OAT_HUMAN - dbPTM
OAT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OAT_HUMAN
UniProt AC P04181
Protein Name Ornithine aminotransferase, mitochondrial
Gene Name OAT
Organism Homo sapiens (Human).
Sequence Length 439
Subcellular Localization Mitochondrion matrix .
Protein Description
Protein Sequence MFSKLAHLQRFAVLSRGVHSSVASATSVATKKTVQGPPTSDDIFEREYKYGAHNYHPLPVALERGKGIYLWDVEGRKYFDFLSSYSAVNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVLGEYEEYITKLFNYHKVLPMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGRTLSAISSSTDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGEAGVVVPDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRPDIVLLGKALSGGLYPVSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIAALEVLEEENLAENADKLGIILRNELMKLPSDVVTAVRGKGLLNAIVIKETKDWDAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVIKEDELRESIEIINKTILSF
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
30PhosphorylationASATSVATKKTVQGP
HCCCCCCCCCCCCCC		30.80-
31UbiquitinationSATSVATKKTVQGPP
CCCCCCCCCCCCCCC		36.39-
322-HydroxyisobutyrylationATSVATKKTVQGPPT
CCCCCCCCCCCCCCC		49.96-
32UbiquitinationATSVATKKTVQGPPT
CCCCCCCCCCCCCCC		49.9621890473
32UbiquitinationATSVATKKTVQGPPT
CCCCCCCCCCCCCCC		49.9621890473
33PhosphorylationTSVATKKTVQGPPTS
CCCCCCCCCCCCCCC		21.4422210691
39PhosphorylationKTVQGPPTSDDIFER
CCCCCCCCCCHHHHH		48.1729396449
40PhosphorylationTVQGPPTSDDIFERE
CCCCCCCCCHHHHHH		38.7722210691
49AcetylationDIFEREYKYGAHNYH
HHHHHHHCCCCCCCC		32.2423236377
49MalonylationDIFEREYKYGAHNYH
HHHHHHHCCCCCCCC		32.2426320211
49UbiquitinationDIFEREYKYGAHNYH
HHHHHHHCCCCCCCC		32.2421890473
49UbiquitinationDIFEREYKYGAHNYH
HHHHHHHCCCCCCCC		32.2421890473
50PhosphorylationIFEREYKYGAHNYHP
HHHHHHCCCCCCCCC		20.7428152594
55PhosphorylationYKYGAHNYHPLPVAL
HCCCCCCCCCCEEEE		8.5728152594
66UbiquitinationPVALERGKGIYLWDV
EEEEECCCCEEEEEC		48.6421890473
66UbiquitinationPVALERGKGIYLWDV
EEEEECCCCEEEEEC		48.6421890473
66MalonylationPVALERGKGIYLWDV
EEEEECCCCEEEEEC		48.6426320211
66AcetylationPVALERGKGIYLWDV
EEEEECCCCEEEEEC		48.64-
69PhosphorylationLERGKGIYLWDVEGR
EECCCCEEEEECCCC		15.4828152594
83PhosphorylationRKYFDFLSSYSAVNQ
CEEHHHHHHHCCCCC		27.5028152594
84PhosphorylationKYFDFLSSYSAVNQG
EEHHHHHHHCCCCCC		25.8428152594
85PhosphorylationYFDFLSSYSAVNQGH
EHHHHHHHCCCCCCC		9.4028152594
86PhosphorylationFDFLSSYSAVNQGHC
HHHHHHHCCCCCCCC		27.9128152594
96AcetylationNQGHCHPKIVNALKS
CCCCCCHHHHHHHHH		35.3026051181
102MalonylationPKIVNALKSQVDKLT
HHHHHHHHHHHCHHH		36.1126320211
