Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
RPT6 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
RPT6 The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex. Belongs to the AAA ATPase family. Note: This description may include information from UniProtKB.
Protein type: Proteasome complex; Ubiquitin conjugating system; Nuclear receptor co-regulator
Cellular Component: nucleoplasm; proteasome complex; cytoplasm; inclusion body; cytoplasmic vesicle; cytosol; nucleus
Molecular Function: thyrotropin-releasing hormone receptor binding; protein binding; TATA-binding protein binding; ATPase activity; transcription cofactor activity; transcription factor binding; ATP binding
Biological Process: positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle; transcription from RNA polymerase II promoter; proteasomal ubiquitin-dependent protein catabolic process; negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle; protein polyubiquitination; viral reproduction; apoptosis; positive regulation of transcription, DNA-dependent; 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; negative regulation of programmed cell death; antigen processing and presentation of exogenous peptide antigen via MHC class I; gene expression; mitotic cell cycle; negative regulation of transcription, DNA-dependent; regulation of amino acid metabolic process; G1/S transition of mitotic cell cycle; negative regulation of apoptosis
Reference #:  P62195 (UniProtKB)
Alt. Names/Synonyms: 26S protease regulatory subunit 8; 26S proteasome AAA-ATPase subunit RPT6; MSUG1 protein; p45; p45/SUG; proteasome (prosome, macropain) 26S subunit, ATPase, 5; proteasome 26S ATPase subunit 5; Proteasome 26S subunit ATPase 5; Proteasome subunit p45; PRS8; PSMC5; RPT6; S8; SUG-1; SUG1; Tat-binding protein homolog 10; TBP10; Thyroid hormone receptor-interacting protein 1; thyroid receptor interactor 1; TRIP1
Gene Symbols: PSMC5
Molecular weight: 45,626 Da
Basal Isoelectric point: 7.11  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RPT6

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Source  |  NURSA  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  Ensembl Protein


Sites Implicated In
activity, induced: S120‑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


 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 1 D4 ____MALDGPEQMEL
0 2 K15-u QMELEEGkAGSGLRQ
0 7 K38-u LQLIVNDkSQNLRRL
0 7 K55-u QRNELNAkVRLLREE
0 4 K88-u DKKKVLVkVHPEGkF
0 21 K94-u VkVHPEGkFVVDVDk
0 29 K101-u kFVVDVDkNIDINDV
6 2 S120-p RVALRNDsyTLHkIL
0 7 Y121-p VALRNDsyTLHkILP
0 3 K125-u NDsyTLHkILPNkVD
0 2 K130-u LHkILPNkVDPLVsL
0 1 S136-p NkVDPLVsLMMVEKV
0 1 K156-u EMIGGLDkQIKEIkE
0 1 K162-u DkQIKEIkEVIELPV
0 2 K170-u EVIELPVkHPELFEA
0 1 K184-u ALGIAQPkGVLLyGP
0 5 Y189-p QPkGVLLyGPPGTGk
0 6 K196-u yGPPGTGktLLARAV
0 1 T197-p GPPGTGktLLARAVA
0 1 K222-a SGSELVQkFIGEGAR
0 13 K222-u SGSELVQkFIGEGAR
0 1 S244-p MAREHAPsIIFMDEI
0 1 S256-p DEIDSIGssRLEGGS
0 1 S257-p EIDSIGssRLEGGSG
0 1 T272 GDSEVQRTMLELLNQ
0 24 K287-u LDGFEATkNIkVIMA
0 13 K290-u FEATkNIkVIMATNR
0 3 S303-p NRIDILDsALLRPGR
0 1 K314-u RPGRIDRkIEFPPPN
0 5 K330-u EARLDILkIHSRKMN
0 2 K346-u TRGINLRkIAELMPG
0 1 K389-u DFEMAVAkVMQKDSE
0 10 K397-u VMQKDSEkNMSIkkL
0 3 K402-u SEkNMSIkkLWK___
0 2 K403-u EkNMSIkkLWK____
  mouse

 
D4-ca ____MALdGPEQMEL
K15 QMELEEGKAGSGLRQ
K38-u LQLIVNDkSQNLRRL
K55 QRNELNAKVRLLREE
K88-u DKKKVLVkVHPEGKF
K94 VkVHPEGKFVVDVDk
K101-u KFVVDVDkNIDINDV
S120-p RVALRNDsYTLHkIL
Y121 VALRNDsYTLHkILP
K125-u NDsYTLHkILPNKVD
K130 LHkILPNKVDPLVSL
S136 NKVDPLVSLMMVEKV
K156 EMIGGLDKQIKEIKE
K162 DKQIKEIKEVIELPV
K170-u EVIELPVkHPELFEA
K184 ALGIAQPKGVLLyGP
Y189-p QPKGVLLyGPPGTGk
K196-u yGPPGTGkTLLARAV
T197 GPPGTGkTLLARAVA
K222 SGSELVQKFIGEGAR
K222-u SGSELVQkFIGEGAR
S244 MAREHAPSIIFMDEI
S256 DEIDSIGSSRLEGGS
S257 EIDSIGSSRLEGGSG
T272-gl GDSEVQRtMLELLNQ
K287-u LDGFEATkNIKVIMA
K290 FEATkNIKVIMATNR
S303 NRIDILDSALLRPGR
K314 RPGRIDRKIEFPPPN
K330-u EARLDILkIHSRKMN
K346 TRGINLRKIAELMPG
K389 DFEMAVAKVMQKDSE
K397 VMQKDSEKNMSIKKL
K402 SEKNMSIKKLWK___
K403 EKNMSIKKLWK____
  rat

 
D4 ____MALDGPEQMEL
K15 QMELEEGKAGSGLRQ
K38 LQLIVNDKSQNLRRL
K55 QRNELNAKVRLLREE
K88 DKKKVLVKVHPEGKF
K94 VKVHPEGKFVVDVDK
K101 KFVVDVDKNIDINDV
S120-p RVALRNDsYTLHKIL
Y121 VALRNDsYTLHKILP
K125 NDsYTLHKILPNKVD
K130 LHKILPNKVDPLVSL
S136 NKVDPLVSLMMVEKV
K156 EMIGGLDKQIKEIKE
K162 DKQIKEIKEVIELPV
K170 EVIELPVKHPELFEA
K184 ALGIAQPKGVLLYGP
Y189 QPKGVLLYGPPGTGK
K196 YGPPGTGKTLLARAV
T197 GPPGTGKTLLARAVA
K222 SGSELVQKFIGEGAR
K222 SGSELVQKFIGEGAR
S244 MAREHAPSIIFMDEI
S256 DEIDSIGSSRLEGGS
S257 EIDSIGSSRLEGGSG
T272 GDSEVQRTMLELLNQ
K287 LDGFEATKNIKVIMA
K290 FEATKNIKVIMATNR
S303 NRIDILDSALLRPGR
K314 RPGRIDRKIEFPPPN
K330 EARLDILKIHSRKMN
K346 TRGINLRKIAELMPG
K389 DFEMAVAKVMQKDSE
K397 VMQKDSEKNMSIKKL
K402 SEKNMSIKKLWK___
K403 EKNMSIKKLWK____
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.