GATM_HUMAN - dbPTM
GATM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GATM_HUMAN
UniProt AC P50440
Protein Name Glycine amidinotransferase, mitochondrial
Gene Name GATM
Organism Homo sapiens (Human).
Sequence Length 423
Subcellular Localization Isoform 1: Mitochondrion inner membrane
Peripheral membrane protein
Intermembrane side. Probably attached to the outer side of the inner membrane.
Isoform 2: Cytoplasm.
Protein Description Catalyzes the biosynthesis of guanidinoacetate, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues. May play a role in embryonic and central nervous system development. May be involved in the response to heart failure by elevating local creatine synthesis..
Protein Sequence MLRVRCLRGGSRGAEAVHYIGSRLGRTLTGWVQRTFQSTQAATASSRNSCAADDKATEPLPKDCPVSSYNEWDPLEEVIVGRAENACVPPFTIEVKANTYEKYWPFYQKQGGHYFPKDHLKKAVAEIEEMCNILKTEGVTVRRPDPIDWSLKYKTPDFESTGLYSAMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYFHRGAKWTTAPKPTMADELYNQDYPIHSVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLAPDYRVHIISFKDPNPMHIDATFNIIGPGIVLSNPDRPCHQIDLFKKAGWTIITPPTPIIPDDHPLWMSSKWLSMNVLMLDEKRVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVRRRGTLQSYLD
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
11 (in isoform 2)Phosphorylation-30.3024275569
22PhosphorylationEAVHYIGSRLGRTLT
HHHHHHHHHHHHHHH		18.12-
27PhosphorylationIGSRLGRTLTGWVQR
HHHHHHHHHHHHHHH		27.20-
38PhosphorylationWVQRTFQSTQAATAS
HHHHHHHHHHHHHHH		20.4920166139
39PhosphorylationVQRTFQSTQAATASS
HHHHHHHHHHHHHHC		16.0820166139
43PhosphorylationFQSTQAATASSRNSC
HHHHHHHHHHCCCCC		30.0420166139
45PhosphorylationSTQAATASSRNSCAA
HHHHHHHHCCCCCCC		26.0220166139
46PhosphorylationTQAATASSRNSCAAD
HHHHHHHCCCCCCCC		32.7720166139
49PhosphorylationATASSRNSCAADDKA
HHHHCCCCCCCCCCC		12.2020166139
67PhosphorylationLPKDCPVSSYNEWDP
CCCCCCCCCCCCCCC		16.5528857561
68PhosphorylationPKDCPVSSYNEWDPL
CCCCCCCCCCCCCCH		32.0128258704
69PhosphorylationKDCPVSSYNEWDPLE
CCCCCCCCCCCCCHH		15.0328258704
92PhosphorylationNACVPPFTIEVKANT
CCCCCCEEEEEECCC		23.2328857561
100PhosphorylationIEVKANTYEKYWPFY
EEEECCCCCCCCCHH		15.3821253578
102AcetylationVKANTYEKYWPFYQK
EECCCCCCCCCHHHC		42.0524885289
103PhosphorylationKANTYEKYWPFYQKQ
ECCCCCCCCCHHHCC		13.3321253578
121AcetylationYFPKDHLKKAVAEIE
CCCHHHHHHHHHHHH		34.9524888387
140PhosphorylationILKTEGVTVRRPDPI
HHHHCCCCEECCCCC		21.10-
150PhosphorylationRPDPIDWSLKYKTPD
CCCCCCCEEEECCCC		15.9626657352
153PhosphorylationPIDWSLKYKTPDFES
CCCCEEEECCCCHHH		25.9526657352
160PhosphorylationYKTPDFESTGLYSAM
ECCCCHHHCCCCCCC		27.9828857561
161PhosphorylationKTPDFESTGLYSAMP
CCCCHHHCCCCCCCC		24.8228857561
164PhosphorylationDFESTGLYSAMPRDI
CHHHCCCCCCCCCEE		8.84-
165PhosphorylationFESTGLYSAMPRDIL
HHHCCCCCCCCCEEE		24.1228857561
198PhosphorylationFEYRAYRSIIKDYFH
HHHHHHHHHHHHHHH		18.9124719451
203PhosphorylationYRSIIKDYFHRGAKW
HHHHHHHHHHCCCCC		9.04-
217PhosphorylationWTTAPKPTMADELYN
CCCCCCCCCHHHHHC		30.9928857561
227PhosphorylationDELYNQDYPIHSVED
HHHHCCCCCCCCHHH		8.3621253578
231PhosphorylationNQDYPIHSVEDRHKL
CCCCCCCCHHHHHHH		28.1120166139
273PhosphorylationFAQRSQVTNYLGIEW
HHCHHHHHHHHCHHH		15.5428857561
275PhosphorylationQRSQVTNYLGIEWMR
CHHHHHHHHCHHHHH		9.28-
289PhosphorylationRRHLAPDYRVHIISF
HHHCCCCCEEEEEEE		17.30-
295PhosphorylationDYRVHIISFKDPNPM
CCEEEEEEECCCCCC		26.1624719451
359PhosphorylationWMSSKWLSMNVLMLD
CCCCCCHHCCEEEEC		13.7528857561
381AcetylationANEVPIQKMFEKLGI
CCCCCHHHHHHHHCC		46.4027178108
385AcetylationPIQKMFEKLGITTIK
CHHHHHHHHCCCEEE		40.5219608861
389PhosphorylationMFEKLGITTIKVNIR
HHHHHCCCEEEEEEC		22.2228857561
390PhosphorylationFEKLGITTIKVNIRN
HHHHCCCEEEEEECC		19.5128857561
400PhosphorylationVNIRNANSLGGGFHC
EEECCCCCCCCCEEE		26.4428857561
409PhosphorylationGGGFHCWTCDVRRRG
CCCEEEEECCCCCCC		12.2928857561
417PhosphorylationCDVRRRGTLQSYLD-
CCCCCCCCHHHHCC-		21.5828192239
420PhosphorylationRRRGTLQSYLD----
CCCCCHHHHCC----		30.6725072903
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 GATM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GATM_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 GATM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GATM_HUMAN !!
Drug and Disease Associations
Kegg Disease
H00849 Creatine deficiency syndrome, including: Arginine:glycine amidinotransferase deficiency (AGAT defici
OMIM Disease
612718Cerebral creatine deficiency syndrome 3 (CCDS3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00145Glycine
DB00129L-Ornithine
Regulatory Network of GATM_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-385, AND MASS SPECTROMETRY.

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