Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Glucocorticoid receptor  

UniProtKB / Swiss-Prot ID :  GCR_HUMAN

Gene Name (Synonyms) : 
NR3C1, GRL  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. Note=Cytoplasmic in the absence of ligand, nuclear after ligand-binding. Isoform Beta: Nucleus. Note=Localized largely in the nucleus. 

Protein Function :  Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE) 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. Involved in nuclear translocation (By similarity). 

Protein Sequence MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRRLLVDFPKGSV...
Predicted Secondary Structure CCCHHHCCCCCCCCCCCCCCCCCCHHHHHHHHHCCCCEEEECCCCCCCCCCCCCCCCCCCCCHHCCCCCC...
Protein Variant
LocationDescription
23R -> K (in dbSNP:rs6190). VAR_014140
29F -> L. VAR_015628
65F -> V (in dbSNP:rs6192). VAR_014622
112L -> F. VAR_015629
233D -> N. VAR_015630
363N -> S (may increase sensitivity toexogenously administered glucocorticoids;
421C -> Y (in a glucocorticoid resistantleukemia cell line).
477R -> H (in GCRES). VAR_013472
559I -> N (in GCRES; interferes withtranslocation to the nucleus and thereby
571V -> A (in pseudohermaphroditism; femalewith hypokalemia due to glucocorticoid
641D -> V (in GCRES). VAR_004676
679G -> S (in GCRES; has 50% bindingaffinity).
729V -> I (in GCRES). VAR_004677
747I -> M (in GCRES; alters interaction withNCOA2 and strongly reduces transcription
753L -> F (in two glucocorticoid resistantleukemia cell lines lacking the normal
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
8PhosphothreonineKESLTPGRE
HHHCCCCCC
32.73HPRD
Link-
8PhosphothreonineKESLTPGRE
HHHCCCCCC
32.73PhosphoELM
Link-
8PhosphothreonineKESLTPGRE
HHHCCCCCC
32.73Phosphositeplus
Link-
8Phosphothreonine.KESLTPGRE
HHHCCCCCC
32.73UniProtKB
Link-
32PhosphothreonineDFYKTLRGG
HHHHHHCCC
15.42HPRD
Link-
32PhosphothreonineDFYKTLRGG
HHHHHHCCC
15.42Phosphositeplus
Link-
38PhosphothreonineRGGATVKVS
CCCCEEEEC
24.92HPRD
Link-
38PhosphothreonineRGGATVKVS
CCCCEEEEC
24.92Phosphositeplus
Link-
45PhosphoserineVSASSPSLA
ECCCCCCCC
20.44HPRD
Link-
45PhosphoserineVSASSPSLA
ECCCCCCCC
20.44PhosphoELM
Link-
45PhosphoserineVSASSPSLA
ECCCCCCCC
20.44Phosphositeplus
Link-
45PhosphoserineVSASSPSLA
ECCCCCCCC
20.44SysPTM
Link-
45Phosphoserine.VSASSPSLA
ECCCCCCCC
20.44UniProtKB
Link-
113PhosphoserineQISLSSGET
CCCCCCCHH
29.52HPRD
Link-
113PhosphoserineQISLSSGET
CCCCCCCHH
29.52PhosphoELM
Link-
134PhosphoserineNRSTSVPEN
HHHCCCCCC
36.60HPRD
Link-
134PhosphoserineNRSTSVPEN
HHHCCCCCC
36.60PhosphoELM
Link-
134PhosphoserineNRSTSVPEN
HHHCCCCCC
36.60Phosphositeplus
Link-
134PhosphoserineNRSTSVPEN
HHHCCCCCC
36.60SysPTM
Link-
134Phosphoserine.NRSTSVPEN
HHHCCCCCC
36.60UniProtKB
Link-
141PhosphoserineENPKSSAST
CCCCCCCCC
32.18HPRD
Link-
141PhosphoserineENPKSSAST
CCCCCCCCC
32.18PhosphoELM
Link-
203PhosphoserineFSSGSPGKE
CCCCCCCCC
32.21HPRD
Link-
