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Protein

Proteasome subunit beta type-9

Gene

PSMB9

Organism
Homo sapiens (Human)
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. Replacement of PSMB6 by PSMB9 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues.1 Publication

Miscellaneous

Encoded in the MHC class II region.
A model for self-activation in which residue Thr-21 serves as nucleophile and Lys-53 as proton donor/acceptor has been proposed. Subunit processing of mammalian beta-subunits proceeds via a novel ordered two-step mechanism involving autocatalysis.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei21Nucleophile1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease
Biological processHost-virus interaction, Immunity

Enzyme and pathway databases

ReactomeiR-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236974 ER-Phagosome pathway
R-HSA-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174113 SCF-beta-TrCP mediated degradation of Emi1
R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-180534 Vpu mediated degradation of CD4
R-HSA-180585 Vif-mediated degradation of APOBEC3G
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253 Degradation of beta-catenin by the destruction complex
R-HSA-202424 Downstream TCR signaling
R-HSA-211733 Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-350562 Regulation of ornithine decarboxylase (ODC)
R-HSA-382556 ABC-family proteins mediated transport
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-4608870 Asymmetric localization of PCP proteins
R-HSA-4641257 Degradation of AXIN
R-HSA-4641258 Degradation of DVL
R-HSA-5358346 Hedgehog ligand biogenesis
R-HSA-5362768 Hh mutants that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5610780 Degradation of GLI1 by the proteasome
R-HSA-5610783 Degradation of GLI2 by the proteasome
R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684 Hedgehog 'on' state
R-HSA-5658442 Regulation of RAS by GAPs
R-HSA-5668541 TNFR2 non-canonical NF-kB pathway
R-HSA-5676590 NIK-->noncanonical NF-kB signaling
R-HSA-5678895 Defective CFTR causes cystic fibrosis
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-68827 CDT1 association with the CDC6:ORC:origin complex
R-HSA-68949 Orc1 removal from chromatin
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-69229 Ubiquitin-dependent degradation of Cyclin D1
R-HSA-69481 G2/M Checkpoints
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

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):
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, PSMB6i, RING12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000240065.7
HGNCiHGNC:9546 PSMB9
MIMi177045 gene
neXtProtiNX_P28065

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi20G → A: Impairs correct processing at the consensus site. 1 Publication1
Mutagenesisi21T → A: Impairs correct processing at the consensus site. 1 Publication1
Mutagenesisi53K → A: Impairs correct processing at the consensus site. 1 Publication1

Organism-specific databases

DisGeNETi5698
OpenTargetsiENSG00000240065
PharmGKBiPA33891

Chemistry databases

ChEMBLiCHEMBL1944495
DrugBankiDB08889 Carfilzomib

Polymorphism and mutation databases

BioMutaiPSMB9
DMDMi417529

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000266191 – 20Removed in mature formAdd BLAST20
ChainiPRO_000002662021 – 219Proteasome subunit beta type-9Add BLAST199

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei53N6-acetyllysineCombined sources1
Modified residuei109N6-acetyllysineCombined sources1

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

EPDiP28065
PaxDbiP28065
PeptideAtlasiP28065
PRIDEiP28065
ProteomicsDBi54439
54440 [P28065-2]

2D gel databases

OGPiP28065

PTM databases

iPTMnetiP28065
PhosphoSitePlusiP28065

Expressioni

Developmental stagei

Highly expressed in immature dendritic cells (at protein level).1 Publication

Inductioni

Up-regulated by interferon gamma (at protein level). Up-regulated by IRF1. Up-regulated by tumor necrosis factor-alpha (at protein level). Up-regulated by tetrodotoxin (TTX) in glial cells. Up-regulated in Crohn's bowel disease (CD). Up-regulated by heat shock treatment. Up-regulated by CD40L via the NFKB1 pathway in cancer cells.7 Publications

Gene expression databases

BgeeiENSG00000240065
CleanExiHS_PSMB9
ExpressionAtlasiP28065 baseline and differential
GenevisibleiP28065 HS

Organism-specific databases

HPAiCAB015180
HPA042818
HPA053280

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.1 Publication
(Microbial infection) Interacts with HIV-1 TAT protein.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi111671, 73 interactors
IntActiP28065, 15 interactors
MINTiP28065
STRINGi9606.ENSP00000363993

