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Protein

Proteasome subunit beta type-11

Gene

Psmb11

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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. 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.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_274287. Degradation of beta-catenin by the destruction complex.
REACT_275686. Activation of NF-kappaB in B cells.
REACT_275732. degradation of AXIN.
REACT_278878. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_289441. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_294625. Ubiquitin-dependent degradation of Cyclin D1.
REACT_297888. degradation of DVL.
REACT_299120. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_301078. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_308964. ER-Phagosome pathway.
REACT_310780. Degradation of GLI2 by the proteasome.
REACT_315933. Orc1 removal from chromatin.
REACT_321346. Separation of Sister Chromatids.
REACT_326233. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_329431. APC/C:Cdc20 mediated degradation of Securin.
REACT_334737. Regulation of ornithine decarboxylase (ODC).
REACT_336463. CDK-mediated phosphorylation and removal of Cdc6.
REACT_336745. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_341044. SCF-beta-TrCP mediated degradation of Emi1.
REACT_341075. ER-Phagosome pathway.
REACT_342636. Asymmetric localization of PCP proteins.
REACT_343561. CDT1 association with the CDC6:ORC:origin complex.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_345193. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_347264. Hedgehog ligand biogenesis.
REACT_351311. Hedgehog 'on' state.
REACT_353777. GLI3 is processed to GLI3R by the proteasome.
REACT_359269. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_359387. Degradation of GLI1 by the proteasome.
REACT_360804. CLEC7A (Dectin-1) signaling.

Protein family/group databases

MEROPSiT01.016.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-11 (EC:3.4.25.1)
Alternative name(s):
Proteasome subunit beta-5t
Gene namesi
Name:Psmb11
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1921152. Psmb11.

Subcellular locationi

  • Cytoplasm PROSITE-ProRule annotation
  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Disruption phenotypei

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 4949Removed in mature formBy similarityPRO_0000300013Add
BLAST
Chaini50 – 302253Proteasome subunit beta type-11PRO_0000300014Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

MaxQBiQ8BG41.
PRIDEiQ8BG41.

PTM databases

PhosphoSiteiQ8BG41.

Expressioni

Tissue specificityi

Expressed exclusively in cortical thymic epithelial cells.1 Publication

Gene expression databases

BgeeiQ8BG41.
GenevisibleiQ8BG41. MM.

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. Incorporated instead of PSMB5 and PSMB8.1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000132140.

Structurei

3D structure databases

ProteinModelPortaliQ8BG41.
SMRiQ8BG41. Positions 50-245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00510000046395.
HOVERGENiHBG108297.
InParanoidiQ8BG41.
KOiK11598.
OMAiSADCATW.
OrthoDBiEOG7FNC86.
PhylomeDBiQ8BG41.
TreeFamiTF106223.

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.

Q8BG41-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALQDVCKWQ TPDTPRPSIH LPQAGGWAVP RGCDPQTFLQ IHGPRLAHGT
60 70 80 90 100
TTLAFRFRHG VIAAADTRSS CGSYVACPAS RKVIPVHQRL LGTTSGTSAD
110 120 130 140 150
CATWYRVLRR ELRLRELREG QLPSVAGTAK LLAAMMSCYR GLDLCVATAL
160 170 180 190 200
CGWDHSGPAL FYVYSDGTCL QGDIFSVGSG SPYAYGVLDR GYHYDMTIQE
210 220 230 240 250
AYTLARCAVA HATHRDAYSG GSVDLFHVRE SGWEYVSRSD ACVLYRELQK
260 270 280 290 300
ARSLEQELEA KACGIYPEPA TPQGARECKE LFVEQEEVTP EDCAIIMKTE

TM
Length:302
Mass (Da):33,220
Last modified:March 1, 2003 - v1
Checksum:iCAF08F2E3E914A13
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti266 – 2661Y → H in AAI17734 (PubMed:15489334).Curated
Sequence conflicti266 – 2661Y → H in AAI17733 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS49491.1.
RefSeqiNP_780413.1. NM_175204.4.
UniGeneiMm.32009.

Genome annotation databases

EnsembliENSMUST00000097177; ENSMUSP00000132140; ENSMUSG00000072423.
GeneIDi73902.
KEGGimmu:73902.
UCSCiuc007twn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS49491.1.
RefSeqiNP_780413.1. NM_175204.4.
UniGeneiMm.32009.

3D structure databases

ProteinModelPortaliQ8BG41.
SMRiQ8BG41. Positions 50-245.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000132140.

Protein family/group databases

MEROPSiT01.016.

PTM databases

PhosphoSiteiQ8BG41.

Proteomic databases

MaxQBiQ8BG41.
PRIDEiQ8BG41.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000097177; ENSMUSP00000132140; ENSMUSG00000072423.
GeneIDi73902.
KEGGimmu:73902.
UCSCiuc007twn.2. mouse.

Organism-specific databases

CTDi122706.
MGIiMGI:1921152. Psmb11.

Phylogenomic databases

GeneTreeiENSGT00510000046395.
HOVERGENiHBG108297.
InParanoidiQ8BG41.
KOiK11598.
OMAiSADCATW.
OrthoDBiEOG7FNC86.
PhylomeDBiQ8BG41.
TreeFamiTF106223.

Enzyme and pathway databases

ReactomeiREACT_274287. Degradation of beta-catenin by the destruction complex.
REACT_275686. Activation of NF-kappaB in B cells.
REACT_275732. degradation of AXIN.
REACT_278878. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_289441. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_294625. Ubiquitin-dependent degradation of Cyclin D1.
REACT_297888. degradation of DVL.
REACT_299120. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_301078. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_308964. ER-Phagosome pathway.
REACT_310780. Degradation of GLI2 by the proteasome.
REACT_315933. Orc1 removal from chromatin.
REACT_321346. Separation of Sister Chromatids.
REACT_326233. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_329431. APC/C:Cdc20 mediated degradation of Securin.
REACT_334737. Regulation of ornithine decarboxylase (ODC).
REACT_336463. CDK-mediated phosphorylation and removal of Cdc6.
REACT_336745. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_341044. SCF-beta-TrCP mediated degradation of Emi1.
REACT_341075. ER-Phagosome pathway.
REACT_342636. Asymmetric localization of PCP proteins.
REACT_343561. CDT1 association with the CDC6:ORC:origin complex.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_345193. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_347264. Hedgehog ligand biogenesis.
REACT_351311. Hedgehog 'on' state.
REACT_353777. GLI3 is processed to GLI3R by the proteasome.
REACT_359269. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_359387. Degradation of GLI1 by the proteasome.
REACT_360804. CLEC7A (Dectin-1) signaling.

Miscellaneous databases

ChiTaRSiPsmb11. mouse.
NextBioi339310.
PROiQ8BG41.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BG41.
GenevisibleiQ8BG41. MM.

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. "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.
    , 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].

Entry informationi

Entry nameiPSB11_MOUSE
AccessioniPrimary (citable) accession number: Q8BG41
Secondary accession number(s): Q149K8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: March 1, 2003
Last modified: June 24, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.