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P28065 (PSB9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 160. 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-9

EC=3.4.25.1
Alternative name(s):
Low molecular mass protein 2
Macropain chain 7
Multicatalytic endopeptidase complex chain 7
Proteasome chain 7
Proteasome subunit beta-1i
Really interesting new gene 12 protein
Gene names
Name:PSMB9
Synonyms:LMP2, PSMB6i, RING12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length219 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 PSMB6 by PSMB9 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. Ref.11

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 houskeeping subunit PSMB6. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Interacts with HIV-1 TAT protein. Ref.12 Ref.16 Ref.19

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 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. Ref.13 Ref.14 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22

Post-translational modification

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

Miscellaneous

Encoded in the MHC class II region.

A model for self-activation in which residue Thr-21 serves as nucleophile and Lys-53 as proton donor/acceptor has been proposed. Subunit processing of mammalian beta-subunits proceeds via a novel ordered two-step mechanism involving autocatalysis.

Sequence similarities

Belongs to the peptidase T1B family.

Ontologies

Keywords
   Biological processHost-virus interaction
Immunity
   Cellular componentCytoplasm
Nucleus
Proteasome
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
Protease
Threonine protease
   PTMAcetylation
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

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

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. 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_functionthreonine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform LMP2.L (identifier: P28065-1)

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 LMP2.S (identifier: P28065-2)

The sequence of this isoform differs from the canonical sequence as follows:
     4-13: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 2020Removed in mature form
PRO_0000026619
Chain21 – 219199Proteasome subunit beta type-9
PRO_0000026620

Sites

Active site211Nucleophile
Site20 – 212Cleavage; by autocatalysis

Amino acid modifications

Modified residue531N6-acetyllysine Ref.23
Modified residue1091N6-acetyllysine Ref.23

Natural variations

Alternative sequence4 – 1310Missing in isoform LMP2.S.
VSP_005288
Natural variant91G → E.
Corresponds to variant rs35100697 [ dbSNP | Ensembl ].
VAR_051551
Natural variant321V → I.
Corresponds to variant rs241419 [ dbSNP | Ensembl ].
VAR_051552
Natural variant601R → H. Ref.3 Ref.25
Corresponds to variant rs17587 [ dbSNP | Ensembl ].
VAR_013578
Natural variant1731R → C.
Corresponds to variant rs17213861 [ dbSNP | Ensembl ].
VAR_051553

Experimental info

Mutagenesis201G → A: Impairs correct processing at the consensus site. Ref.12
Mutagenesis211T → A: Impairs correct processing at the consensus site. Ref.12
Mutagenesis531K → A: Impairs correct processing at the consensus site. Ref.12

Sequences

Sequence LengthMass (Da)Tools
Isoform LMP2.L [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: 3B321F83641941AC

FASTA21923,264
        10         20         30         40         50         60 
MLRAGAPTGD LPRAGEVHTG TTIMAVEFDG GVVMGSDSRV SAGEAVVNRV FDKLSPLHER 

        70         80         90        100        110        120 
IYCALSGSAA DAQAVADMAA YQLELHGIEL EEPPLVLAAA NVVRNISYKY REDLSAHLMV 

       130        140        150        160        170        180 
AGWDQREGGQ VYGTLGGMLT RQPFAIGGSG STFIYGYVDA AYKPGMSPEE CRRFTTDAIA 

       190        200        210 
LAMSRDGSSG GVIYLVTITA AGVDHRVILG NELPKFYDE 

« Hide

Isoform LMP2.S [UniParc].

