GMEB1_HUMAN - dbPTM
GMEB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GMEB1_HUMAN
UniProt AC Q9Y692
Protein Name Glucocorticoid modulatory element-binding protein 1
Gene Name GMEB1
Organism Homo sapiens (Human).
Sequence Length 573
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 MANAEVSVPVGDVVVVPTEGNEGENPEDTKTQVILQLQPVQQGLFIDGHFYNRIYEAGSENNTAVVAVETHTIHKIEEGIDTGTIEANEDMEIAYPITCGESKAILLWKKFVCPGINVKCVKFNDQLISPKHFVHLAGKSTLKDWKRAIRLGGIMLRKMMDSGQIDFYQHDKVCSNTCRSTKFDLLISSARAPVPGQQTSVVQTPTSADGSITQIAISEESMEEAGLEWNSALTAAVTMATEEGVKKDSEEISEDTLMFWKGIADVGLMEEVVCNIQKEIEELLRGVQQRLIQAPFQVTDAAVLNNVAHTFGLMDTVKKVLDNRRNQVEQGEEQFLYTLTDLERQLEEQKKQGQDHRLKSQTVQNVVLMPVSTPKPPKRPRLQRPASTTVLSPSPPVQQPQFTVISPITITPVGQSFSMGNIPVATLSQGSSPVTVHTLPSGPQLFRYATVVSSAKSSSPDTVTIHPSSSLALLSSTAMQDGSTLGNMTTMVSPVELVAMESGLTSAIQAVESTSEDGQTIIEIDPAPDPEAEDTEGKAVILETELRTEEKVVAEMEEHQHQVHNVEIVVLED
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
2Acetylation------MANAEVSVP
------CCCCEEEEE		24.7619413330
110UbiquitinationKAILLWKKFVCPGIN
HHEEEEHHEECCCCC		31.29-
119UbiquitinationVCPGINVKCVKFNDQ
ECCCCCEEEEEECCE		28.90-
122UbiquitinationGINVKCVKFNDQLIS
CCCEEEEEECCEECC		48.17-
129PhosphorylationKFNDQLISPKHFVHL
EECCEECCHHHEEEC		36.1725159151
131UbiquitinationNDQLISPKHFVHLAG
CCEECCHHHEEECCC		42.77-
139UbiquitinationHFVHLAGKSTLKDWK
HEEECCCCCCHHHHH		34.36-
143UbiquitinationLAGKSTLKDWKRAIR
CCCCCCHHHHHHHHH		62.73-
146UbiquitinationKSTLKDWKRAIRLGG
CCCHHHHHHHHHHCH		41.93-
158UbiquitinationLGGIMLRKMMDSGQI
HCHHHHHHHHHCCCC		34.32-
172UbiquitinationIDFYQHDKVCSNTCR
CCEEECCCCCCCCCC		42.91-
182UbiquitinationSNTCRSTKFDLLISS
CCCCCCCCHHEEEEE		37.82-
189PhosphorylationKFDLLISSARAPVPG
CHHEEEEECCCCCCC		18.1228555341
204PhosphorylationQQTSVVQTPTSADGS
CCCEEEECCCCCCCC		19.5426074081
206PhosphorylationTSVVQTPTSADGSIT
CEEEECCCCCCCCEE		39.6826074081
207PhosphorylationSVVQTPTSADGSITQ
EEEECCCCCCCCEEE		26.0926074081
241O-linked_GlycosylationTAAVTMATEEGVKKD
HHHHHHHHHHCCCCC		24.6030059200
249O-linked_GlycosylationEEGVKKDSEEISEDT
HHCCCCCHHHCCHHH		46.1130059200
285MethylationKEIEELLRGVQQRLI
HHHHHHHHHHHHHHH		56.72-
319UbiquitinationGLMDTVKKVLDNRRN
CHHHHHHHHHHCCHH		43.63-
350UbiquitinationERQLEEQKKQGQDHR
HHHHHHHHHCCCCCH		50.79-
372PhosphorylationNVVLMPVSTPKPPKR
EEEEEECCCCCCCCC		32.8729978859
373PhosphorylationVVLMPVSTPKPPKRP
EEEEECCCCCCCCCC		35.2529978859
406PhosphorylationQPQFTVISPITITPV
CCCEEEEECEEEECC		13.1026074081
409PhosphorylationFTVISPITITPVGQS
EEEEECEEEECCCCC		23.3726074081
411PhosphorylationVISPITITPVGQSFS
EEECEEEECCCCCCC		11.8526074081
428O-linked_GlycosylationNIPVATLSQGSSPVT
CCCEEEECCCCCCEE		28.30OGP
432PhosphorylationATLSQGSSPVTVHTL
EEECCCCCCEEEEEC		30.16-
438O-linked_GlycosylationSSPVTVHTLPSGPQL
CCCEEEEECCCCCCE		35.7130059200
441O-linked_GlycosylationVTVHTLPSGPQLFRY
EEEEECCCCCCEEEE		67.2430059200
450O-linked_GlycosylationPQLFRYATVVSSAKS
CCEEEEEEEHHCCCC		16.7130059200
453O-linked_GlycosylationFRYATVVSSAKSSSP
EEEEEEHHCCCCCCC		21.9030059200
454O-linked_GlycosylationRYATVVSSAKSSSPD
EEEEEHHCCCCCCCC		28.2730059200
457PhosphorylationTVVSSAKSSSPDTVT
EEHHCCCCCCCCCEE		35.4526074081
457O-linked_GlycosylationTVVSSAKSSSPDTVT
EEHHCCCCCCCCCEE		35.4530059200
458PhosphorylationVVSSAKSSSPDTVTI
EHHCCCCCCCCCEEE		45.2226074081
458O-linked_GlycosylationVVSSAKSSSPDTVTI
EHHCCCCCCCCCEEE		45.2230059200
459PhosphorylationVSSAKSSSPDTVTIH
HHCCCCCCCCCEEEC		33.6126074081
459O-linked_GlycosylationVSSAKSSSPDTVTIH
HHCCCCCCCCCEEEC		33.6130059200
462PhosphorylationAKSSSPDTVTIHPSS
CCCCCCCCEEECCCC		23.9626074081
464O-linked_GlycosylationSSSPDTVTIHPSSSL
CCCCCCEEECCCCHH		18.7030059200
464PhosphorylationSSSPDTVTIHPSSSL
CCCCCCEEECCCCHH		18.7026074081
468O-linked_GlycosylationDTVTIHPSSSLALLS
CCEEECCCCHHHHHH		20.5630059200
470O-linked_GlycosylationVTIHPSSSLALLSST
EEECCCCHHHHHHCC		23.2330059200
538SumoylationEAEDTEGKAVILETE
CCCCCCCCEEEEEEE		32.99-
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
-KUbiquitinationE3 ubiquitin ligaseTRIM63Q969Q1
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GMEB1_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 GMEB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI63_HUMANTRIM63physical
11927605
UBC9_RATUbe2iphysical
11812797
GMEB2_HUMANGMEB2physical
28514442
MATN4_HUMANMATN4physical
28514442
DHRS2_HUMANDHRS2physical
28514442
WDR54_HUMANWDR54physical
28514442
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 GMEB1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND MASSSPECTROMETRY.

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