GATB_HUMAN - dbPTM
GATB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GATB_HUMAN
UniProt AC O75879
Protein Name Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03147}
Gene Name GATB {ECO:0000255|HAMAP-Rule:MF_03147, ECO:0000312|HGNC:HGNC:8849}
Organism Homo sapiens (Human).
Sequence Length 557
Subcellular Localization Mitochondrion .
Protein Description Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln)..
Protein Sequence MAAPMLRWGCRGRRWAFARVDGGSCHRRGAPTGSTSNQIRGESSVAQQPLHTAQKTRKGEHKWAAVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINKKSLFDRKHYFYADLPAGYQITQQRLPIAVNGSLIYGVCAGKKQSQVIPKTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVVLEPDMSCGEEAATAVRELQLILQALGTSQANMAEGQLRVDANISVHHPGEPLGVRTEVKNLNSIRFLAKAIDYEIQRQINELENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATSLPAGADPQQVINIDQIRETLPELPSVTREKLVQQYGMLLEHSFTLLNEVGLLEFFQNVIKETRAEPKKVTSWVLNTFLGYLKQQNLAVSESPVTPSALAELLDLLDSRTISSSAAKQVFEELWKREGKTPGQIVSEKQLELMQDQGALEQLCHSVMEAHPQVVMDVKNRNPRAINKLIGLVRKATQSRADPVMIKEILEKKLSL
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
36PhosphorylationGAPTGSTSNQIRGES
CCCCCCCCCCCCCCC
28.5622210691
43PhosphorylationSNQIRGESSVAQQPL
CCCCCCCCCCCCCCC
32.7022210691
90PhosphorylationSGSQVRFSAPPNSLV
CCCEEEEECCCCCEE
29.3320068231
95PhosphorylationRFSAPPNSLVSFFDA
EEECCCCCEEEEEEC
35.6020068231
98PhosphorylationAPPNSLVSFFDASLP
CCCCCEEEEEECCCC
26.0320068231
103PhosphorylationLVSFFDASLPGTLPV
EEEEEECCCCCCHHH
36.6220068231
107PhosphorylationFDASLPGTLPVLNRR
EECCCCCCHHHHCHH
26.4220068231
176PhosphorylationVCAGKKQSQVIPKTV
ECCCCCHHCCCCCEE
34.98-
181UbiquitinationKQSQVIPKTVRIKQI
CHHCCCCCEEEEEEE
48.8323503661
181AcetylationKQSQVIPKTVRIKQI
CHHCCCCCEEEEEEE
48.8319608861
186UbiquitinationIPKTVRIKQIQLEQD
CCCEEEEEEEEEECC
30.6823503661
280UbiquitinationLGVRTEVKNLNSIRF
CCCCEEEECHHHHHH
49.86-
284PhosphorylationTEVKNLNSIRFLAKA
EEEECHHHHHHHHHH
20.5024719451
290UbiquitinationNSIRFLAKAIDYEIQ
HHHHHHHHHHCHHHH
48.2823503661
290AcetylationNSIRFLAKAIDYEIQ
HHHHHHHHHHCHHHH
48.2825953088
319UbiquitinationETRSFHHKLGCTMSM
HHHHHHHHHCCCEEC
37.7029967540
329UbiquitinationCTMSMRDKEGKQDYR
CCEECCCCCCCCCCC
58.9824816145
415PhosphorylationFQNVIKETRAEPKKV
HHHHHHHHCCCCCHH
30.12-
460PhosphorylationELLDLLDSRTISSSA
HHHHHHHCCCCCHHH
31.15-
529SuccinylationRNPRAINKLIGLVRK
CCHHHHHHHHHHHHH
35.05-
529MalonylationRNPRAINKLIGLVRK
CCHHHHHHHHHHHHH
35.0526320211
529SuccinylationRNPRAINKLIGLVRK
CCHHHHHHHHHHHHH
35.05-
529AcetylationRNPRAINKLIGLVRK
CCHHHHHHHHHHHHH
35.0525953088
538PhosphorylationIGLVRKATQSRADPV
HHHHHHHHHCCCCHH
30.07-

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 GATB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GATB_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 GATB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GATB_HUMAN !!

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
DB00130L-Glutamine
Regulatory Network of GATB_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-181, AND MASS SPECTROMETRY.

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