P28074 (PSB5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteasome subunit beta type-5
EC=3.4.25.1

Alternative name(s):
Macropain epsilon chain
Multicatalytic endopeptidase complex epsilon chain
Proteasome chain 6
Proteasome epsilon chain
Proteasome subunit MB1
Proteasome subunit X

Gene names

Name:	PSMB5
Synonyms:	LMPX, MB1, X

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	263 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 unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib. May catalyze basal processing of intracellular antigens. Plays a role in the protection against oxidative damage through the Nrf2-ARE pathway By similarity. Ref.21 Ref.22
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 can be displaced by the equivalent immune-specific subunit PSMB8. Directly interacts with POMP. Interacts with HIV-1 TAT protein. Interacts with ABCB1 and TAP1. Ref.13 Ref.16 Ref.17 Ref.18
Subcellular location	Cytoplasm. Nucleus.
Induction	Down-regulated by IFNG/IFN-gamma (at protein level). Induced in breast cancer tissue. Up-regulated by sulforaphane in breast cancer cells. Ref.8 Ref.15 Ref.20 Ref.24
Sequence similarities	Belongs to the peptidase T1B family.
Sequence caution	The sequence AAP35423.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA06097.1 differs from that shown. Reason: Erroneous initiation. The sequence CAD97956.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protease Threonine protease
PTM	Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Traceable author statement. Source: Reactome G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome antigen processing and presentation of 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 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 response to oxidative stress Inferred from electronic annotation. Source: Compara 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	6	EBI-357828,EBI-603319

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P28074-1)

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 2 (identifier: P28074-2)

The sequence of this isoform differs from the canonical sequence as follows:
     169-263: GLYYVDSEGN...LHEKYSGSTP → VSEVLCLKPKSFGMYLFCGCAERIGNMARPLLRGQ

Isoform 3 (identifier: P28074-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-103: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 59	59	Removed in mature form		PRO_0000026589
	Chain	60 – 263	204	Proteasome subunit beta type-5		PRO_0000026590
Sites
	Active site	60	1	Nucleophile
	Binding site	108	1	Bortezomib; via amide nitrogen By similarity
Natural variations
	Alternative sequence	1 – 103	103	Missing in isoform 3.		VSP_045686
	Alternative sequence	169 – 263	95	GLYYV…SGSTP → VSEVLCLKPKSFGMYLFCGC AERIGNMARPLLRGQ in isoform 2.		VSP_041263
	Natural variant	24	1	R → C. Corresponds to variant rs11543947 [ dbSNP | Ensembl ].		VAR_051549
Experimental info
	Mutagenesis	108	1	A → T: Displays resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity. Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity; when associated with V-109. Ref.21 Ref.22 Ref.23
	Mutagenesis	108	1	A → V: Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity. Ref.21 Ref.22 Ref.23
	Mutagenesis	109	1	A → V: Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity; when associated with T-108. Ref.23
	Sequence conflict	3 – 6	4	LASV → IRGR in BAA06097. Ref.8
	Sequence conflict	3 – 5	3	LAS → HEG in BC004146. Ref.6
	Sequence conflict	85	1	I → F AA sequence Ref.11
	Sequence conflict	109	1	A → G in AAB33092. Ref.9
	Sequence conflict	158	1	T → S in AAB33092. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 29, 2008. Version 3. Checksum: AED4A73DF41AA6EF	FASTA	263	28,480
	10 20 30 40 50 60 MALASVLERP LPVNQRGFFG LGGRADLLDL GPGSLSDGLS LAAPGWGVPE EPGIEMLHGT 70 80 90 100 110 120 TTLAFKFRHG VIVAADSRAT AGAYIASQTV KKVIEINPYL LGTMAGGAAD CSFWERLLAR 130 140 150 160 170 180 QCRIYELRNK ERISVAAASK LLANMVYQYK GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI 190 200 210 220 230 240 SGATFSVGSG SVYAYGVMDR GYSYDLEVEQ AYDLARRAIY QATYRDAYSG GAVNLYHVRE 250 260 DGWIRVSSDN VADLHEKYSG STP
	Isoform 2 [UniParc]. Checksum: 29788AD9561905AE	FASTA	203	21,845
	10 20 30 40 50 60 MALASVLERP LPVNQRGFFG LGGRADLLDL GPGSLSDGLS LAAPGWGVPE EPGIEMLHGT 70 80 90 100 110 120 TTLAFKFRHG VIVAADSRAT AGAYIASQTV KKVIEINPYL LGTMAGGAAD CSFWERLLAR 130 140 150 160 170 180 QCRIYELRNK ERISVAAASK LLANMVYQYK GMGLSMGTMI CGWDKRGPVS EVLCLKPKSF 190 200 GMYLFCGCAE RIGNMARPLL RGQ
	Isoform 3 [UniParc]. Checksum: 47A97A3A9A849846	FASTA	160	17,782
	10 20 30 40 50 60 MAGGAADCSF WERLLARQCR IYELRNKERI SVAAASKLLA NMVYQYKGMG LSMGTMICGW 70 80 90 100 110 120 DKRGPGLYYV DSEGNRISGA TFSVGSGSVY AYGVMDRGYS YDLEVEQAYD LARRAIYQAT 130 140 150 160 YRDAYSGGAV NLYHVREDGW IRVSSDNVAD LHEKYSGSTP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Divergent intron arrangement in the MB1/LMP7 proteasome gene pair." Abdulla S., Beck S., Belich M., Jackson A., Nakamura T., Trowsdale J. Immunogenetics 44:254-258(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Skeletal muscle.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Endometrial adenocarcinoma.
[4]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORMS 1 AND 3). Tissue: Embryonic stem cell, Hypothalamus and Skin.
[7]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-203 (ISOFORM 2). Tissue: Cervix carcinoma.
[8]	"cDNA cloning and interferon gamma down-regulation of proteasomal subunits X and Y." Akiyama K.-Y., Yokota K.-Y., Kagawa S., Shimbara N., Tamura T., Akioka H., Nothwang H.G., Noda C., Tanaka K., Ichihara A. Science 265:1231-1234(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-263 (ISOFORM 1), INDUCTION.
[9]	"Proteasome components with reciprocal expression to that of the MHC-encoded LMP proteins." Belich M.P., Glynne R.J., Senger G., Sheer D., Trowsdale J. Curr. Biol. 4:769-776(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-263 (ISOFORM 1).
[10]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-263 (ISOFORM 1).
[11]	"Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome)." Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N., Slaughter C.A. Biochim. Biophys. Acta 1037:178-185(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 60-85.
[12]	"Human proteasome subunits from 2-dimensional gels identified by partial sequencing." Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B. Biochem. Biophys. Res. Commun. 205:1785-1789(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 201-216 AND 226-239.
[13]	"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: PROTEIN SEQUENCE OF 201-216, SUBUNIT. Tissue: Kidney.
[14]	Erratum Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B. Biochem. Biophys. Res. Commun. 207:1059-1059(1995) [PubMed] [Europe PMC] [Abstract]
[15]	"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.
[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]	"Cytoplasmic domains of the transporter associated with antigen processing and P-glycoprotein interact with subunits of the proteasome." Begley G.S., Horvath A.R., Taylor J.C., Higgins C.F. Mol. Immunol. 42:137-141(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ABCB1 AND TAP1.
