P28062 (PSB8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	276 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.24 Ref.28
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. This subunit is part of the immunoproteasome where it displaces the equivalent housekeeping subunit PSMB5. 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.24 Ref.25 Ref.26
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	Defects in PSMB8 are the cause of Nakajo syndrome (NKJO) [MIM:256040]; also called joint contractures muscular atrophy microcytic anemia and panniculitis-induced lipodystrophy. An autosomal recessive autoinflammatory disorder characterized by childhood onset of recurrent fever, joint stiffness and severe contractures of the hands and feet, erythematous skin lesions with subsequent development of lipodystrophy, and laboratory evidence of immune dysregulation. Accompanying features include muscle weakness and atrophy, hepatosplenomegaly, and microcytic anemia. Ref.28 Ref.29 Ref.30 Ref.31 Note=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.30).
Sequence similarities	Belongs to the peptidase T1B family.

Ontologies

Keywords
Biological process	Differentiation Host-virus interaction Immunity
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Molecular function	Hydrolase Protease Threonine protease
PTM	Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA 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 M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle 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 peptide antigen via MHC class I Traceable author statement. Source: Reactome apoptotic process Traceable author statement. Source: Reactome fat cell differentiation Inferred from mutant phenotype Ref.28. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW mRNA metabolic 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 type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome proteasome core complex Inferred from electronic annotation. Source: InterPro
Molecular function	threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 72	72	Removed in mature form By similarity		PRO_0000026597
	Chain	73 – 276	204	Proteasome subunit beta type-8		PRO_0000026598
Sites
	Active site	73	1	Nucleophile By similarity
	Site	72 – 73	2	Cleavage; by autocatalysis By similarity
Natural variations
	Alternative sequence	1 – 49	49	MALLD…PRGMQ → MLIGTPTPRDTTPSSWLTSS LLVEAAPLDDTTLPTPVSSG CPGLE in isoform 2.		VSP_005287
	Natural variant	8	1	G → R in LMP7C.		VAR_006488
	Natural variant	30 – 32	3	PGH → RPD in LPM7C.		VAR_006489
	Natural variant	49	1	Q → K. Ref.7 Corresponds to variant rs2071543 [ dbSNP | Ensembl ].		VAR_065204
	Natural variant	74	1	T → S. Corresponds to variant rs17220206 [ dbSNP | Ensembl ].		VAR_057046
	Natural variant	75	1	T → 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.29 Ref.30		VAR_065291
	Natural variant	201	1	G → V in NKJO; affects immunoproteasome assembly; reduced proteasome levels; reduced chymotrypsin-like activity consistent with a decrease in proteasomal activity. Ref.28 Ref.31		VAR_066449

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (LMP7B) (LMP7-E2) [UniParc]. Last modified May 31, 2011. Version 3. Checksum: 4F689501677DBD44	FASTA	276	30,354
	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
	Isoform 2 (LMP7A) (LMP7-E1) [UniParc]. Checksum: E5A903101BE5C0B7	FASTA	272	29,770
	10 20 30 40 50 60 MLIGTPTPRD TTPSSWLTSS LLVEAAPLDD TTLPTPVSSG CPGLEPTEFF QSLGGDGERN 70 80 90 100 110 120 VQIEMAHGTT TLAFKFQHGV IAAVDSRASA GSYISALRVN KVIEINPYLL GTMSGCAADC 130 140 150 160 170 180 QYWERLLAKE CRLYYLRNGE RISVSAASKL LSNMMCQYRG MGLSMGSMIC GWDKKGPGLY 190 200 210 220 230 240 YVDEHGTRLS GNMFSTGSGN TYAYGVMDSG YRPNLSPEEA YDLGRRAIAY ATHRDSYSGG 250 260 270 VVNMYHMKED GWVKVESTDV SDLLHQYREA NQ