Checksum: 3AD94A5C402BC2A0
Show »

FASTA20922,328

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]"Second proteasome-related gene in the human MHC class II region."
Kelly A., Powis S.H., Glynne R., Radley E., Beck S., Trowsdale J.
Nature 353:667-668(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LMP2.L), VARIANT HIS-60.
[4]"Alternative exon usage and processing of the major histocompatibility complex-encoded proteasome subunits."
Fruh K., Yang Y., Arnold D., Chambers J., Wu L., Waters J.B., Spies T., Peterson P.A.
J. Biol. Chem. 267:22131-22140(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Evolutionary dynamics of non-coding sequences within the class II region of the human MHC."
Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., Hosking L.K., Jackson A., Kelly A., Newell W.R., Sanseau P., Radley E., Thorpe K.L., Trowsdale J.
J. Mol. Biol. 255:1-13(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Major histocompatibility-encoded human proteasome LMP2. Genomic organization and a new form of mRNA."
Singal D.P., Ye M., Quadri S.A.
J. Biol. Chem. 270:1966-1970(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS LMP2.S AND LMP2.L).
[7]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LMP2.L).
[8]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. 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., 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 LMP2.L).
Tissue: Pancreas.
[11]"Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced by interferon-gamma for acquirement of the functional diversity responsible for antigen processing."
Akiyama K., Kagawa S., Tamura T., Shimbara N., Takashina M., Kristensen P., Hendil K.B., Tanaka K., Ichihara A.
FEBS Lett. 343:85-88(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Analysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis."
Schmidtke G., Kraft R., Kostka S., Henklein P., Froemmel C., Loewe J., Huber R., Kloetzel P.-M., Schmidt M.
EMBO J. 15:6887-6898(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-20; THR-21 AND LYS-53, SELF ACTIVATION OF BETA-SUBUNITS MODEL.
[13]"Proteasome subunits X and Y alter peptidase activities in opposite ways to the interferon-gamma-induced subunits LMP2 and LMP7."
Gaczynska M., Goldberg A.L., Tanaka K., Hendil K.B., Rock K.L.
J. Biol. Chem. 271:17275-17280(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[14]"Tumor necrosis factor-alpha induces coordinated changes in major histocompatibility class I presentation pathway, resulting in increased stability of class I complexes at the cell surface."
Hallermalm K., Seki K., Wei C., Castelli C., Rivoltini L., Kiessling R., Levitskaya J.
Blood 98:1108-1115(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY TNF AND IFNG.
[15]"Bipartite regulation of different components of the MHC class I antigen-processing machinery during dendritic cell maturation."
Li J., Schuler-Thurner B., Schuler G., Huber C., Seliger B.
Int. Immunol. 13:1515-1523(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[16]"Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits."
Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E.
FEBS Lett. 553:200-204(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 TAT.
[17]"Potential effects of tetrodotoxin exposure to human glial cells postulated using microarray approach."
Raghavendra Prasad H.S., Qi Z., Srinivasan K.N., Gopalakrishnakone P.
Toxicon 44:597-608(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY TETRODOTOXIN.
[18]"IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted expression of immunosubunits of the proteasome."
Namiki S., Nakamura T., Oshima S., Yamazaki M., Sekine Y., Tsuchiya K., Okamoto R., Kanai T., Watanabe M.
FEBS Lett. 579:2781-2787(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY IFNG AND IRF1.
[19]"The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription."
Zhang H., Sun L., Liang J., Yu W., Zhang Y., Wang Y., Chen Y., Li R., Sun X., Shang Y.
EMBO J. 25:4223-4233(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA1; NCOA2 AND NCOA3.
[20]"Heat shock up-regulates lmp2 and lmp7 and enhances presentation of immunoproteasome-dependent epitopes."
Callahan M.K., Wohlfert E.A., Menoret A., Srivastava P.K.
J. Immunol. 177:8393-8399(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY HEAT SHOCK.
[21]"Genome-wide gene expression differences in Crohn's disease and ulcerative colitis from endoscopic pinch biopsies: insights into distinctive pathogenesis."
Wu F., Dassopoulos T., Cope L., Maitra A., Brant S.R., Harris M.L., Bayless T.M., Parmigiani G., Chakravarti S.
Inflamm. Bowel Dis. 13:807-821(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[22]"CD40 induces antigen transporter and immunoproteasome gene expression in carcinomas via the coordinated action of NF-kappaB and of NF-kappaB-mediated de novo synthesis of IRF-1."
Moschonas A., Kouraki M., Knox P.G., Thymiakou E., Kardassis D., Eliopoulos A.G.
Mol. Cell. Biol. 28:6208-6222(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY CD40L.
[23]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53 AND LYS-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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].
[25]"Complex association analysis of Graves disease using a set of polymorphic markers."
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.
Mol. Genet. Metab. 70:214-218(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-60.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66401 Genomic DNA. Translation: CAA47024.1.
X62741 mRNA. Translation: CAA44603.1.
Z14977 Genomic DNA. Translation: CAA78700.1.
X87344 Genomic DNA. Translation: CAA60784.1.
U01025 mRNA. Translation: AAC50154.1.
S75169 mRNA. Translation: AAC60646.1.
CR541656 mRNA. Translation: CAG46457.1.
AL669918 Genomic DNA. Translation: CAI18141.1.
AL935043 Genomic DNA. Translation: CAI18627.1.
BX088556 Genomic DNA. Translation: CAM26264.1.
BX927138 Genomic DNA. Translation: CAQ08450.1.
CR762476 Genomic DNA. Translation: CAQ08497.1.
CR933844 Genomic DNA. Translation: CAQ08907.1.
CR753889 Genomic DNA. Translation: CAQ10289.1.
CH471081 Genomic DNA. Translation: EAX03654.1.
BC065513 mRNA. Translation: AAH65513.1.
PIRA55632.
S27332.
RefSeqNP_002791.1. NM_002800.4.
UniGeneHs.654585.

3D structure databases

ProteinModelPortalP28065.
SMRP28065. Positions 21-219.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111671. 21 interactions.
IntActP28065. 12 interactions.
MINTMINT-2802096.
STRING9606.ENSP00000396813.

Chemistry

ChEMBLCHEMBL1944495.

Protein family/group databases

MEROPST01.013.

PTM databases

PhosphoSiteP28065.

Polymorphism databases

DMDM417529.

2D gel databases

OGPP28065.

Proteomic databases

PaxDbP28065.
PRIDEP28065.

Protocols and materials databases

DNASU5698.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374859; ENSP00000363993; ENSG00000240065. [P28065-1]
ENST00000383114; ENSP00000372595; ENSG00000240118. [P28065-1]
ENST00000383234; ENSP00000372721; ENSG00000243594. [P28065-1]
ENST00000422729; ENSP00000407233; ENSG00000243067. [P28065-1]
ENST00000427870; ENSP00000412027; ENSG00000242711.
ENST00000434471; ENSP00000393744; ENSG00000243958.
ENST00000444284; ENSP00000396813; ENSG00000239836. [P28065-1]
ENST00000453059; ENSP00000407810; ENSG00000240508.
GeneID5698.
KEGGhsa:5698.
UCSCuc003sga.3. human. [P28065-1]

Organism-specific databases

CTD5698.
GeneCardsGC06P032825.
GC06Pi32796.
GC06Pj32735.
GC06Pk32790.
GC06Pl32966.
GC06Pm32847.
GC06Pn32741.
GC06Po32903.
H-InvDBHIX0166929.
HIX0207611.
HIX0207787.
HGNCHGNC:9546. PSMB9.
HPACAB015180.
HPA042818.
HPA053280.
MIM177045. gene.
neXtProtNX_P28065.
PharmGKBPA33891.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091079.
HOVERGENHBG000123.
InParanoidP28065.
KOK02741.
OMAQVYGTMG.
PhylomeDBP28065.
TreeFamTF106221.

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

ArrayExpressP28065.
BgeeP28065.
CleanExHS_PSMB9.
GenevestigatorP28065.

Family and domain databases

InterProIPR000243. 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.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPSMB9.
GenomeRNAi5698.
NextBio22136.
PROP28065.
SOURCESearch...

Entry information

Entry namePSB9_HUMAN
AccessionPrimary (citable) accession number: P28065
Secondary accession number(s): B0V0T1, Q16523, Q5JNW4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 160 of the entry and version 2 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