[18]	"IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response." Heink S., Ludwig D., Kloetzel P.-M., Krueger E. Proc. Natl. Acad. Sci. U.S.A. 102:9241-9246(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH POMP.
[19]	"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex." Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L. Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[20]	"Over-expression of genes and proteins of ubiquitin specific peptidases (USPs) and proteasome subunits (PSs) in breast cancer tissue observed by the methods of RFDD-PCR and proteomics." Deng S., Zhou H., Xiong R., Lu Y., Yan D., Xing T., Dong L., Tang E., Yang H. Breast Cancer Res. Treat. 104:21-30(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[21]	"Molecular basis of bortezomib resistance: proteasome subunit beta5 (PSMB5) gene mutation and overexpression of PSMB5 protein." Oerlemans R., Franke N.E., Assaraf Y.G., Cloos J., van Zantwijk I., Berkers C.R., Scheffer G.L., Debipersad K., Vojtekova K., Lemos C., van der Heijden J.W., Ylstra B., Peters G.J., Kaspers G.L., Dijkmans B.A., Scheper R.J., Jansen G. Blood 112:2489-2499(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ALA-108.
[22]	"Point mutation of the proteasome beta5 subunit gene is an important mechanism of bortezomib resistance in bortezomib-selected variants of Jurkat T cell lymphoblastic lymphoma/leukemia line." Lue S., Yang J., Song X., Gong S., Zhou H., Guo L., Song N., Bao X., Chen P., Wang J. J. Pharmacol. Exp. Ther. 326:423-431(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ALA-108.
[23]	"Different mutants of PSMB5 confer varying bortezomib resistance in T lymphoblastic lymphoma/leukemia cells derived from the Jurkat cell line." Lue S., Yang J., Chen Z., Gong S., Zhou H., Xu X., Wang J. Exp. Hematol. 37:831-837(2009) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ALA-108 AND ALA-109.
[24]	"Regulation of estrogen receptor alpha expression in human breast cancer cells by sulforaphane." Ramirez M.C., Singletary K. J. Nutr. Biochem. 20:195-201(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY SULFORAPHANE.
[25]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X95586 Genomic DNA. Translation: CAA64838.1. AK300714 mRNA. Translation: BAG62391.1. AK311895 mRNA. Translation: BAG34836.1. BX538001 mRNA. Translation: CAD97956.1. Different initiation. AL132780 Genomic DNA. No translation available. CH471078 Genomic DNA. Translation: EAW66193.1. CH471078 Genomic DNA. Translation: EAW66195.1. BC004146 mRNA. No translation available. BC057840 mRNA. Translation: AAH57840.1. BC107720 mRNA. Translation: AAI07721.1. CD048996 mRNA. No translation available. BX248299 mRNA. Translation: CAD62626.1. D29011 mRNA. Translation: BAA06097.1. Different initiation. S74378 mRNA. Translation: AAB33092.1. BT006777 mRNA. Translation: AAP35423.1. Different initiation.
IPI	IPI00383971. IPI00479306. IPI00910237.
PIR	A54589. I52906. PC2328. S08189.
RefSeq	NP_001124197.1. NM_001130725.1. NP_001138404.1. NM_001144932.1. NP_002788.1. NM_002797.3.
UniGene	Hs.422990.
3D structure databases
ProteinModelPortal	P28074.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27540N.
IntAct	P28074. 19 interactions.
MINT	MINT-1161576.
STRING	9606.ENSP00000355325.
Protein family/group databases
MEROPS	T01.P01.
PTM databases
PhosphoSite	P28074.
Polymorphism databases
DMDM	187608890.
2D gel databases
REPRODUCTION-2DPAGE	IPI00479306.
Proteomic databases
PaxDb	P28074.
PRIDE	P28074.
Protocols and materials databases
DNASU	5693.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361611; ENSP00000355325; ENSG00000100804. ENST00000425762; ENSP00000395206; ENSG00000100804. ENST00000493471; ENSP00000452424; ENSG00000100804.
GeneID	5693.
KEGG	hsa:5693.
UCSC	uc001wii.3. human. uc001wij.3. human.
Organism-specific databases
CTD	5693.
GeneCards	GC14M023485.
HGNC	HGNC:9542. PSMB5.
HPA	HPA049518.
MIM	600306. gene.
neXtProt	NX_P28074.
PharmGKB	PA33887.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0638.
HOVERGEN	HBG108297.
InParanoid	P28074.
KO	K02737.
OMA	QTFAYGV.
OrthoDB	EOG4M91S6.
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	P28074.
Bgee	P28074.
CleanEx	HS_PSMB5.
Genevestigator	P28074.
GermOnline	ENSG00000100804. 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
BindingDB	P28074.
ChEMBL	CHEMBL4662.
DrugBank	DB00188. Bortezomib.
GenomeRNAi	5693.
NextBio	22114.
SOURCE	Search...

Entry information

Entry name

PSB5_HUMAN

Accession

Primary (citable) accession number: P28074
Secondary accession number(s): B2R4N9 , B4DUM9, D3DS43, E9PAV2, Q16242, Q6PEW2, Q7Z3B5, Q86T01, Q9TNN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	April 29, 2008
Last modified:	May 1, 2013
This is version 151 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.