PSB9_HUMAN
ID PSB9_HUMAN Reviewed; 219 AA.
AC P28065; B0V0T1; Q16523; Q5JNW4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=Proteasome subunit beta type-9;
DE EC=3.4.25.1;
DE AltName: Full=Low molecular mass protein 2;
DE AltName: Full=Macropain chain 7;
DE AltName: Full=Multicatalytic endopeptidase complex chain 7;
DE AltName: Full=Proteasome chain 7;
DE AltName: Full=Proteasome subunit beta-1i;
DE AltName: Full=Really interesting new gene 12 protein;
DE Flags: Precursor;
GN Name=PSMB9; Synonyms=LMP2, PSMB6i, RING12;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8458375; DOI=10.1002/eji.1830230414;
RA Glynne R., Kerr L.A., Mockridge I., Beck S., Kelly A., Trowsdale J.;
RT "The major histocompatibility complex-encoded proteasome component LMP7:
RT alternative first exons and post-translational processing.";
RL Eur. J. Immunol. 23:860-866(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1453454; DOI=10.1016/0022-2836(92)90832-5;
RA Beck S., Kelly A., Radley E., Khurshid F., Alderton R.P., Trowsdale J.;
RT "DNA sequence analysis of 66 kb of the human MHC class II region encoding a
RT cluster of genes for antigen processing.";
RL J. Mol. Biol. 228:433-441(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LMP2.L), AND VARIANT HIS-60.
RX PubMed=1922385; DOI=10.1038/353667a0;
RA Kelly A., Powis S.H., Glynne R., Radley E., Beck S., Trowsdale J.;
RT "Second proteasome-related gene in the human MHC class II region.";
RL Nature 353:667-668(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1429565; DOI=10.1016/s0021-9258(18)41645-6;
RA Fruh K., Yang Y., Arnold D., Chambers J., Wu L., Waters J.B., Spies T.,
RA Peterson P.A.;
RT "Alternative exon usage and processing of the major histocompatibility
RT complex-encoded proteasome subunits.";
RL J. Biol. Chem. 267:22131-22140(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8568858; DOI=10.1006/jmbi.1996.0001;
RA Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., Hosking L.K.,
RA Jackson A., Kelly A., Newell W.R., Sanseau P., Radley E., Thorpe K.L.,
RA Trowsdale J.;
RT "Evolutionary dynamics of non-coding sequences within the class II region
RT of the human MHC.";
RL J. Mol. Biol. 255:1-13(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS LMP2.S AND LMP2.L).
RX PubMed=7829535; DOI=10.1074/jbc.270.4.1966;
RA Singal D.P., Ye M., Quadri S.A.;
RT "Major histocompatibility-encoded human proteasome LMP2. Genomic
RT organization and a new form of mRNA.";
RL J. Biol. Chem. 270:1966-1970(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LMP2.L).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LMP2.L).
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP FUNCTION.
RX PubMed=8163024; DOI=10.1016/0014-5793(94)80612-8;
RA Akiyama K., Kagawa S., Tamura T., Shimbara N., Takashina M., Kristensen P.,
RA Hendil K.B., Tanaka K., Ichihara A.;
RT "Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced by
RT interferon-gamma for acquirement of the functional diversity responsible
RT for antigen processing.";
RL FEBS Lett. 343:85-88(1994).
RN [12]
RP MUTAGENESIS OF GLY-20; THR-21 AND LYS-53, AND SELF ACTIVATION OF
RP BETA-SUBUNITS MODEL.
RX PubMed=9003765; DOI=10.1002/j.1460-2075.1996.tb01081.x;
RA Schmidtke G., Kraft R., Kostka S., Henklein P., Froemmel C., Loewe J.,
RA Huber R., Kloetzel P.-M., Schmidt M.;
RT "Analysis of mammalian 20S proteasome biogenesis: the maturation of beta-
RT subunits is an ordered two-step mechanism involving autocatalysis.";
RL EMBO J. 15:6887-6898(1996).
RN [13]
RP INDUCTION.
RX PubMed=8663318; DOI=10.1074/jbc.271.29.17275;
RA Gaczynska M., Goldberg A.L., Tanaka K., Hendil K.B., Rock K.L.;
RT "Proteasome subunits X and Y alter peptidase activities in opposite ways to
RT the interferon-gamma-induced subunits LMP2 and LMP7.";
RL J. Biol. Chem. 271:17275-17280(1996).
RN [14]
RP INDUCTION BY TNF AND IFNG.
RX PubMed=11493458; DOI=10.1182/blood.v98.4.1108;
RA Hallermalm K., Seki K., Wei C., Castelli C., Rivoltini L., Kiessling R.,
RA Levitskaya J.;
RT "Tumor necrosis factor-alpha induces coordinated changes in major
RT histocompatibility class I presentation pathway, resulting in increased
RT stability of class I complexes at the cell surface.";
RL Blood 98:1108-1115(2001).
RN [15]
RP DEVELOPMENTAL STAGE.
RX PubMed=11717192; DOI=10.1093/intimm/13.12.1515;
RA Li J., Schuler-Thurner B., Schuler G., Huber C., Seliger B.;
RT "Bipartite regulation of different components of the MHC class I antigen-
RT processing machinery during dendritic cell maturation.";
RL Int. Immunol. 13:1515-1523(2001).
RN [16]
RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
RX PubMed=14550573; DOI=10.1016/s0014-5793(03)01025-1;
RA Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
RA Mayer R.J., Krueger E.;
RT "Human immunodeficiency virus-1 Tat protein interacts with distinct
RT proteasomal alpha and beta subunits.";
RL FEBS Lett. 553:200-204(2003).
RN [17]
RP INDUCTION BY TETRODOTOXIN.
RX PubMed=15501285; DOI=10.1016/j.toxicon.2004.07.018;
RA Raghavendra Prasad H.S., Qi Z., Srinivasan K.N., Gopalakrishnakone P.;
RT "Potential effects of tetrodotoxin exposure to human glial cells postulated
RT using microarray approach.";
RL Toxicon 44:597-608(2004).
RN [18]
RP INDUCTION BY IFNG AND IRF1.
RX PubMed=15907481; DOI=10.1016/j.febslet.2005.04.012;
RA Namiki S., Nakamura T., Oshima S., Yamazaki M., Sekine Y., Tsuchiya K.,
RA Okamoto R., Kanai T., Watanabe M.;
RT "IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted expression
RT of immunosubunits of the proteasome.";
RL FEBS Lett. 579:2781-2787(2005).
RN [19]
RP INTERACTION WITH NCOA1; NCOA2 AND NCOA3.
RX PubMed=16957778; DOI=10.1038/sj.emboj.7601306;
RA Zhang H., Sun L., Liang J., Yu W., Zhang Y., Wang Y., Chen Y., Li R.,
RA Sun X., Shang Y.;
RT "The catalytic subunit of the proteasome is engaged in the entire process
RT of estrogen receptor-regulated transcription.";
RL EMBO J. 25:4223-4233(2006).
RN [20]
RP INDUCTION BY HEAT SHOCK.
RX PubMed=17142736; DOI=10.4049/jimmunol.177.12.8393;
RA Callahan M.K., Wohlfert E.A., Menoret A., Srivastava P.K.;
RT "Heat shock up-regulates lmp2 and lmp7 and enhances presentation of
RT immunoproteasome-dependent epitopes.";
RL J. Immunol. 177:8393-8399(2006).
RN [21]
RP INDUCTION.
RX PubMed=17262812; DOI=10.1002/ibd.20110;
RA Wu F., Dassopoulos T., Cope L., Maitra A., Brant S.R., Harris M.L.,
RA Bayless T.M., Parmigiani G., Chakravarti S.;
RT "Genome-wide gene expression differences in Crohn's disease and ulcerative
RT colitis from endoscopic pinch biopsies: insights into distinctive
RT pathogenesis.";
RL Inflamm. Bowel Dis. 13:807-821(2007).
RN [22]
RP INDUCTION BY CD40L.
RX PubMed=18694960; DOI=10.1128/mcb.00611-08;
RA Moschonas A., Kouraki M., Knox P.G., Thymiakou E., Kardassis D.,
RA Eliopoulos A.G.;
RT "CD40 induces antigen transporter and immunoproteasome gene expression in
RT carcinomas via the coordinated action of NF-kappaB and of NF-kappaB-
RT mediated de novo synthesis of IRF-1.";
RL Mol. Cell. Biol. 28:6208-6222(2008).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53 AND LYS-109, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [25]
RP VARIANT HIS-60.
RX PubMed=10924276; DOI=10.1006/mgme.2000.3007;
RA Chistyakov D.A., Savost'anov K.V., Turakulov R.I., Petunina N.A.,
RA Trukhina L.V., Kudinova A.V., Balabolkin M.I., Nosikov V.V.;
RT "Complex association analysis of Graves disease using a set of polymorphic
RT markers.";
RL Mol. Genet. Metab. 70:214-218(2000).
RN [26]
RP VARIANT PRAAS3 ASP-165, AND CHARACTERIZATION OF VARIANT PRAAS3 ASP-165.