Chemistry databases

BindingDBiP28065

Structurei

3D structure databases

ProteinModelPortaliP28065
SMRiP28065
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0174 Eukaryota
ENOG410XS23 LUCA
GeneTreeiENSGT00510000046484
HOGENOMiHOG000091079
HOVERGENiHBG000123
InParanoidiP28065
KOiK02741
OMAiHERIYCA
OrthoDBiEOG091G0GUI
PhylomeDBiP28065
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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform LMP2.L (identifier: P28065-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLRAGAPTGD LPRAGEVHTG TTIMAVEFDG GVVMGSDSRV SAGEAVVNRV
60 70 80 90 100
FDKLSPLHER IYCALSGSAA DAQAVADMAA YQLELHGIEL EEPPLVLAAA
110 120 130 140 150
NVVRNISYKY REDLSAHLMV AGWDQREGGQ VYGTLGGMLT RQPFAIGGSG
160 170 180 190 200
STFIYGYVDA AYKPGMSPEE CRRFTTDAIA LAMSRDGSSG GVIYLVTITA
210
AGVDHRVILG NELPKFYDE
Length:219
Mass (Da):23,264
Last modified:October 1, 1993 - v2
Checksum:i3B321F83641941AC
GO
Isoform LMP2.S (identifier: P28065-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     4-13: Missing.

Show »
Length:209
Mass (Da):22,328
Checksum:i3AD94A5C402BC2A0
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0515519G → E. Corresponds to variant dbSNP:rs35100697Ensembl.1
Natural variantiVAR_05155232V → I. Corresponds to variant dbSNP:rs241419Ensembl.1
Natural variantiVAR_01357860R → H2 PublicationsCorresponds to variant dbSNP:rs17587Ensembl.1
Natural variantiVAR_075258165G → D Found in a patient with Nakajo syndrome who also carries a mutation in PSMB4; unknown pathological significance; patients' cells show reduction of proteasome content and cysteine-type endopeptidase activity of the proteasome. 1 PublicationCorresponds to variant dbSNP:rs369359789Ensembl.1
Natural variantiVAR_051553173R → C. Corresponds to variant dbSNP:rs17213861Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0052884 – 13Missing in isoform LMP2.S. 1 Publication10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66401 Genomic DNA Translation: CAA47024.1
X62741 mRNA Translation: CAA44603.1
Z14977 Genomic DNA Translation: CAA78700.1
X87344 Genomic DNA Translation: CAA60784.1
U01025 mRNA Translation: AAC50154.1
S75169 mRNA Translation: AAC60646.1
CR541656 mRNA Translation: CAG46457.1
AL669918 Genomic DNA No translation available.
AL935043 Genomic DNA No translation available.
BX088556 Genomic DNA No translation available.
BX927138 Genomic DNA No translation available.
CR753889 Genomic DNA No translation available.
CR762476 Genomic DNA No translation available.
CR933844 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX03654.1
BC065513 mRNA Translation: AAH65513.1
CCDSiCCDS4759.1 [P28065-1]
PIRiA55632
S27332
RefSeqiNP_002791.1, NM_002800.4 [P28065-1]
UniGeneiHs.654585

Genome annotation databases

EnsembliENST00000374859; ENSP00000363993; ENSG00000240065 [P28065-1]
ENST00000383114; ENSP00000372595; ENSG00000240118 [P28065-1]
ENST00000383234; ENSP00000372721; ENSG00000243594 [P28065-1]
ENST00000422729; ENSP00000407233; ENSG00000243067 [P28065-1]
ENST00000427870; ENSP00000412027; ENSG00000242711
ENST00000434471; ENSP00000393744; ENSG00000243958
ENST00000444284; ENSP00000396813; ENSG00000239836 [P28065-1]
ENST00000453059; ENSP00000407810; ENSG00000240508
GeneIDi5698
KEGGihsa:5698
UCSCiuc003sga.4 human [P28065-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPSB9_HUMAN
AccessioniPrimary (citable) accession number: P28065
Secondary accession number(s): B0V0T1, Q16523, Q5JNW4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 1, 1993
Last modified: July 18, 2018
This is version 204 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

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