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Protein Page:
PSMA7 (human)
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
PSMA7 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. Plays an important role in the regulation of cell proliferation or cell cycle control, transcriptional regulation, immune and stress response, cell differentiation, and apoptosis. Interacts with some important proteins involved in transcription factor regulation, cell cycle transition, viral replication and even tumor initiation and progression. Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response. 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. PSMA7 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly. Interacts with HIV-1 TAT protein. Interacts with hepatitis B virus X protein (HBX). Interacts with HIF1A. Interacts with RAB7A. Interacts with PARK2. Interacts with ABL1 and ABL2. Interacts with EMAP2. Interacts with MAVS. Down-regulated by the ribozyme Rz3'X. Up-regulated in colorectal cancer tissues. Belongs to the peptidase T1A family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.25.1; Protease; Proteasome complex
Chromosomal Location of Human Ortholog: 20q13.33
Cellular Component: cytosol; nucleoplasm; nucleus; proteasome complex; proteasome core complex
Molecular Function: identical protein binding; protein binding
Biological Process: anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; MAPKKK cascade; negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle; positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle; proteasomal ubiquitin-dependent protein catabolic process; protein polyubiquitination; regulation of amino acid metabolic process; regulation of mRNA stability; stimulatory C-type lectin receptor signaling pathway; T cell receptor signaling pathway; tumor necrosis factor-mediated signaling pathway; Wnt receptor signaling pathway, planar cell polarity pathway
Reference #:  O14818 (UniProtKB)
Alt. Names/Synonyms: C6; HSPC; MGC3755; proteasome (prosome, macropain) subunit, alpha type, 7; proteasome subunit alpha 4; Proteasome subunit alpha type-7; Proteasome subunit RC6-1; Proteasome subunit XAPC7; PSA7; PSMA7; RC6-1; XAPC7
Gene Symbols: PSMA7
Molecular weight: 27,887 Da
Basal Isoelectric point: 8.6  Predict pI for various phosphorylation states
Select Structure to View Below

PSMA7

Protein Structure Not Found.
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Download ChimeraX Script


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Sites Implicated In
cell cycle regulation: Y153‑p
enzymatic activity, inhibited: Y153‑p
protein stabilization: Y106‑p
ubiquitination: Y106‑p

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



 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

► Hide Isoforms
 
0 1 S2‑p ______MsYDRAITV
0 6 S11‑p DRAITVFsPDGHLFQ
0 1 Y21‑p GHLFQVEyAQEAVKk
0 6 K28‑ub yAQEAVKkGSTAVGV
0 1 S30 QEAVKkGSTAVGVRG
0 1 T31 EAVKkGSTAVGVRGR
0 1 R38 TAVGVRGRDIVVLGV
0 1 K47 IVVLGVEKKSVAkLQ
0 3 K52‑ac VEKKSVAkLQDERTV
0 30 K52‑ub VEKKSVAkLQDERTV
1 3 Y106‑p EDPVTVEyItRYIAS
0 1 T108‑p PVTVEyItRYIASLk
0 2 K115‑ub tRYIASLkQRYTQSN
0 1 K115‑sc tRYIASLkQRYTQSN
0 1 S130 GRRPFGISALIVGFD
2 68 Y153‑p QTDPSGTyHAWkANA
0 3 K157‑ac SGTyHAWkANAIGrG
0 8 K157‑ub SGTyHAWkANAIGrG
0 1 R163‑m1 WkANAIGrGAKsVRE
0 1 S167‑p AIGrGAKsVREFLEk
0 1 K174 sVREFLEKNYtDEAI
0 18 K174‑ub sVREFLEkNYtDEAI
0 1 T177‑p EFLEkNYtDEAIEtD
0 1 T183‑p YtDEAIEtDDLTIKL
0 4 K193‑ub LTIKLVIkALLEVVQ
0 4 S201‑p ALLEVVQsGGkNIEL
0 19 K204‑ub EVVQsGGkNIELAVM
0 3 K218‑ub MRRDQSLkILNPEEI
0 2 K227‑ac LNPEEIEkYVAEIEk
0 4 K227‑ub LNPEEIEkYVAEIEk
0 2 K234‑ac kYVAEIEkEKEENEK
0 2 K234‑ub kYVAEIEkEKEENEK
  PSMA7 iso2  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
Y36 EDPVTVEYITRYIAS
T38 PVTVEYITRYIASLK
K45 TRYIASLKQRYTQSN
K45 TRYIASLKQRYTQSN
S60 GRRPFGISALIVGFD
Y83 QTDPSGTYHAWKANA
K87 SGTYHAWKANAIGRG
K87 SGTYHAWKANAIGRG
R93 WKANAIGRGAKSVRE
S97 AIGRGAKSVREFLEK
K104 SVREFLEKNYTDEAI
K104 SVREFLEKNYTDEAI
T107 EFLEKNYTDEAIETD
T113 YTDEAIETDDLTIKL
K123 LTIKLVIKALLEVVQ
S131 ALLEVVQSGGKNIEL
K134 EVVQSGGKNIELAVM
K148 MRRDQSLKILNPEEI
K157 LNPEEIEKYVAEIEK
K157 LNPEEIEKYVAEIEK
K164 KYVAEIEKEKEENEK
K164 KYVAEIEKEKEENEK
  mouse

