CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023132
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 BAG family molecular chaperone regulator 5 
Protein Synonyms/Alias
 BAG-5; Bcl-2-associated athanogene 5 
Gene Name
 BAG5 
Gene Synonyms/Alias
 KIAA0873 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
59SRLQEIQKEVKSVEQubiquitination[1]
81LSDDKNYKKLERILTubiquitination[1]
89KLERILTKQLFEIDSubiquitination[1, 2]
292EVVEDINKLLKYLDLubiquitination[1]
295EDINKLLKYLDLEEEubiquitination[1]
397KEALEKRKLFACEEHubiquitination[1]
445RLEELLTKQLLALDAubiquitination[1]
Reference
 [1] 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]
 [2] 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
Functional Description
 Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 (By similarity). May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. 
Sequence Annotation
 DOMAIN 9 86 BAG 1.
 DOMAIN 95 167 BAG 2.
 DOMAIN 182 260 BAG 3.
 DOMAIN 275 350 BAG 4.
 DOMAIN 365 442 BAG 5.  
Keyword
 3D-structure; Alternative splicing; Chaperone; Complete proteome; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 447 AA 
Protein Sequence
MRFHWLPTLS EPFDRNQELE TCIRPLWTPS GSACETEHNK SMDMGNQHPS ISRLQEIQKE 60
VKSVEQQVIG FSGLSDDKNY KKLERILTKQ LFEIDSVDTE GKGDIQQARK RAAQETERLL 120
KELEQNANHP HRIEIQNIFE EAQSLVREKI VPFYNGGNCV TDEFEEGIQD IILRLTHVKT 180
GGKISLRKAR YHTLTKICAV QEIIEDCMKK QPSLPLSEDA HPSVAKINFV MCEVNKARGV 240
LIALLMGVNN NETCRHLSCV LSGLIADLDA LDVCGRTEIR NYRREVVEDI NKLLKYLDLE 300
EEADTTKAFD LRQNHSILKI EKVLKRMREI KNELLQAQNP SELYLSSKTE LQGLIGQLDE 360
VSLEKNPCIR EARRRAVIEV QTLITYIDLK EALEKRKLFA CEEHPSHKAV WNVLGNLSEI 420
QGEVLSFDGN RTDKNYIRLE ELLTKQLLAL DAVDPQGEEK CKAARKQAVR LAQNILSYLD 480
LKSDEWEY 488 
Gene Ontology
 GO:0016234; C:inclusion body; IDA:BHF-UCL.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
 GO:0031625; F:ubiquitin protein ligase binding; ISS:BHF-UCL.
 GO:0061084; P:negative regulation of protein refolding; ISS:BHF-UCL.
 GO:0051444; P:negative regulation of ubiquitin-protein ligase activity; ISS:BHF-UCL.
 GO:0070997; P:neuron death; ISS:BHF-UCL.
 GO:0006457; P:protein folding; TAS:ProtInc.
 GO:0090083; P:regulation of inclusion body assembly; IMP:BHF-UCL. 
Interpro
 IPR003103; BAG_domain. 
Pfam
 PF02179; BAG 
SMART
 SM00264; BAG 
PROSITE
 PS51035; BAG 
PRINTS