MYEF2_HUMAN - dbPTM
MYEF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYEF2_HUMAN
UniProt AC Q9P2K5
Protein Name Myelin expression factor 2
Gene Name MYEF2
Organism Homo sapiens (Human).
Sequence Length 600
Subcellular Localization Nucleus.
Protein Description Transcriptional repressor of the myelin basic protein gene (MBP). Binds to the proximal MB1 element 5'-TTGTCC-3' of the MBP promoter. Its binding to MB1 and function are inhibited by PURA (By similarity)..
Protein Sequence MADANKAEVPGATGGDSPHLQPAEPPGEPRREPHPAEAEKQQPQHSSSSNGVKMENDESAKEEKSDLKEKSTGSKKANRFHPYSKDKNSGAGEKKGPNRNRVFISNIPYDMKWQAIKDLMREKVGEVTYVELFKDAEGKSRGCGVVEFKDEEFVKKALETMNKYDLSGRPLNIKEDPDGENARRALQRTGGSFPGGHVPDMGSGLMNLPPSILNNPNIPPEVISNLQAGRLGSTIFVANLDFKVGWKKLKEVFSIAGTVKRADIKEDKDGKSRGMGTVTFEQAIEAVQAISMFNGQFLFDRPMHVKMDDKSVPHEEYRSHDGKTPQLPRGLGGIGMGLGPGGQPISASQLNIGGVMGNLGPGGMGMDGPGFGGMNRIGGGIGFGGLEAMNSMGGFGGVGRMGELYRGAMTSSMERDFGRGDIGINQGFGDSFGRLGSAMIGGFAGRIGSSNMGPVGSGISGGMGSMNSVTGGMGMGLDRMSSSFDRMGPGIGAILERSIDMDRGFLSGPMGSGMRERIGSKGNQIFVRNLPFDLTWQKLKEKFSQCGHVMFAEIKMENGKSKGCGTVRFDSPESAEKACRIMNGIKISGREIDVRLDRNA
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------MADANKAEV
------CCCCCCCCC		25.32-
13PhosphorylationKAEVPGATGGDSPHL
CCCCCCCCCCCCCCC		47.8429255136
17PhosphorylationPGATGGDSPHLQPAE
CCCCCCCCCCCCCCC		19.9329255136
40AcetylationPHPAEAEKQQPQHSS
CCHHHHHHHCCCCCC		62.3725953088
53SumoylationSSSSNGVKMENDESA
CCCCCCCCCCCCHHH		41.7328112733
53 (in isoform 3)Phosphorylation-41.7322210691
56 (in isoform 3)Phosphorylation-55.6522210691
59PhosphorylationVKMENDESAKEEKSD
CCCCCCHHHHHHHHH		47.7230576142
71 (in isoform 3)Phosphorylation-38.8122210691
85UbiquitinationNRFHPYSKDKNSGAG
HCCCCCCCCCCCCCC		67.87-
117UbiquitinationDMKWQAIKDLMREKV
HHHHHHHHHHHHHHC		48.07-
123AcetylationIKDLMREKVGEVTYV
HHHHHHHHCCCEEEE		45.2130590555
134UbiquitinationVTYVELFKDAEGKSR
EEEEEEEECCCCCCC		69.52-
139AcetylationLFKDAEGKSRGCGVV
EEECCCCCCCCCEEE		28.6030590561
163UbiquitinationKALETMNKYDLSGRP
HHHHHCCCCCCCCCC		29.35-
164PhosphorylationALETMNKYDLSGRPL
HHHHCCCCCCCCCCC		19.67-
174SumoylationSGRPLNIKEDPDGEN
CCCCCCCCCCCCCHH		55.80-
189PhosphorylationARRALQRTGGSFPGG
HHHHHHHHCCCCCCC		32.6928787133
211PhosphorylationGLMNLPPSILNNPNI
CHHCCCHHHHCCCCC		37.4628787133
233PhosphorylationLQAGRLGSTIFVANL
HCCCCCCCEEEEEEC		23.9521406692
234PhosphorylationQAGRLGSTIFVANLD
CCCCCCCEEEEEECC		19.3521406692
254PhosphorylationKKLKEVFSIAGTVKR
HHHHHHHHHCEEEEH		19.3923403867
258PhosphorylationEVFSIAGTVKRADIK
HHHHHCEEEEHHHHC		17.52-
260UbiquitinationFSIAGTVKRADIKED
HHHCEEEEHHHHCCC		41.53-
265UbiquitinationTVKRADIKEDKDGKS
EEEHHHHCCCCCCCC		61.48-
310UbiquitinationMHVKMDDKSVPHEEY
EEECCCCCCCCCHHH		49.44-
317PhosphorylationKSVPHEEYRSHDGKT
CCCCCHHHHCCCCCC		17.90-
323UbiquitinationEYRSHDGKTPQLPRG
HHHCCCCCCCCCCCC		64.19-
406MethylationGRMGELYRGAMTSSM
HHHHHHHHHHHCCCC		38.7316186495
411PhosphorylationLYRGAMTSSMERDFG
HHHHHHCCCCCCCCC		18.0128348404
412PhosphorylationYRGAMTSSMERDFGR
HHHHHCCCCCCCCCC		18.5928348404
431PhosphorylationINQGFGDSFGRLGSA
CCCCCCCCCHHHHHH		29.9428112733
437PhosphorylationDSFGRLGSAMIGGFA
CCCHHHHHHHHHHHH		21.1825954137
441 (in isoform 2)Phosphorylation-16.4522210691
444 (in isoform 2)Phosphorylation-15.0522210691
450PhosphorylationFAGRIGSSNMGPVGS
HHCCCCCCCCCCCCC		26.1422210691
457PhosphorylationSNMGPVGSGISGGMG
CCCCCCCCCCCCCCC		32.9422210691
459 (in isoform 2)Phosphorylation-3.5622210691
460PhosphorylationGPVGSGISGGMGSMN
CCCCCCCCCCCCCCC		32.5922210691
465PhosphorylationGISGGMGSMNSVTGG
CCCCCCCCCCHHCCC		13.0919845377
468PhosphorylationGGMGSMNSVTGGMGM
CCCCCCCHHCCCCCC		16.6519845377
470PhosphorylationMGSMNSVTGGMGMGL
CCCCCHHCCCCCCCH		28.0419845377
482PhosphorylationMGLDRMSSSFDRMGP
CCHHHHHCCCHHCCC		26.1924719451
483PhosphorylationGLDRMSSSFDRMGPG
CHHHHHCCCHHCCCC		24.7022199227
487SulfoxidationMSSSFDRMGPGIGAI
HHCCCHHCCCCHHHH		9.0421406390
498PhosphorylationIGAILERSIDMDRGF
HHHHHHHHCCCCCCC		17.3622199227
503MethylationERSIDMDRGFLSGPM
HHHCCCCCCCCCCCC		31.00115484107
507PhosphorylationDMDRGFLSGPMGSGM
CCCCCCCCCCCCCHH		38.29-
512PhosphorylationFLSGPMGSGMRERIG
CCCCCCCCHHHHHHC		24.1427732954
520PhosphorylationGMRERIGSKGNQIFV
HHHHHHCCCCCEEEE		34.7123312004
521UbiquitinationMRERIGSKGNQIFVR
HHHHHCCCCCEEEEE		57.58-
540UbiquitinationDLTWQKLKEKFSQCG
CCCHHHHHHHHHHCC		66.93-
561PhosphorylationIKMENGKSKGCGTVR
EEECCCCCCCCCEEE		35.3622210691
571PhosphorylationCGTVRFDSPESAEKA
CCEEECCCHHHHHHH		28.0527732954
577UbiquitinationDSPESAEKACRIMNG
CCHHHHHHHHHHHCC		53.13-
577AcetylationDSPESAEKACRIMNG
CCHHHHHHHHHHHCC		53.1325953088
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 MYEF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYEF2_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 MYEF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMCA4_HUMANSMARCA4physical
15870273
HDAC5_HUMANHDAC5physical
15111488
PRGC1_HUMANPPARGC1Aphysical
15111488
MK14_HUMANMAPK14physical
15111488
ATX1_HUMANATXN1physical
17646162
TEX11_HUMANTEX11physical
25416956
COG8_HUMANCOG8physical
25416956
ACTN4_HUMANACTN4physical
26496610
VAS1_HUMANATP6AP1physical
26496610
FLOT2_HUMANFLOT2physical
26496610
HNRPD_HUMANHNRNPDphysical
26496610
LAMB3_HUMANLAMB3physical
26496610
HNRPM_HUMANHNRNPMphysical
26496610
STX3_HUMANSTX3physical
26496610
EXO1_HUMANEXO1physical
26496610
FLOT1_HUMANFLOT1physical
26496610
ANM5_HUMANPRMT5physical
26496610
SSA27_HUMANSSSCA1physical
26496610
ERLN1_HUMANERLIN1physical
26496610
ADNP2_HUMANADNP2physical
26496610
PR40B_HUMANPRPF40Bphysical
26496610
STML2_HUMANSTOML2physical
26496610
KDIS_HUMANKIDINS220physical
26496610
NKAP_HUMANNKAPphysical
26496610
SFXN1_HUMANSFXN1physical
26496610
NSUN4_HUMANNSUN4physical
26496610
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 MYEF2_HUMAN

loading...

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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-17, AND MASS SPECTROMETRY.
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-17, AND MASSSPECTROMETRY.
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-17, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory