CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002098
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
 CAA26976.1; CAA27054.1; AAB64353.1; AAB64353.1; AAB64353.1; AAB64353.1; AAB64353.1; AAB64353.1; AAB64353.1; AAB64353.1; AAB64354.1; AAB64354.1; AAB64354.1; AAB64354.1; AAB64354.1; AAB64354.1; AAB64354.1; AAB64354.1; ADP91135.1; ADP91138.1; ADP91141.1; ADP91144.1; ADP91147.1; ADP91150.1; ADP91153.1; ADP91156.1; ADP91159.1; ADP91162.1; ADP91165.1; ADP91168.1; ADP91171.1; ADP91174.1; ADP91177.1; ADP91180.1; ADP91183.1; ADP91186.1; ADP91189.1; ADP91192.1; ADP91195.1; ADP91198.1; ADP91201.1; ADP91204.1; ADP91207.1; ADP91210.1; ADP91213.1; ADP91216.1; ADP91219.1; ADP91222.1; ADP91225.1; ADP91228.1; ADP91231.1; ADP91234.1; ADP91237.1; ADP91240.1; ADP91243.1; ADP91246.1; ADP91249.1; ADP91252.1; CAJ65924.1; AAA16603.1; BAD97314.1; CAE45716.1; AAQ97180.1; ABY87547.1; AAC34207.1; EAW61872.1; EAW61873.1; AAH15610.1; AAA88049.1; AAA53151.1; AAB20466.1 
Protein Name
 Glucocorticoid receptor 
Protein Synonyms/Alias
 GR; Nuclear receptor subfamily 3 group C member 1 
Gene Name
 NR3C1 
Gene Synonyms/Alias
 GRL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
277NVTLPQVKTEKEDFIsumoylation[1, 2]
293LCTPGVIKQEKLGTVsumoylation[1, 2]
494NLEARKTKKKIKGIQacetylation[3]
495LEARKTKKKIKGIQQacetylation[3]
681SVPKDGLKSQELFDEubiquitination[4]
703ELGKAIVKREGNSSQsumoylation[1]
Reference
 [1] Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor.
 Tian S, Poukka H, Palvimo JJ, Jänne OA.
 Biochem J. 2002 Nov 1;367(Pt 3):907-11. [PMID: 12144530]
 [2] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [3] Histone deacetylase 2-mediated deacetylation of the glucocorticoid receptor enables NF-kappaB suppression.
 Ito K, Yamamura S, Essilfie-Quaye S, Cosio B, Ito M, Barnes PJ, Adcock IM.
 J Exp Med. 2006 Jan 23;203(1):7-13. [PMID: 16380507]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983
Functional Description
 Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth. Involved in chromatin remodeling. Plays a significant role in transactivation. 
Sequence Annotation
 DNA_BIND 421 486 Nuclear receptor.
 ZN_FING 421 441 NR C4-type.
 ZN_FING 457 481 NR C4-type.
 REGION 1 420 Modulating.
 REGION 487 527 Hinge.
 REGION 528 777 Steroid-binding.
 MOD_RES 113 113 Phosphoserine (By similarity).
 MOD_RES 134 134 Phosphoserine.
 MOD_RES 141 141 Phosphoserine (By similarity).
 MOD_RES 203 203 Phosphoserine.
 MOD_RES 211 211 Phosphoserine.
 MOD_RES 226 226 Phosphoserine.
 MOD_RES 267 267 Phosphoserine.
 CROSSLNK 277 277 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 293 293 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 419 419 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Alternative initiation; Alternative splicing; Chromatin regulator; Complete proteome; Cytoplasm; Disease mutation; DNA-binding; Isopeptide bond; Lipid-binding; Metal-binding; Mitochondrion; Nucleus; Phosphoprotein; Polymorphism; Pseudohermaphroditism; Receptor; Reference proteome; Steroid-binding; Transcription; Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 777 AA 
Protein Sequence
MDSKESLTPG REENPSSVLA QERGDVMDFY KTLRGGATVK VSASSPSLAV ASQSDSKQRR 60
LLVDFPKGSV SNAQQPDLSK AVSLSMGLYM GETETKVMGN DLGFPQQGQI SLSSGETDLK 120
LLEESIANLN RSTSVPENPK SSASTAVSAA PTEKEFPKTH SDVSSEQQHL KGQTGTNGGN 180
VKLYTTDQST FDILQDLEFS SGSPGKETNE SPWRSDLLID ENCLLSPLAG EDDSFLLEGN 240
SNEDCKPLIL PDTKPKIKDN GDLVLSSPSN VTLPQVKTEK EDFIELCTPG VIKQEKLGTV 300
YCQASFPGAN IIGNKMSAIS VHGVSTSGGQ MYHYDMNTAS LSQQQDQKPI FNVIPPIPVG 360
SENWNRCQGS GDDNLTSLGT LNFPGRTVFS NGYSSPSMRP DVSSPPSSSS TATTGPPPKL 420
CLVCSDEASG CHYGVLTCGS CKVFFKRAVE GQHNYLCAGR NDCIIDKIRR KNCPACRYRK 480
CLQAGMNLEA RKTKKKIKGI QQATTGVSQE TSENPGNKTI VPATLPQLTP TLVSLLEVIE 540
PEVLYAGYDS SVPDSTWRIM TTLNMLGGRQ VIAAVKWAKA IPGFRNLHLD DQMTLLQYSW 600
MFLMAFALGW RSYRQSSANL LCFAPDLIIN EQRMTLPCMY DQCKHMLYVS SELHRLQVSY 660
EEYLCMKTLL LLSSVPKDGL KSQELFDEIR MTYIKELGKA IVKREGNSSQ NWQRFYQLTK 720
LLDSMHEVVE NLLNYCFQTF LDKTMSIEFP EMLAEIITNQ IPKYSNGNIK KLLFHQK 777 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0016020; C:membrane; IEA:Compara.
 GO:0005759; C:mitochondrial matrix; TAS:ProtInc.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0004883; F:glucocorticoid receptor activity; TAS:ProtInc.
 GO:0043565; F:sequence-specific DNA binding; IEA:Compara.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
 GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0030325; P:adrenal gland development; IEA:Compara.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0008211; P:glucocorticoid metabolic process; IEA:Compara.
 GO:0060603; P:mammary gland duct morphogenesis; IEA:Compara.
 GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Compara.
 GO:0031946; P:regulation of glucocorticoid biosynthetic process; IEA:Compara.
 GO:0006111; P:regulation of gluconeogenesis; IEA:Compara.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome. 
Interpro
 IPR001409; Glcrtcd_rcpt.
 IPR008946; Nucl_hormone_rcpt_ligand-bd.
 IPR000536; Nucl_hrmn_rcpt_lig-bd_core.
 IPR001723; Str_hrmn_rcpt.
 IPR001628; Znf_hrmn_rcpt.
 IPR013088; Znf_NHR/GATA. 
Pfam
 PF02155; GCR
 PF00104; Hormone_recep
 PF00105; zf-C4 
SMART
 SM00430; HOLI
 SM00399; ZnF_C4 
PROSITE
 PS00031; NUCLEAR_REC_DBD_1
 PS51030; NUCLEAR_REC_DBD_2 
PRINTS
 PR00528; GLCORTICOIDR.
 PR00398; STRDHORMONER.
 PR00047; STROIDFINGER.