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P28074

- PSB5_HUMAN

UniProt

P28074 - PSB5_HUMAN

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Protein
Proteasome subunit beta type-5
Gene
PSMB5, LMPX, MB1, X
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei60 – 601Nucleophile
Binding sitei108 – 1081Bortezomib; via amide nitrogen By similarity

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  2. G1/S transition of mitotic cell cycle Source: Reactome
  3. RNA metabolic process Source: Reactome
  4. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  5. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  6. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  7. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  8. apoptotic process Source: Reactome
  9. cellular nitrogen compound metabolic process Source: Reactome
  10. gene expression Source: Reactome
  11. mRNA metabolic process Source: Reactome
  12. mitotic cell cycle Source: Reactome
  13. negative regulation of apoptotic process Source: Reactome
  14. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  15. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  16. protein polyubiquitination Source: Reactome
  17. regulation of apoptotic process Source: Reactome
  18. regulation of cellular amino acid metabolic process Source: Reactome
  19. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  20. response to oxidative stress Source: Ensembl
  21. small molecule metabolic process Source: Reactome
  22. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Protein family/group databases

MEROPSiT01.P01.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PSMB5
Synonyms:LMPX, MB1, X
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:9542. PSMB5.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProt
  5. proteasome complex Source: ProtInc
  6. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1081A → 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. 3 Publications
Mutagenesisi108 – 1081A → V: Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity. 3 Publications
Mutagenesisi109 – 1091A → V: Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity; when associated with T-108. 1 Publication

Organism-specific databases

PharmGKBiPA33887.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 5959Removed in mature form
PRO_0000026589Add
BLAST
Chaini60 – 263204Proteasome subunit beta type-5
PRO_0000026590Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

MaxQBiP28074.
PaxDbiP28074.
PRIDEiP28074.

2D gel databases

REPRODUCTION-2DPAGEIPI00479306.

PTM databases

PhosphoSiteiP28074.

Expressioni

Inductioni

Down-regulated by IFNG/IFN-gamma (at protein level). Induced in breast cancer tissue. Up-regulated by sulforaphane in breast cancer cells.4 Publications

Gene expression databases

ArrayExpressiP28074.
BgeeiP28074.
CleanExiHS_PSMB5.
GenevestigatoriP28074.

Organism-specific databases

HPAiHPA049518.

Interactioni

Subunit structurei

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 TAP1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
POMPQ9Y2443EBI-357828,EBI-696895
PSMB1P206183EBI-357828,EBI-372273
PSMB7Q994367EBI-357828,EBI-603319

Protein-protein interaction databases

BioGridi111666. 75 interactions.
DIPiDIP-27540N.
IntActiP28074. 24 interactions.
MINTiMINT-1161576.
STRINGi9606.ENSP00000355325.

Structurei

3D structure databases

ProteinModelPortaliP28074.
SMRiP28074. Positions 34-260.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.

Phylogenomic databases

eggNOGiCOG0638.
HOVERGENiHBG108297.
InParanoidiP28074.
KOiK02737.
OMAiLRAIMHA.
PhylomeDBiP28074.
TreeFamiTF106223.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P28074-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MALASVLERP LPVNQRGFFG LGGRADLLDL GPGSLSDGLS LAAPGWGVPE    50
EPGIEMLHGT TTLAFKFRHG VIVAADSRAT AGAYIASQTV KKVIEINPYL 100
LGTMAGGAAD CSFWERLLAR QCRIYELRNK ERISVAAASK LLANMVYQYK 150
GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI SGATFSVGSG SVYAYGVMDR 200
GYSYDLEVEQ AYDLARRAIY QATYRDAYSG GAVNLYHVRE DGWIRVSSDN 250
VADLHEKYSG STP 263
Length:263
Mass (Da):28,480
Last modified:April 29, 2008 - v3
Checksum:iAED4A73DF41AA6EF
GO
Isoform 2 (identifier: P28074-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:203
Mass (Da):21,845
Checksum:i29788AD9561905AE
GO
Isoform 3 (identifier: P28074-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:160
Mass (Da):17,782
Checksum:i47A97A3A9A849846
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 241R → C.
Corresponds to variant rs11543947 [ dbSNP | Ensembl ].
VAR_051549

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 103103Missing in isoform 3.
VSP_045686Add
BLAST
Alternative sequencei169 – 26395GLYYV…SGSTP → VSEVLCLKPKSFGMYLFCGC AERIGNMARPLLRGQ in isoform 2.
VSP_041263Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 64LASV → IRGR in BAA06097. 1 Publication
Sequence conflicti3 – 53LAS → HEG in BC004146. 1 Publication
Sequence conflicti85 – 851I → F AA sequence 1 Publication
Sequence conflicti109 – 1091A → G in AAB33092. 1 Publication
Sequence conflicti158 – 1581T → S in AAB33092. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS45083.1. [P28074-3]
CCDS45084.1. [P28074-2]
CCDS9584.1. [P28074-1]
PIRiA54589.
I52906.
PC2328.
S08189.
RefSeqiNP_001124197.1. NM_001130725.1. [P28074-3]
NP_001138404.1. NM_001144932.2. [P28074-2]
NP_002788.1. NM_002797.4. [P28074-1]
UniGeneiHs.422990.

Genome annotation databases

EnsembliENST00000361611; ENSP00000355325; ENSG00000100804. [P28074-1]
ENST00000425762; ENSP00000395206; ENSG00000100804. [P28074-3]
ENST00000493471; ENSP00000452424; ENSG00000100804. [P28074-2]
GeneIDi5693.
KEGGihsa:5693.
UCSCiuc001wii.3. human. [P28074-1]
uc001wij.3. human. [P28074-2]

Polymorphism databases

DMDMi187608890.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS45083.1. [P28074-3 ]
CCDS45084.1. [P28074-2 ]
CCDS9584.1. [P28074-1 ]
PIRi A54589.
I52906.
PC2328.
S08189.
RefSeqi NP_001124197.1. NM_001130725.1. [P28074-3 ]
NP_001138404.1. NM_001144932.2. [P28074-2 ]
NP_002788.1. NM_002797.4. [P28074-1 ]
UniGenei Hs.422990.

3D structure databases

ProteinModelPortali P28074.
SMRi P28074. Positions 34-260.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111666. 75 interactions.
DIPi DIP-27540N.
IntActi P28074. 24 interactions.
MINTi MINT-1161576.
STRINGi 9606.ENSP00000355325.

Chemistry

BindingDBi P28074.
ChEMBLi CHEMBL2364701.
DrugBanki DB00188. Bortezomib.
GuidetoPHARMACOLOGYi 2406.

Protein family/group databases

MEROPSi T01.P01.

PTM databases

PhosphoSitei P28074.

Polymorphism databases

DMDMi 187608890.

2D gel databases

REPRODUCTION-2DPAGE IPI00479306.

Proteomic databases

MaxQBi P28074.
PaxDbi P28074.
PRIDEi P28074.

Protocols and materials databases

DNASUi 5693.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361611 ; ENSP00000355325 ; ENSG00000100804 . [P28074-1 ]
ENST00000425762 ; ENSP00000395206 ; ENSG00000100804 . [P28074-3 ]
ENST00000493471 ; ENSP00000452424 ; ENSG00000100804 . [P28074-2 ]
GeneIDi 5693.
KEGGi hsa:5693.
UCSCi uc001wii.3. human. [P28074-1 ]
uc001wij.3. human. [P28074-2 ]

Organism-specific databases

CTDi 5693.
GeneCardsi GC14M023485.
HGNCi HGNC:9542. PSMB5.
HPAi HPA049518.
MIMi 600306. gene.
neXtProti NX_P28074.
PharmGKBi PA33887.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0638.
HOVERGENi HBG108297.
InParanoidi P28074.
KOi K02737.
OMAi LRAIMHA.
PhylomeDBi P28074.
TreeFami TF106223.

Enzyme and pathway databases

Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

GeneWikii PSMB5.
GenomeRNAii 5693.
NextBioi 22114.
PROi P28074.
SOURCEi Search...

Gene expression databases

ArrayExpressi P28074.
Bgeei P28074.
CleanExi HS_PSMB5.
Genevestigatori P28074.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
PRINTSi PR00141. PROTEASOME.
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. "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.
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.
  23. "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.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSB5_HUMAN
AccessioniPrimary (citable) accession number: P28074
Secondary accession number(s): B2R4N9
, B4DUM9, D3DS43, E9PAV2, Q16242, Q6PEW2, Q7Z3B5, Q86T01, Q9TNN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: April 29, 2008
Last modified: September 3, 2014
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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