ERR3_HUMAN - dbPTM
ERR3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERR3_HUMAN
UniProt AC P62508
Protein Name Estrogen-related receptor gamma
Gene Name ESRRG
Organism Homo sapiens (Human).
Sequence Length 458
Subcellular Localization Nucleus .
Protein Description Orphan receptor that acts as transcription activator in the absence of bound ligand. Binds specifically to an estrogen response element and activates reporter genes controlled by estrogen response elements (By similarity). Induces the expression of PERM1 in the skeletal muscle..
Protein Sequence MDSVELCLPESFSLHYEEELLCRMSNKDRHIDSSCSSFIKTEPSSPASLTDSVNHHSPGGSSDASGSYSSTMNGHQNGLDSPPLYPSAPILGGSGPVRKLYDDCSSTIVEDPQTKCEYMLNSMPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRIDAENSPYLNPQLVQPAKKPYNKIVSHLLVAEPEKIYAMPDPTVPDSDIKALTTLCDLADRELVVIIGWAKHIPGFSTLSLADQMSLLQSAWMEILILGVVYRSLSFEDELVYADDYIMDEDQSKLAGLLDLNNAILQLVKKYKSMKLEKEEFVTLKAIALANSDSMHIEDVEAVQKLQDVLHEALQDYEAGQHMEDPRRAGKMLMTLPLLRQTSTKAVQHFYNIKLEGKVPMHKLFLEMLEAKV
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
33PhosphorylationNKDRHIDSSCSSFIK
CCCCCCCCCCHHCCC
32.42-
34PhosphorylationKDRHIDSSCSSFIKT
CCCCCCCCCHHCCCC
17.80-
36PhosphorylationRHIDSSCSSFIKTEP
CCCCCCCHHCCCCCC
30.17-
37PhosphorylationHIDSSCSSFIKTEPS
CCCCCCHHCCCCCCC
35.0124719451
40SumoylationSSCSSFIKTEPSSPA
CCCHHCCCCCCCCCC
44.84-
40SumoylationSSCSSFIKTEPSSPA
CCCHHCCCCCCCCCC
44.84-
45PhosphorylationFIKTEPSSPASLTDS
CCCCCCCCCCCCCCC
34.8914702039
101PhosphorylationSGPVRKLYDDCSSTI
CCCCHHHCCCCCCCC
16.8729083192
105PhosphorylationRKLYDDCSSTIVEDP
HHHCCCCCCCCCCCC
37.1927732954
106PhosphorylationKLYDDCSSTIVEDPQ
HHCCCCCCCCCCCCH
28.6027251275
107PhosphorylationLYDDCSSTIVEDPQT
HCCCCCCCCCCCCHH
16.8527251275
112PhosphorylationSSTIVEDPQTKCEYM
CCCCCCCCHHHHHHH
30.1827251275
114PhosphorylationTIVEDPQTKCEYMLN
CCCCCCHHHHHHHHH
42.9529083192
118PhosphorylationDPQTKCEYMLNSMPK
CCHHHHHHHHHHCCC
19.1724275569
122PhosphorylationKCEYMLNSMPKRLCL
HHHHHHHHCCCEEEE
32.2829083192
136PhosphorylationLVCGDIASGYHYGVA
EEECCCCCCCCCCHH
39.9724275569
144PhosphorylationGYHYGVASCEACKAF
CCCCCHHCHHHHHHH
15.3024275569
195UbiquitinationCLKVGMLKEGVRLDR
HHHHCCCCCCCCHHH
43.46-
195AcetylationCLKVGMLKEGVRLDR
HHHHCCCCCCCCHHH
43.4612654505
219PhosphorylationRRIDAENSPYLNPQL
HHCCCCCCCCCCHHH
13.3628857561
221PhosphorylationIDAENSPYLNPQLVQ
CCCCCCCCCCHHHCC
20.9428857561
239PhosphorylationKPYNKIVSHLLVAEP
CCCHHHHHHHHHCCH
16.3422210691
256PhosphorylationIYAMPDPTVPDSDIK
EEECCCCCCCHHHHH
52.6422210691
260PhosphorylationPDPTVPDSDIKALTT
CCCCCCHHHHHHHHH
34.8522210691
356PhosphorylationILQLVKKYKSMKLEK
HHHHHHHHHCCCCCH
11.54-
363UbiquitinationYKSMKLEKEEFVTLK
HHCCCCCHHHHHHHH
73.34-
377PhosphorylationKAIALANSDSMHIED
HHHHHHCCCCCCCCH
26.0021601212
420PhosphorylationRAGKMLMTLPLLRQT
HHHHHHHHHHHHHHC
22.66-