 
S2 ______MSYDRAITV
S11 DRAITVFSPDGHLFQ
Y21 GHLFQVEYAQEAVKK
K28 YAQEAVKKGstAVGV
S30‑p QEAVKKGstAVGVRG
T31‑p EAVKKGstAVGVRGk
K38‑ub tAVGVRGkDIVVLGV
K47‑sc IVVLGVEkKSVAkLQ
K52‑ac VEkKSVAkLQDERTV
K52 VEkKSVAKLQDERTV
Y106 EDPVTVEYITRYIAS
T108 PVTVEYITRYIASLk
K115‑ub TRYIASLkQRYTQSN
K115 TRYIASLKQRYTQSN
S130‑gl GRRPFGIsALIVGFD
Y153‑p QTDPSGTyHAWkANA
K157 SGTyHAWKANAIGRG
K157‑ub SGTyHAWkANAIGRG
R163 WkANAIGRGAKSVRE
S167 AIGRGAKSVREFLEk
K174‑ac SVREFLEkNYTDDAI
K174‑ub SVREFLEkNYTDDAI
T177 EFLEkNYTDDAIETD
T183 YTDDAIETDDLTIKL
K193 LTIKLVIKALLEVVQ
S201 ALLEVVQSGGkNIEL
K204‑ub EVVQSGGkNIELAVM
K218 MRRDQPLKILNPEEI
K227‑ac LNPEEIEkYVAEIEk
K227‑ub LNPEEIEkYVAEIEk
K234‑ac kYVAEIEkEKEENEK
K234‑ub kYVAEIEkEKEENEK
  rat

 
S2 ______MSYDRAITV
S11 DRAITVFSPDGHLFQ
Y21 GHLFQVEYAQEAVKK
K28 YAQEAVKKGSTAVGV
S30 QEAVKKGSTAVGVRG
T31 EAVKKGSTAVGVRGR
R38 TAVGVRGRDIVVLGV
K47 IVVLGVEKKSVAkLQ
K52‑ac VEKKSVAkLQDERTV
K52 VEKKSVAKLQDERTV
Y106‑p EDPVTVEyITRYIAS
T108 PVTVEyITRYIASLK
K115 TRYIASLKQRYTQSN
K115 TRYIASLKQRYTQSN
S130 GRRPFGISALIVGFD
Y153 QTDPSGTYHAWKANA
K157 SGTYHAWKANAIGRG
K157 SGTYHAWKANAIGRG
R163 WKANAIGRGAKSVRE
S167 AIGRGAKSVREFLEK
K174 SVREFLEKNYTDDAI
K174 SVREFLEKNYTDDAI
T177 EFLEKNYTDDAIETD
T183 YTDDAIETDDLTIKL
K193 LTIKLVIKALLEVVQ
S201 ALLEVVQSGGKNIEL
K204 EVVQSGGKNIELAVM
K218 MRRDQPLKILSPEEI
K227 LSPEEIEKYVAEIEK
K227 LSPEEIEKYVAEIEK
K234 KYVAEIEKEKEENEK
K234 KYVAEIEKEKEENEK
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