BAG6_RAT - dbPTM
BAG6_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BAG6_RAT
UniProt AC Q6MG49
Protein Name Large proline-rich protein BAG6 {ECO:0000305}
Gene Name Bag6 {ECO:0000312|RGD:71064}
Organism Rattus norvegicus (Rat).
Sequence Length 1146
Subcellular Localization Cytoplasm, cytosol . Nucleus . Secreted, exosome . Normally localized in cytosol and nucleus, it can also be released extracellularly, in exosomes, by tumor and myeloid dendritic cells.
Protein Description ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates to their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum. Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and are sorted to the proteasome. SGTA which prevents the recruitment of RNF126 to BAG6 may negatively regulate the ubiquitination and the proteasomal degradation of client proteins. Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome. BAG6 is also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, it may participate to the production of antigenic peptides and play a role in antigen presentation in immune response. BAG6 is also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. BAG6 may ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress. By inhibiting the polyubiquitination and subsequent proteasomal degradation of HSPA2 it may also play a role in the assembly of the synaptonemal complex during spermatogenesis. Also positively regulates apoptosis by interacting with and stabilizing the proapoptotic factor AIFM1. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway.; Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2).; Released extracellularly via exosomes, it is a ligand of the natural killer/NK cells receptor NCR3 and stimulates NK cells cytotoxicity. It may thereby trigger NK cells cytotoxicity against neighboring tumor cells and immature myeloid dendritic cells (DC).; May mediate ricin-induced apoptosis..
Protein Sequence MEPSDSTSTAMEEPDSLEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQDYNVGGKVIHLVERAPPQTQLPSGASSGTGSASATHGGGPLPGTRGPGASGHDRNANSYVMVGTFNLPSDGSAVDVHINMEQAPIQSEPRVRLVMAQHMIRDIQTLLSRMECRGGTQAQASQPPPQTPTVASETVALNSQTSEPVESEAPPREPMESEEMEERPPTQTPELPPSGPAPAGPAPAPETNAPNHPSPAEHVEVLQELQRLQRRLQPFLQRYCEVLGAAATTDYNNNHEGREEDQRLINLVGESLRLLGNTFVALSDLRCNLACAPPRHLHVVRPMSHYTTPMVLQQAAIPIQINVGTTVTMTGNGARPPPAPGAEAASPGSGQASSLPPSSATVDSSTEGAPPPGPAPPPATSHPRVIRISHQSVEPVVMMHMNIQDSGAQPGGVPSAPTGPLGPPGHGQSLGQQVPGFPTAPTRVVIARPTPPQARPSHPGGPPVSGALQGAGLGTNTSLAQMVSGLVGQLLMQPVLVAQGTPGMAPASASAPATAQAQAPAPAPAPAPAPATASASAGTTNTATTAGPAPGGPAQPPPPQPSAADLQFSQLLGNLLGPAGPGAGGPSLASPTITVAVPGVPAFLQGMTEFLQASQAAPPPPPPPPPPPPAPEQQTTPPPGSPSGGTASPGGLGPESLPPEFFTSVVQGVLSSLLGSLGARAGSSESIAAFIQRLSGSSNIFEPGADGALGFFGALLSLLCQNFSMVDVVMLLHGHFQPLQRLQPQLRSFFHQHYLGGQEPTSSNIRMATHTLITGLEEYVRESFSLVQVQPGVDIIRTNLEFLQEQFNSIAAHVLHCTDSGFGARLLELCNQGLFECLALNLHCLGGQQMELAAVINGRIRRMSRGVNPSLVSWLTTMMGLRLQVVLEHMPVGPDAILRYVRRIGDPPQALPEEPMEVQGAERTSPEPQREDASPAPGTTAEEAMSRGPPPAPEGGSRDEQDGASADAEPWAAAVPPEWVPIIQQDIQSQRKVKPQPPLSDAYLSGMPAKRRKTMQGEGPQLLLSEAVSRAAKAAGARPLTSPESLSRDLEAPEVQESYRQQLRSDIQKRLQEDPNYSPQRFPNAHRAFADDP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MEPSDSTS
-------CCCCCCCC
59.92-
56UbiquitinationSVSIPSEKQRLIYQG
HCCCCHHHHHHHEEC
45.09-
96PhosphorylationPPQTQLPSGASSGTG
CCCCCCCCCCCCCCC
56.43-
117PhosphorylationGGGPLPGTRGPGASG
CCCCCCCCCCCCCCC
30.43-
977PhosphorylationEVQGAERTSPEPQRE
CCCCCCCCCCCCCCC
39.8923589303
978PhosphorylationVQGAERTSPEPQRED
CCCCCCCCCCCCCCC
33.2223712012
987PhosphorylationEPQREDASPAPGTTA
CCCCCCCCCCCCCCH
33.6423712012
992PhosphorylationDASPAPGTTAEEAMS
CCCCCCCCCHHHHHH
23.0527097102
993PhosphorylationASPAPGTTAEEAMSR
CCCCCCCCHHHHHHC
37.6827097102
999PhosphorylationTTAEEAMSRGPPPAP
CCHHHHHHCCCCCCC
40.9328551015
1067PhosphorylationMPAKRRKTMQGEGPQ
CCCCCCCCCCCCCHH
16.9623984901
1094PhosphorylationAAGARPLTSPESLSR
HCCCCCCCCHHHHHH
44.9427097102
1095PhosphorylationAGARPLTSPESLSRD
CCCCCCCCHHHHHHC
34.0627097102
1098PhosphorylationRPLTSPESLSRDLEA
CCCCCHHHHHHCCCC
34.7228432305
1100PhosphorylationLTSPESLSRDLEAPE
CCCHHHHHHCCCCHH
32.7822673903
1130PhosphorylationRLQEDPNYSPQRFPN
HHHHCCCCCCCCCCC
27.4126022182
1131PhosphorylationLQEDPNYSPQRFPNA
HHHCCCCCCCCCCCH
22.6127097102

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of BAG6_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BAG6_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of BAG6_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of BAG6_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BAG6_RAT

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Related Literatures of Post-Translational Modification

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