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Protein Page:
PSMB5 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PSMB5 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. Belongs to the peptidase T1B family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Proteasome complex; EC 3.4.25.1; Protease
Cellular Component: proteasome complex; nucleoplasm; proteasome core complex; nucleolus; nucleus; cytosol
Molecular Function: threonine endopeptidase activity; protein binding
Biological Process: positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle; negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle; protein polyubiquitination; viral reproduction; apoptosis; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; mRNA metabolic process; regulation of apoptosis; antigen processing and presentation of peptide antigen via MHC class I; regulation of ubiquitin-protein ligase activity during mitotic cell cycle; RNA metabolic process; anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; antigen processing and presentation of exogenous peptide antigen via MHC class I; gene expression; mitotic cell cycle; response to oxidative stress; regulation of amino acid metabolic process; G1/S transition of mitotic cell cycle; negative regulation of apoptosis
Reference #:  P28074 (UniProtKB)
Alt. Names/Synonyms: LMPX; Macropain epsilon chain; MB1; MGC104214; Multicatalytic endopeptidase complex epsilon chain; proteasome (prosome, macropain) subunit, beta type, 5; proteasome beta 5 subunit; proteasome catalytic subunit 3; Proteasome chain 6; Proteasome epsilon chain; Proteasome subunit beta type-5; Proteasome subunit MB1; Proteasome subunit X; proteasome subunit, beta type, 5; PSB5; PSMB5; PSX large multifunctional protease X; X
Gene Symbols: PSMB5
Molecular weight: 28,480 Da
Basal Isoelectric point: 6.44  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PSMB5

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 S87-p TAGAYIAsQTVkkVI
0 53 K91-ub YIAsQTVkkVIEINP
0 6 K92-ub IAsQTVkkVIEINPy
0 5 Y99-p kVIEINPyLLGTMAG
0 2 S139-p RISVAAAsKLLANMV
0 40 Y149-p LANMVYQyKGMGLSM
0 1 T158 GMGLSMGTMICGWDK
0 15 Y171-p DKRGPGLyYVDSEGN
0 1 E207 RGYSYDLEVEQAYDL
0 3 E207 RGYSYDLEVEQAYDL
0 124 Y220-p DLARRAIyQATYRDA
0 34 Y228-p QATYRDAySGGAVNL
0 62 Y236-p SGGAVNLyHVREDGW
0 1 K257-ac NVADLHEkYSGstP_
0 3 K257-ub NVADLHEkYSGstP_
0 2 S261-p LHEkYSGstP_____
0 17 T262-p HEkYSGstP______
  PSMB5 iso2  
S87 TAGAYIASQTVKKVI
K91 YIASQTVKKVIEINP
K92 IASQTVKKVIEINPY
Y99 KVIEINPYLLGTMAG
S139 RISVAAASKLLANMV
Y149 LANMVYQYKGMGLSM
T158-p GMGLSMGtMICGWDK
Y183 KPKSFGMYLFCGCAE
- under review  
- gap
- gap
- gap
- gap
P198 RIGNMARPLLRGQ__
- gap
- gap
- gap
  mouse

 
S87 TAGAYIASQTVkkVI
K91-ub YIASQTVkkVIEINP
K92-ub IASQTVkkVIEINPY
Y99 kVIEINPYLLGTMAG
S139 RISVAAASKLLANMV
Y149 LANMVYQYKGMGLSM
T158 GMGLSMGTMICGWDK
Y171-p DKRGPGLyYVDSEGN
K207-ac RGYSYDLkVEEAYDL
K207-ub RGYSYDLkVEEAYDL
Y220-p DLARRAIyQATYRDA
Y228 QATYRDAYSGGAVNL
Y236-p SGGAVNLyHVREDGW
K257-ac NVADLHDkYSSVSVP
K257 NVADLHDKYSSVSVP
S262 HDkYSSVSVP_____
V263 DkYSSVSVP______
  rat

 
S87 TAGAYIASQTVkKVI
K91-ub YIASQTVkKVIEINP
K92 IASQTVkKVIEINPY
Y99 KVIEINPYLLGTMAG
S139 RISVAAASKLLANMV
Y149-p LANMVYQyKGMGLSM
T158 GMGLSMGTMICGWDK
Y171 DKRGPGLYYVDSEGN
Q207 RGYSYDLQVEEAYDL
Q207 RGYSYDLQVEEAYDL
Y220 DLARRAIYQATYRDA
Y228 QATYRDAYSGGAVNL
Y236 SGGAVNLYHVREDGW
K257 NVADLHDKYTSSIP_
K257 NVADLHDKYTSSIP_
S261 LHDKYTSSIP_____
I262 HDKYTSSIP______
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