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
33UbiquitinationREDPDPRKVNLGVGA
CCCCCCCCEEECCCC		40.6421906983
35UbiquitinationDPDPRKVNLGVGAYR
CCCCCCEEECCCCEE		33.83-
39UbiquitinationRKVNLGVGAYRTDDC
CCEEECCCCEECCCC		18.32-
41PhosphorylationVNLGVGAYRTDDCHP
EEECCCCEECCCCCC		14.23-
46S-nitrosocysteineGAYRTDDCHPWVLPV
CCEECCCCCCCHHHH		4.64-
46S-nitrosylationGAYRTDDCHPWVLPV
CCEECCCCCCCHHHH		4.6419483679
55UbiquitinationPWVLPVVKKVEQKIA
CCHHHHHHHHHHHHH		51.87-
56UbiquitinationWVLPVVKKVEQKIAN
CHHHHHHHHHHHHHC		39.1221906983
60UbiquitinationVVKKVEQKIANDNSL
HHHHHHHHHHCCCCC		30.22-
66PhosphorylationQKIANDNSLNHEYLP
HHHHCCCCCCCCCHH		33.1526356563
71PhosphorylationDNSLNHEYLPILGLA
CCCCCCCCHHHHHHH		15.3821082442
76UbiquitinationHEYLPILGLAEFRSC
CCCHHHHHHHHHHHH		24.46-
78UbiquitinationYLPILGLAEFRSCAS
CHHHHHHHHHHHHHH		16.45-
82PhosphorylationLGLAEFRSCASRLAL
HHHHHHHHHHHHHHC		21.2526437602
93PhosphorylationRLALGDDSPALKEKR
HHHCCCCCHHHHHHC		19.4721815630
97UbiquitinationGDDSPALKEKRVGGV
CCCCHHHHHHCCCCC		64.3921906983
97AcetylationGDDSPALKEKRVGGV
CCCCHHHHHHCCCCC		64.3926051181
99UbiquitinationDSPALKEKRVGGVQS
CCHHHHHHCCCCCCC		51.2821906983
109UbiquitinationGGVQSLGGTGALRIG
CCCCCCCCCCCHHCC		26.69-
130UbiquitinationWYNGTNNKNTPVYVS
CCCCCCCCCCCEEEE		65.35-
133UbiquitinationGTNNKNTPVYVSSPT
CCCCCCCCEEEECCC		25.49-
137PhosphorylationKNTPVYVSSPTWENH
CCCCEEEECCCCCCC		16.9528152594
138PhosphorylationNTPVYVSSPTWENHN
CCCEEEECCCCCCCC		19.1228152594
140PhosphorylationPVYVSSPTWENHNAV
CEEEECCCCCCCCCH		47.5628152594
145UbiquitinationSPTWENHNAVFSAAG
CCCCCCCCCHHCCCC		49.75-
149PhosphorylationENHNAVFSAAGFKDI
CCCCCHHCCCCCCCH		15.6026437602
154AcetylationVFSAAGFKDIRSYRY
HHCCCCCCCHHHHCC		51.8620167786
154UbiquitinationVFSAAGFKDIRSYRY
HHCCCCCCCHHHHCC		51.86-
158PhosphorylationAGFKDIRSYRYWDAE
CCCCCHHHHCCCCHH		17.8122673903
166AcetylationYRYWDAEKRGLDLQG
HCCCCHHHCCCCHHH		54.1915618217
166UbiquitinationYRYWDAEKRGLDLQG
HCCCCHHHCCCCHHH		54.1921906983
211PhosphorylationEQWKQIASVMKHRFL
HHHHHHHHHHHHHHH		25.1126437602
214AcetylationKQIASVMKHRFLFPF
HHHHHHHHHHHHHHH		29.4926210075
224PhosphorylationFLFPFFDSAYQGFAS
HHHHHHCHHHHHHHC		24.58-
226PhosphorylationFPFFDSAYQGFASGN
HHHHCHHHHHHHCCC		17.0821253578
255UbiquitinationGFEFFCAQSFSKNFG
CCCEEEEEHHHHHCC		46.30-
256PhosphorylationFEFFCAQSFSKNFGL
CCEEEEEHHHHHCCC		16.9824719451
259OtherFCAQSFSKNFGLYNE
EEEEHHHHHCCCCCC		55.04-
259N6-(pyridoxal phosphate)lysineFCAQSFSKNFGLYNE
EEEEHHHHHCCCCCC		55.04-
264PhosphorylationFSKNFGLYNERVGNL
HHHHCCCCCCEECEE		18.5028152594
269UbiquitinationGLYNERVGNLTVVGK
CCCCCEECEEEEECC		29.65-
276UbiquitinationGNLTVVGKEPESILQ
CEEEEECCCHHHHHH		59.49-
290UbiquitinationQVLSQMEKIVRITWS
HHHHHHHHHHHEECC		40.95-
295PhosphorylationMEKIVRITWSNPPAQ
HHHHHHEECCCCCCC		16.57-
297PhosphorylationKIVRITWSNPPAQGA
HHHHEECCCCCCCCC		30.7028857561
304UbiquitinationSNPPAQGARIVASTL
CCCCCCCCEEEEECC		5.97-
312PhosphorylationRIVASTLSNPELFEE
EEEEECCCCHHHHHH		50.8828857561
321PhosphorylationPELFEEWTGNVKTMA
HHHHHHHHCCHHHHH		23.3522673903
325UbiquitinationEEWTGNVKTMADRIL
HHHHCCHHHHHHHHH		36.2621906983
325UbiquitinationEEWTGNVKTMADRIL
HHHHCCHHHHHHHHH		36.26-
326PhosphorylationEWTGNVKTMADRILT
HHHCCHHHHHHHHHH		17.2022673903
330MethylationNVKTMADRILTMRSE
CHHHHHHHHHHHHHH		19.11-
333PhosphorylationTMADRILTMRSELRA
HHHHHHHHHHHHHHH		14.2520166139
336PhosphorylationDRILTMRSELRARLE
HHHHHHHHHHHHHHH		30.1126437602
346UbiquitinationRARLEALKTPGTWNH
HHHHHHHCCCCCCCH		60.77-
357AcetylationTWNHITDQIGMFSFT
CCCHHHCCCCCEEEC		26.03-
357UbiquitinationTWNHITDQIGMFSFT
CCCHHHCCCCCEEEC		26.03-
373PhosphorylationLNPKQVEYLVNEKHI
CCHHHEEEEECCCEE		19.6626437602
375UbiquitinationPKQVEYLVNEKHIYL
HHHEEEEECCCEEEE		9.47-
378AcetylationVEYLVNEKHIYLLPS
EEEEECCCEEEECCC		30.0521466224
378UbiquitinationVEYLVNEKHIYLLPS
EEEEECCCEEEECCC		30.0521906983
381PhosphorylationLVNEKHIYLLPSGRI
EECCCEEEECCCCCE		11.2528152594
385PhosphorylationKHIYLLPSGRINVSG
CEEEECCCCCEEECC		40.4526437602
390UbiquitinationLPSGRINVSGLTTKN
CCCCCEEECCCCCCC		4.46-
391PhosphorylationPSGRINVSGLTTKNL
CCCCEEECCCCCCCC		24.4819764811
394PhosphorylationRINVSGLTTKNLDYV
CEEECCCCCCCCCEE		38.9722673903
395PhosphorylationINVSGLTTKNLDYVA
EEECCCCCCCCCEEE		23.9926437602
396UbiquitinationNVSGLTTKNLDYVAT
EECCCCCCCCCEEEH		50.7221906983
400PhosphorylationLTTKNLDYVATSIHE
CCCCCCCEEEHHHHH		8.6422210691
403PhosphorylationKNLDYVATSIHEAVT
CCCCEEEHHHHHHHH		20.4019764811
404PhosphorylationNLDYVATSIHEAVTK
CCCEEEHHHHHHHHH		16.5322210691
411UbiquitinationSIHEAVTKIQ-----
HHHHHHHHCC-----		32.2921906983
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 AATC_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AATC_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 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
Regulatory Network of AATC_HUMAN

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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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