BAG1_HUMAN - dbPTM
BAG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BAG1_HUMAN
UniProt AC Q99933
Protein Name BAG family molecular chaperone regulator 1
Gene Name BAG1
Organism Homo sapiens (Human).
Sequence Length 345
Subcellular Localization Isoform 1: Nucleus. Cytoplasm. Isoform 1 localizes predominantly to the nucleus.
Isoform 2: Cytoplasm. Nucleus. Isoform 2 localizes to the cytoplasm and shuttles into the nucleus in response to heat shock.
Isoform 4: Cytoplasm. Nucleus. I
Protein Description Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. [PubMed: 27474739]
Protein Sequence MAQRGGARRPRGDRERLGSRLRALRPGREPRQSEPPAQRGPPPSGRPPARSTASGHDRPTRGAAAGARRPRMKKKTRRRSTRSEELTRSEELTLSEEATWSEEATQSEEATQGEEMNRSQEVTRDEESTRSEEVTREEMAAAGLTVTVTHSNEKHDLHVTSQQGSSEPVVQDLAQVVEEVIGVPQSFQKLIFKGKSLKEMETPLSALGIQDGCRVMLIGKKNSPQEEVELKKLKHLEKSVEKIADQLEELNKELTGIQQGFLPKDLQAEALCKLDRRVKATIEQFMKILEEIDTLILPENFKDSRLKRKGLVKKVQAFLAECDTVEQNICQETERLQSTNFALAE
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
4 (in isoform 4)Phosphorylation-35.6526425664
33PhosphorylationPGREPRQSEPPAQRG
CCCCCCCCCCCHHCC
54.0428555341
52PhosphorylationGRPPARSTASGHDRP
CCCCCCCCCCCCCCC
21.2024719451
54PhosphorylationPPARSTASGHDRPTR
CCCCCCCCCCCCCCC
36.4324719451
58MethylationSTASGHDRPTRGAAA
CCCCCCCCCCCCCCC
28.90-
61MethylationSGHDRPTRGAAAGAR
CCCCCCCCCCCCCCC
35.12-
68MethylationRGAAAGARRPRMKKK
CCCCCCCCCHHHCHH
48.49-
80PhosphorylationKKKTRRRSTRSEELT
CHHHHCCCCCHHHHH
26.7625159151
81PhosphorylationKKTRRRSTRSEELTR
HHHHCCCCCHHHHHH
36.0827251275
83PhosphorylationTRRRSTRSEELTRSE
HHCCCCCHHHHHHHH
35.2033259812
87PhosphorylationSTRSEELTRSEELTL
CCCHHHHHHHHHCCC
35.1123312004
93UbiquitinationLTRSEELTLSEEATW
HHHHHHCCCCCCCCC
31.3633845483
116UbiquitinationEATQGEEMNRSQEVT
HHHCHHHCHHHHCCC
4.3733845483
119PhosphorylationQGEEMNRSQEVTRDE
CHHHCHHHHCCCCCH
26.2025159151
123PhosphorylationMNRSQEVTRDEESTR
CHHHHCCCCCHHHHC
31.4829083192
127UbiquitinationQEVTRDEESTRSEEV
HCCCCCHHHHCCHHH
62.7929967540
128PhosphorylationEVTRDEESTRSEEVT
CCCCCHHHHCCHHHH
27.3721815630
129PhosphorylationVTRDEESTRSEEVTR
CCCCHHHHCCHHHHH
41.3022985185
131PhosphorylationRDEESTRSEEVTREE
CCHHHHCCHHHHHHH
37.8921815630
135UbiquitinationSTRSEEVTREEMAAA
HHCCHHHHHHHHHHC
35.3333845483
137UbiquitinationRSEEVTREEMAAAGL
CCHHHHHHHHHHCCC
42.6429967540
145PhosphorylationEMAAAGLTVTVTHSN
HHHHCCCEEEEEECC
17.1420068231
149UbiquitinationAGLTVTVTHSNEKHD
CCCEEEEEECCCEEE
15.3829967540
149PhosphorylationAGLTVTVTHSNEKHD
CCCEEEEEECCCEEE
15.3820068231
158 (in isoform 4)Ubiquitination-27.2021890473
158UbiquitinationSNEKHDLHVTSQQGS
CCCEEEEEEEECCCC
27.2023000965
160UbiquitinationEKHDLHVTSQQGSSE
CEEEEEEEECCCCCC
15.2933845483
164UbiquitinationLHVTSQQGSSEPVVQ
EEEEECCCCCCHHHH
26.0423000965
187UbiquitinationVIGVPQSFQKLIFKG
HHCCCHHHHHHHHCC
6.6429967540
196PhosphorylationKLIFKGKSLKEMETP
HHHHCCCCHHHCCCC
54.0328857561
202UbiquitinationKSLKEMETPLSALGI
CCHHHCCCCHHHCCC
28.3733845483
202PhosphorylationKSLKEMETPLSALGI
CCHHHCCCCHHHCCC
28.3728857561
202 (in isoform 3)Ubiquitination-28.3721890473
205PhosphorylationKEMETPLSALGIQDG
HHCCCCHHHCCCCCC
23.7428857561
220AcetylationCRVMLIGKKNSPQEE
CEEEEEECCCCCHHH
41.6125953088
223PhosphorylationMLIGKKNSPQEEVEL
EEEECCCCCHHHHHH
36.5225159151
231UbiquitinationPQEEVELKKLKHLEK
CHHHHHHHHHHHHHH
42.4233845483
231AcetylationPQEEVELKKLKHLEK
CHHHHHHHHHHHHHH
42.4223749302
238AcetylationKKLKHLEKSVEKIAD
HHHHHHHHHHHHHHH
67.1925953088
242UbiquitinationHLEKSVEKIADQLEE
HHHHHHHHHHHHHHH
40.8329967540
252UbiquitinationDQLEELNKELTGIQQ
HHHHHHHHHHHHCCC
67.7229967540
264UbiquitinationIQQGFLPKDLQAEAL
CCCCCCCHHHHHHHH
73.5429967540
273UbiquitinationLQAEALCKLDRRVKA
HHHHHHHHHHHHHHH
55.0323000965
273 (in isoform 1)Ubiquitination-55.0321890473
273 (in isoform 2)Ubiquitination-55.0321890473
279UbiquitinationCKLDRRVKATIEQFM
HHHHHHHHHHHHHHH
37.6923000965
302UbiquitinationLILPENFKDSRLKRK
HHCCCCCCCHHHHHH
67.3929967540

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
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:11676916
-KUbiquitinationE3 ubiquitin ligaseSIAH1Q8IUQ4
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseSIAH2O43255
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BAG1_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 BAG1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP7C_HUMANHSPA8physical
9305631
ANDR_HUMANARphysical
14517289
PR15A_HUMANPPP1R15Aphysical
12724406
RARA_HUMANRARAphysical
9642262
ANDR_HUMANARphysical
11278763
HSP7C_HUMANHSPA8physical
9873016
RAF1_HUMANRAF1physical
8692945
CHIP_HUMANSTUB1physical
11676916
SIAH1_HUMANSIAH1physical
9582267
VDR_HUMANVDRphysical
10967105
VDR_HUMANVDRgenetic
10967105
GCR_HUMANNR3C1physical
11101523
HSP74_HUMANHSPA4physical
9305631
BCL2_HUMANBCL2physical
9305631
HSP7C_HUMANHSPA8physical
17954934
TAU_HUMANMAPTphysical
17954934
ABL1_HUMANABL1physical
20675402
CBL_HUMANCBLphysical
20675402
HSP7C_HUMANHSPA8physical
20675402
HSP74_HUMANHSPA4physical
15603737
HSP74_HUMANHSPA4physical
19229298
HSP7C_HUMANHSPA8physical
10671488
HSP74_HUMANHSPA4physical
10671488
PSA3_HUMANPSMA3physical
10671488
PSMD1_HUMANPSMD1physical
10671488
HSP74_HUMANHSPA4physical
12874020
HSP7C_HUMANHSPA8physical
12874020
HSP7C_HUMANHSPA8physical
14978028
HSP74_HUMANHSPA4physical
11520069
PARK7_HUMANPARK7physical
20156966
HSP74_HUMANHSPA4physical
20156966
BAG3_HUMANBAG3physical
22939629
TRI23_HUMANTRIM23physical
19060904
HSP74_HUMANHSPA4physical
11231577
RAF1_HUMANRAF1physical
11231577
HSP7C_HUMANHSPA8physical
19800331
HSP7C_HUMANHSPA8physical
11222862
HSP7C_HUMANHSPA8physical
9774640
PYGL_HUMANPYGLphysical
21988832
ARP2_HUMANACTR2physical
22863883
AN32A_HUMANANP32Aphysical
22863883
AN32B_HUMANANP32Bphysical
22863883
ARPC4_HUMANARPC4physical
22863883
FUBP1_HUMANFUBP1physical
22863883
GRPE1_HUMANGRPEL1physical
22863883
NIF3L_HUMANNIF3L1physical
22863883
OSGEP_HUMANOSGEPphysical
22863883
PANK4_HUMANPANK4physical
22863883
PEG10_HUMANPEG10physical
22863883
RAGP1_HUMANRANGAP1physical
22863883
SH3G1_HUMANSH3GL1physical
22863883
TM1L1_HUMANTOM1L1physical
22863883
XPO5_HUMANXPO5physical
22863883
ZPR1_HUMANZPR1physical
22863883
MLF2_HUMANMLF2physical
25036637
CHIP_HUMANSTUB1physical
25036637
DNJB6_HUMANDNAJB6physical
25036637
LTN1_HUMANLTN1physical
25036637
DNJB4_HUMANDNAJB4physical
25036637
DNJB1_HUMANDNAJB1physical
25036637
HSP7C_HUMANHSPA8physical
25416956
PSMD2_HUMANPSMD2physical
25416956
TRI27_HUMANTRIM27physical
25416956
ECM29_HUMANKIAA0368physical
26344197
KIFC1_HUMANKIFC1physical
26344197
THUM1_HUMANTHUMPD1physical
26344197
SYVN1_HUMANSYVN1genetic
26424800

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 BAG1_HUMAN

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Related Literatures of Post-Translational Modification

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