References

	« Hide 'large scale' referencesShow '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: 8458375] [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: 1453454] [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: 1922342] [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: 1429565] [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: 8344725] [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: 8568858] [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. , 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: 14574404] [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. , 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: 15489334] [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: 9157092] [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: 8163024] [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: 8663318] [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: 11493458] [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: 11717192] [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: 14550573] [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: 15501285] [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: 15907481] [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: 15488952] [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: 15944226] [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: 16423992] [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: 17142736] [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: 17262812] [Abstract] Cited for: INDUCTION.
[24]	"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: 19443843] [Abstract] Cited for: INDUCTION BY IFNG, FUNCTION.
[25]	"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: 19619915] [Abstract] Cited for: INDUCTION.
[26]	"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: 19525961] [Abstract] Cited for: INDUCTION BY PR-957.
[27]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]	"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: 21881205] [Abstract] Cited for: FUNCTION IN ADIPOCYTE DIFFERENTIATION, VARIANT NKJO VAL-201, CHARACTERIZATION OF VARIANT NKJO VAL-201.
[29]	"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: 21129723] [Abstract] Cited for: VARIANT NKJO MET-75, CHARACTERIZATION OF VARIANT NKJO MET-75.
[30]	"Mutations in PSMB8 cause CANDLE syndrome 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. 0:0-0(2011) [PubMed: 21953331] [Abstract] Cited for: INVOLVEMENT OF VARIANT NKJO MET-75 IN CANDLE SYNDROME.
[31]	"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. , 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: 21852578] [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.
IPI	IPI00000783. IPI00215824.
PIR	A44324. C44324. G01564. G02018.
RefSeq	NP_004150.1. NM_004159.4. NP_683720.2. NM_148919.3.
UniGene	Hs.180062.
3D structure databases
ProteinModelPortal	P28062.
SMR	P28062. Positions 50-272.
ModBase	Search...
Protein-protein interaction databases
IntAct	P28062. 7 interactions.
STRING	P28062.
Protein family/group databases
MEROPS	T01.015.
PTM databases
PhosphoSite	P28062.
Polymorphism databases
DMDM	1172602.
Proteomic databases
PRIDE	P28062.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000446762; ENSP00000406878; ENSG00000230034.
GeneID	5696.
KEGG	hsa:5696.
Organism-specific databases
CTD	5696.
GeneCards	GC06M032808.
HGNC	HGNC:9545. PSMB8.
MIM	177046. gene. 256040. phenotype.
neXtProt	NX_P28062.
Orphanet	254356. Joint contractures - muscle atrophy - microcytic anemia -panniculitis-induced lipodystrophy.
PharmGKB	PA33890.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16993.
HOVERGEN	HBG108297.
InParanoid	P28062.
OMA	DLMHQYR.
OrthoDB	EOG4WM4V9.
PhylomeDB	P28062.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_13505. Proteasome mediated degradation of PAK-2p34. REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_383. DNA Replication. REACT_578. Apoptosis. REACT_6185. HIV Infection. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_6900. Immune System.
Gene expression databases
CleanEx	HS_PSMB8.
Genevestigator	P28062.
GermOnline	ENSG00000204264. Homo sapiens.
Family and domain databases
InterPro	IPR000243. Pept_T1A_subB. IPR016050. Proteasome_bsu_CS. IPR001353. Proteasome_sua/b. IPR023333. Proteasome_suB-type. [Graphical view]
KO	K02740.
Pfam	PF00227. Proteasome. 1 hit. [Graphical view]
PRINTS	PR00141. PROTEASOME.
PROSITE	PS00854. PROTEASOME_B_1. 1 hit. PS51476. PROTEASOME_B_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	22126.
SOURCE	Search...

Entry information

Entry name

PSB8_HUMAN

Accession

Primary (citable) accession number: P28062
Secondary accession number(s): B0UZC0 , Q29824, Q5JNW6, Q5QNR8, Q96J48

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	May 31, 2011
Last modified:	January 25, 2012
This is version 142 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.