102UbiquitinationPKIVNALKSQVDKLT
HHHHHHHHHHHCHHH		36.11-
102AcetylationPKIVNALKSQVDKLT
HHHHHHHHHHHCHHH		36.1125953088
102SuccinylationPKIVNALKSQVDKLT
HHHHHHHHHHHCHHH		36.11-
102SuccinylationPKIVNALKSQVDKLT
HHHHHHHHHHHCHHH		36.1127452117
103PhosphorylationKIVNALKSQVDKLTL
HHHHHHHHHHCHHHH		35.9621406692
107UbiquitinationALKSQVDKLTLTSRA
HHHHHHCHHHHHHHH		44.51-
1072-HydroxyisobutyrylationALKSQVDKLTLTSRA
HHHHHHCHHHHHHHH		44.51-
107SuccinylationALKSQVDKLTLTSRA
HHHHHHCHHHHHHHH		44.51-
107SuccinylationALKSQVDKLTLTSRA
HHHHHHCHHHHHHHH		44.51-
107AcetylationALKSQVDKLTLTSRA
HHHHHHCHHHHHHHH		44.5125953088
109PhosphorylationKSQVDKLTLTSRAFY
HHHHCHHHHHHHHHH		33.4621406692
111PhosphorylationQVDKLTLTSRAFYNN
HHCHHHHHHHHHHHH		15.7821406692
112PhosphorylationVDKLTLTSRAFYNNV
HCHHHHHHHHHHHHH		25.4021406692
123PhosphorylationYNNVLGEYEEYITKL
HHHHHHHHHHHHHHH		16.56-
126PhosphorylationVLGEYEEYITKLFNY
HHHHHHHHHHHHHCC		11.27-
133PhosphorylationYITKLFNYHKVLPMN
HHHHHHCCCCEECCC		8.83-
139SulfoxidationNYHKVLPMNTGVEAG
CCCCEECCCCCCCHH		6.4921406390
148PhosphorylationTGVEAGETACKLARK
CCCCHHHHHHHHHHH		36.1224532841
151UbiquitinationEAGETACKLARKWGY
CHHHHHHHHHHHHCC		42.59-
186PhosphorylationGRTLSAISSSTDPTS
HHHHHHHHCCCCCCC		20.2528348404
187PhosphorylationRTLSAISSSTDPTSY
HHHHHHHCCCCCCCC		31.0128348404
188PhosphorylationTLSAISSSTDPTSYD
HHHHHHCCCCCCCCC		30.0028348404
189PhosphorylationLSAISSSTDPTSYDG
HHHHHCCCCCCCCCC		48.2028348404
192PhosphorylationISSSTDPTSYDGFGP
HHCCCCCCCCCCCCC		42.6128348404
193PhosphorylationSSSTDPTSYDGFGPF
HCCCCCCCCCCCCCC		26.9828348404
194PhosphorylationSSTDPTSYDGFGPFM
CCCCCCCCCCCCCCC		23.6728348404
272PhosphorylationIQTGLARTGRWLAVD
HHHCCCCCCCEEEEC		26.0320068231
280PhosphorylationGRWLAVDYENVRPDI
CCEEEECCCCCCCCE		11.64-
292N6-(pyridoxal phosphate)lysinePDIVLLGKALSGGLY
CCEEEEEHHHCCCCC		46.23-
292OtherPDIVLLGKALSGGLY
CCEEEEEHHHCCCCC		46.233754226
351UbiquitinationNLAENADKLGIILRN
CHHHHHHHHHHHHHH		46.32-
362SuccinylationILRNELMKLPSDVVT
HHHHHHHCCCCCHHH		70.62-
362SuccinylationILRNELMKLPSDVVT
HHHHHHHCCCCCHHH		70.6221890473
362AcetylationILRNELMKLPSDVVT
HHHHHHHCCCCCHHH		70.6223236377
362UbiquitinationILRNELMKLPSDVVT
HHHHHHHCCCCCHHH		70.62-
365PhosphorylationNELMKLPSDVVTAVR
HHHHCCCCCHHHHHC		54.1720068231
369PhosphorylationKLPSDVVTAVRGKGL
CCCCCHHHHHCCCCC		21.2020068231
374UbiquitinationVVTAVRGKGLLNAIV
HHHHHCCCCCEEEEE		35.5021890473
374MalonylationVVTAVRGKGLLNAIV
HHHHHCCCCCEEEEE		35.5026320211
374UbiquitinationVVTAVRGKGLLNAIV
HHHHHCCCCCEEEEE		35.5021890473
3742-HydroxyisobutyrylationVVTAVRGKGLLNAIV
HHHHHCCCCCEEEEE		35.50-
383UbiquitinationLLNAIVIKETKDWDA
CEEEEEEEECCCCCH		48.73-
386AcetylationAIVIKETKDWDAWKV
EEEEEECCCCCHHHH		58.8923236377
386UbiquitinationAIVIKETKDWDAWKV
EEEEEECCCCCHHHH		58.89-
392UbiquitinationTKDWDAWKVCLRLRD
CCCCCHHHHHHHCCC		25.4521890473
392UbiquitinationTKDWDAWKVCLRLRD
CCCCCHHHHHHHCCC		25.4521890473
392AcetylationTKDWDAWKVCLRLRD
CCCCCHHHHHHHCCC		25.45-
405UbiquitinationRDNGLLAKPTHGDII
CCCCEECCCCCCCCE		50.87-
405SuccinylationRDNGLLAKPTHGDII
CCCCEECCCCCCCCE		50.8721890473
405SuccinylationRDNGLLAKPTHGDII
CCCCEECCCCCCCCE		50.87-
405AcetylationRDNGLLAKPTHGDII
CCCCEECCCCCCCCE		50.8723236377
421UbiquitinationFAPPLVIKEDELRES
CCCCEEECHHHHHHH		52.19-
421MalonylationFAPPLVIKEDELRES
CCCCEEECHHHHHHH		52.1926320211
421AcetylationFAPPLVIKEDELRES
CCCCEEECHHHHHHH		52.19-
4212-HydroxyisobutyrylationFAPPLVIKEDELRES
CCCCEEECHHHHHHH		52.19-
426MethylationVIKEDELRESIEIIN
EECHHHHHHHHHHHH		33.30115485971
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 OAT_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OAT_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 OAT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
S35F6_HUMANSLC35F6physical
16169070
PPGB_HUMANCTSAphysical
22939629
PURA2_HUMANADSSphysical
26344197
ALDR_HUMANAKR1B1physical
26344197
AL1B1_HUMANALDH1B1physical
26344197
CBS_HUMANCBSphysical
26344197
ESTD_HUMANESDphysical
26344197
AATC_HUMANGOT1physical
26344197
NDKB_HUMANNME2physical
26344197
PDXK_HUMANPDXKphysical
26344197
PGM1_HUMANPGM1physical
26344197
PIPNB_HUMANPITPNBphysical
26344197
PPID_HUMANPPIDphysical
26344197
PPCE_HUMANPREPphysical
26344197
SODM_HUMANSOD2physical
26344197
UAP1L_HUMANUAP1L1physical
26344197
UCRI_HUMANUQCRFS1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
258870Hyperornithinemia with gyrate atrophy of choroid and retina (HOGA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00129L-Ornithine
Regulatory Network of OAT_HUMAN

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Related Literatures of Post-Translational Modification
Pyridoxal phosphate
ReferencePubMed
"The primary structure of ornithine aminotransferase. Identificationof active-site sequence and site of post-translational proteolysis.";
Simmaco M., John R.A., Barra D., Bossa F.;
FEBS Lett. 199:39-42(1986).
Cited for: PARTIAL PROTEIN SEQUENCE, PYRIDOXAL PHOSPHATE AT LYS-292, ANDPROTEOLYTIC PROCESSING.

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