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O35955

- PSB10_MOUSE

UniProt

O35955 - PSB10_MOUSE

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Protein

Proteasome subunit beta type-10

Gene

Psmb10

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. This subunit is involved in antigen processing to generate class I binding peptides. Plays a role in determining the T-cell repertoire for an antiviral T-cell response.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei39 – 402Cleavage; by autocatalysis
Active sitei40 – 401Nucleophile

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. cell morphogenesis Source: MGI
  2. proteolysis involved in cellular protein catabolic process Source: InterPro
  3. T cell proliferation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.

Protein family/group databases

MEROPSiT01.014.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-10 (EC:3.4.25.1)
Alternative name(s):
Low molecular mass protein 10
Macropain subunit MECl-1
Multicatalytic endopeptidase complex subunit MECl-1
Proteasome MECl-1
Proteasome subunit beta-2i
Gene namesi
Name:Psmb10
Synonyms:Lmp10, Mecl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1096380. Psmb10.

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleus Source: UniProtKB-KW
  3. proteasome core complex Source: UniProtKB
  4. spermatoproteasome complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Disruption phenotypei

Impaired response of cytotoxic T-lymphocyte (CTL) to dominant epitopes of lymphocytic choriomeningitis virus (LCMV).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401T → A: Prevents the correct removal of the propeptide. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 3939Removed in mature formPRO_0000026653Add
BLAST
Chaini40 – 273234Proteasome subunit beta type-10PRO_0000026654Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Post-translational modificationi

Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity.

Keywords - PTMi

Acetylation, Zymogen

Proteomic databases

MaxQBiO35955.
PaxDbiO35955.
PRIDEiO35955.

PTM databases

PhosphoSiteiO35955.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Inductioni

Up-regulated by interferon gamma (at protein level). Up-regulated by IRF1.1 Publication

Gene expression databases

BgeeiO35955.
ExpressionAtlasiO35955. baseline and differential.
GenevestigatoriO35955.

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. Component of the immunoproteasome, where it displaces the equivalent houskeeping subunit PSMB7. Component of the spermatoproteasome, a form of the proteasome specifically found in testis.3 Publications

Protein-protein interaction databases

IntActiO35955. 5 interactions.
MINTiMINT-4108870.

Structurei

Secondary structure

1
273
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 466
Beta strandi48 – 558
Beta strandi59 – 613
Beta strandi64 – 696
Beta strandi73 – 775
Beta strandi80 – 878
Helixi88 – 10922
Helixi115 – 12814
Turni129 – 1313
Beta strandi135 – 1439
Beta strandi146 – 1527
Beta strandi158 – 1603
Beta strandi162 – 1676
Helixi170 – 18011
Helixi187 – 20418
Beta strandi205 – 2073
Beta strandi212 – 2209
Beta strandi222 – 2298
Beta strandi250 – 2578

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNFX-ray2.90H/V40-273[»]
3UNHX-ray3.20H/V40-273[»]
ProteinModelPortaliO35955.
SMRiO35955. Positions 40-258.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00510000046533.
HOGENOMiHOG000182856.
HOVERGENiHBG093416.
InParanoidiO35955.
KOiK02733.
OMAiQYRFAPG.
OrthoDBiEOG7CRTQJ.
PhylomeDBiO35955.
TreeFamiTF106222.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF12465. Pr_beta_C. 1 hit.
PF00227. 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.

O35955-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLKQAVEPTG GFSFENCQRN ASLEHVLPGL RVPHARKTGT TIAGLVFRDG
60 70 80 90 100
VILGADTRAT NDSVVADKSC EKIHFIAPKI YCCGAGVAAD TEMTTRMAAS
110 120 130 140 150
KMELHALSTG REPRVATVTR ILRQTLFRYQ GHVGASLVVG GVDLNGPQLY
160 170 180 190 200
EVHPHGSYSR LPFTALGSGQ GAAVALLEDR FQPNMTLEAA QELLVEAITA
210 220 230 240 250
GILSDLGSGG NVDACVITAG GAKLQRALST PTEPVQRAGR YRFAPGTTPV
260 270
LTREVRPLTL ELLEETVQAM EVE
Length:273
Mass (Da):29,063
Last modified:January 1, 1998 - v1
Checksum:i9A1AAE55888FA905
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41Q → E in AAH04730. (PubMed:15489334)Curated
Sequence conflicti9 – 91T → R in AAH04730. (PubMed:15489334)Curated
Sequence conflicti189 – 1891A → L in CAA71825. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U77784 mRNA. Translation: AAB86994.1.
U77785 Genomic DNA. Translation: AAB87637.1.
D85561 mRNA. Translation: BAA22855.1.
D85562 Genomic DNA. Translation: BAA22856.1.
Y10875 mRNA. Translation: CAA71825.1.
BC004730 mRNA. Translation: AAH04730.1.
CCDSiCCDS22621.1.
RefSeqiNP_038668.2. NM_013640.3.
UniGeneiMm.787.

Genome annotation databases

EnsembliENSMUST00000034369; ENSMUSP00000034369; ENSMUSG00000031897.
GeneIDi19171.
KEGGimmu:19171.
UCSCiuc009nep.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U77784 mRNA. Translation: AAB86994.1 .
U77785 Genomic DNA. Translation: AAB87637.1 .
D85561 mRNA. Translation: BAA22855.1 .
D85562 Genomic DNA. Translation: BAA22856.1 .
Y10875 mRNA. Translation: CAA71825.1 .
BC004730 mRNA. Translation: AAH04730.1 .
CCDSi CCDS22621.1.
RefSeqi NP_038668.2. NM_013640.3.
UniGenei Mm.787.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UNF X-ray 2.90 H/V 40-273 [» ]
3UNH X-ray 3.20 H/V 40-273 [» ]
ProteinModelPortali O35955.
SMRi O35955. Positions 40-258.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O35955. 5 interactions.
MINTi MINT-4108870.

Protein family/group databases

MEROPSi T01.014.

PTM databases

PhosphoSitei O35955.

Proteomic databases

MaxQBi O35955.
PaxDbi O35955.
PRIDEi O35955.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034369 ; ENSMUSP00000034369 ; ENSMUSG00000031897 .
GeneIDi 19171.
KEGGi mmu:19171.
UCSCi uc009nep.2. mouse.

Organism-specific databases

CTDi 5699.
MGIi MGI:1096380. Psmb10.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00510000046533.
HOGENOMi HOG000182856.
HOVERGENi HBG093416.
InParanoidi O35955.
KOi K02733.
OMAi QYRFAPG.
OrthoDBi EOG7CRTQJ.
PhylomeDBi O35955.
TreeFami TF106222.

Enzyme and pathway databases

Reactomei REACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.

Miscellaneous databases

ChiTaRSi PSMB10. mouse.
NextBioi 295842.
PROi O35955.
SOURCEi Search...

Gene expression databases

Bgeei O35955.
ExpressionAtlasi O35955. baseline and differential.
Genevestigatori O35955.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF12465. Pr_beta_C. 1 hit.
PF00227. Proteasome. 1 hit.
[Graphical view ]
PRINTSi PR00141. PROTEASOME.
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. "DNA sequence, chromosomal localization, and tissue expression of the mouse proteasome subunit lmp10 (Psmb10) gene."
    Cruz M., Elenich L.A., Smolarek T.A., Menon A.G., Monaco J.J.
    Genomics 45:618-622(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: 129/SvJ and BALB/c.
    Tissue: Liver.
  2. "The mouse genes encoding the third pair of beta-type proteasome subunits regulated reciprocally by IFN-gamma: structural comparison, chromosomal localization, and analysis of the promoter."
    Hayashi M., Ishibashi T., Tanaka K., Kasahara M.
    J. Immunol. 159:2760-2770(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: BALB/c and C57BL/6.
  3. "Molecular cloning of the mouse proteasome subunits MC14 and MECL-1: reciprocally regulated tisue expression of interferon-gamma-modulated proteasome subunits."
    Stohwasser R., Standera S., Peters I., Kloetzel P.-M., Groettrup M.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
    Tissue: Spleen.
  4. "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].
  5. "Mutational analysis of subunit i beta2 (MECL-1) demonstrates conservation of cleavage specificity between yeast and mammalian proteasomes."
    Salzmann U., Kral S., Braun B., Standera S., Schmidt M., Kloetzel P.M., Sijts A.
    FEBS Lett. 454:11-15(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF THR-40, AUTOCATALYTIC CLEAVAGE.
  6. "IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted expression of immunosubunits of the proteasome."
    Namiki S., Nakamura T., Oshima S., Yamazaki M., Sekine Y., Tsuchiya K., Okamoto R., Kanai T., Watanabe M.
    FEBS Lett. 579:2781-2787(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY INTERFERON GAMMA AND IRF1.
  7. "An altered T cell repertoire in MECL-1-deficient mice."
    Basler M., Moebius J., Elenich L., Groettrup M., Monaco J.J.
    J. Immunol. 176:6665-6672(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  8. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
  9. Cited for: IDENTIFICATION IN THE SPERMATOPROTEASOME.
  10. "Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity."
    Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M., Groll M.
    Cell 148:727-738(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT, FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPSB10_MOUSE
AccessioniPrimary (citable) accession number: O35955
Secondary accession number(s): O08687, Q99KC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 124 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3