AATC_HUMAN - dbPTM
AATC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AATC_HUMAN
UniProt AC P17174
Protein Name Aspartate aminotransferase, cytoplasmic
Gene Name GOT1
Organism Homo sapiens (Human).
Sequence Length 413
Subcellular Localization Cytoplasm .
Protein Description Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain..
Protein Sequence MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQKIANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFLARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLENAPEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWAIRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPPAQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGMFSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ
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
33UbiquitinlysineREDPDPRKVNLGVGA
CCCCCCCCEEECCCC
40.6421906983
41PhosphotyrosineVNLGVGAYRTDDCHP
EEECCCCEECCCCCC
14.2322135298
46 S-nitrosocysteineGAYRTDDCHPWVLPV
CCEECCCCCCCHHHH
4.6419483679
56UbiquitinlysineWVLPVVKKVEQKIAN
CHHHHHHHHHHHHHC
39.1221906983
66PhosphoserineQKIANDNSLNHEYLP
HHHHCCCCCCCCCHH
33.1519060867
22135298
71PhosphotyrosineDNSLNHEYLPILGLA
CCCCCCCCHHHHHHH
15.3818083107
97N6-acetyllysineGDDSPALKEKRVGGV
CCCCHHHHHHCCCCC
64.3926051181
97UbiquitinlysineGDDSPALKEKRVGGV
CCCCHHHHHHCCCCC
64.3921906983
99UbiquitinlysineDSPALKEKRVGGVQS
CCHHHHHHCCCCCCC
51.2821906983
137PhosphoserineKNTPVYVSSPTWENH
CCCCEEEECCCCCCC
16.9525627689
138PhosphoserineNTPVYVSSPTWENHN
CCCEEEECCCCCCCC
19.1222135298
25627689
23186163
149PhosphoserineENHNAVFSAAGFKDI
CCCCCHHCCCCCCCH
15.6022135298
154N6-acetyllysineVFSAAGFKDIRSYRY
HHCCCCCCCHHHHCC
51.8620167786
25953088
26051181
158PhosphoserineAGFKDIRSYRYWDAE
CCCCCHHHHCCCCHH
17.8122135298
166 N-acetyllysineYRYWDAEKRGLDLQG
HCCCCHHHCCCCHHH
54.1915618217
166UbiquitinlysineYRYWDAEKRGLDLQG
HCCCCHHHCCCCHHH
54.1921906983
211PhosphoserineEQWKQIASVMKHRFL
HHHHHHHHHHHHHHH
25.1122135298
214N6-acetyllysineKQIASVMKHRFLFPF
HHHHHHHHHHHHHHH
29.4926210075
27452117
224PhosphoserineFLFPFFDSAYQGFAS
HHHHHHCHHHHHHHC
24.5822135298
226PhosphotyrosineFPFFDSAYQGFASGN
HHHHCHHHHHHHCCC
17.0821253578
16381945
23193290
22135298
264PhosphotyrosineFSKNFGLYNERVGNL
HHHHCCCCCCEECEE
18.5021253578
16381945
23193290
22135298
325UbiquitinlysineEEWTGNVKTMADRIL
HHHHCCHHHHHHHHH
36.2621906983
333PhosphothreonineTMADRILTMRSELRA
HHHHHHHHHHHHHHH
14.2520166139
373PhosphotyrosineLNPKQVEYLVNEKHI
CCHHHEEEEECCCEE
19.6622135298
378N6-acetyllysineVEYLVNEKHIYLLPS
EEEEECCCEEEECCC
30.0521466224
378UbiquitinlysineVEYLVNEKHIYLLPS
EEEEECCCEEEECCC
30.0521906983
381PhosphotyrosineLVNEKHIYLLPSGRI
EECCCEEEECCCCCE
11.2522135298
385PhosphoserineKHIYLLPSGRINVSG
CEEEECCCCCEEECC
40.4522135298
391PhosphoserinePSGRINVSGLTTKNL
CCCCEEECCCCCCCC
24.4822135298
396UbiquitinlysineNVSGLTTKNLDYVAT
EECCCCCCCCCEEEH
50.7221906983
403PhosphothreonineKNLDYVATSIHEAVT
CCCCEEEHHHHHHHH
20.4022135298
411UbiquitinlysineSIHEAVTKIQ-----
HHHHHHHHCC-----
32.2921906983

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 AATC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANXA6_HUMANANXA6physical
22863883
HPRT_HUMANHPRT1physical
22863883
IDHC_HUMANIDH1physical
22863883
MTAP_HUMANMTAPphysical
22863883
SBDS_HUMANSBDSphysical
22863883
TYSY_HUMANTYMSphysical
22863883
UBE2H_HUMANUBE2Hphysical
22863883
PPAC_HUMANACP1physical
26344197
ANX11_HUMANANXA11physical
26344197
CK054_HUMANC11orf54physical
26344197
CBR1_HUMANCBR1physical
26344197
CCS_HUMANCCSphysical
26344197
FAHD1_HUMANFAHD1physical
26344197
GLOD4_HUMANGLOD4physical
26344197
CH10_HUMANHSPE1physical
26344197
NDKA_HUMANNME1physical
26344197
NQO1_HUMANNQO1physical
26344197
PIPNA_HUMANPITPNAphysical
26344197
PIPNB_HUMANPITPNBphysical
26344197
PPIL3_HUMANPPIL3physical
26344197
RIFK_HUMANRFKphysical
26344197
SNX3_HUMANSNX3physical
26344197
SRXN1_HUMANSRXN1physical
26344197
TALDO_HUMANTALDO1physical
26344197
TPIS_HUMANTPI1physical
26344197
UFM1_HUMANUFM1physical
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
DB00128L-Aspartic Acid
DB00151L-Cysteine
Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-71, AND MASSSPECTROMETRY.

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