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 ERR3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
40KPhosphorylation

16371476
40KPhosphorylation

16371476
40KSumoylation

16371476
40KSumoylation

16371476
45SPhosphorylation

19067653
45SPhosphorylation

19067653
45SSumoylation

19067653
45SSumoylation

19067653

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 ERR3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERR3_HUMANESRRGphysical
11864604
NCOA1_HUMANNCOA1physical
11864604
ERR3_HUMANESRRGphysical
12180985
ERR1_HUMANESRRAphysical
17157980
NRIP1_HUMANNRIP1physical
16439465
PRGC1_HUMANPPARGC1Aphysical
15821111
NR0B2_HUMANNR0B2physical
20516075
NR0B1_HUMANNR0B1physical
15604093
DUT_HUMANDUTphysical
15604093
PROX1_HUMANPROX1physical
15604093
NRIP1_HUMANNRIP1physical
15604093
ERR1_HUMANESRRAphysical
15604093
EBP_HUMANEBPphysical
15604093
PNRC1_HUMANPNRC1physical
15604093
PNRC2_HUMANPNRC2physical
15604093
ARHGF_HUMANARHGEF15physical
15604093
NR0B2_HUMANNR0B2physical
21459093
TLE1_HUMANTLE1physical
14651967
ERR3_HUMANESRRGphysical
14651967
A4_HUMANAPPphysical
21832049
PRGC1_HUMANPPARGC1Aphysical
19171140
SRA1_HUMANSRA1physical
20398657
ERR3_HUMANESRRGphysical
25416956
KIFC3_HUMANKIFC3physical
25416956
MEOX2_HUMANMEOX2physical
25416956
NU160_HUMANNUP160physical
25416956
SHOT1_HUMANKIAA1598physical
25416956
DEUP1_HUMANCCDC67physical
25416956
PRS8_HUMANPSMC5physical
15604093
NCOA1_HUMANNCOA1physical
15604093

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
DB02659Cholic Acid
DB00255Diethylstilbestrol
Regulatory Network of ERR3_HUMAN

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Related Literatures of Post-Translational Modification
Sumoylation
ReferencePubMed
"Phosphorylation-dependent sumoylation regulates estrogen-relatedreceptor-alpha and -gamma transcriptional activity through a synergycontrol motif.";
Tremblay A.M., Wilson B.J., Yang X.-J., Giguere V.;
Mol. Endocrinol. 22:570-584(2008).
Cited for: SUMOYLATION AT LYS-40, PHOSPHORYLATION AT SER-45, FUNCTION, ANDMUTAGENESIS OF LYS-40 AND SER-45.
"Transcriptional ERRgamma2-mediated activation is regulated bysentrin-specific proteases.";
Hentschke M., Suesens U., Borgmeyer U.;
Biochem. J. 419:167-176(2009).
Cited for: SUMOYLATION AT LYS-40, PHOSPHORYLATION AT SER-45, FUNCTION, ANDMUTAGENESIS OF PHE-38; ILE-39; LYS-40; THR-41; GLU-42; SER-44 ANDSER-45.
"PDSM, a motif for phosphorylation-dependent SUMO modification.";
Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J.,Nakai A., Sistonen L.;
Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006).
Cited for: SUMOYLATION AT LYS-40, AND MUTAGENESIS OF LYS-40.

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