

Miscellaneous databases

NextBioi609975.

Gene expression databases

GenevestigatoriP28073.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
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
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    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 Norway.
  3. "Molecular cloning of cDNAs for rat proteasomes: deduced primary structures of four other subunits."
    Tamura T., Shimbara N., Aki M., Ishida N., Bey F., Scherrer K., Tanaka K., Ichihara A.
    J. Biochem. 112:530-534(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-238.
  4. "N-terminal sequence similarities between components of the multicatalytic proteinase complex."
    Lilley K.S., Davison M.D., Rivett A.J.
    FEBS Lett. 262:327-329(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-51.
  5. Lubec G., Diao W.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 67-78 AND 209-229, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  6. "A genomic analysis of rat proteases and protease inhibitors."
    Puente X.S., Lopez-Otin C.
    Genome Res. 14:609-622(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiPSB6_RAT
AccessioniPrimary (citable) accession number: P28073
Secondary accession number(s): Q6IE68, Q6PDW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 20, 2005
Last modified: March 4, 2015
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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.