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P28073 (PSB6_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Psmb6
Synonyms:Psmb6l
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length238 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

Cleavage of peptide bonds with very broad specificity.

Subunit structure

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.

Subcellular location

Cytoplasm. Nucleus.

Sequence similarities

Belongs to the peptidase T1B family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Propeptide2 – 3332Removed in mature form
PRO_0000026617
Chain34 – 238205Proteasome subunit beta type-6
PRO_0000026618

Sites

Active site341Nucleophile By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
P28073 [UniParc].

Last modified December 20, 2005. Version 3.
Checksum: 4B051AF11D78E49B

FASTA23825,290
        10         20         30         40         50         60 
MAAALAVRGA VSAPAFGPEA LTPDWENREV STGTTIMAVQ FDGGVVLGAD SRTTTGSYIA 

        70         80         90        100        110        120 
NRVTDKLTPI HDHIFCCRSG SAADTQAVAD AVTYQLGFHS IELNEPPLVH TAASLFKEMC 

       130        140        150        160        170        180 
YRYREDLMAG IIIAGWDPQE GGQVYSVPMG GMMVRQSFAI GGSGSSYIYG YVDATYREGM 

       190        200        210        220        230 
TKDECLQFTA NALALAMERD GSSGGVIRLA AIQQSGVERQ VLLGDQIPKV TISTLPPP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC058451 mRNA. Translation: AAH58451.1.
AABR03076595 Genomic DNA. No translation available.
D10754 mRNA. Translation: BAA01586.1. Different initiation.
BN000325 mRNA. Translation: CAE48380.1.
PIRJX0228.
S09086.
RefSeqNP_476440.2. NM_057099.3.
UniGeneRn.8118.

3D structure databases

ProteinModelPortalP28073.
SMRP28073. Positions 34-235.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248287. 1 interaction.
IntActP28073. 1 interaction.

Protein family/group databases

MEROPST01.010.

2D gel databases

World-2DPAGE0004:P28073.

Proteomic databases

PaxDbP28073.
PRIDEP28073.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015746; ENSRNOP00000015747; ENSRNOG00000011827.
ENSRNOT00000026507; ENSRNOP00000026507; ENSRNOG00000019551.
GeneID29666.
KEGGrno:29666.
UCSCRGD:61881. rat.

Organism-specific databases

CTD5694.
RGD61881. Psmb6.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00510000046484.
HOGENOMHOG000091079.
HOVERGENHBG000123.
InParanoidP28073.
KOK02738.
OMACIRMCVI.
OrthoDBEOG79GT80.
PhylomeDBP28073.
TreeFamTF106221.

Gene expression databases

GenevestigatorP28073.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSPR00141. PROTEASOME.
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio609975.

Entry information

Entry namePSB6_RAT
AccessionPrimary (citable) accession number: P28073
Secondary accession number(s): Q6IE68, Q6PDW5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 20, 2005
Last modified: June 11, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries