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P28062 (PSB8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit beta type-8

EC=3.4.25.1
Alternative name(s):
Low molecular mass protein 7
Macropain subunit C13
Multicatalytic endopeptidase complex subunit C13
Proteasome component C13
Proteasome subunit beta-5i
Really interesting new gene 10 protein
Gene names
Name:PSMB8
Synonyms:LMP7, PSMB5i, RING10, Y2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length276 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. Replacement of PSMB5 by PSMB8 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. Acts as a major component of interferon gamma-induced sensitivity. Plays a key role in apoptosis via the degradation of the apoptotic inhibitor MCL1. May be involved in the inflammatory response pathway. In cancer cells, substitution of isoform 1 (E2) by isoform 2 (E1) results in immunoproteasome deficiency. Required for the differentiation of preadipocytes into adipocytes. Ref.12 Ref.21 Ref.25 Ref.29

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 housekeeping subunit PSMB5. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Directly interacts with POMP. Interacts with HIV-1 TAT protein. Interacts with TAP1. Ref.16 Ref.19 Ref.20

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Developmental stage

Highly expressed in immature dendritic cells (at protein level). Ref.15

Induction

Up-regulated by IFNG/IFN-gamma and IRF1 (at protein level). Up-regulated by TNF (at protein level). Up-regulated by tetrodotoxin (TTX) in glial cells. Up-regulated in Crohn's bowel disease (CD). Down-regulated by the selective inhibitor PR-957. Down-regulated in mature dendritic cells by HSV-1 infection. Up-regulated by heat shock treatment. Ref.13 Ref.14 Ref.17 Ref.18 Ref.22 Ref.23 Ref.25 Ref.26 Ref.27

Post-translational modification

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

Involvement in disease

Nakajo syndrome (NKJO) [MIM:256040]: An autosomal recessive autoinflammatory disorder characterized by early childhood onset of recurrent fever, joint stiffness and severe contractures of the hands and feet, and erythematous skin lesions with subsequent development of lipodystrophy and laboratory evidence of immune dysregulation. Accompanying features may include muscle weakness and atrophy, hepatosplenomegaly, and microcytic anemia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.29 Ref.30 Ref.31 Ref.32

Mutation Met-75 has been found in chronic atypical neutrophilic dermatosis with lipodystrophy and elevated temperature syndrome (CANDLE syndrome). CANDLE patients have some overlapping features with NKJO patients, including a cutaneous eruption and lipodystrophy. They show a characteristic neutrophilic dermatosis with a mononuclear interstitial infiltrate in the dermis that seems pathognomonic for CANDLE syndrome (Ref.31).

Sequence similarities

Belongs to the peptidase T1B family.

Ontologies

Keywords
   Biological processDifferentiation
Host-virus interaction
Immunity
   Cellular componentCytoplasm
Nucleus
Proteasome
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   Molecular functionHydrolase
Protease
Threonine protease
   PTMPhosphoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Traceable author statement. Source: Reactome

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

RNA metabolic process

Traceable author statement. Source: Reactome

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

fat cell differentiation

Inferred from mutant phenotype Ref.29. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Traceable author statement. Source: Reactome

negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein polyubiquitination

Traceable author statement. Source: Reactome

regulation of apoptotic process

Traceable author statement. Source: Reactome

regulation of cellular amino acid metabolic process

Traceable author statement. Source: Reactome

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

type I interferon signaling pathway

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

proteasome complex

Traceable author statement PubMed 8666937. Source: ProtInc

proteasome core complex

Inferred from sequence or structural similarity. Source: UniProtKB

spermatoproteasome complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 15303969. Source: IntAct

threonine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P279584EBI-372294,EBI-3649474From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P28062-1)

Also known as: LMP7B; LMP7-E2;

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.
Isoform 2 (identifier: P28062-2)

Also known as: LMP7A; LMP7-E1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: MALLDVCGAP...PELALPRGMQ → MLIGTPTPRD...PVSSGCPGLE
Note: Contains a phosphothreonine at position 5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 7272Removed in mature form By similarity
PRO_0000026597
Chain73 – 276204Proteasome subunit beta type-8
PRO_0000026598

Sites

Active site731Nucleophile By similarity
Site72 – 732Cleavage; by autocatalysis By similarity

Natural variations

Alternative sequence1 – 4949MALLD…PRGMQ → MLIGTPTPRDTTPSSWLTSS LLVEAAPLDDTTLPTPVSSG CPGLE in isoform 2.
VSP_005287
Natural variant81G → R in LMP7C.
Corresponds to variant rs114772012 [ dbSNP | Ensembl ].
VAR_006488
Natural variant30 – 323PGH → RPD in LPM7C.
VAR_006489
Natural variant491Q → K. Ref.7
Corresponds to variant rs2071543 [ dbSNP | Ensembl ].
VAR_065204
Natural variant741T → S.
Corresponds to variant rs17220206 [ dbSNP | Ensembl ].
VAR_057046
Natural variant751T → M in NKJO; also found in patients with CANDLE syndrome; markedly decreased chymotrypsin-like activity consistent with a decrease in proteasomal activity and loss of function. Ref.30 Ref.31
VAR_065291
Natural variant2011G → V in NKJO; affects immunoproteasome assembly; reduced proteasome levels; reduced chymotrypsin-like activity consistent with a decrease in proteasomal activity. Ref.29 Ref.32
VAR_066449

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (LMP7B) (LMP7-E2) [UniParc].

Last modified May 31, 2011. Version 3.
Checksum: 4F689501677DBD44

FASTA27630,354
        10         20         30         40         50         60 
MALLDVCGAP RGQRPESALP VAGSGRRSDP GHYSFSMRSP ELALPRGMQP TEFFQSLGGD 

        70         80         90        100        110        120 
GERNVQIEMA HGTTTLAFKF QHGVIAAVDS RASAGSYISA LRVNKVIEIN PYLLGTMSGC 

       130        140        150        160        170        180 
AADCQYWERL LAKECRLYYL RNGERISVSA ASKLLSNMMC QYRGMGLSMG SMICGWDKKG 

       190        200        210        220        230        240 
PGLYYVDEHG TRLSGNMFST GSGNTYAYGV MDSGYRPNLS PEEAYDLGRR AIAYATHRDS 

       250        260        270 
YSGGVVNMYH MKEDGWVKVE STDVSDLLHQ YREANQ 

« Hide

Isoform 2 (LMP7A) (LMP7-E1) [UniParc].

Checksum: E5A903101BE5C0B7
Show »

FASTA27229,770

References

« Hide 'large scale' references
[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]"A proteasome-related gene between the two ABC transporter loci in the class II region of the human MHC."
Glynne R., Powis S.H., Beck S., Kelly A., Kerr L.A., Trowsdale J.
Nature 353:357-360(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[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]"Different genomic structure of mouse and human Lmp7 genes: characterization of MHC-encoded proteasome genes."
Meinhardt T., Graf U., Hammerling G.J.
Immunogenetics 38:373-379(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"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].
[7]"Sequence analysis of the HLA-linked LMP7 gene."
Maksymowych W.P.
Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE LMP7C), VARIANT LYS-49.
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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 2).
Tissue: Skin.
[11]"Two newly discovered alleles of major histocompatibility complex-encoded LMP7 in Korean populations."
Kim T.G., Lee Y.H., Choi H.B., Han H.
Hum. Immunol. 46:61-64(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-269.
Tissue: Blood.
[12]"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.
[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]"Cytoplasmic domains of the transporter associated with antigen processing and P-glycoprotein interact with subunits of the proteasome."
Begley G.S., Horvath A.R., Taylor J.C., Higgins C.F.
Mol. Immunol. 42:137-141(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TAP1.
[20]"IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response."
Heink S., Ludwig D., Kloetzel P.-M., Krueger E.
Proc. Natl. Acad. Sci. U.S.A. 102:9241-9246(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH POMP.
[21]"Tumor cell lines expressing the proteasome subunit isoform LMP7E1 exhibit immunoproteasome deficiency."
Heink S., Fricke B., Ludwig D., Kloetzel P.M., Krueger E.
Cancer Res. 66:649-652(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"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.
[23]"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.
[24]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Cardiovascular inflammation and lesion cell apoptosis: a novel connection via the interferon-inducible immunoproteasome."
Yang Z., Gagarin D., St Laurent G. III, Hammell N., Toma I., Hu C.A., Iwasa A., McCaffrey T.A.
Arterioscler. Thromb. Vasc. Biol. 29:1213-1219(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY IFNG, FUNCTION.
[26]"Herpes simplex virus type I infection of mature dendritic cells leads to reduced LMP7-mRNA-expression levels."
Eisemann J., Prechtel A.T., Muehl-Zuerbes P., Steinkasserer A., Kummer M.
Immunobiology 214:861-867(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[27]"A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis."
Muchamuel T., Basler M., Aujay M.A., Suzuki E., Kalim K.W., Lauer C., Sylvain C., Ring E.R., Shields J., Jiang J., Shwonek P., Parlati F., Demo S.D., Bennett M.K., Kirk C.J., Groettrup M.
Nat. Med. 15:781-787(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY PR-957.
[28]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"A mutation in the immunoproteasome subunit PSMB8 causes autoinflammation and lipodystrophy in humans."
Kitamura A., Maekawa Y., Uehara H., Izumi K., Kawachi I., Nishizawa M., Toyoshima Y., Takahashi H., Standley D.M., Tanaka K., Hamazaki J., Murata S., Obara K., Toyoshima I., Yasutomo K.
J. Clin. Invest. 121:4150-4160(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ADIPOCYTE DIFFERENTIATION, VARIANT NKJO VAL-201, CHARACTERIZATION OF VARIANT NKJO VAL-201.
[30]"PSMB8 encoding the beta5i proteasome subunit is mutated in joint contractures, muscle atrophy, microcytic anemia, and panniculitis-induced lipodystrophy syndrome."
Agarwal A.K., Xing C., DeMartino G.N., Mizrachi D., Hernandez M.D., Sousa A.B., Martinez de Villarreal L., dos Santos H.G., Garg A.
Am. J. Hum. Genet. 87:866-872(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NKJO MET-75, CHARACTERIZATION OF VARIANT NKJO MET-75.
[31]"Mutations in proteasome subunit beta type 8 cause chronic atypical neutrophilic dermatosis with lipodystrophy and elevated temperature with evidence of genetic and phenotypic heterogeneity."
Liu Y., Ramot Y., Torrelo A., Paller A.S., Si N., Babay S., Kim P.W., Sheikh A., Lee C.C., Chen Y., Vera A., Zhang X., Goldbach-Mansky R., Zlotogorski A.
Arthritis Rheum. 64:895-907(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT OF VARIANT NKJO MET-75 IN CANDLE SYNDROME.
[32]"Proteasome assembly defect due to a proteasome subunit beta type 8 (PSMB8) mutation causes the autoinflammatory disorder, Nakajo-Nishimura syndrome."
Arima K., Kinoshita A., Mishima H., Kanazawa N., Kaneko T., Mizushima T., Ichinose K., Nakamura H., Tsujino A., Kawakami A., Matsunaka M., Kasagi S., Kawano S., Kumagai S., Ohmura K., Mimori T., Hirano M., Ueno S. expand/collapse author list , Tanaka K., Tanaka M., Toyoshima I., Sugino H., Yamakawa A., Tanaka K., Niikawa N., Furukawa F., Murata S., Eguchi K., Ida H., Yoshiura K.
Proc. Natl. Acad. Sci. U.S.A. 108:14914-14919(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NKJO VAL-201, CHARACTERIZATION OF VARIANT NKJO VAL-201.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66401 Genomic DNA. Translation: CAA47026.1.
X62598 mRNA. Translation: CAA44482.1.
Z14982 Genomic DNA. Translation: CAA78705.1.
Z14982 Genomic DNA. Translation: CAA78706.1.
L11045 Genomic DNA. No translation available.
X87344 Genomic DNA. Translation: CAA60786.1.
X87344 Genomic DNA. Translation: CAA60787.1.
U17496 mRNA. Translation: AAA56777.1.
U17497 mRNA. Translation: AAA56778.1.
AL671681 Genomic DNA. Translation: CAI17712.1.
AL671681 Genomic DNA. Translation: CAI17713.1.
AL669918 Genomic DNA. Translation: CAI18138.1.
AL669918 Genomic DNA. Translation: CAI18139.1.
AL935043 Genomic DNA. Translation: CAI18623.1.
AL935043 Genomic DNA. Translation: CAI18625.1.
BX682530, BX088556 Genomic DNA. Translation: CAM25945.1.
BX682530, BX088556 Genomic DNA. Translation: CAM25947.1.
BX088556, BX682530 Genomic DNA. Translation: CAM26261.1.
BX088556, BX682530 Genomic DNA. Translation: CAM26262.1.
CT009502 Genomic DNA. Translation: CAQ07779.1.
CT009502 Genomic DNA. Translation: CAQ07781.1.
BX927138 Genomic DNA. Translation: CAQ08445.1.
BX927138 Genomic DNA. Translation: CAQ08448.1.
CR762476 Genomic DNA. Translation: CAQ08492.1.
CR762476 Genomic DNA. Translation: CAQ08494.1.
CR753889 Genomic DNA. Translation: CAQ10284.1.
CR753889 Genomic DNA. Translation: CAQ10286.1.
CH471081 Genomic DNA. Translation: EAX03644.1.
CH471081 Genomic DNA. Translation: EAX03645.1.
BC001114 mRNA. Translation: AAH01114.1.
U32863 Genomic DNA. Translation: AAA80235.1.
U32862 Genomic DNA. Translation: AAA80234.1.
CCDSCCDS4756.1. [P28062-2]
CCDS4757.1. [P28062-1]
PIRA44324.
C44324.
G01564.
G02018.
RefSeqNP_004150.1. NM_004159.4. [P28062-2]
NP_683720.2. NM_148919.3. [P28062-1]
UniGeneHs.180062.

3D structure databases

ProteinModelPortalP28062.
SMRP28062. Positions 73-273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111669. 43 interactions.
IntActP28062. 8 interactions.
MINTMINT-3010850.
STRING9606.ENSP00000402406.

Chemistry

BindingDBP28062.
ChEMBLCHEMBL5620.

Protein family/group databases

MEROPST01.015.

PTM databases

PhosphoSiteP28062.

Polymorphism databases

DMDM334302881.

Proteomic databases

MaxQBP28062.
PaxDbP28062.
PRIDEP28062.

Protocols and materials databases

DNASU5696.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374881; ENSP00000364015; ENSG00000204264. [P28062-2]
ENST00000374882; ENSP00000364016; ENSG00000204264. [P28062-1]
ENST00000383236; ENSP00000372723; ENSG00000206298. [P28062-1]
ENST00000383238; ENSP00000372725; ENSG00000206298. [P28062-2]
ENST00000416134; ENSP00000397057; ENSG00000235715. [P28062-2]
ENST00000416564; ENSP00000408825; ENSG00000226201. [P28062-2]
ENST00000421445; ENSP00000402406; ENSG00000236443. [P28062-1]
ENST00000429645; ENSP00000394155; ENSG00000226201. [P28062-1]
ENST00000435978; ENSP00000414731; ENSG00000231631. [P28062-2]
ENST00000436627; ENSP00000392693; ENSG00000230669. [P28062-2]
ENST00000438442; ENSP00000404585; ENSG00000231631. [P28062-1]
ENST00000441960; ENSP00000407539; ENSG00000230034. [P28062-2]
ENST00000452573; ENSP00000412618; ENSG00000236443. [P28062-2]
ENST00000455660; ENSP00000406797; ENSG00000230669. [P28062-1]
ENST00000457261; ENSP00000414770; ENSG00000235715. [P28062-1]
ENST00000546794; ENSP00000448520; ENSG00000230034. [P28062-1]
GeneID5696.
KEGGhsa:5696.
UCSCuc003oce.3. human. [P28062-1]
uc003ocf.3. human. [P28062-2]

Organism-specific databases

CTD5696.
GeneCardsGC06M032808.
GC06Mi32792.
GC06Mj32730.
GC06Mk32786.
GC06Ml32962.
GC06Mm32841.
GC06Mn32737.
GC06Mo32898.
HGNCHGNC:9545. PSMB8.
HPAHPA046995.
HPA050327.
MIM177046. gene.
256040. phenotype.
neXtProtNX_P28062.
Orphanet325004. CANDLE syndrome.
324999. JMP syndrome.
2615. Nakajo-Nishimura syndrome.
PharmGKBPA33890.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091082.
HOVERGENHBG108297.
InParanoidP28062.
KOK02740.
OMASDLMHQY.
PhylomeDBP28062.
TreeFamTF106223.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_13505. Proteasome mediated degradation of PAK-2p34.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.
REACT_578. Apoptosis.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP28062.
BgeeP28062.
CleanExHS_PSMB8.
GenevestigatorP28062.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. 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

ChiTaRSPSMB8. human.
GeneWikiPSMB8.
GenomeRNAi5696.
NextBio22126.
PROP28062.
SOURCESearch...

Entry information

Entry namePSB8_HUMAN
AccessionPrimary (citable) accession number: P28062
Secondary accession number(s): B0UZC0 expand/collapse secondary AC list , Q29824, Q5JNW6, Q5QNR8, Q96J48
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: May 31, 2011
Last modified: July 9, 2014
This is version 170 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM