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Proteasome subunit beta type-9 (EC 3.4.25.1) (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)

 PSB9_HUMAN              Reviewed;         219 AA.
P28065; B0V0T1; Q16523; Q5JNW4;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 2.
27-SEP-2017, entry version 197.
RecName: Full=Proteasome subunit beta type-9;
EC=3.4.25.1;
AltName: Full=Low molecular mass protein 2;
AltName: Full=Macropain chain 7;
AltName: Full=Multicatalytic endopeptidase complex chain 7;
AltName: Full=Proteasome chain 7;
AltName: Full=Proteasome subunit beta-1i;
AltName: Full=Really interesting new gene 12 protein;
Flags: Precursor;
Name=PSMB9; Synonyms=LMP2, PSMB6i, RING12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8458375; DOI=10.1002/eji.1830230414;
Glynne R., Kerr L.A., Mockridge I., Beck S., Kelly A., Trowsdale J.;
"The major histocompatibility complex-encoded proteasome component
LMP7: alternative first exons and post-translational processing.";
Eur. J. Immunol. 23:860-866(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1453454; DOI=10.1016/0022-2836(92)90832-5;
Beck S., Kelly A., Radley E., Khurshid F., Alderton R.P.,
Trowsdale J.;
"DNA sequence analysis of 66 kb of the human MHC class II region
encoding a cluster of genes for antigen processing.";
J. Mol. Biol. 228:433-441(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LMP2.L), AND VARIANT HIS-60.
PubMed=1922385; DOI=10.1038/353667a0;
Kelly A., Powis S.H., Glynne R., Radley E., Beck S., Trowsdale J.;
"Second proteasome-related gene in the human MHC class II region.";
Nature 353:667-668(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1429565;
Fruh K., Yang Y., Arnold D., Chambers J., Wu L., Waters J.B.,
Spies T., Peterson P.A.;
"Alternative exon usage and processing of the major histocompatibility
complex-encoded proteasome subunits.";
J. Biol. Chem. 267:22131-22140(1992).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8568858; DOI=10.1006/jmbi.1996.0001;
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.;
"Evolutionary dynamics of non-coding sequences within the class II
region of the human MHC.";
J. Mol. Biol. 255:1-13(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS LMP2.S AND LMP2.L).
PubMed=7829535; DOI=10.1074/jbc.270.4.1966;
Singal D.P., Ye M., Quadri S.A.;
"Major histocompatibility-encoded human proteasome LMP2. Genomic
organization and a new form of mRNA.";
J. Biol. Chem. 270:1966-1970(1995).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LMP2.L).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LMP2.L).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
FUNCTION.
PubMed=8163024; DOI=10.1016/0014-5793(94)80612-8;
Akiyama K., Kagawa S., Tamura T., Shimbara N., Takashina M.,
Kristensen P., Hendil K.B., Tanaka K., Ichihara A.;
"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.";
FEBS Lett. 343:85-88(1994).
[12]
MUTAGENESIS OF GLY-20; THR-21 AND LYS-53, AND SELF ACTIVATION OF
BETA-SUBUNITS MODEL.
PubMed=9003765;
Schmidtke G., Kraft R., Kostka S., Henklein P., Froemmel C., Loewe J.,
Huber R., Kloetzel P.-M., Schmidt M.;
"Analysis of mammalian 20S proteasome biogenesis: the maturation of
beta-subunits is an ordered two-step mechanism involving
autocatalysis.";
EMBO J. 15:6887-6898(1996).
[13]
INDUCTION.
PubMed=8663318; DOI=10.1074/jbc.271.29.17275;
Gaczynska M., Goldberg A.L., Tanaka K., Hendil K.B., Rock K.L.;
"Proteasome subunits X and Y alter peptidase activities in opposite
ways to the interferon-gamma-induced subunits LMP2 and LMP7.";
J. Biol. Chem. 271:17275-17280(1996).
[14]
INDUCTION BY TNF AND IFNG.
PubMed=11493458; DOI=10.1182/blood.V98.4.1108;
Hallermalm K., Seki K., Wei C., Castelli C., Rivoltini L.,
Kiessling R., Levitskaya J.;
"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.";
Blood 98:1108-1115(2001).
[15]
DEVELOPMENTAL STAGE.
