GMFG_HUMAN - dbPTM
GMFG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GMFG_HUMAN
UniProt AC O60234
Protein Name Glia maturation factor gamma
Gene Name GMFG
Organism Homo sapiens (Human).
Sequence Length 142
Subcellular Localization
Protein Description
Protein Sequence MSDSLVVCEVDPELTEKLRKFRFRKETDNAAIIMKVDKDRQMVVLEEEFQNISPEELKMELPERQPRFVVYSYKYVHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKNRLVQTAELTKVFEIRTTDDLTEAWLQEKLSFFR
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------MSDSLVVCE
------CCCCEEEEE
35.5916873721
2Acetylation------MSDSLVVCE
------CCCCEEEEE
35.5925944712
4Phosphorylation----MSDSLVVCEVD
----CCCCEEEEECC
18.7616873721
17UbiquitinationVDPELTEKLRKFRFR
CCHHHHHHHHHHHCC
48.64-
20UbiquitinationELTEKLRKFRFRKET
HHHHHHHHHHCCCCC
51.86-
25UbiquitinationLRKFRFRKETDNAAI
HHHHHCCCCCCCEEE
63.35-
27PhosphorylationKFRFRKETDNAAIIM
HHHCCCCCCCEEEEE
37.2723882029
34SulfoxidationTDNAAIIMKVDKDRQ
CCCEEEEEEECCCCC
2.5721406390
35AcetylationDNAAIIMKVDKDRQM
CCEEEEEEECCCCCE
36.5525953088
35UbiquitinationDNAAIIMKVDKDRQM
CCEEEEEEECCCCCE
36.5519608861
38UbiquitinationAIIMKVDKDRQMVVL
EEEEEECCCCCEEEE
58.77-
42SulfoxidationKVDKDRQMVVLEEEF
EECCCCCEEEEHHHH
2.0421406390
74AcetylationRFVVYSYKYVHDDGR
CEEEEEEEEECCCCC
34.5525953088
74UbiquitinationRFVVYSYKYVHDDGR
CEEEEEEEEECCCCC
34.55-
83PhosphorylationVHDDGRVSYPLCFIF
ECCCCCEECEEEEEE
21.48-
84PhosphorylationHDDGRVSYPLCFIFS
CCCCCEECEEEEEEC
9.4319060867
97UbiquitinationFSSPVGCKPEQQMMY
ECCCCCCCHHHHHCC
45.73-
104PhosphorylationKPEQQMMYAGSKNRL
CHHHHHCCCCCCCCE
11.50-
108UbiquitinationQMMYAGSKNRLVQTA
HHCCCCCCCCEEEEE
45.21-
119UbiquitinationVQTAELTKVFEIRTT
EEEEHHEEEEEEECC
58.5121890473
119UbiquitinationVQTAELTKVFEIRTT
EEEEHHEEEEEEECC
58.5121890473
119AcetylationVQTAELTKVFEIRTT
EEEEHHEEEEEEECC
58.5119608861
125PhosphorylationTKVFEIRTTDDLTEA
EEEEEEECCCCCHHH
39.9927251275
126PhosphorylationKVFEIRTTDDLTEAW
EEEEEECCCCCHHHH
20.0527251275
137UbiquitinationTEAWLQEKLSFFR--
HHHHHHHHHHCCC--
36.1521890473
139PhosphorylationAWLQEKLSFFR----
HHHHHHHHCCC----
33.1524719451

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
104YPhosphorylationKinaseABLP00519
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GMFG_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 GMFG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VANG1_HUMANVANGL1physical
21988832
PRUN1_HUMANPRUNEphysical
28514442
LANC2_HUMANLANCL2physical
28514442
HSP7E_HUMANHSPA14physical
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 GMFG_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-119, AND MASS SPECTROMETRY.

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