RX PubMed=26524591; DOI=10.1172/jci81260;
RA Brehm A., Liu Y., Sheikh A., Marrero B., Omoyinmi E., Zhou Q.,
RA Montealegre G., Biancotto A., Reinhardt A., Almeida de Jesus A.,
RA Pelletier M., Tsai W.L., Remmers E.F., Kardava L., Hill S., Kim H.,
RA Lachmann H.J., Megarbane A., Chae J.J., Brady J., Castillo R.D., Brown D.,
RA Casano A.V., Gao L., Chapelle D., Huang Y., Stone D., Chen Y., Sotzny F.,
RA Lee C.C., Kastner D.L., Torrelo A., Zlotogorski A., Moir S., Gadina M.,
RA McCoy P., Wesley R., Rother K., Hildebrand P.W., Brogan P., Krueger E.,
RA Aksentijevich I., Goldbach-Mansky R.;
RT "Additive loss-of-function proteasome subunit mutations in CANDLE/PRAAS
RT patients promote type I IFN production.";
RL J. Clin. Invest. 125:4196-4211(2015).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity. This
CC subunit is involved in antigen processing to generate class I binding
CC peptides. Replacement of PSMB6 by PSMB9 increases the capacity of the
CC immunoproteasome to cleave model peptides after hydrophobic and basic
CC residues. {ECO:0000269|PubMed:8163024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1;
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel. Component of the immunoproteasome, where it displaces
CC the equivalent housekeeping subunit PSMB6. Component of the
CC spermatoproteasome, a form of the proteasome specifically found in
CC testis. {ECO:0000269|PubMed:16957778}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 TAT protein.
CC {ECO:0000269|PubMed:14550573}.
CC -!- INTERACTION:
CC P28065; Q24JT5: CRYGA; NbExp=3; IntAct=EBI-603300, EBI-10239205;
CC P28065; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-603300, EBI-742054;
CC P28065; Q9Y3R0: GRIP1; NbExp=3; IntAct=EBI-603300, EBI-5349621;
CC P28065; Q14657: LAGE3; NbExp=4; IntAct=EBI-603300, EBI-1052105;
CC P28065; Q15788: NCOA1; NbExp=3; IntAct=EBI-603300, EBI-455189;
CC P28065; Q9Y6Q9: NCOA3; NbExp=3; IntAct=EBI-603300, EBI-81196;
CC P28065; Q9Y244: POMP; NbExp=3; IntAct=EBI-603300, EBI-696895;
CC P28065; Q99436: PSMB7; NbExp=7; IntAct=EBI-603300, EBI-603319;
CC P28065; PRO_0000037548 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-603300, EBI-6863741;
CC P28065; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-603300, EBI-6863748;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=LMP2.L;
CC IsoId=P28065-1; Sequence=Displayed;
CC Name=LMP2.S;
CC IsoId=P28065-2; Sequence=VSP_005288;
CC -!- DEVELOPMENTAL STAGE: Highly expressed in immature dendritic cells (at
CC protein level). {ECO:0000269|PubMed:11717192}.
CC -!- INDUCTION: Up-regulated by interferon gamma (at protein level). Up-
CC regulated by IRF1. Up-regulated by tumor necrosis factor-alpha (at
CC protein level). Up-regulated by tetrodotoxin (TTX) in glial cells. Up-
CC regulated in Crohn's bowel disease (CD). Up-regulated by heat shock
CC treatment. Up-regulated by CD40L via the NFKB1 pathway in cancer cells.
CC {ECO:0000269|PubMed:11493458, ECO:0000269|PubMed:15501285,
CC ECO:0000269|PubMed:15907481, ECO:0000269|PubMed:17142736,
CC ECO:0000269|PubMed:17262812, ECO:0000269|PubMed:18694960,
CC ECO:0000269|PubMed:8663318}.
CC -!- PTM: Autocleaved. The resulting N-terminal Thr residue of the mature
CC subunit is responsible for the nucleophile proteolytic activity.
CC {ECO:0000250|UniProtKB:O35955}.
CC -!- DISEASE: Proteasome-associated autoinflammatory syndrome 3 (PRAAS3)
CC [MIM:617591]: An autoinflammatory disorder characterized by onset in
CC early infancy and recurrent fever, nodular dermatitis, myositis,
CC panniculitis-induced lipodystrophy, lymphadenopathy, and immune
CC dysregulation. Variable accompanying features may include joint
CC contractures, hepatosplenomegaly, anemia, thrombocytopenia, recurrent
CC infections, autoantibodies, and hypergammaglobulinemia. Some patients
CC may have intracranial calcifications. PRAAS3 inheritance is autosomal
CC recessive or digenic. {ECO:0000269|PubMed:26524591}. Note=The disease
CC may be caused by variants affecting distinct genetic loci, including
CC the gene represented in this entry.
CC -!- MISCELLANEOUS: Encoded in the MHC class II region.
CC -!- MISCELLANEOUS: A model for self-activation in which residue Thr-21
CC serves as nucleophile and Lys-53 as proton donor/acceptor has been
CC proposed. Subunit processing of mammalian beta-subunits proceeds via a
CC novel ordered two-step mechanism involving autocatalysis.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X66401; CAA47024.1; -; Genomic_DNA.
DR EMBL; X62741; CAA44603.1; -; mRNA.
DR EMBL; Z14977; CAA78700.1; -; Genomic_DNA.
DR EMBL; X87344; CAA60784.1; -; Genomic_DNA.
DR EMBL; U01025; AAC50154.1; -; mRNA.
DR EMBL; S75169; AAC60646.1; -; mRNA.
DR EMBL; CR541656; CAG46457.1; -; mRNA.
DR EMBL; AL669918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL935043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX088556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR762476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR933844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03654.1; -; Genomic_DNA.
DR EMBL; BC065513; AAH65513.1; -; mRNA.
DR CCDS; CCDS4759.1; -. [P28065-1]
DR PIR; A55632; A55632.
DR PIR; S27332; S27332.
DR RefSeq; NP_002791.1; NM_002800.4. [P28065-1]
DR PDB; 6AVO; EM; 3.80 A; A/F=21-219.
DR PDB; 6E5B; X-ray; 2.77 A; N/b=1-219.
DR PDB; 7AWE; X-ray; 2.29 A; H/V=21-219.
DR PDB; 7B12; X-ray; 2.43 A; H/V=21-219.
DR PDBsum; 6AVO; -.
DR PDBsum; 6E5B; -.
DR PDBsum; 7AWE; -.
DR PDBsum; 7B12; -.
DR AlphaFoldDB; P28065; -.
DR SMR; P28065; -.
DR BioGRID; 111671; 95.
DR IntAct; P28065; 67.
DR MINT; P28065; -.
DR STRING; 9606.ENSP00000363993; -.
DR BindingDB; P28065; -.
DR ChEMBL; CHEMBL1944495; -.
DR DrugBank; DB08889; Carfilzomib.
DR GuidetoPHARMACOLOGY; 2409; -.
DR MEROPS; T01.013; -.
DR iPTMnet; P28065; -.
DR PhosphoSitePlus; P28065; -.
DR BioMuta; PSMB9; -.
DR DMDM; 417529; -.
DR OGP; P28065; -.
DR EPD; P28065; -.
DR jPOST; P28065; -.
DR MassIVE; P28065; -.
DR MaxQB; P28065; -.
DR PaxDb; P28065; -.
DR PeptideAtlas; P28065; -.
DR PRIDE; P28065; -.
DR ProteomicsDB; 54439; -. [P28065-1]
DR ProteomicsDB; 54440; -. [P28065-2]
DR Antibodypedia; 28726; 450 antibodies from 38 providers.
DR DNASU; 5698; -.
DR Ensembl; ENST00000374859.3; ENSP00000363993.2; ENSG00000240065.8. [P28065-1]
DR Ensembl; ENST00000383114.8; ENSP00000372595.4; ENSG00000240118.7. [P28065-1]
DR Ensembl; ENST00000383234.8; ENSP00000372721.4; ENSG00000243594.7. [P28065-1]
DR Ensembl; ENST00000422729.6; ENSP00000407233.2; ENSG00000243067.7. [P28065-1]
DR Ensembl; ENST00000427870.6; ENSP00000412027.2; ENSG00000242711.8.
DR Ensembl; ENST00000434471.6; ENSP00000393744.2; ENSG00000243958.7.
DR Ensembl; ENST00000444284.6; ENSP00000396813.2; ENSG00000239836.7. [P28065-1]
DR Ensembl; ENST00000453059.6; ENSP00000407810.2; ENSG00000240508.7.
DR GeneID; 5698; -.
DR KEGG; hsa:5698; -.
DR MANE-Select; ENST00000374859.3; ENSP00000363993.2; NM_002800.5; NP_002791.1.
DR UCSC; uc003sga.4; human. [P28065-1]
DR CTD; 5698; -.
DR DisGeNET; 5698; -.
DR GeneCards; PSMB9; -.
DR HGNC; HGNC:9546; PSMB9.
DR HPA; ENSG00000240065; Tissue enhanced (lymphoid).
DR MalaCards; PSMB9; -.
DR MIM; 177045; gene.
DR MIM; 617591; phenotype.
DR neXtProt; NX_P28065; -.
DR NIAGADS; ENSG00000240065; -.
DR OpenTargets; ENSG00000240065; -.
DR PharmGKB; PA33891; -.
DR VEuPathDB; HostDB:ENSG00000240065; -.
DR eggNOG; KOG0174; Eukaryota.
DR GeneTree; ENSGT00940000159897; -.
DR InParanoid; P28065; -.
DR OMA; LPWAGEV; -.
DR PhylomeDB; P28065; -.
DR TreeFam; TF106221; -.
DR PathwayCommons; P28065; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P28065; -.
DR SIGNOR; P28065; -.
DR BioGRID-ORCS; 5698; 16 hits in 1090 CRISPR screens.
DR GeneWiki; PSMB9; -.
DR GenomeRNAi; 5698; -.
DR Pharos; P28065; Tchem.
DR PRO; PR:P28065; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P28065; protein.
DR Bgee; ENSG00000240065; Expressed in granulocyte and 97 other tissues.
DR ExpressionAtlas; P28065; baseline and differential.
DR Genevisible; P28065; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000502; C:proteasome complex; TAS:ProtInc.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:2000116; P:regulation of cysteine-type endopeptidase activity; IMP:UniProtKB.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR034383; Proteasome_beta9.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF50; PTHR11599:SF50; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Host-virus interaction; Hydrolase; Immunity; Nucleus; Protease; Proteasome;
KW Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..20
FT /note="Removed in mature form"
FT /id="PRO_0000026619"
FT CHAIN 21..219
FT /note="Proteasome subunit beta type-9"
FT /id="PRO_0000026620"
FT ACT_SITE 21
FT /note="Nucleophile"
FT SITE 20..21
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O35955"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 4..13
FT /note="Missing (in isoform LMP2.S)"
FT /evidence="ECO:0000303|PubMed:7829535"
FT /id="VSP_005288"
FT VARIANT 9
FT /note="G -> E (in dbSNP:rs35100697)"
FT /id="VAR_051551"
FT VARIANT 32
FT /note="V -> I (in dbSNP:rs241419)"
FT /id="VAR_051552"
FT VARIANT 60
FT /note="R -> H (in dbSNP:rs17587)"
FT /evidence="ECO:0000269|PubMed:10924276,
FT ECO:0000269|PubMed:1922385"
FT /id="VAR_013578"
FT VARIANT 165
FT /note="G -> D (in PRAAS3; digenic inheritance; patient also
FT carries a mutation in PSMB4; patients' cells show reduction
FT of proteasome content and cysteine-type endopeptidase
FT activity of the proteasome; dbSNP:rs369359789)"
FT /evidence="ECO:0000269|PubMed:26524591"
FT /id="VAR_075258"
FT VARIANT 173
FT /note="R -> C (in dbSNP:rs17213861)"
FT /id="VAR_051553"
FT MUTAGEN 20
FT /note="G->A: Impairs correct processing at the consensus
FT site."
FT /evidence="ECO:0000269|PubMed:9003765"
FT MUTAGEN 21
FT /note="T->A: Impairs correct processing at the consensus
FT site."
FT /evidence="ECO:0000269|PubMed:9003765"
FT MUTAGEN 53
FT /note="K->A: Impairs correct processing at the consensus
FT site."
FT /evidence="ECO:0000269|PubMed:9003765"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:7AWE"
FT HELIX 69..89
FT /evidence="ECO:0007829|PDB:7AWE"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:7AWE"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:7AWE"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:7AWE"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:7AWE"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:7AWE"
FT HELIX 155..161
FT /evidence="ECO:0007829|PDB:7AWE"
FT HELIX 168..185
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6E5B"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:7AWE"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:7B12"
SQ SEQUENCE 219 AA; 23264 MW; 3B321F83641941AC CRC64;
MLRAGAPTGD LPRAGEVHTG TTIMAVEFDG GVVMGSDSRV SAGEAVVNRV FDKLSPLHER
IYCALSGSAA DAQAVADMAA YQLELHGIEL EEPPLVLAAA NVVRNISYKY REDLSAHLMV
AGWDQREGGQ VYGTLGGMLT RQPFAIGGSG STFIYGYVDA AYKPGMSPEE CRRFTTDAIA
LAMSRDGSSG GVIYLVTITA AGVDHRVILG NELPKFYDE