PubMed=11717192; DOI=10.1093/intimm/13.12.1515;
Li J., Schuler-Thurner B., Schuler G., Huber C., Seliger B.;
"Bipartite regulation of different components of the MHC class I
antigen-processing machinery during dendritic cell maturation.";
Int. Immunol. 13:1515-1523(2001).
[16]
INTERACTION WITH HIV-1 TAT.
PubMed=14550573; DOI=10.1016/S0014-5793(03)01025-1;
Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
Mayer R.J., Krueger E.;
"Human immunodeficiency virus-1 Tat protein interacts with distinct
proteasomal alpha and beta subunits.";
FEBS Lett. 553:200-204(2003).
[17]
INDUCTION BY TETRODOTOXIN.
PubMed=15501285; DOI=10.1016/j.toxicon.2004.07.018;
Raghavendra Prasad H.S., Qi Z., Srinivasan K.N., Gopalakrishnakone P.;
"Potential effects of tetrodotoxin exposure to human glial cells
postulated using microarray approach.";
Toxicon 44:597-608(2004).
[18]
INDUCTION BY IFNG AND IRF1.
PubMed=15907481; DOI=10.1016/j.febslet.2005.04.012;
Namiki S., Nakamura T., Oshima S., Yamazaki M., Sekine Y.,
Tsuchiya K., Okamoto R., Kanai T., Watanabe M.;
"IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted
expression of immunosubunits of the proteasome.";
FEBS Lett. 579:2781-2787(2005).
[19]
INTERACTION WITH NCOA1; NCOA2 AND NCOA3.
PubMed=16957778; DOI=10.1038/sj.emboj.7601306;
Zhang H., Sun L., Liang J., Yu W., Zhang Y., Wang Y., Chen Y., Li R.,
Sun X., Shang Y.;
"The catalytic subunit of the proteasome is engaged in the entire
process of estrogen receptor-regulated transcription.";
EMBO J. 25:4223-4233(2006).
[20]
INDUCTION BY HEAT SHOCK.
PubMed=17142736; DOI=10.4049/jimmunol.177.12.8393;
Callahan M.K., Wohlfert E.A., Menoret A., Srivastava P.K.;
"Heat shock up-regulates lmp2 and lmp7 and enhances presentation of
immunoproteasome-dependent epitopes.";
J. Immunol. 177:8393-8399(2006).
[21]
INDUCTION.
PubMed=17262812; DOI=10.1002/ibd.20110;
Wu F., Dassopoulos T., Cope L., Maitra A., Brant S.R., Harris M.L.,
Bayless T.M., Parmigiani G., Chakravarti S.;
"Genome-wide gene expression differences in Crohn's disease and
ulcerative colitis from endoscopic pinch biopsies: insights into
distinctive pathogenesis.";
Inflamm. Bowel Dis. 13:807-821(2007).
[22]
INDUCTION BY CD40L.
PubMed=18694960; DOI=10.1128/MCB.00611-08;
Moschonas A., Kouraki M., Knox P.G., Thymiakou E., Kardassis D.,
Eliopoulos A.G.;
"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.";
Mol. Cell. Biol. 28:6208-6222(2008).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53 AND LYS-109, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
VARIANT HIS-60.
PubMed=10924276; DOI=10.1006/mgme.2000.3007;
Chistyakov D.A., Savost'anov K.V., Turakulov R.I., Petunina N.A.,
Trukhina L.V., Kudinova A.V., Balabolkin M.I., Nosikov V.V.;
"Complex association analysis of Graves disease using a set of
polymorphic markers.";
Mol. Genet. Metab. 70:214-218(2000).
[26]
VARIANT ASP-165, AND CHARACTERIZATION OF VARIANT ASP-165.
PubMed=26524591; DOI=10.1172/JCI81260;
Brehm A., Liu Y., Sheikh A., Marrero B., Omoyinmi E., Zhou Q.,
Montealegre G., Biancotto A., Reinhardt A., Almeida de Jesus A.,
Pelletier M., Tsai W.L., Remmers E.F., Kardava L., Hill S., Kim H.,
Lachmann H.J., Megarbane A., Chae J.J., Brady J., Castillo R.D.,
Brown D., Casano A.V., Gao L., Chapelle D., Huang Y., Stone D.,
Chen Y., Sotzny F., Lee C.C., Kastner D.L., Torrelo A.,
Zlotogorski A., Moir S., Gadina M., McCoy P., Wesley R., Rother K.,
Hildebrand P.W., Brogan P., Krueger E., Aksentijevich I.,
Goldbach-Mansky R.;
"Additive loss-of-function proteasome subunit mutations in
CANDLE/PRAAS patients promote type I IFN production.";
J. Clin. Invest. 125:4196-4211(2015).
-!- 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 PSMB6 by PSMB9
increases the capacity of the immunoproteasome to cleave model
peptides after hydrophobic and basic residues.
