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Protein Page:
PSMA5 (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
PSMA5 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. 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. PSMA5 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly. Up-regulated in colon cancer cell lines. Up-regulated in fetal Down syndrome (DS) brain. May be the target of the transcriptional activator NFE2L2. Expressed in fetal brain. Belongs to the peptidase T1A family. Note: This description may include information from UniProtKB.
Protein type: Proteasome complex; EC 3.4.25.1; Protease
Chromosomal Location of Human Ortholog: 1p13
Cellular Component: proteasome complex; nucleoplasm; proteasome core complex; cytoplasm; 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; anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; RNA metabolic process; antigen processing and presentation of exogenous peptide antigen via MHC class I; gene expression; mitotic cell cycle; regulation of amino acid metabolic process; negative regulation of apoptosis; G1/S transition of mitotic cell cycle
Reference #:  P28066 (UniProtKB)
Alt. Names/Synonyms: macropain subunit zeta; Macropain zeta chain; MGC117302; MGC125802; MGC125803; MGC125804; Multicatalytic endopeptidase complex zeta chain; proteasome (prosome, macropain) subunit, alpha type, 5; proteasome alpha 5 subunit; proteasome component 5; Proteasome subunit alpha type-5; proteasome subunit zeta; Proteasome zeta chain; PSA5; PSC5; PSMA5; ZETA
Gene Symbols: PSMA5
Molecular weight: 26,411 Da
Basal Isoelectric point: 4.74  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PSMA5

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

 
0 2 S6-p __MFLTRsEyDRGVN
0 54 Y8-p MFLTRsEyDRGVNTF
0 22 S16-p DRGVNTFsPEGRLFQ
0 38 Y26-p GRLFQVEyAIEAIKL
0 1 T36-p EAIKLGStAIGIQTs
0 1 S43-p tAIGIQTsEGVCLAV
0 7 T55-p LAVEKRItsPLMEPS
0 28 S56-p AVEKRItsPLMEPSs
0 4 S63-p sPLMEPSsIEKIVEI
0 1 S79-p AHIGCAMsGLIADAk
0 9 K86-ub sGLIADAkTLIDkAR
0 9 K91-ub DAkTLIDkARVETQN
0 1 K91-ac DAkTLIDkARVETQN
0 1 K149-ub LFGGVDEkGPQLFHM
0 1 S172-p CDARAIGsASEGAQS
0 1 Y185-p QSSLQEVyHkSMTLk
0 8 K187-ub SLQEVyHkSMTLkEA
0 36 K192-ub yHkSMTLkEAIkSSL
0 1 K192-sc yHkSMTLkEAIkSSL
0 4 K196-ub MTLkEAIkSSLIILk
0 1 S198 LkEAIkSSLIILkQV
1 0 K203 kSSLIILKQVMEEkL
0 7 K203-ub kSSLIILkQVMEEkL
0 1 K209-ac LkQVMEEkLNATNIE
0 6 K209-ub LkQVMEEkLNATNIE
0 3 K231-ub QNFHMFTkEELEEVI
0 1 K239 EELEEVIKDI_____
0 5 K239-ub EELEEVIkDI_____
0 1 K239-sc EELEEVIkDI_____
  mouse

 
S6 __MFLTRSEYDRGVN
Y8 MFLTRSEYDRGVNTF
S16-p DRGVNTFsPEGRLFQ
Y26-p GRLFQVEyAIEAIKL
T36 EAIKLGSTAIGIQTS
S43 TAIGIQTSEGVCLAV
T55-p LAVEKRItsPLMEPS
S56-p AVEKRItsPLMEPSS
S63 sPLMEPSSIEKIVEI
S79 AHIGCAMSGLIADAK
K86 SGLIADAKTLIDKAR
K91 DAKTLIDKARVETQN
K91 DAKTLIDKARVETQN
K149 LFGGVDEKGPQLFHM
S172 CDARAIGSASEGAQS
Y185 QSSLQEVYHkSMTLk
K187-ub SLQEVYHkSMTLkEA
K192-ub YHkSMTLkEAIkSsL
K192-sc YHkSMTLkEAIkSsL
K196-ub MTLkEAIkSsLIILk
S198-gl LkEAIkSsLIILkQV
K203-ac kSsLIILkQVMEEKL
K203 kSsLIILKQVMEEKL
K209 LkQVMEEKLNATNIE
K209 LkQVMEEKLNATNIE
K231 QNFHMFTKEELEEVI
K239-ac EELEEVIkDI_____
K239 EELEEVIKDI_____
K239 EELEEVIKDI_____
  rat

 
S6 __MFLTRSEYDRGVN
Y8 MFLTRSEYDRGVNTF
S16-p DRGVNTFsPEGRLFQ
Y26 GRLFQVEYAIEGHKL
T36 EGHKLGSTAIGIQTS
S43 TAIGIQTSEGVCLAV
T55 LAVEKRITsPLMEPS
S56-p AVEKRITsPLMEPSS
S63 sPLMEPSSIEKIVEI
S79 AHIGCAMSGLIADAK
K86 SGLIADAKTLIDkAR
K91 DAKTLIDKARVETQN
K91-ac DAKTLIDkARVETQN
K149 LFGGVDEKGPQLFHM
S172 CDARAIGSASEGAQS
Y185 QSSLQEVYHKSTTLK
K187 SLQEVYHKSTTLKEA
K192 YHKSTTLKEAIKSSL
K192 YHKSTTLKEAIKSSL
K196 TTLKEAIKSSLIILK
S198 LKEAIKSSLIILKQV
K203 KSSLIILKQVMEEKL
K203 KSSLIILKQVMEEKL
K209 LKQVMEEKLNATNIE
K209 LKQVMEEKLNATNIE
K231 QNFHMFTKEELEEVI
K239 EELEEVIKDI_____
K239 EELEEVIKDI_____
K239 EELEEVIKDI_____
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