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P28065

- PSB9_HUMAN

UniProt

P28065 - PSB9_HUMAN

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Protein
Proteasome subunit beta type-9
Gene
PSMB9, LMP2, PSMB6i, RING12
Organism
Homo sapiens (Human)
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. Replacement of PSMB6 by PSMB9 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei20 – 212Cleavage; by autocatalysis
Active sitei21 – 211Nucleophile

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  2. G1/S transition of mitotic cell cycle Source: Reactome
  3. RNA metabolic process Source: Reactome
  4. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  5. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  6. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  7. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  8. apoptotic process Source: Reactome
  9. cellular nitrogen compound metabolic process Source: Reactome
  10. gene expression Source: Reactome
  11. mRNA metabolic process Source: Reactome
  12. mitotic cell cycle Source: Reactome
  13. negative regulation of apoptotic process Source: Reactome
  14. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  15. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  16. protein polyubiquitination Source: Reactome
  17. regulation of apoptotic process Source: Reactome
  18. regulation of cellular amino acid metabolic process Source: Reactome
  19. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  20. small molecule metabolic process Source: Reactome
  21. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Host-virus interaction, Immunity

Enzyme and pathway databases

ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

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
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:9546. PSMB9.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. nucleoplasm Source: Reactome
  5. proteasome complex Source: ProtInc
  6. proteasome core complex Source: UniProtKB
  7. spermatoproteasome complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201G → A: Impairs correct processing at the consensus site. 1 Publication
Mutagenesisi21 – 211T → A: Impairs correct processing at the consensus site. 1 Publication
Mutagenesisi53 – 531K → A: Impairs correct processing at the consensus site. 1 Publication

Organism-specific databases

PharmGKBiPA33891.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 2020Removed in mature form
PRO_0000026619Add
BLAST
Chaini21 – 219199Proteasome subunit beta type-9
PRO_0000026620Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysine1 Publication
Modified residuei109 – 1091N6-acetyllysine1 Publication

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

MaxQBiP28065.
PaxDbiP28065.
PRIDEiP28065.

2D gel databases

OGPiP28065.

PTM databases

PhosphoSiteiP28065.

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

ArrayExpressiP28065.
BgeeiP28065.
CleanExiHS_PSMB9.
GenevestigatoriP28065.

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 houskeeping subunit PSMB6. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Interacts with HIV-1 TAT protein.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9WMX22EBI-603300,EBI-6863741From a different organism.
GRIP1Q9Y3R03EBI-603300,EBI-5349621
NCOA1Q157883EBI-603300,EBI-455189
NCOA3Q9Y6Q93EBI-603300,EBI-81196
PSMB7Q994365EBI-603300,EBI-603319

Protein-protein interaction databases

BioGridi111671. 21 interactions.
IntActiP28065. 12 interactions.
MINTiMINT-2802096.
STRINGi9606.ENSP00000396813.

Structurei

3D structure databases

ProteinModelPortaliP28065.
SMRiP28065. Positions 21-219.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091079.
HOVERGENiHBG000123.
InParanoidiP28065.
KOiK02741.
OMAiQVYGTMG.
PhylomeDBiP28065.
TreeFamiTF106221.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. 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]

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. Align

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

MLRAGAPTGD LPRAGEVHTG TTIMAVEFDG GVVMGSDSRV SAGEAVVNRV    50
FDKLSPLHER IYCALSGSAA DAQAVADMAA YQLELHGIEL EEPPLVLAAA 100
NVVRNISYKY REDLSAHLMV AGWDQREGGQ VYGTLGGMLT RQPFAIGGSG 150
STFIYGYVDA AYKPGMSPEE CRRFTTDAIA LAMSRDGSSG GVIYLVTITA 200
AGVDHRVILG NELPKFYDE 219
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91G → E.
Corresponds to variant rs35100697 [ dbSNP | Ensembl ].
VAR_051551
Natural varianti32 – 321V → I.
Corresponds to variant rs241419 [ dbSNP | Ensembl ].
VAR_051552
Natural varianti60 – 601R → H.2 Publications
Corresponds to variant rs17587 [ dbSNP | Ensembl ].
VAR_013578
Natural varianti173 – 1731R → C.
Corresponds to variant rs17213861 [ dbSNP | Ensembl ].
VAR_051553

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei4 – 1310Missing in isoform LMP2.S.
VSP_005288

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. Translation: CAI18141.1.
AL935043 Genomic DNA. Translation: CAI18627.1.
BX088556 Genomic DNA. Translation: CAM26264.1.
BX927138 Genomic DNA. Translation: CAQ08450.1.
CR762476 Genomic DNA. Translation: CAQ08497.1.
CR933844 Genomic DNA. Translation: CAQ08907.1.
CR753889 Genomic DNA. Translation: CAQ10289.1.
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.3. human. [P28065-1]

Polymorphism databases

DMDMi417529.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. Translation: CAI18141.1 .
AL935043 Genomic DNA. Translation: CAI18627.1 .
BX088556 Genomic DNA. Translation: CAM26264.1 .
BX927138 Genomic DNA. Translation: CAQ08450.1 .
CR762476 Genomic DNA. Translation: CAQ08497.1 .
CR933844 Genomic DNA. Translation: CAQ08907.1 .
CR753889 Genomic DNA. Translation: CAQ10289.1 .
CH471081 Genomic DNA. Translation: EAX03654.1 .
BC065513 mRNA. Translation: AAH65513.1 .
CCDSi CCDS4759.1. [P28065-1 ]
PIRi A55632.
S27332.
RefSeqi NP_002791.1. NM_002800.4. [P28065-1 ]
UniGenei Hs.654585.

3D structure databases

ProteinModelPortali P28065.
SMRi P28065. Positions 21-219.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111671. 21 interactions.
IntActi P28065. 12 interactions.
MINTi MINT-2802096.
STRINGi 9606.ENSP00000396813.

Chemistry

ChEMBLi CHEMBL2364701.

Protein family/group databases

MEROPSi T01.013.

PTM databases

PhosphoSitei P28065.

Polymorphism databases

DMDMi 417529.

2D gel databases

OGPi P28065.

Proteomic databases

MaxQBi P28065.
PaxDbi P28065.
PRIDEi P28065.

Protocols and materials databases

DNASUi 5698.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374859 ; 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 .
GeneIDi 5698.
KEGGi hsa:5698.
UCSCi uc003sga.3. human. [P28065-1 ]

Organism-specific databases

CTDi 5698.
GeneCardsi GC06P032825.
GC06Pi32796.
GC06Pj32735.
GC06Pk32790.
GC06Pl32966.
GC06Pm32847.
GC06Pn32741.
GC06Po32903.
H-InvDB HIX0166929.
HIX0207611.
HIX0207787.
HGNCi HGNC:9546. PSMB9.
HPAi CAB015180.
HPA042818.
HPA053280.
MIMi 177045. gene.
neXtProti NX_P28065.
PharmGKBi PA33891.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0638.
HOGENOMi HOG000091079.
HOVERGENi HBG000123.
InParanoidi P28065.
KOi K02741.
OMAi QVYGTMG.
PhylomeDBi P28065.
TreeFami TF106221.

Enzyme and pathway databases

Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

GeneWikii PSMB9.
GenomeRNAii 5698.
NextBioi 22136.
PROi P28065.
SOURCEi Search...