{ECO:0000269|PubMed:8163024}.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:14550573, ECO:0000269|PubMed:16957778}.
-!- INTERACTION:
Q9WMX2:- (xeno); NbExp=2; IntAct=EBI-603300, EBI-6863748;
Q9Y3R0:GRIP1; NbExp=3; IntAct=EBI-603300, EBI-5349621;
Q15788:NCOA1; NbExp=3; IntAct=EBI-603300, EBI-455189;
Q9Y6Q9:NCOA3; NbExp=3; IntAct=EBI-603300, EBI-81196;
Q99436:PSMB7; NbExp=5; IntAct=EBI-603300, EBI-603319;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-
ProRule:PRU00809}. Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=LMP2.L;
IsoId=P28065-1; Sequence=Displayed;
Name=LMP2.S;
IsoId=P28065-2; Sequence=VSP_005288;
-!- DEVELOPMENTAL STAGE: Highly expressed in immature dendritic cells
(at protein level). {ECO:0000269|PubMed:11717192}.
-!- INDUCTION: 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. {ECO:0000269|PubMed:11493458,
ECO:0000269|PubMed:15501285, ECO:0000269|PubMed:15907481,
ECO:0000269|PubMed:17142736, ECO:0000269|PubMed:17262812,
ECO:0000269|PubMed:18694960, ECO:0000269|PubMed:8663318}.
-!- PTM: Autocleaved. The resulting N-terminal Thr residue of the
mature subunit is responsible for the nucleophile proteolytic
activity. {ECO:0000250|UniProtKB:O35955}.
-!- MISCELLANEOUS: Encoded in the MHC class II region.
-!- MISCELLANEOUS: 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.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000255|PROSITE-ProRule:PRU00809}.
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EMBL; X66401; CAA47024.1; -; Genomic_DNA.
EMBL; X62741; CAA44603.1; -; mRNA.
EMBL; Z14977; CAA78700.1; -; Genomic_DNA.
EMBL; X87344; CAA60784.1; -; Genomic_DNA.
EMBL; U01025; AAC50154.1; -; mRNA.
EMBL; S75169; AAC60646.1; -; mRNA.
EMBL; CR541656; CAG46457.1; -; mRNA.
EMBL; AL669918; CAI18141.1; -; Genomic_DNA.
EMBL; AL935043; CAI18627.1; -; Genomic_DNA.
EMBL; BX088556; CAM26264.1; -; Genomic_DNA.
EMBL; BX927138; CAQ08450.1; -; Genomic_DNA.
EMBL; CR762476; CAQ08497.1; -; Genomic_DNA.
EMBL; CR933844; CAQ08907.1; -; Genomic_DNA.
EMBL; CR753889; CAQ10289.1; -; Genomic_DNA.
EMBL; CH471081; EAX03654.1; -; Genomic_DNA.
EMBL; BC065513; AAH65513.1; -; mRNA.
CCDS; CCDS4759.1; -. [P28065-1]
PIR; A55632; A55632.
PIR; S27332; S27332.
RefSeq; NP_002791.1; NM_002800.4. [P28065-1]
UniGene; Hs.654585; -.
ProteinModelPortal; P28065; -.
SMR; P28065; -.
BioGrid; 111671; 73.
IntAct; P28065; 14.
MINT; MINT-2802096; -.
STRING; 9606.ENSP00000363993; -.
BindingDB; P28065; -.
ChEMBL; CHEMBL1944495; -.
DrugBank; DB08889; Carfilzomib.
MEROPS; T01.013; -.
iPTMnet; P28065; -.
PhosphoSitePlus; P28065; -.
BioMuta; PSMB9; -.
DMDM; 417529; -.
OGP; P28065; -.
EPD; P28065; -.
PaxDb; P28065; -.
PeptideAtlas; P28065; -.
PRIDE; P28065; -.
DNASU; 5698; -.
Ensembl; ENST00000374859; ENSP00000363993; ENSG00000240065. [P28065-1]
Ensembl; ENST00000383114; ENSP00000372595; ENSG00000240118. [P28065-1]
Ensembl; ENST00000383234; ENSP00000372721; ENSG00000243594. [P28065-1]
Ensembl; ENST00000422729; ENSP00000407233; ENSG00000243067. [P28065-1]
Ensembl; ENST00000427870; ENSP00000412027; ENSG00000242711.
Ensembl; ENST00000434471; ENSP00000393744; ENSG00000243958.
Ensembl; ENST00000444284; ENSP00000396813; ENSG00000239836. [P28065-1]
Ensembl; ENST00000453059; ENSP00000407810; ENSG00000240508.
GeneID; 5698; -.
KEGG; hsa:5698; -.
UCSC; uc003sga.4; human. [P28065-1]
CTD; 5698; -.
DisGeNET; 5698; -.
EuPathDB; HostDB:ENSG00000240065.7; -.
GeneCards; PSMB9; -.
H-InvDB; HIX0166929; -.
H-InvDB; HIX0207611; -.
H-InvDB; HIX0207787; -.
HGNC; HGNC:9546; PSMB9.
HPA; CAB015180; -.
HPA; HPA042818; -.
HPA; HPA053280; -.
MIM; 177045; gene.
neXtProt; NX_P28065; -.
OpenTargets; ENSG00000240065; -.
PharmGKB; PA33891; -.
eggNOG; KOG0174; Eukaryota.
eggNOG; ENOG410XS23; LUCA.
GeneTree; ENSGT00510000046484; -.
HOGENOM; HOG000091079; -.
HOVERGEN; HBG000123; -.
InParanoid; P28065; -.
KO; K02741; -.
OMA; HERIYCA; -.
OrthoDB; EOG091G0GUI; -.
PhylomeDB; P28065; -.
TreeFam; TF106221; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
GeneWiki; PSMB9; -.
GenomeRNAi; 5698; -.
PRO; PR:P28065; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000240065; -.
CleanEx; HS_PSMB9; -.
ExpressionAtlas; P28065; baseline and differential.
Genevisible; P28065; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000502; C:proteasome complex; TAS:ProtInc.
GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
GO; GO:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
GO; GO:2000116; P:regulation of cysteine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR000243; Pept_T1A_subB.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
Pfam; PF00227; Proteasome; 1.
PRINTS; PR00141; PROTEASOME.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00854; PROTEASOME_BETA_1; 1.
PROSITE; PS51476; PROTEASOME_BETA_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Host-virus interaction; Hydrolase; Immunity; Nucleus; Polymorphism;
Protease; Proteasome; Reference proteome; Threonine protease; Zymogen.
PROPEP 1 20 Removed in mature form.
/FTId=PRO_0000026619.
CHAIN 21 219 Proteasome subunit beta type-9.
/FTId=PRO_0000026620.
ACT_SITE 21 21 Nucleophile.
SITE 20 21 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:O35955}.
MOD_RES 53 53 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 109 109 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 4 13 Missing (in isoform LMP2.S).
{ECO:0000303|PubMed:7829535}.
/FTId=VSP_005288.
VARIANT 9 9 G -> E (in dbSNP:rs35100697).
/FTId=VAR_051551.
VARIANT 32 32 V -> I (in dbSNP:rs241419).
/FTId=VAR_051552.
VARIANT 60 60 R -> H (in dbSNP:rs17587).
{ECO:0000269|PubMed:10924276,
ECO:0000269|PubMed:1922385}.
/FTId=VAR_013578.
VARIANT 165 165 G -> D (found in a patient with Nakajo
syndrome who also carries a mutation in
PSMB4; unknown pathological significance;
patients' cells show reduction of
proteasome content and cysteine-type
endopeptidase activity of the proteasome;
dbSNP:rs369359789).
{ECO:0000269|PubMed:26524591}.
/FTId=VAR_075258.
VARIANT 173 173 R -> C (in dbSNP:rs17213861).
/FTId=VAR_051553.
MUTAGEN 20 20 G->A: Impairs correct processing at the
consensus site.
{ECO:0000269|PubMed:9003765}.
MUTAGEN 21 21 T->A: Impairs correct processing at the
consensus site.
{ECO:0000269|PubMed:9003765}.
MUTAGEN 53 53 K->A: Impairs correct processing at the
consensus site.
{ECO:0000269|PubMed:9003765}.
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


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