BAG5_HUMAN - dbPTM
BAG5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BAG5_HUMAN
UniProt AC Q9UL15
Protein Name BAG family molecular chaperone regulator 5
Gene Name BAG5
Organism Homo sapiens (Human).
Sequence Length 447
Subcellular Localization
Protein Description Inhibits both auto-ubiquitination of PRKN and ubiquitination of target proteins by PRKN (By similarity). May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding..
Protein Sequence MDMGNQHPSISRLQEIQKEVKSVEQQVIGFSGLSDDKNYKKLERILTKQLFEIDSVDTEGKGDIQQARKRAAQETERLLKELEQNANHPHRIEIQNIFEEAQSLVREKIVPFYNGGNCVTDEFEEGIQDIILRLTHVKTGGKISLRKARYHTLTKICAVQEIIEDCMKKQPSLPLSEDAHPSVAKINFVMCEVNKARGVLIALLMGVNNNETCRHLSCVLSGLIADLDALDVCGRTEIRNYRREVVEDINKLLKYLDLEEEADTTKAFDLRQNHSILKIEKVLKRMREIKNELLQAQNPSELYLSSKTELQGLIGQLDEVSLEKNPCIREARRRAVIEVQTLITYIDLKEALEKRKLFACEEHPSHKAVWNVLGNLSEIQGEVLSFDGNRTDKNYIRLEELLTKQLLALDAVDPQGEEKCKAARKQAVRLAQNILSYLDLKSDEWEY
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
9PhosphorylationDMGNQHPSISRLQEI
CCCCCCCCHHHHHHH		30.9525693802
11PhosphorylationGNQHPSISRLQEIQK
CCCCCCHHHHHHHHH		31.1325693802
18UbiquitinationSRLQEIQKEVKSVEQ
HHHHHHHHHHHCHHH		70.86-
21UbiquitinationQEIQKEVKSVEQQVI
HHHHHHHHCHHHHHH		50.29-
22PhosphorylationEIQKEVKSVEQQVIG
HHHHHHHCHHHHHHC		35.7421406692
31PhosphorylationEQQVIGFSGLSDDKN
HHHHHCCCCCCCCCC		33.3421406692
34PhosphorylationVIGFSGLSDDKNYKK
HHCCCCCCCCCCHHH		47.4921406692
37UbiquitinationFSGLSDDKNYKKLER
CCCCCCCCCHHHHHH		68.14-
47PhosphorylationKKLERILTKQLFEID
HHHHHHHHHHHHCCC		17.86-
48UbiquitinationKLERILTKQLFEIDS
HHHHHHHHHHHCCCC		41.37-
55PhosphorylationKQLFEIDSVDTEGKG
HHHHCCCCCCCCCCC		27.7930622161
58PhosphorylationFEIDSVDTEGKGDIQ
HCCCCCCCCCCCHHH		44.4730622161
59 (in isoform 2)Ubiquitination-55.21-
61UbiquitinationDSVDTEGKGDIQQAR
CCCCCCCCCHHHHHH		47.37-
75PhosphorylationRKRAAQETERLLKEL
HHHHHHHHHHHHHHH		17.8324702127
80UbiquitinationQETERLLKELEQNAN
HHHHHHHHHHHHHCC		65.92-
81 (in isoform 2)Ubiquitination-58.47-
89 (in isoform 2)Ubiquitination-20.47-
103PhosphorylationNIFEEAQSLVREKIV
HHHHHHHHHHHHHCC		35.5624719451
108UbiquitinationAQSLVREKIVPFYNG
HHHHHHHHCCCCCCC		38.14-
113PhosphorylationREKIVPFYNGGNCVT
HHHCCCCCCCCCCCC		13.5629083192
120PhosphorylationYNGGNCVTDEFEEGI
CCCCCCCCHHHHHHH		31.8229083192
138UbiquitinationILRLTHVKTGGKISL
HHHHHCCCCCCEEEE		33.57-
142UbiquitinationTHVKTGGKISLRKAR
HCCCCCCEEEECHHH		30.39-
150PhosphorylationISLRKARYHTLTKIC
EEECHHHHHHHHHHH		12.2022798277
152PhosphorylationLRKARYHTLTKICAV
ECHHHHHHHHHHHHH		27.4722798277
169UbiquitinationIIEDCMKKQPSLPLS
HHHHHHHHCCCCCCC		40.32-
190SulfoxidationVAKINFVMCEVNKAR
HHHCCEEEEECHHHH		1.0921406390
195AcetylationFVMCEVNKARGVLIA
EEEEECHHHHHHHHH		44.6425953088
241PhosphorylationGRTEIRNYRREVVED
CCHHHHHHHHHHHHH		10.95-
251UbiquitinationEVVEDINKLLKYLDL
HHHHHHHHHHHHCCH		56.37-
254UbiquitinationEDINKLLKYLDLEEE
