CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007792
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Large proline-rich protein BAG6 
Protein Synonyms/Alias
 BAG family molecular chaperone regulator 6; BCL2-associated athanogene 6; BAG-6; BAG6; HLA-B-associated transcript 3; Protein G3; Protein Scythe 
Gene Name
 BAG6 
Gene Synonyms/Alias
 BAT3; G3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
22DSLEVLVKTLDSQTRubiquitination[1, 2]
40VGAQMNVKEFKEHIAubiquitination[1, 2, 3, 4]
56SVSIPSEKQRLIYQGacetylation[5]
56SVSIPSEKQRLIYQGubiquitination[1, 3]
70GRVLQDDKKLQEYNVubiquitination[6]
71RVLQDDKKLQEYNVGubiquitination[3, 6]
80QEYNVGGKVIHLVERubiquitination[1, 3, 7]
1033IQSQRKVKPQPPLSDubiquitination[3, 4]
1049YLSGMPAKRRKTMQGubiquitination[1]
1052GMPAKRRKTMQGEGPubiquitination[1, 3]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 Chaperone that plays a key role in various processes such as apoptosis, insertion of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane and regulation of chromatin. Acts in part by regulating stability of proteins and their degradation by the proteasome. Participates in endoplasmic reticulum stress-induced apoptosis via its interaction with AIFM1/AIF by regulating AIFM1/AIF stability and preventing its degradation. Also required during spermatogenesis for synaptonemal complex assembly via its interaction with HSPA2, by inhibiting polyubiquitination and subsequent proteasomal degradation of HSPA2. Required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, may play a role in immuno-proteasomes to generate antigenic peptides via targeted degradation, thereby playing a role in antigen presentation in immune response. Key component of the BAG6/BAT3 complex, a cytosolic multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. BAG6/BAT3 acts by facilitating TA membrane proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins and transfers them to ASNA1/TRC40 for targeting to the endoplasmic reticulum membrane. 
Sequence Annotation
 DOMAIN 17 92 Ubiquitin-like.
 REPEAT 242 270 1.
 REPEAT 415 443 2.
 REPEAT 574 602 3.
 REPEAT 608 636 4.
 REGION 242 636 4 X 29 AA approximate repeats.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 113 113 Phosphoserine.
 MOD_RES 350 350 Phosphothreonine.
 MOD_RES 964 964 Phosphoserine.
 MOD_RES 973 973 Phosphoserine.
 MOD_RES 1081 1081 Phosphoserine.
 MOD_RES 1117 1117 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Apoptosis; Chaperone; Chromatin regulator; Complete proteome; Cytoplasm; Differentiation; Immunity; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Spermatogenesis; Transport; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1132 AA 
Protein Sequence
MEPNDSTSTA VEEPDSLEVL VKTLDSQTRT FIVGAQMNVK EFKEHIAASV SIPSEKQRLI 60
YQGRVLQDDK KLQEYNVGGK VIHLVERAPP QTHLPSGASS GTGSASATHG GGSPPGTRGP 120
GASVHDRNAN SYVMVGTFNL PSDGSAVDVH INMEQAPIQS EPRVRLVMAQ HMIRDIQTLL 180
SRMETLPYLQ CRGGPQPQHS QPPPQPPAVT PEPVALSSQT SEPVESEAPP REPMEAEEVE 240
ERAPAQNPEL TPGPAPAGPT PAPETNAPNH PSPAEYVEVL QELQRLESRL QPFLQRYYEV 300
LGAAATTDYN NNHEGREEDQ RLINLVGESL RLLGNTFVAL SDLRCNLACT PPRHLHVVRP 360
MSHYTTPMVL QQAAIPIQIN VGTTVTMTGN GTRPPPTPNA EAPPPGPGQA SSVAPSSTNV 420
ESSAEGAPPP GPAPPPATSH PRVIRISHQS VEPVVMMHMN IQDSGTQPGG VPSAPTGPLG 480
PPGHGQTLGQ QVPGFPTAPT RVVIARPTPP QARPSHPGGP PVSGTLQGAG LGTNASLAQM 540
VSGLVGQLLM QPVLVAQGTP GMAPPPAPAT ASASAGTTNT ATTAGPAPGG PAQPPPTPQP 600
SMADLQFSQL LGNLLGPAGP GAGGSGVASP TITVAMPGVP AFLQGMTDFL QATQTAPPPP 660
PPPPPPPPAP EQQTMPPPGS PSGGAGSPGG LGLESLSPEF FTSVVQGVLS SLLGSLGARA 720
GSSESIAAFI QRLSGSSNIF EPGADGALGF FGALLSLLCQ NFSMVDVVML LHGHFQPLQR 780
LQPQLRSFFH QHYLGGQEPT PSNIRMATHT LITGLEEYVR ESFSLVQVQP GVDIIRTNLE 840
FLQEQFNSIA AHVLHCTDSG FGARLLELCN QGLFECLALN LHCLGGQQME LAAVINGRIR 900
RMSRGVNPSL VSWLTTMMGL RLQVVLEHMP VGPDAILRYV RRVGDPPQPL PEEPMEVQGA 960
ERASPEPQRE NASPAPGTTA EEAMSRGPPP APEGGSRDEQ DGASAETEPW AAAVPPEWVP 1020
IIQQDIQSQR KVKPQPPLSD AYLSGMPAKR RKTMQGEGPQ LLLSEAVSRA AKAAGARPLT 1080
SPESLSRDLE APEVQESYRQ QLRSDIQKRL QEDPNYSPQR FPNAQRAFAD DP 1132 
Gene Ontology
 GO:0071818; C:BAT3 complex; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0031593; F:polyubiquitin binding; ISS:UniProtKB.
 GO:0070628; F:proteasome binding; ISS:UniProtKB.
 GO:0043022; F:ribosome binding; IDA:UniProtKB.
 GO:0007420; P:brain development; ISS:UniProtKB.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0009790; P:embryo development; ISS:UniProtKB.
 GO:0018393; P:internal peptidyl-lysine acetylation; IDA:UniProtKB.
 GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:UniProtKB.
 GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
 GO:0001822; P:kidney development; ISS:UniProtKB.
 GO:0030324; P:lung development; ISS:UniProtKB.
 GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
 GO:0050821; P:protein stabilization; ISS:UniProtKB.
 GO:0042127; P:regulation of cell proliferation; IEA:Compara.
 GO:0007283; P:spermatogenesis; ISS:UniProtKB.
 GO:0007130; P:synaptonemal complex assembly; ISS:UniProtKB.
 GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:UniProtKB.
 GO:0006810; P:transport; IEA:UniProtKB-KW.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB. 
Interpro
 IPR021925; DUF3538.
 IPR000626; Ubiquitin.
 IPR019954; Ubiquitin_CS.
 IPR019955; Ubiquitin_supergroup. 
Pfam
 PF12057; DUF3538
 PF00240; ubiquitin 
SMART
 SM00213; UBQ 
PROSITE
 PS00299; UBIQUITIN_1
 PS50053; UBIQUITIN_2 
PRINTS