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Protein Page:
PSMA6 (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PSMA6 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. 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: 14q13
Cellular Component: cytoplasm; cytosol; myofibril; nuclear matrix; nucleoplasm; nucleus; polysome; proteasome complex; proteasome core complex; sarcomere
Molecular Function: endopeptidase activity; NF-kappaB binding; protein binding; RNA binding; threonine endopeptidase activity
Biological Process: activation of MAPKK activity; activation of NF-kappaB transcription factor; anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; antigen processing and presentation of exogenous peptide antigen via MHC class I; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; antigen processing and presentation of peptide antigen via MHC class I; apoptosis; axon guidance; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; epidermal growth factor receptor signaling pathway; fibroblast growth factor receptor signaling pathway; G1/S transition of mitotic cell cycle; gene expression; innate immune response; insulin receptor signaling pathway; MAPKKK cascade; mitotic cell cycle; negative regulation of apoptosis; negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle; nerve growth factor receptor signaling pathway; polyamine metabolic process; positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle; programmed cell death; protein polyubiquitination; proteolysis involved in cellular protein catabolic process; Ras protein signal transduction; regulation of amino acid metabolic process; regulation of apoptosis; regulation of inflammatory response; regulation of mRNA stability; regulation of ubiquitin-protein ligase activity during mitotic cell cycle; small GTPase mediated signal transduction; stimulatory C-type lectin receptor signaling pathway; T cell receptor signaling pathway; tumor necrosis factor-mediated signaling pathway; vascular endothelial growth factor receptor signaling pathway; viral reproduction
Disease: Myocardial Infarction, Susceptibility To
Reference #:  P60900 (UniProtKB)
Alt. Names/Synonyms: 27 kDa prosomal protein; IOTA; Macropain iota chain; macropain subunit iota; MGC22756; MGC2333; MGC23846; Multicatalytic endopeptidase complex iota chain; p27K; PROS-27; PROS27; prosomal P27K protein; proteasome (prosome, macropain) subunit, alpha type, 6; Proteasome iota chain; Proteasome subunit alpha type-6; proteasome subunit iota; PSA6; PSMA6
Gene Symbols: PSMA6
Molecular weight: 27,399 Da
Basal Isoelectric point: 6.35  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PSMA6

Protein Structure Not Found.


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Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: 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.


 HTP 

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


       human

 
0 3 S5‑p ___MSRGssAGFDRH
0 1 S5 ___MSRGSsAGFDRH
0 1 S6‑p __MSRGssAGFDRHI
0 1 T14‑p AGFDRHItIFsPEGR
0 7 S17‑p DRHItIFsPEGRLyQ
0 109 Y23‑p FsPEGRLyQVEyAFk
0 3 Y27‑p GRLyQVEyAFkAINQ
0 1 K30 yQVEyAFKAINQGGL
0 7 K30‑ub yQVEyAFkAINQGGL
0 24 K45‑ub TSVAVRGkDCAVIVT
0 1 K45‑ac TSVAVRGkDCAVIVT
0 1 K55‑ac AVIVTQKkVPDkLLD
0 89 K55‑ub AVIVTQKkVPDkLLD
0 2 K59‑ac TQKkVPDkLLDssTV
1 17 K59‑ub TQKkVPDkLLDssTV
0 2 S63‑p VPDkLLDssTVTHLF
0 2 S64‑p PDkLLDssTVTHLFk
0 1 K71‑ub sTVTHLFkItENIGC
0 1 T73‑p VTHLFkItENIGCVM
0 16 Y96‑p SQVQRARyEAANWky
0 2 K102‑ac RyEAANWkykyGyEI
0 93 K102‑ub RyEAANWkykyGyEI
0 1 K102‑sc RyEAANWkykyGyEI
0 12 Y103‑p yEAANWkykyGyEIP
1 22 K104‑ac EAANWkykyGyEIPV
0 8 K104‑ub EAANWkykyGyEIPV
0 4 Y105‑p AANWkykyGyEIPVD
0 1 Y107‑p NWkykyGyEIPVDML
0 15 K116‑ac IPVDMLCkRIADISQ
0 5 K116‑ub IPVDMLCkRIADISQ
0 2 K153‑ub EQGPQVYkCDPAGyy
0 46 Y159‑p YkCDPAGyyCGFkAT
0 37 Y160‑p kCDPAGyyCGFkATA
0 18 K164‑ub AGyyCGFkATAAGVk
0 16 K171‑ub kATAAGVkQTESTSF
0 7 K181‑ac ESTSFLEkkVKKKFD
0 16 K181‑ub ESTSFLEkkVKKKFD
0 1 K181‑sc ESTSFLEkkVKKKFD
0 1 K182‑ub STSFLEkkVKKKFDW
  mouse

 
S5 ___MSRGSSAGFDRH
S5‑gl ___MSRGsSAGFDRH
S6 __MSRGsSAGFDRHI
T14 AGFDRHITIFsPEGR
S17‑p DRHITIFsPEGRLyQ
Y23‑p FsPEGRLyQVEYAFk
Y27 GRLyQVEYAFkAINQ
K30‑ac yQVEYAFkAINQGGL
K30 yQVEYAFKAINQGGL
K45‑ub TSVAVRGkDCAVIVT
K45 TSVAVRGKDCAVIVT
K55 AVIVTQKKVPDKLLD
K55‑ub AVIVTQKkVPDKLLD
K59 TQKkVPDKLLDssTV
K59 TQKkVPDKLLDssTV
S63‑p VPDKLLDssTVTHLF
S64‑p PDKLLDssTVTHLFK
K71 sTVTHLFKITESIGC
T73 VTHLFKITESIGCVM
Y96‑p SQVQRARyEAANWky
K102‑ac RyEAANWkykYGYEI
K102‑ub RyEAANWkykYGYEI
K102 RyEAANWKykYGYEI
Y103‑p yEAANWkykYGYEIP
K104‑ac EAANWkykYGYEIPV
K104 EAANWkyKYGYEIPV
Y105 AANWkykYGYEIPVD
Y107 NWkykYGYEIPVDML
K116 IPVDMLCKRIADISQ
K116 IPVDMLCKRIADISQ
K153 EQGPQVYKCDPAGyy
Y159‑p YKCDPAGyyCGFKAT
Y160‑p KCDPAGyyCGFKATA
K164 AGyyCGFKATAAGVk
K171‑ub KATAAGVkQTESTSF
K181‑ac ESTSFLEkKVKKKFD
K181‑ub ESTSFLEkKVKKKFD
K181‑sc ESTSFLEkKVKKKFD
K182 STSFLEkKVKKKFDW
  rat

 
S5 ___MSRGSSAGFDRH
S5 ___MSRGSSAGFDRH
S6 __MSRGSSAGFDRHI
T14 AGFDRHITIFSPEGR
S17 DRHITIFSPEGRLyQ
Y23‑p FSPEGRLyQVEYAFK
Y27 GRLyQVEYAFKAINQ
K30 yQVEYAFKAINQGGL
K30 yQVEYAFKAINQGGL
K45 TSVAVRGKDCAVIVT
K45 TSVAVRGKDCAVIVT
K55 AVIVTQKKVPDkLLD
K55 AVIVTQKKVPDkLLD
K59‑ac TQKKVPDkLLDSSTV
K59 TQKKVPDKLLDSSTV
S63 VPDkLLDSSTVTHLF
S64 PDkLLDSSTVTHLFK
K71 STVTHLFKITENIGC
T73 VTHLFKITENIGCVM
Y96‑p SQVQRARyEAANWkY
K102 RyEAANWKYkYGYEI
K102‑ub RyEAANWkYkYGYEI
K102 RyEAANWKYkYGYEI
Y103 yEAANWkYkYGYEIP
K104‑ac EAANWkYkYGYEIPV
K104 EAANWkYKYGYEIPV
Y105 AANWkYkYGYEIPVD
Y107 NWkYkYGYEIPVDML
K116 IPVDMLCKRIADISQ
K116 IPVDMLCKRIADISQ
K153 EQGPQVYKCDPAGYY
Y159 YKCDPAGYYCGFKAT
Y160 KCDPAGYYCGFKATA
K164 AGYYCGFKATAAGVK
K171 KATAAGVKQTESTSF
K181‑ac ESTSFLEkKVKKKFD
K181 ESTSFLEKKVKKKFD
K181 ESTSFLEKKVKKKFD
K182 STSFLEkKVKKKFDW
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