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Protein

Proteasome subunit beta type-9

Gene

Psmb9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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. Contributes to NFKBIA degradation and subsequently NFKB1 generation.2 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei21NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease
Biological processImmunity

Protein family/group databases

MEROPSiT01.013

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-9 (EC:3.4.25.1)
Alternative name(s):
LMP-2d
Low molecular mass protein 2
Macropain chain 7
Multicatalytic endopeptidase complex chain 7
Proteasome chain 7
Proteasome subunit beta-1i
Really interesting new gene 12 protein
Gene namesi
Name:Psmb9
Synonyms:Lmp2, Ring12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1346526 Psmb9

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Disruption phenotypei

Depletion of LMP2 by RNAi suppresses expression and activities of the matrix metalloproteinase MMP2 and MMP9 by blocking the transfer of active NF-kappa-B heterodimers into the nucleus.1 Publication

Chemistry databases

ChEMBLiCHEMBL1944491

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000266211 – 20Removed in mature formBy similarityAdd BLAST20
ChainiPRO_000002662221 – 219Proteasome subunit beta type-9Add BLAST199

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei53N6-acetyllysineBy similarity1
Modified residuei109N6-acetyllysineBy similarity1

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei20 – 21Cleavage; by autolysisBy similarity2

Keywords - PTMi

Acetylation, Zymogen

Proteomic databases

EPDiP28076
MaxQBiP28076
PaxDbiP28076
PeptideAtlasiP28076
PRIDEiP28076

PTM databases

iPTMnetiP28076
PhosphoSitePlusiP28076

Expressioni

Tissue specificityi

Detected in liver (at protein level). Expressed at high levels in the thymus, spleen, lung, heart and liver. Expressed at moderate levels in the kidney.2 Publications

Inductioni

Up-regulated by interferon gamma (at protein level). Up-regulated by IRF1. Up-regulated by heat shock treatment. Down-regulated by EGR1 in neuronal cells.3 Publications

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 housekeeping subunit PSMB6. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Interacts with NCOA1, NCOA2 and NCOA3.3 Publications

Protein-protein interaction databases

CORUMiP28076
IntActiP28076, 7 interactors
MINTiP28076
STRINGi10090.ENSMUSP00000133499

Structurei

Secondary structure

1219
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP28076
SMRiP28076
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0174 Eukaryota
ENOG410XS23 LUCA
HOGENOMiHOG000091079
HOVERGENiHBG000123
InParanoidiP28076
KOiK02741
PhylomeDBiP28076
TreeFamiTF106221

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR000243 Pept_T1A_subB
IPR034383 Proteasome_beta9
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type
PANTHERiPTHR11599:SF50 PTHR11599:SF50, 1 hit
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
PRINTSiPR00141 PROTEASOME
SUPFAMiSSF56235 SSF56235, 1 hit
PROSITEiView protein in PROSITE
PS00854 PROTEASOME_BETA_1, 1 hit
PS51476 PROTEASOME_BETA_2, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.iShow all

P28076-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLRAGAPTAG SFRTEEVHTG TTIMAVEFDG GVVVGSDSRV SAGTAVVNRV
60 70 80 90 100
FDKLSPLHQR IFCALSGSAA DAQAIADMAA YQLELHGLEL EEPPLVLAAA
110 120 130 140 150
NVVKNISYKY REDLLAHLIV AGWDQREGGQ VYGTMGGMLI RQPFTIGGSG
160 170 180 190 200
SSYIYGYVDA AYKPGMTPEE CRRFTTNAIT LAMNRDGSSG GVIYLVTITA
210
AGVDHRVILG DELPKFYDE
Length:219
Mass (Da):23,397
Last modified:August 1, 1992 - v1
Checksum:i036BC558E770BD3E
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0R4J256A0A0R4J256_MOUSE
Proteasome subunit beta type
Psmb9
219Annotation score:
G3UYK5G3UYK5_MOUSE
Proteasome subunit beta type-9
Psmb9
63Annotation score:
F6QXK7F6QXK7_MOUSE
Proteasome subunit beta type-9
Psmb9
44Annotation score:

Sequence cautioni

The sequence AAA39439 differs from that shown. Reason: Frameshift at positions 10 and 130.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti60R → H in LMP-2b. 1
Natural varianti126R → C in LMP-2b. 1
Natural varianti177N → D in LMP-2b and LMP-2q. Combined sources1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S59862 mRNA Translation: AAB20105.1
U22448 mRNA Translation: AAA75305.1
U22447 mRNA Translation: AAA75304.1
S58203 mRNA Translation: AAP13903.1
L11613 Genomic DNA Translation: AAA39439.1 Frameshift.
U22919 mRNA Translation: AAA75306.1
U22920 mRNA Translation: AAA75307.1
U35323 Genomic DNA Translation: AAA98932.1
D14566 Genomic DNA Translation: BAA40680.1
D44454 mRNA Translation: BAA22575.1
D44457 mRNA Translation: BAA22578.1
D44458 mRNA Translation: BAA22579.1
D44460 mRNA Translation: BAA22581.1
D44461 mRNA Translation: BAA22582.1
D44462 mRNA Translation: BAA22583.1
D43620 Genomic DNA Translation: BAA19855.1
AF027865 Genomic DNA Translation: AAB81528.1
AF100956 Genomic DNA Translation: AAC69911.1
AK008429 mRNA Translation: BAB25664.1
CCDSiCCDS28642.1
PIRiJC2019
RefSeqiNP_038613.1, NM_013585.2
UniGeneiMm.390983

Genome annotation databases

GeneIDi16912
KEGGimmu:16912

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPSB9_MOUSE
AccessioniPrimary (citable) accession number: P28076
Secondary accession number(s): O09085
, O09151, Q07704, Q60827, Q64278
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 18, 2018
This is version 170 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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