203PhosphoserineFSSGSPGKE
CCCCCCCCC
32.21PhosphoELM
Link-
203PhosphoserineFSSGSPGKE
CCCCCCCCC
32.21Phosphositeplus
Link-
203Phosphoserine.FSSGSPGKE
CCCCCCCCC
32.21UniProtKB
Link-
211PhosphoserineETNESPWRS
CCCCCCCCC
31.65HPRD
Link-
211PhosphoserineETNESPWRS
CCCCCCCCC
31.65PhosphoELM
Link-
211PhosphoserineETNESPWRS
CCCCCCCCC
31.65Phosphositeplus
Link-
211Phosphoserine.ETNESPWRS
CCCCCCCCC
31.65UniProtKB
Link-
226PhosphoserineNCLLSPLAG
HHCCCCCCC
12.62Phosphositeplus
Link-
226PhosphoserineNCLLSPLAG
HHCCCCCCC
12.62SysPTM
Link-
226Phosphoserine (JNK_group;MAPK_group)NCLLSPLAG
HHCCCCCCC
12.62PhosphoELM
Link-
226Phosphoserine (MAPK1)NCLLSPLAG
HHCCCCCCC
12.62HPRD
Link-
226Phosphoserine (MAPK8)NCLLSPLAG
HHCCCCCCC
12.62HPRD
Link-
226Phosphoserine.NCLLSPLAG
HHCCCCCCC
12.62UniProtKB
Link-
234PhosphoserineGEDDSFLLE
CCCCCEEEE
30.07HPRD
Link-
234PhosphoserineGEDDSFLLE
CCCCCEEEE
30.07PhosphoELM
Link-
234PhosphoserineGEDDSFLLE
CCCCCEEEE
30.07SysPTM
Link-
234Phosphoserine.GEDDSFLLE
CCCCCEEEE
30.07UniProtKB
Link-
266PhosphoserineDLVLSSPSN
HHHCCCCCC
32.49HPRD
Link-
267PhosphoserineLVLSSPSNV
HHCCCCCCC
28.34HPRD
Link-
267PhosphoserineLVLSSPSNV
HHCCCCCCC
28.34PhosphoELM
Link-
267PhosphoserineLVLSSPSNV
HHCCCCCCC
28.34Phosphositeplus
Link-
267PhosphoserineLVLSSPSNV
HHCCCCCCC
28.34SysPTM
Link-
267Phosphoserine.LVLSSPSNV
HHCCCCCCC
28.34UniProtKB
Link-
277Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)LPQVKTEKE
CCEEECCCC
45.80HPRD
Link-
277Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)LPQVKTEKE
CCEEECCCC
45.80HPRD
Link-
277Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)LPQVKTEKE
CCEEECCCC
45.80Phosphositeplus
Link-
277Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO).LPQVKTEKE
CCEEECCCC
45.80UniProtKB
Link-
293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)PGVIKQEKL
CCCEEECCC
50.42HPRD
Link-
293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)PGVIKQEKL
CCCEEECCC
50.42HPRD
Link-
293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)PGVIKQEKL
CCCEEECCC
50.42Phosphositeplus
Link-
293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO).PGVIKQEKL
CCCEEECCC
50.42UniProtKB
Link-
404PhosphoserinePDVSSPPSS
CCCCCCCCC
40.45Phosphositeplus
Link-
419Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GPPPKLCLV
CCCCCCCCC
58.57HPRD
Link-
480N6-acetyllysineCRYRKCLQA
HHHHHHHHH
30.29Phosphositeplus
Link-
492N6-acetyllysineLEARKTKKK
HHHHHHHHH
72.28Phosphositeplus
Link-
494N6-acetyllysineARKTKKKIK
HHHHHHHHH
55.92Phosphositeplus
Link-
495N6-acetyllysineRKTKKKIKG
HHHHHHHHH
66.03Phosphositeplus
Link-
508Phosphoserine (DNA-PK)TTGVSQETS
CCCCCCCCC
24.52PhosphoELM
Link-
508Phosphoserine (PRKDC)TTGVSQETS
CCCCCCCCC
24.52HPRD
Link-
648PhosphotyrosineKHMLYVSSE
HHHHHHHHH
7.24HPRD
Link
650PhosphoserineMLYVSSELH
HHHHHHHHH
12.44HPRD
Link
651PhosphoserineLYVSSELHR
HHHHHHHHH
33.85HPRD
Link
703Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)KAIVKREGN