HHHHHHHHHCCHHHH		54.96-
266UbiquitinationEEEADTTKAFDLRQN
HHHHCCCHHHHHHHH		49.50-
275PhosphorylationFDLRQNHSILKIEKV
HHHHHHHHHHHHHHH		36.8524719451
278AcetylationRQNHSILKIEKVLKR
HHHHHHHHHHHHHHH		47.3423236377
278UbiquitinationRQNHSILKIEKVLKR
HHHHHHHHHHHHHHH		47.3419608861
290UbiquitinationLKRMREIKNELLQAQ
HHHHHHHHHHHHHCC		39.35-
292 (in isoform 2)Ubiquitination-45.94-
295 (in isoform 2)Ubiquitination-54.23-
300PhosphorylationLLQAQNPSELYLSSK
HHHCCCHHHHHHCCH		48.0228060719
303PhosphorylationAQNPSELYLSSKTEL
CCCHHHHHHCCHHHH		10.6528060719
305PhosphorylationNPSELYLSSKTELQG
CHHHHHHCCHHHHCH		19.0728060719
306PhosphorylationPSELYLSSKTELQGL
HHHHHHCCHHHHCHH		40.7928060719
307UbiquitinationSELYLSSKTELQGLI
HHHHHCCHHHHCHHH		42.51-
308PhosphorylationELYLSSKTELQGLIG
HHHHCCHHHHCHHHC		43.8228060719
319AcetylationGLIGQLDEVSLEKNP
HHHCCCCHHCCHHCH		42.4719608861
321PhosphorylationIGQLDEVSLEKNPCI
HCCCCHHCCHHCHHH		28.8528060719
341PhosphorylationRAVIEVQTLITYIDL
HHHHHHHHHHHHHCH		25.8826552605
344PhosphorylationIEVQTLITYIDLKEA
HHHHHHHHHHCHHHH		19.9626552605
345PhosphorylationEVQTLITYIDLKEAL
HHHHHHHHHCHHHHH		5.8526552605
356UbiquitinationKEALEKRKLFACEEH
HHHHHHCCCCCCCCC		60.05-
393UbiquitinationFDGNRTDKNYIRLEE
ECCCCCCCCCCCHHH		51.54-
395PhosphorylationGNRTDKNYIRLEELL
CCCCCCCCCCHHHHH		7.9922985185
397 (in isoform 2)Ubiquitination-26.20-
403PhosphorylationIRLEELLTKQLLALD
CCHHHHHHHHHHHHH		29.3922985185
404UbiquitinationRLEELLTKQLLALDA
CHHHHHHHHHHHHHC		38.63-
419UbiquitinationVDPQGEEKCKAARKQ
CCCCCHHHHHHHHHH		36.41-
436PhosphorylationRLAQNILSYLDLKSD
HHHHHHHHHHCCCCC		21.6125690035
437PhosphorylationLAQNILSYLDLKSDE
HHHHHHHHHCCCCCC		10.7825690035
445 (in isoform 2)Ubiquitination-18.38-
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 BAG5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BAG5_HUMAN !!
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 BAG5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHIP_HUMANSTUB1physical
21358815
HSP74_HUMANHSPA4physical
21358815
SYUA_HUMANSNCAphysical
21358815
HSP74_HUMANHSPA4physical
15603737
PRKN_HUMANPARK2physical
15603737
CIRBP_HUMANCIRBPphysical
21988832
MD1L1_HUMANMAD1L1physical
22863883
DLG5_HUMANDLG5physical
25036637
MD1L1_HUMANMAD1L1physical
25036637
MD2L1_HUMANMAD2L1physical
25036637
BANP_HUMANBANPphysical
25416956
THAP1_HUMANTHAP1physical
25416956
F118B_HUMANFAM118Bphysical
25416956
KASH5_HUMANCCDC155physical
25416956
MD1L1_HUMANMAD1L1physical
26186194
DJC13_HUMANDNAJC13physical
26186194
ABL2_HUMANABL2physical
26186194
PINK1_HUMANPINK1physical
24475098
P53_HUMANTP53physical
27807478
MD1L1_HUMANMAD1L1physical
28514442
ABL2_HUMANABL2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BAG5_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-278, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory