GMEB2_HUMAN - dbPTM
GMEB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GMEB2_HUMAN
UniProt AC Q9UKD1
Protein Name Glucocorticoid modulatory element-binding protein 2
Gene Name GMEB2
Organism Homo sapiens (Human).
Sequence Length 530
Subcellular Localization Nucleus. Cytoplasm. May be also cytoplasmic.
Protein Description Trans-acting factor that binds to glucocorticoid modulatory elements (GME) present in the TAT (tyrosine aminotransferase) promoter and increases sensitivity to low concentrations of glucocorticoids. Binds also to the transferrin receptor promoter. Essential auxiliary factor for the replication of parvoviruses..
Protein Sequence MATPDVSVHMEEVVVVTTPDTAVDGSGVEGVKTVLVTTNLAPHGGDLTEDNMETENAAAAAAAAFTASSQLKEAVLVKMAEEGENLEAEIVYPITCGDSRANLIWRKFVCPGINVKCVQYDEHVISPKEFVHLAGKSTLKDWKRAIRMNGIMLRKIMDSGELDFYQHDKVCSNTCRSTKIDLSGARVSLSSPTSAEYIPLTPAAADVNGSPATITIETCEDPGDWTAAIGDDTFTFWRGLKDAGLLDEVIQEFHQELVETMRGLQQRVQDPPLQLRDAVLLNNIVQNFGMLDLVKKVLASHKCQMDRSREQYARDLAALEQQCDEHRRRAKELKHKSQHLSNVLMTLTPVSLPPPVKRPRLARATSGPAAMASQVLTQSAQLALGPGVPVPQLTSVPLGKVVSTLPSTVLGKGSLQAPPASSPASPLLGGYTVLASSGSTYPSTVEIHPDASSLTVLSTAAVQDGSTVFKVVSPLQLLTLPGLGPTLQNVAQASPGSSTIVTVPAGAAPGPEEHTATIEVAAMAEDHERK
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
3Phosphorylation-----MATPDVSVHM
-----CCCCCCEEEC		20.8020068231
7Phosphorylation-MATPDVSVHMEEVV
-CCCCCCEEECEEEE		17.4320068231
17PhosphorylationMEEVVVVTTPDTAVD
CEEEEEEECCCCCCC		22.4720068231
18PhosphorylationEEVVVVTTPDTAVDG
EEEEEEECCCCCCCC		13.9320068231
21PhosphorylationVVVTTPDTAVDGSGV
EEEECCCCCCCCCCC		29.7720068231
26PhosphorylationPDTAVDGSGVEGVKT
CCCCCCCCCCCCCEE		34.8920068231
107UbiquitinationRANLIWRKFVCPGIN
HHHEEHHHHCCCCCC		27.44-
116UbiquitinationVCPGINVKCVQYDEH
CCCCCCEEEEEECCC		24.97-
126PhosphorylationQYDEHVISPKEFVHL
EECCCCCCHHHHHHH		28.9125159151
128UbiquitinationDEHVISPKEFVHLAG
CCCCCCHHHHHHHCC		57.92-
136UbiquitinationEFVHLAGKSTLKDWK
HHHHHCCCCCHHHHH		34.36-
140UbiquitinationLAGKSTLKDWKRAIR
HCCCCCHHHHHHHHH		62.73-
143UbiquitinationKSTLKDWKRAIRMNG
CCCHHHHHHHHHHCC		41.93-
155SumoylationMNGIMLRKIMDSGEL
HCCEEEEEHHCCCCC		38.1225114211
155UbiquitinationMNGIMLRKIMDSGEL
HCCEEEEEHHCCCCC		38.12-
155SumoylationMNGIMLRKIMDSGEL
HCCEEEEEHHCCCCC		38.12-
169UbiquitinationLDFYQHDKVCSNTCR
CCEEECCHHCCCCCC		42.91-
179SumoylationSNTCRSTKIDLSGAR
CCCCCCCEEECCCCE		35.15-
179SumoylationSNTCRSTKIDLSGAR
CCCCCCCEEECCCCE		35.15-
179UbiquitinationSNTCRSTKIDLSGAR
CCCCCCCEEECCCCE		35.15-
183PhosphorylationRSTKIDLSGARVSLS
CCCEEECCCCEEECC		27.0221815630
190PhosphorylationSGARVSLSSPTSAEY
CCCEEECCCCCCCCC		27.1126074081
191PhosphorylationGARVSLSSPTSAEYI
CCEEECCCCCCCCCC		37.1726074081
193PhosphorylationRVSLSSPTSAEYIPL
EEECCCCCCCCCCCC		42.3826074081
194PhosphorylationVSLSSPTSAEYIPLT
EECCCCCCCCCCCCC		23.6126074081
201PhosphorylationSAEYIPLTPAAADVN
CCCCCCCCCCCCCCC		12.9126074081
296UbiquitinationGMLDLVKKVLASHKC
CHHHHHHHHHHHCCC		34.69-
302UbiquitinationKKVLASHKCQMDRSR
HHHHHHCCCCCHHHH		24.54-
337PhosphorylationAKELKHKSQHLSNVL
HHHHHHHHHHHHHHH		23.66-
341PhosphorylationKHKSQHLSNVLMTLT
HHHHHHHHHHHHHCC		23.8329978859
346PhosphorylationHLSNVLMTLTPVSLP
HHHHHHHHCCCCCCC		24.2621712546
348PhosphorylationSNVLMTLTPVSLPPP
HHHHHHCCCCCCCCC		16.6925159151
351PhosphorylationLMTLTPVSLPPPVKR
HHHCCCCCCCCCCCC		36.0429978859
357AcetylationVSLPPPVKRPRLARA
CCCCCCCCCCCCCCC		63.5625953088
365PhosphorylationRPRLARATSGPAAMA
CCCCCCCCCCHHHHH		28.7626657352
366PhosphorylationPRLARATSGPAAMAS
CCCCCCCCCHHHHHH		41.6228464451
373PhosphorylationSGPAAMASQVLTQSA
CCHHHHHHHHHHHHH		14.0328112733
377PhosphorylationAMASQVLTQSAQLAL
HHHHHHHHHHHHHHC		22.9427080861
379PhosphorylationASQVLTQSAQLALGP
HHHHHHHHHHHHCCC		16.8528464451
394PhosphorylationGVPVPQLTSVPLGKV
CCCCCCCEECCCCCH		23.5622210691
395PhosphorylationVPVPQLTSVPLGKVV
CCCCCCEECCCCCHH		30.2622210691
403O-linked_GlycosylationVPLGKVVSTLPSTVL
CCCCCHHHCCCHHHC		27.4930059200
404O-linked_GlycosylationPLGKVVSTLPSTVLG
CCCCHHHCCCHHHCC		30.9520068230
404O-linked_GlycosylationPLGKVVSTLPSTVLG
CCCCHHHCCCHHHCC		30.9530059200
407PhosphorylationKVVSTLPSTVLGKGS
CHHHCCCHHHCCCCC		33.9728555341
407O-linked_GlycosylationKVVSTLPSTVLGKGS
CHHHCCCHHHCCCCC		33.9730059200
408O-linked_GlycosylationVVSTLPSTVLGKGSL
HHHCCCHHHCCCCCC		20.1530059200
414O-linked_GlycosylationSTVLGKGSLQAPPAS
HHHCCCCCCCCCCCC		22.3130059200
421PhosphorylationSLQAPPASSPASPLL
CCCCCCCCCCCCCCC		42.5026074081
421O-linked_GlycosylationSLQAPPASSPASPLL
CCCCCCCCCCCCCCC		42.5030059200
422O-linked_GlycosylationLQAPPASSPASPLLG
CCCCCCCCCCCCCCC		26.9630059200
422PhosphorylationLQAPPASSPASPLLG
CCCCCCCCCCCCCCC		26.9626074081
425O-linked_GlycosylationPPASSPASPLLGGYT
CCCCCCCCCCCCCEE		21.3330059200
425PhosphorylationPPASSPASPLLGGYT
CCCCCCCCCCCCCEE		21.3326074081
431PhosphorylationASPLLGGYTVLASSG
CCCCCCCEEEEECCC		7.5926074081
432O-linked_GlycosylationSPLLGGYTVLASSGS
CCCCCCEEEEECCCC		16.5930059200
436O-linked_GlycosylationGGYTVLASSGSTYPS
CCEEEEECCCCCCCC		30.9430059200
437O-linked_GlycosylationGYTVLASSGSTYPST
CEEEEECCCCCCCCC		31.0230059200
443O-linked_GlycosylationSSGSTYPSTVEIHPD
CCCCCCCCCEEECCC		34.3730059200
444O-linked_GlycosylationSGSTYPSTVEIHPDA
CCCCCCCCEEECCCC		20.0430059200
453O-linked_GlycosylationEIHPDASSLTVLSTA
EECCCCCCCEEEEEE		29.7630059200
455O-linked_GlycosylationHPDASSLTVLSTAAV
CCCCCCCEEEEEEEE		22.7330059200
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 GMEB2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GMEB2_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 GMEB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC9_RATUbe2iphysical
11812797
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 GMEB2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, AND MASSSPECTROMETRY.

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