HHHHHCCCC
38.32HPRD
Link
703Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)KAIVKREGN
HHHHHCCCC
38.32HPRD
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CD4_HUMANphysical interactionMINT-3373972MINT16888650
THIO_HUMANphysical interactionMINT-15481MINT9915858
THIO_HUMANphysical interactionMINT-15483MINT9915858
1433S_HUMANphysical interactionMINT-14116MINT12730237
STA5A_HUMANphysical interactionMINT-13762MINT8878484
TF65_HUMANphysical interactionMINT-17322MINT8290595
MED25_HUMANphysical interactionMINT-5210024MINT17641689
NRIP1_HUMANphysical interactionDIP:10800EDIP9920921
TP53B_HUMANphysical interaction
physical interaction
DIP:10822EDIP11562347
11320256
SMCA4_HUMANphysical interactionEBI-493544
intact9590696
SMRC1_HUMANphysical interactionEBI-493549
intact9590696
STAT3_HUMANin vivoHPRD:00679HPRD14522952
9388192
ADA_HUMANin vitroHPRD:00679HPRD9154805
ADT1_HUMANin vivoHPRD:00679HPRD12039962
CALR_HUMANin vivoHPRD:00679HPRD8107808
9089287
1433F_HUMANin vitro
yeast 2-hybrid
HPRD:00679HPRD9079630
12730237
11266503
CEBPA_HUMANin vitro
in vivo
HPRD:00679HPRD11818365
COT2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:00679HPRD14739255
CREB1_HUMANin vitroHPRD:00679HPRD7621901
8449898
NR2F6_HUMANin vitroHPRD:00679HPRD10713182
GCR_HUMANin vitro
yeast 2-hybrid
HPRD:00679HPRD12773573
9482670
10364267
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Disease Reference
Kegg disease
OMIM disease
615962Glucocorticoid resistance, generalized (GCCR)
138040Glucocorticoid resistance (GCRES)
Drug Reference
DrugBank
DB00240Alclometasone
DB00288Amcinonide
DB00394Beclomethasone
DB00443Betamethasone
DB01222Budesonide
DB01410Ciclesonide
DB01013Clobetasol propionate
DB00838Clocortolone
DB01380Cortisone acetate
DB01260Desonide
DB00547Desoximetasone
DB01234Dexamethasone
DB00223Diflorasone
DB06781Difluprednate
DB00687Fludrocortisone
DB00663Flumethasone Pivalate
DB00180Flunisolide
DB00591Fluocinolone Acetonide
DB01047Fluocinonide
DB00324Fluorometholone
DB01185Fluoxymesterone
DB00846Flurandrenolide
DB08906Fluticasone furoate
DB00588Fluticasone Propionate
DB00596Halobetasol Propionate
DB00769Hydrocortamate
DB00741Hydrocortisone
DB00873Loteprednol
DB00253Medrysone
DB00351Megestrol acetate
DB00959Methylprednisolone
DB00834Mifepristone
DB00764Mometasone
DB01384Paramethasone
DB01130Prednicarbate
DB00860Prednisolone
DB00635Prednisone
DB00896Rimexolone
DB00421Spironolactone
DB00620Triamcinolone
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Deciphering the phosphorylation 'code' of the glucocorticoid receptorin vivo.";
Wang Z., Frederick J., Garabedian M.J.;
J. Biol. Chem. 277:26573-26580(2002).
Cited for: PHOSPHORYLATION AT SER-203 AND SER-211.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8 AND SER-45, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-226; SER-234AND SER-267, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures