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Protein

Proteasome subunit beta type-10

Gene

Psmb10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei40Nucleophile1

GO - Molecular functioni

GO - Biological processi

  • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  • cell morphogenesis Source: MGI
  • proteolysis involved in cellular protein catabolic process Source: InterPro
  • T cell proliferation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-MMU-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-MMU-350562. Regulation of ornithine decarboxylase (ODC).
R-MMU-382556. ABC-family proteins mediated transport.
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641257. Degradation of AXIN.
R-MMU-4641258. Degradation of DVL.
R-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-5689603. UCH proteinases.
R-MMU-5689880. Ub-specific processing proteases.
R-MMU-68827. CDT1 association with the CDC6:ORC:origin complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69481. G2/M Checkpoints.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-MMU-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1096380. Psmb10.

Subcellular locationi

  • Cytoplasm PROSITE-ProRule annotation
  • Nucleus By similarity

GO - Cellular componenti

  • cytosol Source: Reactome
  • nucleus Source: UniProtKB-SubCell
  • proteasome core complex Source: UniProtKB
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi40T → A: Prevents the correct removal of the propeptide. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000266531 – 39Removed in mature formAdd BLAST39
ChainiPRO_000002665440 – 273Proteasome subunit beta type-10Add BLAST234

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1

Post-translational modificationi

Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei39 – 40Cleavage; by autolysis1 Publication2

Keywords - PTMi

Acetylation, Zymogen

Proteomic databases

EPDiO35955.
MaxQBiO35955.
PaxDbiO35955.
PeptideAtlasiO35955.
PRIDEiO35955.

PTM databases

iPTMnetiO35955.
PhosphoSitePlusiO35955.

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

BgeeiENSMUSG00000031897.
GenevisibleiO35955. 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. 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 interactors.
MINTiMINT-4108870.
STRINGi10090.ENSMUSP00000034369.

Structurei

Secondary structure

1273
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi41 – 46Combined sources6
Beta strandi48 – 55Combined sources8
Beta strandi59 – 61Combined sources3
Beta strandi64 – 69Combined sources6
Beta strandi73 – 77Combined sources5
Beta strandi80 – 87Combined sources8
Helixi88 – 109Combined sources22
Helixi115 – 128Combined sources14
Turni129 – 131Combined sources3
Beta strandi135 – 143Combined sources9
Beta strandi146 – 152Combined sources7
Beta strandi158 – 160Combined sources3
Beta strandi162 – 167Combined sources6
Helixi170 – 180Combined sources11
Helixi187 – 204Combined sources18
Beta strandi205 – 207Combined sources3
Beta strandi212 – 220Combined sources9
Beta strandi222 – 229Combined sources8
Beta strandi250 – 257Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNFX-ray2.90H/V40-273[»]
3UNHX-ray3.20H/V40-273[»]
ProteinModelPortaliO35955.
SMRiO35955.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0173. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00510000046533.
HOGENOMiHOG000182856.
HOVERGENiHBG093416.
InParanoidiO35955.
KOiK02733.
OMAiQTLFRYR.
OrthoDBiEOG091G0E5S.
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)DescriptionActionsGraphical viewLength
Sequence conflicti4Q → E in AAH04730 (PubMed:15489334).Curated1
Sequence conflicti9T → R in AAH04730 (PubMed:15489334).Curated1
Sequence conflicti189A → L in CAA71825 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNFX-ray2.90H/V40-273[»]
3UNHX-ray3.20H/V40-273[»]
ProteinModelPortaliO35955.
SMRiO35955.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO35955. 5 interactors.
MINTiMINT-4108870.
STRINGi10090.ENSMUSP00000034369.

Protein family/group databases

MEROPSiT01.014.

PTM databases

iPTMnetiO35955.
PhosphoSitePlusiO35955.

Proteomic databases

EPDiO35955.
MaxQBiO35955.
PaxDbiO35955.
PeptideAtlasiO35955.
PRIDEiO35955.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5699.
MGIiMGI:1096380. Psmb10.

Phylogenomic databases

eggNOGiKOG0173. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00510000046533.
HOGENOMiHOG000182856.
HOVERGENiHBG093416.
InParanoidiO35955.
KOiK02733.
OMAiQTLFRYR.
OrthoDBiEOG091G0E5S.
PhylomeDBiO35955.
TreeFamiTF106222.

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-MMU-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-MMU-350562. Regulation of ornithine decarboxylase (ODC).
R-MMU-382556. ABC-family proteins mediated transport.
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641257. Degradation of AXIN.
R-MMU-4641258. Degradation of DVL.
R-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-5689603. UCH proteinases.
R-MMU-5689880. Ub-specific processing proteases.
R-MMU-68827. CDT1 association with the CDC6:ORC:origin complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69481. G2/M Checkpoints.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-MMU-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiPsmb10. mouse.
PROiO35955.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031897.
GenevisibleiO35955. MM.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 141 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

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 one 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.