AATC_MOUSE - dbPTM
AATC_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AATC_MOUSE
UniProt AC P05201
Protein Name Aspartate aminotransferase, cytoplasmic
Gene Name Got1
Organism Mus musculus (Mouse).
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 (By similarity)..
Protein Sequence MAPPSVFAQVPQAPPVLVFKLTADFRDDPDPRKVNLGVGAYRTDESQPWVLPVVRKVEQKIANDNSLNHEYLPILGLAEFRSCASRLVLGDNSLAIRENRVGGVQSLGGTGALRIGADFLGRWYNGTDNKNTPIYVSSPTWENHNAVFSAAGFKDIRPYCYWDAEKRGLDLQGFLNDLENAPEFSIFVLHACAHNPTGTDPTPEQWKQIAAVMQRRFLFPFFDSAYQGFASGDLEKDAWAIRYFVSEGFELFCAQSFSKNFGLYNERVGNLTVVGKESDSVLRVLSQMEKIVRITWSNPPAQGARIVAATLSDPELFKEWKGNVKTMADRILTMRSELRARLEALKTPGTWSHITEQIGMFSFTGLNPKQVEYLVNEKHIYLLPSGRINMCGLTTKNLDYVATSIHEAVTKIQ
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
33UbiquitinationRDDPDPRKVNLGVGA
CCCCCCCCEEEECCC		40.6422790023
43PhosphorylationLGVGAYRTDESQPWV
EECCCEECCCCCCCC		31.2923737553
46PhosphorylationGAYRTDESQPWVLPV
CCEECCCCCCCCHHH		44.3323737553
60UbiquitinationVVRKVEQKIANDNSL
HHHHHHHHHHCCCCC		30.2222790023
66PhosphorylationQKIANDNSLNHEYLP
HHHHCCCCCCCCCHH		33.1519060867
71PhosphorylationDNSLNHEYLPILGLA
CCCCCCCCHHHHHHH		15.3829899451
71NitrationDNSLNHEYLPILGLA
CCCCCCCCHHHHHHH		15.38-
82PhosphorylationLGLAEFRSCASRLVL
HHHHHHHHHHHHHHC		21.2529899451
85PhosphorylationAEFRSCASRLVLGDN
HHHHHHHHHHHCCCC		30.4029899451
93PhosphorylationRLVLGDNSLAIRENR
HHHCCCCCEEEECCC		24.7424719451
130UbiquitinationWYNGTDNKNTPIYVS
CCCCCCCCCCCEEEE		66.0822790023
132PhosphorylationNGTDNKNTPIYVSSP
CCCCCCCCCEEEECC		16.8123984901
135PhosphorylationDNKNTPIYVSSPTWE
CCCCCCEEEECCCCC		8.7623984901
137PhosphorylationKNTPIYVSSPTWENH
CCCCEEEECCCCCCC		17.3923984901
138PhosphorylationNTPIYVSSPTWENHN
CCCEEEECCCCCCCC		19.1223984901
140PhosphorylationPIYVSSPTWENHNAV
CEEEECCCCCCCCHH		47.5626745281
149PhosphorylationENHNAVFSAAGFKDI
CCCCHHHHCCCCCCC		15.6022817900
160S-nitrosylationFKDIRPYCYWDAEKR
CCCCCCCEEECHHHC		2.8421278135
160S-nitrosocysteineFKDIRPYCYWDAEKR
CCCCCCCEEECHHHC		2.84-
166UbiquitinationYCYWDAEKRGLDLQG
CEEECHHHCCCCHHH		54.1922790023
166AcetylationYCYWDAEKRGLDLQG
CEEECHHHCCCCHHH		54.1922826441
253S-nitrosocysteineSEGFELFCAQSFSKN
HCCHHHEEEEHHHHH		5.42-
253S-nitrosylationSEGFELFCAQSFSKN
HCCHHHEEEEHHHHH		5.4221278135
259N6-(pyridoxal phosphate)lysineFCAQSFSKNFGLYNE
EEEEHHHHHCCCCCC		55.04-
259OtherFCAQSFSKNFGLYNE
EEEEHHHHHCCCCCC		55.04-
264PhosphorylationFSKNFGLYNERVGNL
HHHHCCCCCCCCCCE		18.5025367039
276UbiquitinationGNLTVVGKESDSVLR
CCEEEEECCCHHHHH		42.3022790023
278PhosphorylationLTVVGKESDSVLRVL
EEEEECCCHHHHHHH		38.3822210690
280PhosphorylationVVGKESDSVLRVLSQ
EEECCCHHHHHHHHH		32.1222210690
286PhosphorylationDSVLRVLSQMEKIVR
HHHHHHHHHHHHHEE		25.3222210690
290MalonylationRVLSQMEKIVRITWS
HHHHHHHHHEEEECC		40.9526073543
290GlutarylationRVLSQMEKIVRITWS
HHHHHHHHHEEEECC		40.9524703693
290UbiquitinationRVLSQMEKIVRITWS
HHHHHHHHHEEEECC		40.9527667366
290AcetylationRVLSQMEKIVRITWS
HHHHHHHHHEEEECC		40.9522826441
310PhosphorylationGARIVAATLSDPELF
CCEEEEEECCCHHHH		19.6323984901
312PhosphorylationRIVAATLSDPELFKE
EEEEEECCCHHHHHH		46.9222817900
318AcetylationLSDPELFKEWKGNVK
CCCHHHHHHHCCCHH		75.2523806337
318UbiquitinationLSDPELFKEWKGNVK
CCCHHHHHHHCCCHH		75.25-
318SuccinylationLSDPELFKEWKGNVK
CCCHHHHHHHCCCHH		75.2523806337
318SuccinylationLSDPELFKEWKGNVK
CCCHHHHHHHCCCHH		75.25-
321UbiquitinationPELFKEWKGNVKTMA
HHHHHHHCCCHHHHH		41.5227667366
321MalonylationPELFKEWKGNVKTMA
HHHHHHHCCCHHHHH		41.5226320211
325UbiquitinationKEWKGNVKTMADRIL
HHHCCCHHHHHHHHH		36.2627667366
325MalonylationKEWKGNVKTMADRIL
HHHCCCHHHHHHHHH		36.2626320211
336PhosphorylationDRILTMRSELRARLE
HHHHHHHHHHHHHHH		30.1128464351
369AcetylationSFTGLNPKQVEYLVN
EECCCCHHHEEEEEC		66.9423954790
373PhosphorylationLNPKQVEYLVNEKHI
CCHHHEEEEECCCEE		19.6628464351
378AcetylationVEYLVNEKHIYLLPS
EEEEECCCEEEECCC		30.0522826441
378UbiquitinationVEYLVNEKHIYLLPS
EEEEECCCEEEECCC		30.0522790023
381PhosphorylationLVNEKHIYLLPSGRI
EECCCEEEECCCCCE		11.25-
385PhosphorylationKHIYLLPSGRINMCG
CEEEECCCCCEEECC		40.4528464351
391S-nitrosylationPSGRINMCGLTTKNL
CCCCEEECCCCCCCH		3.3221278135
391S-palmitoylationPSGRINMCGLTTKNL
CCCCEEECCCCCCCH		3.3228526873
391S-nitrosocysteinePSGRINMCGLTTKNL
CCCCEEECCCCCCCH		3.32-
396AcetylationNMCGLTTKNLDYVAT
EECCCCCCCHHHEEH		50.7222826441
400PhosphorylationLTTKNLDYVATSIHE
CCCCCHHHEEHHHHH		8.64-
403PhosphorylationKNLDYVATSIHEAVT
CCHHHEEHHHHHHHH		20.4022210690
404PhosphorylationNLDYVATSIHEAVTK
CHHHEEHHHHHHHHH		16.5322210690
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of AATC_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AATC_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-71, AND MASSSPECTROMETRY.

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