P28065 (PSB9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	219 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 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. This subunit is part of the immunoproteasome where it displaces the equivalent houskeeping subunit PSMB6. 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 process	Host-virus interaction Immunity
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protease Threonine protease
PTM	Acetylation 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 phase 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 exogenous peptide antigen via MHC class I, TAP-dependent Traceable author statement. Source: Reactome apoptotic process Traceable author statement. Source: Reactome gene expression Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome mitotic anaphase 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 small molecule metabolic process Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome proteasome core complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PSMB7	Q99436	5	EBI-603300,EBI-603319

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 20	20	Removed in mature form		PRO_0000026619
	Chain	21 – 219	199	Proteasome subunit beta type-9		PRO_0000026620
Sites
	Active site	21	1	Nucleophile
	Site	20 – 21	2	Cleavage; by autocatalysis
Amino acid modifications
	Modified residue	53	1	N6-acetyllysine Ref.23
	Modified residue	109	1	N6-acetyllysine Ref.23
Natural variations
	Alternative sequence	4 – 13	10	Missing in isoform LMP2.S.		VSP_005288
	Natural variant	9	1	G → E. Corresponds to variant rs35100697 [ dbSNP | Ensembl ].		VAR_051551
	Natural variant	32	1	V → I. Corresponds to variant rs241419 [ dbSNP | Ensembl ].		VAR_051552
	Natural variant	60	1	R → H. Ref.3 Ref.25 Corresponds to variant rs17587 [ dbSNP | Ensembl ].		VAR_013578
	Natural variant	173	1	R → C. Corresponds to variant rs17213861 [ dbSNP | Ensembl ].		VAR_051553
Experimental info
	Mutagenesis	20	1	G → A: Impairs correct processing at the consensus site. Ref.12
	Mutagenesis	21	1	T → A: Impairs correct processing at the consensus site. Ref.12
	Mutagenesis	53	1	K → A: Impairs correct processing at the consensus site. Ref.12

Sequences

	Sequence		Length	Mass (Da)
	Isoform LMP2.L [UniParc]. Last modified October 1, 1993. Version 2. Checksum: 3B321F83641941AC	FASTA	219	23,264
	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
	Isoform LMP2.S [UniParc]. Checksum: 3AD94A5C402BC2A0	FASTA	209	22,328
	10 20 30 40 50 60 MLRAGEVHTG TTIMAVEFDG GVVMGSDSRV SAGEAVVNRV FDKLSPLHER IYCALSGSAA 70 80 90 100 110 120 DAQAVADMAA YQLELHGIEL EEPPLVLAAA NVVRNISYKY REDLSAHLMV AGWDQREGGQ 130 140 150 160 170 180 VYGTLGGMLT RQPFAIGGSG STFIYGYVDA AYKPGMSPEE CRRFTTDAIA LAMSRDGSSG 190 200 GVIYLVTITA AGVDHRVILG NELPKFYDE

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] [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. , 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. , 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, MASS SPECTROMETRY.
[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.
IPI	IPI00000787. IPI00170899.
PIR	A55632. S27332.
RefSeq	NP_002791.1. NM_002800.4.
UniGene	Hs.654585.
3D structure databases
ProteinModelPortal	P28065.
ModBase	Search...
Protein-protein interaction databases
IntAct	P28065. 7 interactions.
MINT	MINT-2802096.
STRING	9606.ENSP00000396813.
Protein family/group databases
MEROPS	T01.013.
PTM databases
PhosphoSite	P28065.
Polymorphism databases
DMDM	417529.
2D gel databases
OGP	P28065.
Proteomic databases
PaxDb	P28065.
PRIDE	P28065.
Protocols and materials databases
DNASU	5698.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374859; ENSP00000363993; ENSG00000240065. ENST00000383114; ENSP00000372595; ENSG00000240118. ENST00000383234; ENSP00000372721; ENSG00000243594. ENST00000422729; ENSP00000407233; ENSG00000243067. ENST00000427870; ENSP00000412027; ENSG00000242711. ENST00000434471; ENSP00000393744; ENSG00000243958. ENST00000444284; ENSP00000396813; ENSG00000239836. ENST00000453059; ENSP00000407810; ENSG00000240508.
GeneID	5698.
KEGG	hsa:5698.
UCSC	uc003sga.3. human.
Organism-specific databases
CTD	5698.
GeneCards	GC06P032815.
H-InvDB	HIX0166929. HIX0207611. HIX0207787.
HGNC	HGNC:9546. PSMB9.
HPA	CAB015180.
MIM	177045. gene.
neXtProt	NX_P28065.
PharmGKB	PA33891.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0638.
HOGENOM	HOG000091079.
HOVERGEN	HBG000123.
InParanoid	P28065.
KO	K02741.
OMA	CRRFTTN.
PhylomeDB	P28065.
Enzyme and pathway databases
Reactome	REACT_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
ArrayExpress	P28065.
Bgee	P28065.
CleanEx	HS_PSMB9.
Genevestigator	P28065.
GermOnline	ENSG00000204261. 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]
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
ChEMBL	CHEMBL1944495.
GenomeRNAi	5698.
NextBio	22136.
SOURCE	Search...

Entry information

Entry name

PSB9_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 152 of the entry and version 2 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.