KAD3_HUMAN - dbPTM
KAD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KAD3_HUMAN
UniProt AC Q9UIJ7
Protein Name GTP:AMP phosphotransferase AK3, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03169}
Gene Name AK3 {ECO:0000255|HAMAP-Rule:MF_03169}
Organism Homo sapiens (Human).
Sequence Length 227
Subcellular Localization Mitochondrion matrix .
Protein Description Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities..
Protein Sequence MGASARLLRAVIMGAPGSGKGTVSSRITTHFELKHLSSGDLLRDNMLRGTEIGVLAKAFIDQGKLIPDDVMTRLALHELKNLTQYSWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEVIKQRLTARWIHPASGRVYNIEFNPPKTVGIDDLTGEPLIQREDDKPETVIKRLKAYEDQTKPVLEYYQKKGVLETFSGTETNKIWPYVYAFLQTKVPQRSQKASVTP
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
4Phosphorylation----MGASARLLRAV
----CCHHHHHHHHH
14.2724719451
18PhosphorylationVIMGAPGSGKGTVSS
HHHCCCCCCCCCCCC
35.9528857561
20SuccinylationMGAPGSGKGTVSSRI
HCCCCCCCCCCCCCE
53.7823954790
20SuccinylationMGAPGSGKGTVSSRI
HCCCCCCCCCCCCCE
53.78-
20AcetylationMGAPGSGKGTVSSRI
HCCCCCCCCCCCCCE
53.782402139
20MalonylationMGAPGSGKGTVSSRI
HCCCCCCCCCCCCCE
53.7826320211
22PhosphorylationAPGSGKGTVSSRITT
CCCCCCCCCCCCEEC
22.2428857561
24PhosphorylationGSGKGTVSSRITTHF
CCCCCCCCCCEECCE
17.4628857561
25PhosphorylationSGKGTVSSRITTHFE
CCCCCCCCCEECCEE
24.3024719451
34AcetylationITTHFELKHLSSGDL
EECCEEEECCCCCCH
34.9925825284
34MalonylationITTHFELKHLSSGDL
EECCEEEECCCCCCH
34.9926320211
37PhosphorylationHFELKHLSSGDLLRD
CEEEECCCCCCHHHH
31.8128450419
38PhosphorylationFELKHLSSGDLLRDN
EEEECCCCCCHHHHC
42.5630108239
48MethylationLLRDNMLRGTEIGVL
HHHHCCCCCCHHHHH
38.94-
57AcetylationTEIGVLAKAFIDQGK
CHHHHHHHHHHHCCC
39.4025953088
57SuccinylationTEIGVLAKAFIDQGK
CHHHHHHHHHHHCCC
39.40-
57SuccinylationTEIGVLAKAFIDQGK
CHHHHHHHHHHHCCC
39.40-
64MalonylationKAFIDQGKLIPDDVM
HHHHHCCCCCCHHHH
37.3026320211
64SuccinylationKAFIDQGKLIPDDVM
HHHHHCCCCCCHHHH
37.30-
64AcetylationKAFIDQGKLIPDDVM
HHHHHCCCCCCHHHH
37.30-
64SuccinylationKAFIDQGKLIPDDVM
HHHHHCCCCCCHHHH
37.30-
72PhosphorylationLIPDDVMTRLALHEL
CCCHHHHHHHHHHHH
23.5220068231
80SuccinylationRLALHELKNLTQYSW
HHHHHHHHHHHHHHH
47.10-
80AcetylationRLALHELKNLTQYSW
HHHHHHHHHHHHHHH
47.10-
80SuccinylationRLALHELKNLTQYSW
HHHHHHHHHHHHHHH
47.10-
85PhosphorylationELKNLTQYSWLLDGF
HHHHHHHHHHHHHCC
9.1420562437
138PhosphorylationHPASGRVYNIEFNPP
ECCCCCEEEEEECCC
14.7321406692
147PhosphorylationIEFNPPKTVGIDDLT
EEECCCCCCCCCCCC
29.7321406692
154PhosphorylationTVGIDDLTGEPLIQR
CCCCCCCCCCCCEEC
46.6321406692
165AcetylationLIQREDDKPETVIKR
CEECCCCCCHHHHHH
58.0123954790
174MalonylationETVIKRLKAYEDQTK
HHHHHHHHHHCCCCH
53.6126320211
174SuccinylationETVIKRLKAYEDQTK
HHHHHHHHHHCCCCH
53.61-
174SuccinylationETVIKRLKAYEDQTK
HHHHHHHHHHCCCCH
53.61-
174AcetylationETVIKRLKAYEDQTK
HHHHHHHHHHCCCCH
53.61-
176PhosphorylationVIKRLKAYEDQTKPV
HHHHHHHHCCCCHHH
20.6029496907
181UbiquitinationKAYEDQTKPVLEYYQ
HHHCCCCHHHHHHHH
27.74-
181AcetylationKAYEDQTKPVLEYYQ
HHHCCCCHHHHHHHH
27.7420167786
181SuccinylationKAYEDQTKPVLEYYQ
HHHCCCCHHHHHHHH
27.7423954790
181MalonylationKAYEDQTKPVLEYYQ
HHHCCCCHHHHHHHH
27.7426320211
186PhosphorylationQTKPVLEYYQKKGVL
CCHHHHHHHHHHCCE
13.67119557
189SuccinylationPVLEYYQKKGVLETF
HHHHHHHHHCCEECC
35.06-
189SuccinylationPVLEYYQKKGVLETF
HHHHHHHHHCCEECC
35.0623954790
189AcetylationPVLEYYQKKGVLETF
HHHHHHHHHCCEECC
35.0623236377
190AcetylationVLEYYQKKGVLETFS
HHHHHHHHCCEECCC
38.436271573
197PhosphorylationKGVLETFSGTETNKI
HCCEECCCCCCCCCH
52.83110760127
203AcetylationFSGTETNKIWPYVYA
CCCCCCCCHHHHHHH
54.27-
207PhosphorylationETNKIWPYVYAFLQT
CCCCHHHHHHHHHHC
7.3546161143
209PhosphorylationNKIWPYVYAFLQTKV
CCHHHHHHHHHHCCC
5.9446161149
220PhosphorylationQTKVPQRSQKASVTP
HCCCCCHHHCCCCCC
30.6826437602
224PhosphorylationPQRSQKASVTP----
CCHHHCCCCCC----
33.2926437602

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 KAD3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KAD3_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 KAD3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DAPK3_HUMANDAPK3physical
21988832
CAF17_HUMANIBA57physical
26186194
HNRL2_HUMANHNRNPUL2physical
26344197
RS14_HUMANRPS14physical
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
There are no disease associations of PTM sites.
Regulatory Network of KAD3_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-34, AND MASS SPECTROMETRY.

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