GMFB_HUMAN - dbPTM
GMFB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GMFB_HUMAN
UniProt AC P60983
Protein Name Glia maturation factor beta
Gene Name GMFB
Organism Homo sapiens (Human).
Sequence Length 142
Subcellular Localization
Protein Description This protein causes differentiation of brain cells, stimulation of neural regeneration, and inhibition of proliferation of tumor cells..
Protein Sequence MSESLVVCDVAEDLVEKLRKFRFRKETNNAAIIMKIDKDKRLVVLDEELEGISPDELKDELPERQPRFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKNKLVQTAELTKVFEIRNTEDLTEEWLREKLGFFH
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
2Phosphorylation------MSESLVVCD
------CCCCEEEEE
35.5729514088
2Acetylation------MSESLVVCD
------CCCCEEEEE
35.5719413330
4Phosphorylation----MSESLVVCDVA
----CCCCEEEEECH
21.1129514088
17UbiquitinationVAEDLVEKLRKFRFR
CHHHHHHHHHHHCCC
46.2224816145
25UbiquitinationLRKFRFRKETNNAAI
HHHHCCCCCCCCEEE
67.2033845483
27PhosphorylationKFRFRKETNNAAIIM
HHCCCCCCCCEEEEE
36.499030586
35UbiquitinationNNAAIIMKIDKDKRL
CCEEEEEEECCCCCE
37.0322817900
35UbiquitinationNNAAIIMKIDKDKRL
CCEEEEEEECCCCCE
37.0321890473
35UbiquitinationNNAAIIMKIDKDKRL
CCEEEEEEECCCCCE
37.0321890473
38UbiquitinationAIIMKIDKDKRLVVL
EEEEEECCCCCEEEE
69.4922817900
40UbiquitinationIMKIDKDKRLVVLDE
EEEECCCCCEEEECH
54.0622817900
53PhosphorylationDEELEGISPDELKDE
CHHHCCCCHHHHHHH
36.849030586
58UbiquitinationGISPDELKDELPERQ
CCCHHHHHHHCCCCC
47.3021906983
58UbiquitinationGISPDELKDELPERQ
CCCHHHHHHHCCCCC
47.3021890473
72PhosphorylationQPRFIVYSYKYQHDD
CCCEEEEEEEEECCC
12.319030586
74UbiquitinationRFIVYSYKYQHDDGR
CEEEEEEEEECCCCC
32.2821890473
74UbiquitinationRFIVYSYKYQHDDGR
CEEEEEEEEECCCCC
32.2821890473
74AcetylationRFIVYSYKYQHDDGR
CEEEEEEEEECCCCC
32.2825953088
74UbiquitinationRFIVYSYKYQHDDGR
CEEEEEEEEECCCCC
32.2821906983
83PhosphorylationQHDDGRVSYPLCFIF
ECCCCCEEEEEEEEE
21.489030586
84PhosphorylationHDDGRVSYPLCFIFS
CCCCCEEEEEEEEEC
9.4321082442
97UbiquitinationFSSPVGCKPEQQMMY
ECCCCCCCHHHHHCC
45.73-
110AcetylationMYAGSKNKLVQTAEL
CCCCCCCCEEEEHHH
54.4925953088
110UbiquitinationMYAGSKNKLVQTAEL
CCCCCCCCEEEEHHH
54.4933845483
119UbiquitinationVQTAELTKVFEIRNT
EEEHHHEEEEEECCC
58.51-
119UbiquitinationVQTAELTKVFEIRNT
EEEHHHEEEEEECCC
58.5123000965
119AcetylationVQTAELTKVFEIRNT
EEEHHHEEEEEECCC
58.5124620447
1372-HydroxyisobutyrylationTEEWLREKLGFFH--
CHHHHHHHHCCCC--
47.69-
137UbiquitinationTEEWLREKLGFFH--
CHHHHHHHHCCCC--
47.6933845483

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
27TPhosphorylationKinasePRKACAP17612
GPS
27TPhosphorylationKinaseRPS6KA1Q15418
GPS
27TPhosphorylationKinasePKA-FAMILY-GPS
27TPhosphorylationKinaseRSK-SUBFAMILY-GPS
27TPhosphorylationKinasePKA_GROUP-PhosphoELM
27TPhosphorylationKinaseRSK_GROUP-PhosphoELM
53SPhosphorylationKinaseCSNK2A1P68400
GPS
72SPhosphorylationKinasePRKCAP17252
GPS
83SPhosphorylationKinasePRKACAP17612
GPS
83SPhosphorylationKinasePKA-FAMILY-GPS
83SPhosphorylationKinasePKA_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GMFB_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 GMFB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MK03_HUMANMAPK3physical
8639570
HNRH2_HUMANHNRNPH2physical
26344197
PFD6_HUMANPFDN6physical
26344197
SETD3_HUMANSETD3physical
26344197

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 GMFB_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-84, AND MASSSPECTROMETRY.

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