Gene expression databases

ArrayExpressi P28065.
Bgeei P28065.
CleanExi HS_PSMB9.
Genevestigatori P28065.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami 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. "The major histocompatibility complex-encoded proteasome component LMP7: alternative first exons and post-translational processing."
    Glynne R., Kerr L.A., Mockridge I., Beck S., Kelly A., Trowsdale J.
    Eur. J. Immunol. 23:860-866(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "DNA sequence analysis of 66 kb of the human MHC class II region encoding a cluster of genes for antigen processing."
    Beck S., Kelly A., Radley E., Khurshid F., Alderton R.P., Trowsdale J.
    J. Mol. Biol. 228:433-441(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Second proteasome-related gene in the human MHC class II region."
    Kelly A., Powis S.H., Glynne R., Radley E., Beck S., Trowsdale J.
    Nature 353:667-668(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LMP2.L), VARIANT HIS-60.
  4. "Alternative exon usage and processing of the major histocompatibility complex-encoded proteasome subunits."
    Fruh K., Yang Y., Arnold D., Chambers J., Wu L., Waters J.B., Spies T., Peterson P.A.
    J. Biol. Chem. 267:22131-22140(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Evolutionary dynamics of non-coding sequences within the class II region of the human MHC."
    Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., Hosking L.K., Jackson A., Kelly A., Newell W.R., Sanseau P., Radley E., Thorpe K.L., Trowsdale J.
    J. Mol. Biol. 255:1-13(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "Major histocompatibility-encoded human proteasome LMP2. Genomic organization and a new form of mRNA."
    Singal D.P., Ye M., Quadri S.A.
    J. Biol. Chem. 270:1966-1970(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS LMP2.S AND LMP2.L).
  7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LMP2.L).
  8. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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] (ISOFORM LMP2.L).
    Tissue: Pancreas.
  11. "Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced by interferon-gamma for acquirement of the functional diversity responsible for antigen processing."
    Akiyama K., Kagawa S., Tamura T., Shimbara N., Takashina M., Kristensen P., Hendil K.B., Tanaka K., Ichihara A.
    FEBS Lett. 343:85-88(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Analysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis."
    Schmidtke G., Kraft R., Kostka S., Henklein P., Froemmel C., Loewe J., Huber R., Kloetzel P.-M., Schmidt M.
    EMBO J. 15:6887-6898(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-20; THR-21 AND LYS-53, SELF ACTIVATION OF BETA-SUBUNITS MODEL.
  13. "Proteasome subunits X and Y alter peptidase activities in opposite ways to the interferon-gamma-induced subunits LMP2 and LMP7."
    Gaczynska M., Goldberg A.L., Tanaka K., Hendil K.B., Rock K.L.
    J. Biol. Chem. 271:17275-17280(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  14. "Tumor necrosis factor-alpha induces coordinated changes in major histocompatibility class I presentation pathway, resulting in increased stability of class I complexes at the cell surface."
    Hallermalm K., Seki K., Wei C., Castelli C., Rivoltini L., Kiessling R., Levitskaya J.
    Blood 98:1108-1115(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY TNF AND IFNG.
  15. "Bipartite regulation of different components of the MHC class I antigen-processing machinery during dendritic cell maturation."
    Li J., Schuler-Thurner B., Schuler G., Huber C., Seliger B.
    Int. Immunol. 13:1515-1523(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  16. "Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits."
    Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E.
    FEBS Lett. 553:200-204(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT.
  17. "Potential effects of tetrodotoxin exposure to human glial cells postulated using microarray approach."
    Raghavendra Prasad H.S., Qi Z., Srinivasan K.N., Gopalakrishnakone P.
    Toxicon 44:597-608(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY TETRODOTOXIN.
  18. "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 IFNG AND IRF1.
  19. "The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription."
    Zhang H., Sun L., Liang J., Yu W., Zhang Y., Wang Y., Chen Y., Li R., Sun X., Shang Y.
    EMBO J. 25:4223-4233(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA1; NCOA2 AND NCOA3.
  20. "Heat shock up-regulates lmp2 and lmp7 and enhances presentation of immunoproteasome-dependent epitopes."
    Callahan M.K., Wohlfert E.A., Menoret A., Srivastava P.K.
    J. Immunol. 177:8393-8399(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY HEAT SHOCK.
  21. "Genome-wide gene expression differences in Crohn's disease and ulcerative colitis from endoscopic pinch biopsies: insights into distinctive pathogenesis."
    Wu F., Dassopoulos T., Cope L., Maitra A., Brant S.R., Harris M.L., Bayless T.M., Parmigiani G., Chakravarti S.
    Inflamm. Bowel Dis. 13:807-821(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  22. "CD40 induces antigen transporter and immunoproteasome gene expression in carcinomas via the coordinated action of NF-kappaB and of NF-kappaB-mediated de novo synthesis of IRF-1."
    Moschonas A., Kouraki M., Knox P.G., Thymiakou E., Kardassis D., Eliopoulos A.G.
    Mol. Cell. Biol. 28:6208-6222(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY CD40L.
  23. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53 AND LYS-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: VARIANT HIS-60.

Entry informationi

Entry nameiPSB9_HUMAN
AccessioniPrimary (citable) accession number: P28065
Secondary accession number(s): B0V0T1, Q16523, Q5JNW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 1, 1993
Last modified: September 3, 2014
This is version 164 of the entry and version 2 of the sequence. [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

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.

Keywords - Technical termi

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. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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