GNMT_HUMAN - dbPTM
GNMT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GNMT_HUMAN
UniProt AC Q14749
Protein Name Glycine N-methyltransferase
Gene Name GNMT
Organism Homo sapiens (Human).
Sequence Length 295
Subcellular Localization Cytoplasm.
Protein Description Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue concentration of AdoMet and of metabolism of methionine..
Protein Sequence MVDSVYRTRSLGVAAEGLPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCQRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRHEPAFDKWVIEEANWMTLDKDVPQSAEGGFDAVICLGNSFAHLPDCKGDQSEHRLALKNIASMVRAGGLLVIDHRNYDHILSTGCAPPGKNIYYKSDLTKDVTTSVLIVNNKAHMVTLDYTVQVPGAGQDGSPGLSKFRLSYYPHCLASFTELLQAAFGGKCQHSVLGDFKPYKPGQTYIPCYFIHVLKRTD
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------MVDSVYRTR
------CCCCEEHHH
8.26-
10PhosphorylationDSVYRTRSLGVAAEG
CCEEHHHHHCCCCCC
28.9422798277
22PhosphorylationAEGLPDQYADGEAAR
CCCCCHHCCCCHHHE
17.65-
34PhosphorylationAARVWQLYIGDTRSR
HHEEEEEEECCCCCC
6.43-
46SuccinylationRSRTAEYKAWLLGLL
CCCCHHHHHHHHHHH
25.29-
46SuccinylationRSRTAEYKAWLLGLL
CCCCHHHHHHHHHHH
25.29-
81PhosphorylationMLVEEGFSVTSVDAS
EEEECCCCCEEECCC
35.0324275569
97AcetylationKMLKYALKERWNRRH
HHHHHHHHHHHHHCC
36.747674065
193SuccinylationTGCAPPGKNIYYKSD
CCCCCCCCCEEECCC
46.04-
193SuccinylationTGCAPPGKNIYYKSD
CCCCCCCCCEEECCC
46.04-
196PhosphorylationAPPGKNIYYKSDLTK
CCCCCCEEECCCCCC
17.77-
197PhosphorylationPPGKNIYYKSDLTKD
CCCCCEEECCCCCCC
10.5421253578
198SuccinylationPGKNIYYKSDLTKDV
CCCCEEECCCCCCCC
22.11-
198SuccinylationPGKNIYYKSDLTKDV
CCCCEEECCCCCCCC
22.11-
199PhosphorylationGKNIYYKSDLTKDVT
CCCEEECCCCCCCCE
23.02-
203SuccinylationYYKSDLTKDVTTSVL
EECCCCCCCCEEEEE
58.46-
203SuccinylationYYKSDLTKDVTTSVL
EECCCCCCCCEEEEE
58.46-
220PhosphorylationNNKAHMVTLDYTVQV
CCCEEEEEEEEEEEC
13.3125693802
224PhosphorylationHMVTLDYTVQVPGAG
EEEEEEEEEECCCCC
12.25-
235PhosphorylationPGAGQDGSPGLSKFR
CCCCCCCCCCHHHHH
24.8819060867
239PhosphorylationQDGSPGLSKFRLSYY
CCCCCCHHHHHHHCC
35.3525693802
252PhosphorylationYYPHCLASFTELLQA
CCHHHHHHHHHHHHH
21.54-

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
10SPhosphorylationKinasePKCAP17252
PSP
10SPhosphorylationKinaseJNK1P45983
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GNMT_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 GNMT_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PKHF2_HUMANPLEKHF2physical
16189514
NIF3L_HUMANNIF3L1physical
16189514
NUD18_HUMANNUDT18physical
16189514
GNMT_HUMANGNMTphysical
16189514
RSSA_HUMANRPSAphysical
21988832
GNMT_HUMANGNMTphysical
25416956
ATL4_HUMANADAMTSL4physical
25416956
NTAQ1_HUMANWDYHV1physical
25416956
KRA42_HUMANKRTAP4-2physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
HDAC7_HUMANHDAC7physical
21516116
PREX2_HUMANPREX2physical
28205209

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
606664Glycine N-methyltransferase deficiency (GNMT deficiency)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00145Glycine
DB00118S-Adenosylmethionine
Regulatory Network of GNMT_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP