GAMT_HUMAN - dbPTM
GAMT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GAMT_HUMAN
UniProt AC Q14353
Protein Name Guanidinoacetate N-methyltransferase
Gene Name GAMT
Organism Homo sapiens (Human).
Sequence Length 236
Subcellular Localization
Protein Description Converts guanidinoacetate to creatine, using S-adenosylmethionine as the methyl donor. [PubMed: 26003046]
Protein Sequence MSAPSATPIFAPGENCSPAWGAAPAAYDAADTHLRILGKPVMERWETPYMHALAAAASSKGGRVLEVGFGMAIAASKVQEAPIDEHWIIECNDGVFQRLRDWAPRQTHKVIPLKGLWEDVAPTLPDGHFDGILYDTYPLSEETWHTHQFNFIKNHAFRLLKPGGVLTYCNLTSWGELMKSKYSDITIMFEETQVPALLEAGFRRENIRTEVMALVPPADCRYYAFPQMITPLVTKG
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------MSAPSATPI
------CCCCCCCCC
49.2222223895
2Phosphorylation------MSAPSATPI
------CCCCCCCCC
49.2227251275
5Phosphorylation---MSAPSATPIFAP
---CCCCCCCCCCCC
44.4827251275
7Phosphorylation-MSAPSATPIFAPGE
-CCCCCCCCCCCCCC
22.6627251275
17PhosphorylationFAPGENCSPAWGAAP
CCCCCCCCCCCCCCC
29.2727251275
27PhosphorylationWGAAPAAYDAADTHL
CCCCCHHHHHHHHHH
14.2826552605
32PhosphorylationAAYDAADTHLRILGK
HHHHHHHHHHHHCCC
20.3427251275
39UbiquitinationTHLRILGKPVMERWE
HHHHHCCCCHHHHCC
30.87-
60UbiquitinationLAAAASSKGGRVLEV
HHHHHHCCCCEEEEE
63.99-
109UbiquitinationWAPRQTHKVIPLKGL
CCCCCCCEEEECCCH
45.29-
222PhosphorylationVPPADCRYYAFPQMI
CCCCHHCCEECCCCC
12.8917053785
223PhosphorylationPPADCRYYAFPQMIT
CCCHHCCEECCCCCC
5.1717053785
235UbiquitinationMITPLVTKG------
CCCCCCCCC------
55.962190698

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 GAMT_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GAMT_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 GAMT_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYFM_HUMANFARS2physical
26186194
SYFM_HUMANFARS2physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612736Cerebral creatine deficiency syndrome 2 (CCDS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00148Creatine
DB00536Guanidine
Regulatory Network of GAMT_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-222 AND TYR-223, ANDMASS SPECTROMETRY.

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