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P28074 (PSB5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. 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-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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length263 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 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 processHost-virus interaction
   Cellular componentCytoplasm
Nucleus
Proteasome
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
Protease
Threonine protease
   PTMZymogen
   Technical termComplete proteome
Direct protein sequencing
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

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

proteasome complex

Traceable author statement PubMed 8811196. Source: ProtInc

proteasome core complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 14733938PubMed 17948026PubMed 20723761. Source: IntAct

threonine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 5959Removed in mature form
PRO_0000026589
Chain60 – 263204Proteasome subunit beta type-5
PRO_0000026590

Sites

Active site601Nucleophile
Binding site1081Bortezomib; via amide nitrogen By similarity

Natural variations

Alternative sequence1 – 103103Missing in isoform 3.
VSP_045686
Alternative sequence169 – 26395GLYYV…SGSTP → VSEVLCLKPKSFGMYLFCGC AERIGNMARPLLRGQ in isoform 2.
VSP_041263
Natural variant241R → C.
Corresponds to variant rs11543947 [ dbSNP | Ensembl ].
VAR_051549

Experimental info

Mutagenesis1081A → 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
Mutagenesis1081A → V: Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity. Ref.21 Ref.22 Ref.23
Mutagenesis1091A → V: Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity; when associated with T-108. Ref.23
Sequence conflict3 – 64LASV → IRGR in BAA06097. Ref.8
Sequence conflict3 – 53LAS → HEG in BC004146. Ref.6
Sequence conflict851I → F AA sequence Ref.11
Sequence conflict1091A → G in AAB33092. Ref.9
Sequence conflict1581T → S in AAB33092. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 29, 2008. Version 3.
Checksum: AED4A73DF41AA6EF

FASTA26328,480
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 29788AD9561905AE
Show »

FASTA20321,845
Isoform 3 [UniParc].

Checksum: 47A97A3A9A849846
Show »

FASTA16017,782

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. 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 (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.
CCDSCCDS45083.1. [P28074-3]
CCDS45084.1. [P28074-2]
CCDS9584.1. [P28074-1]
PIRA54589.
I52906.
PC2328.
S08189.
RefSeqNP_001124197.1. NM_001130725.1. [P28074-3]
NP_001138404.1. NM_001144932.2. [P28074-2]
NP_002788.1. NM_002797.4. [P28074-1]
UniGeneHs.422990.

3D structure databases

ProteinModelPortalP28074.
SMRP28074. Positions 34-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111666. 83 interactions.
DIPDIP-27540N.
IntActP28074. 24 interactions.
MINTMINT-1161576.
STRING9606.ENSP00000355325.

Chemistry

BindingDBP28074.
ChEMBLCHEMBL2364701.
DrugBankDB00188. Bortezomib.
GuidetoPHARMACOLOGY2406.

Protein family/group databases

MEROPST01.P01.

PTM databases

PhosphoSiteP28074.

Polymorphism databases

DMDM187608890.

2D gel databases

REPRODUCTION-2DPAGEIPI00479306.

Proteomic databases

MaxQBP28074.
PaxDbP28074.
PRIDEP28074.

Protocols and materials databases

DNASU5693.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361611; ENSP00000355325; ENSG00000100804. [P28074-1]
ENST00000425762; ENSP00000395206; ENSG00000100804. [P28074-3]
ENST00000493471; ENSP00000452424; ENSG00000100804. [P28074-2]
GeneID5693.
KEGGhsa:5693.
UCSCuc001wii.3. human. [P28074-1]
uc001wij.3. human. [P28074-2]

Organism-specific databases

CTD5693.
GeneCardsGC14M023485.
HGNCHGNC:9542. PSMB5.
HPAHPA049518.
MIM600306. gene.
neXtProtNX_P28074.
PharmGKBPA33887.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0638.
HOVERGENHBG108297.
InParanoidP28074.
KOK02737.
OMALRAIMHA.
PhylomeDBP28074.
TreeFamTF106223.

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

ArrayExpressP28074.
BgeeP28074.
CleanExHS_PSMB5.
GenevestigatorP28074.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000243. 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.
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPSMB5.
GenomeRNAi5693.
NextBio22114.
PROP28074.
SOURCESearch...

Entry information

Entry namePSB5_HUMAN
AccessionPrimary (citable) accession number: P28074
Secondary accession number(s): B2R4N9 expand/collapse secondary AC list , 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: July 9, 2014
This is version 165 of the entry and version 3 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 14

Human chromosome 14: entries, gene names and cross-references to MIM