AMPD_ARATH - dbPTM
AMPD_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMPD_ARATH
UniProt AC O80452
Protein Name AMP deaminase {ECO:0000303|PubMed:15918887}
Gene Name AMPD {ECO:0000303|PubMed:15918887}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 839
Subcellular Localization Membrane
Single-pass membrane protein . Microsome membrane . Might be associated with the inner mitochondrial membrane..
Protein Description AMP deaminase plays a critical role in energy metabolism. Essential for the transition from zygote to embryo..
Protein Sequence MEPNIYQLALAALFGASFVAVSGFFMHFKALNLVLERGKERKENPDGDEPQNPTLVRRRSQVRRKVNDQYGRSPASLPDATPFTDGGGGGGGDTGRSNGHVYVDEIPPGLPRLHTPSEGRASVHGASSIRKTGSFVRPISPKSPVASASAFESVEESDDDDNLTNSEGLDASYLQANGDNEMPADANEEQISMAASSMIRSHSVSGDLHGVQPDPIAADILRKEPEQETFVRLNVPLEVPTSDEVEAYKCLQECLELRKRYVFQETVAPWEKEVISDPSTPKPNTEPFAHYPQGKSDHCFEMQDGVVHVFANKDAKEDLFPVADATAFFTDLHHVLKVIAAGNIRTLCHRRLVLLEQKFNLHLMLNADKEFLAQKSAPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGTYLTLREVFESLDLTGYDLNVDLLDVHADKSTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLGEITKQVFSDLEASKYQMAEYRISIYGRKMSEWDQLASWIVNNDLYSENVVWLIQLPRLYNIYKDMGIVTSFQNILDNIFIPLFEATVDPDSHPQLHVFLKQVVGFDLVDDESKPERRPTKHMPTPAQWTNAFNPAFSYYVYYCYANLYVLNKLRESKGMTTITLRPHSGEAGDIDHLAATFLTCHSIAHGINLRKSPVLQYLYYLAQIGLAMSPLSNNSLFLDYHRNPFPVFFLRGLNVSLSTDDPLQIHLTKEPLVEEYSIAASVWKLSACDLCEIARNSVYQSGFSHALKSHWIGKDYYKRGPDGNDIHKTNVPHIRVEFRDTIWKEEMQQVYLGKAVISDEVVP
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
70PhosphorylationRRKVNDQYGRSPASL
HHHHHHCCCCCCCCC
19.8523172892
73PhosphorylationVNDQYGRSPASLPDA
HHHCCCCCCCCCCCC
22.0630291188
76PhosphorylationQYGRSPASLPDATPF
CCCCCCCCCCCCCCC
43.7623172892
81PhosphorylationPASLPDATPFTDGGG
CCCCCCCCCCCCCCC
26.7323172892
84PhosphorylationLPDATPFTDGGGGGG
CCCCCCCCCCCCCCC
34.6325561503
94PhosphorylationGGGGGGDTGRSNGHV
CCCCCCCCCCCCCEE
37.4625561503
97PhosphorylationGGGDTGRSNGHVYVD
CCCCCCCCCCEEEEC
48.8125368622
102PhosphorylationGRSNGHVYVDEIPPG
CCCCCEEEECCCCCC
9.1225368622
115PhosphorylationPGLPRLHTPSEGRAS
CCCCCCCCCCCCCCC
32.8525368622
117PhosphorylationLPRLHTPSEGRASVH
CCCCCCCCCCCCCCC
54.5625368622
122PhosphorylationTPSEGRASVHGASSI
CCCCCCCCCCCCCCC
17.1825368622
127PhosphorylationRASVHGASSIRKTGS
CCCCCCCCCCEECCC
30.7825368622
128PhosphorylationASVHGASSIRKTGSF
CCCCCCCCCEECCCC
26.3625368622
132PhosphorylationGASSIRKTGSFVRPI
CCCCCEECCCCEEEC
28.3623111157
134PhosphorylationSSIRKTGSFVRPISP
CCCEECCCCEEECCC
26.2927532006
140PhosphorylationGSFVRPISPKSPVAS
CCCEEECCCCCCCCC
29.0230291188
201PhosphorylationAASSMIRSHSVSGDL
HHHHHHHHCCCCCCC
14.8023776212
203PhosphorylationSSMIRSHSVSGDLHG
HHHHHHCCCCCCCCC
21.1630291188
205PhosphorylationMIRSHSVSGDLHGVQ
HHHHCCCCCCCCCCC
29.6023776212
229PhosphorylationRKEPEQETFVRLNVP
HCCCCCCCEEEECCC
27.4225368622
276PhosphorylationPWEKEVISDPSTPKP
CCCCCCCCCCCCCCC
48.9523776212
279PhosphorylationKEVISDPSTPKPNTE
CCCCCCCCCCCCCCC
63.4323776212
280PhosphorylationEVISDPSTPKPNTEP
CCCCCCCCCCCCCCC
40.4923776212
285PhosphorylationPSTPKPNTEPFAHYP
CCCCCCCCCCCCCCC
54.2723776212
291PhosphorylationNTEPFAHYPQGKSDH
CCCCCCCCCCCCCCC
8.2023776212

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 AMPD_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMPD_ARATH !!

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 AMPD_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STLP2_ARATHSTL2Pphysical
16543243
CD48A_ARATHCDC48physical
16543243
AMPD_ARATHFAC1physical
16543243

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AMPD_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; THR-132; SER-140AND SER-279, AND MASS SPECTROMETRY.
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis.";
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.;
J. Proteome Res. 7:2458-2470(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-140 ANDSER-203, AND MASS SPECTROMETRY.

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