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Q8BG41 (PSB11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-11

EC=3.4.25.1
Alternative name(s):
Proteasome subunit beta-5t
Gene names
Name:Psmb11
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length302 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. Incorporated instead of PSMB5 or PSMB8, this unit reduces the chymotrypsin-like activity of the proteasome. Plays a pivotal role in development of CD8-positive T-cells. Ref.1

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. Incorporated instead of PSMB5 and PSMB8. Ref.1

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Tissue specificity

Expressed exclusively in cortical thymic epithelial cells. Ref.1

Disruption phenotype

Displays defective development of CD8-positive T-cells in the thymus. Ref.1

Sequence similarities

Belongs to the peptidase T1B family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 4949Removed in mature form By similarity
PRO_0000300013
Chain50 – 302253Proteasome subunit beta type-11
PRO_0000300014

Sites

Active site501Nucleophile By similarity

Experimental info

Sequence conflict2661Y → H in AAI17734. Ref.3
Sequence conflict2661Y → H in AAI17733. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8BG41 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: CAF08F2E3E914A13

FASTA30233,220
        10         20         30         40         50         60 
MALQDVCKWQ TPDTPRPSIH LPQAGGWAVP RGCDPQTFLQ IHGPRLAHGT TTLAFRFRHG 

        70         80         90        100        110        120 
VIAAADTRSS CGSYVACPAS RKVIPVHQRL LGTTSGTSAD CATWYRVLRR ELRLRELREG 

       130        140        150        160        170        180 
QLPSVAGTAK LLAAMMSCYR GLDLCVATAL CGWDHSGPAL FYVYSDGTCL QGDIFSVGSG 

       190        200        210        220        230        240 
SPYAYGVLDR GYHYDMTIQE AYTLARCAVA HATHRDAYSG GSVDLFHVRE SGWEYVSRSD 

       250        260        270        280        290        300 
ACVLYRELQK ARSLEQELEA KACGIYPEPA TPQGARECKE LFVEQEEVTP EDCAIIMKTE 


TM 

« Hide

References

« Hide 'large scale' references
[1]"Regulation of CD8+ T cell development by thymus-specific proteasomes."
Murata S., Sasaki K., Kishimoto T., Niwa S., Hayashi H., Takahama Y., Tanaka K.
Science 316:1349-1353(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Thymus.
[3]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB299436 mRNA. Translation: BAF63539.1.
AK041393 mRNA. Translation: BAC30929.1.
AK162727 mRNA. Translation: BAE37039.1.
AK037368 mRNA. Translation: BAC29796.1.
BC117732 mRNA. Translation: AAI17733.1.
BC117733 mRNA. Translation: AAI17734.1.
CCDSCCDS49491.1.
RefSeqNP_780413.1. NM_175204.4.
UniGeneMm.32009.

3D structure databases

ProteinModelPortalQ8BG41.
SMRQ8BG41. Positions 50-272.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPST01.016.

PTM databases

PhosphoSiteQ8BG41.

Proteomic databases

MaxQBQ8BG41.
PRIDEQ8BG41.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000097177; ENSMUSP00000132140; ENSMUSG00000072423.
GeneID73902.
KEGGmmu:73902.
UCSCuc007twn.2. mouse.

Organism-specific databases

CTD122706.
MGIMGI:1921152. Psmb11.

Phylogenomic databases

GeneTreeENSGT00510000046395.
HOVERGENHBG108297.
KOK11598.
OMAIERRICE.
OrthoDBEOG7FNC86.
PhylomeDBQ8BG41.
TreeFamTF106223.

Gene expression databases

BgeeQ8BG41.
GenevestigatorQ8BG41.

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

ChiTaRSPSMB11. mouse.
NextBio339310.
PROQ8BG41.
SOURCESearch...

Entry information

Entry namePSB11_MOUSE
AccessionPrimary (citable) accession number: Q8BG41
Secondary accession number(s): Q149K8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 94 of the entry and version 1 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot