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 | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
33 | Phosphorylation | NKDRHIDSSCSSFIK CCCCCCCCCCHHCCC | 32.42 | - | |
34 | Phosphorylation | KDRHIDSSCSSFIKT CCCCCCCCCHHCCCC | 17.80 | - | |
36 | Phosphorylation | RHIDSSCSSFIKTEP CCCCCCCHHCCCCCC | 30.17 | - | |
37 | Phosphorylation | HIDSSCSSFIKTEPS CCCCCCHHCCCCCCC | 35.01 | 24719451 | |
40 | Sumoylation | SSCSSFIKTEPSSPA CCCHHCCCCCCCCCC | 44.84 | - | |
40 | Sumoylation | SSCSSFIKTEPSSPA CCCHHCCCCCCCCCC | 44.84 | - | |
45 | Phosphorylation | FIKTEPSSPASLTDS CCCCCCCCCCCCCCC | 34.89 | 14702039 | |
101 | Phosphorylation | SGPVRKLYDDCSSTI CCCCHHHCCCCCCCC | 16.87 | 29083192 | |
105 | Phosphorylation | RKLYDDCSSTIVEDP HHHCCCCCCCCCCCC | 37.19 | 27732954 | |
106 | Phosphorylation | KLYDDCSSTIVEDPQ HHCCCCCCCCCCCCH | 28.60 | 27251275 | |
107 | Phosphorylation | LYDDCSSTIVEDPQT HCCCCCCCCCCCCHH | 16.85 | 27251275 | |
112 | Phosphorylation | SSTIVEDPQTKCEYM CCCCCCCCHHHHHHH | 30.18 | 27251275 | |
114 | Phosphorylation | TIVEDPQTKCEYMLN CCCCCCHHHHHHHHH | 42.95 | 29083192 | |
118 | Phosphorylation | DPQTKCEYMLNSMPK CCHHHHHHHHHHCCC | 19.17 | 24275569 | |
122 | Phosphorylation | KCEYMLNSMPKRLCL HHHHHHHHCCCEEEE | 32.28 | 29083192 | |
136 | Phosphorylation | LVCGDIASGYHYGVA EEECCCCCCCCCCHH | 39.97 | 24275569 | |
144 | Phosphorylation | GYHYGVASCEACKAF CCCCCHHCHHHHHHH | 15.30 | 24275569 | |
195 | Ubiquitination | CLKVGMLKEGVRLDR HHHHCCCCCCCCHHH | 43.46 | - | |
195 | Acetylation | CLKVGMLKEGVRLDR HHHHCCCCCCCCHHH | 43.46 | 12654505 | |
219 | Phosphorylation | RRIDAENSPYLNPQL HHCCCCCCCCCCHHH | 13.36 | 28857561 | |
221 | Phosphorylation | IDAENSPYLNPQLVQ CCCCCCCCCCHHHCC | 20.94 | 28857561 | |
239 | Phosphorylation | KPYNKIVSHLLVAEP CCCHHHHHHHHHCCH | 16.34 | 22210691 | |
256 | Phosphorylation | IYAMPDPTVPDSDIK EEECCCCCCCHHHHH | 52.64 | 22210691 | |
260 | Phosphorylation | PDPTVPDSDIKALTT CCCCCCHHHHHHHHH | 34.85 | 22210691 | |
356 | Phosphorylation | ILQLVKKYKSMKLEK HHHHHHHHHCCCCCH | 11.54 | - | |
363 | Ubiquitination | YKSMKLEKEEFVTLK HHCCCCCHHHHHHHH | 73.34 | - | |
377 | Phosphorylation | KAIALANSDSMHIED HHHHHHCCCCCCCCH | 26.00 | 21601212 | |
420 | Phosphorylation | RAGKMLMTLPLLRQT HHHHHHHHHHHHHHC | 22.66 | - |
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 !! |
* 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 !! |
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Sumoylation | |
Reference | PubMed |
"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. |