Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O35955 (PSB10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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-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 names
Name:Psmb10
Synonyms:Lmp10, Mecl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length273 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. 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. Ref.10

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. 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. Ref.8 Ref.9 Ref.10

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Tissue specificity

Detected in liver (at protein level). Ref.10

Induction

Up-regulated by interferon gamma (at protein level). Up-regulated by IRF1. Ref.6

Post-translational modification

Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity. Ref.5

Disruption phenotype

Impaired response of cytotoxic T-lymphocyte (CTL) to dominant epitopes of lymphocytic choriomeningitis virus (LCMV). Ref.7

Sequence similarities

Belongs to the peptidase T1B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 3939Removed in mature form
PRO_0000026653
Chain40 – 273234Proteasome subunit beta type-10
PRO_0000026654

Sites

Active site401Nucleophile
Site39 – 402Cleavage; by autocatalysis

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Experimental info

Mutagenesis401T → A: Prevents the correct removal of the propeptide. Ref.5
Sequence conflict41Q → E in AAH04730. Ref.4
Sequence conflict91T → R in AAH04730. Ref.4
Sequence conflict1891A → L in CAA71825. Ref.3

Secondary structure

.................................... 273
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O35955 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 9A1AAE55888FA905

FASTA27329,063
        10         20         30         40         50         60 
MLKQAVEPTG GFSFENCQRN ASLEHVLPGL RVPHARKTGT TIAGLVFRDG VILGADTRAT 

        70         80         90        100        110        120 
NDSVVADKSC EKIHFIAPKI YCCGAGVAAD TEMTTRMAAS KMELHALSTG REPRVATVTR 

       130        140        150        160        170        180 
ILRQTLFRYQ GHVGASLVVG GVDLNGPQLY EVHPHGSYSR LPFTALGSGQ GAAVALLEDR 

       190        200        210        220        230        240 
FQPNMTLEAA QELLVEAITA GILSDLGSGG NVDACVITAG GAKLQRALST PTEPVQRAGR 

       250        260        270 
YRFAPGTTPV LTREVRPLTL ELLEETVQAM EVE 

« Hide

References

« Hide 'large scale' references
[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]"Mapping the murine cardiac 26S proteasome complexes."
Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J., Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.
Circ. Res. 99:362-371(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
[9]"Acetylation-mediated proteasomal degradation of core histones during DNA repair and spermatogenesis."
Qian M.X., Pang Y., Liu C.H., Haratake K., Du B.Y., Ji D.Y., Wang G.F., Zhu Q.Q., Song W., Yu Y., Zhang X.X., Huang H.T., Miao S., Chen L.B., Zhang Z.H., Liang Y.N., Liu S., Cha H. expand/collapse author list , Yang D., Zhai Y., Komatsu T., Tsuruta F., Li H., Cao C., Li W., Li G.H., Cheng Y., Chiba T., Wang L., Goldberg A.L., Shen Y., Qiu X.B.
Cell 153:1012-1024(2013) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS22621.1.
RefSeqNP_038668.2. NM_013640.3.
UniGeneMm.787.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNFX-ray2.90H/V40-273[»]
3UNHX-ray3.20H/V40-273[»]
ProteinModelPortalO35955.
SMRO35955. Positions 40-258.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO35955. 5 interactions.
MINTMINT-4108870.

Protein family/group databases

MEROPST01.014.

PTM databases

PhosphoSiteO35955.

Proteomic databases

MaxQBO35955.
PaxDbO35955.
PRIDEO35955.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034369; ENSMUSP00000034369; ENSMUSG00000031897.
GeneID19171.
KEGGmmu:19171.
UCSCuc009nep.2. mouse.

Organism-specific databases

CTD5699.
MGIMGI:1096380. Psmb10.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00510000046533.
HOGENOMHOG000182856.
HOVERGENHBG093416.
InParanoidO35955.
KOK02733.
OMAQYRFAPG.
OrthoDBEOG7CRTQJ.
PhylomeDBO35955.
TreeFamTF106222.

Gene expression databases

ArrayExpressO35955.
BgeeO35955.
GenevestigatorO35955.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. 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]
PfamPF12465. Pr_beta_C. 1 hit.
PF00227. 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

ChiTaRSPSMB10. mouse.
NextBio295842.
PROO35955.
SOURCESearch...

Entry information

Entry namePSB10_MOUSE
AccessionPrimary (citable) accession number: O35955
Secondary accession number(s): O08687, Q99KC5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 121 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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