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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
70 | Phosphorylation | RRKVNDQYGRSPASL HHHHHHCCCCCCCCC | 19.85 | 23172892 | |
73 | Phosphorylation | VNDQYGRSPASLPDA HHHCCCCCCCCCCCC | 22.06 | 30291188 | |
76 | Phosphorylation | QYGRSPASLPDATPF CCCCCCCCCCCCCCC | 43.76 | 23172892 | |
81 | Phosphorylation | PASLPDATPFTDGGG CCCCCCCCCCCCCCC | 26.73 | 23172892 | |
84 | Phosphorylation | LPDATPFTDGGGGGG CCCCCCCCCCCCCCC | 34.63 | 25561503 | |
94 | Phosphorylation | GGGGGGDTGRSNGHV CCCCCCCCCCCCCEE | 37.46 | 25561503 | |
97 | Phosphorylation | GGGDTGRSNGHVYVD CCCCCCCCCCEEEEC | 48.81 | 25368622 | |
102 | Phosphorylation | GRSNGHVYVDEIPPG CCCCCEEEECCCCCC | 9.12 | 25368622 | |
115 | Phosphorylation | PGLPRLHTPSEGRAS CCCCCCCCCCCCCCC | 32.85 | 25368622 | |
117 | Phosphorylation | LPRLHTPSEGRASVH CCCCCCCCCCCCCCC | 54.56 | 25368622 | |
122 | Phosphorylation | TPSEGRASVHGASSI CCCCCCCCCCCCCCC | 17.18 | 25368622 | |
127 | Phosphorylation | RASVHGASSIRKTGS CCCCCCCCCCEECCC | 30.78 | 25368622 | |
128 | Phosphorylation | ASVHGASSIRKTGSF CCCCCCCCCEECCCC | 26.36 | 25368622 | |
132 | Phosphorylation | GASSIRKTGSFVRPI CCCCCEECCCCEEEC | 28.36 | 23111157 | |
134 | Phosphorylation | SSIRKTGSFVRPISP CCCEECCCCEEECCC | 26.29 | 27532006 | |
140 | Phosphorylation | GSFVRPISPKSPVAS CCCEEECCCCCCCCC | 29.02 | 30291188 | |
201 | Phosphorylation | AASSMIRSHSVSGDL HHHHHHHHCCCCCCC | 14.80 | 23776212 | |
203 | Phosphorylation | SSMIRSHSVSGDLHG HHHHHHCCCCCCCCC | 21.16 | 30291188 | |
205 | Phosphorylation | MIRSHSVSGDLHGVQ HHHHCCCCCCCCCCC | 29.60 | 23776212 | |
229 | Phosphorylation | RKEPEQETFVRLNVP HCCCCCCCEEEECCC | 27.42 | 25368622 | |
276 | Phosphorylation | PWEKEVISDPSTPKP CCCCCCCCCCCCCCC | 48.95 | 23776212 | |
279 | Phosphorylation | KEVISDPSTPKPNTE CCCCCCCCCCCCCCC | 63.43 | 23776212 | |
280 | Phosphorylation | EVISDPSTPKPNTEP CCCCCCCCCCCCCCC | 40.49 | 23776212 | |
285 | Phosphorylation | PSTPKPNTEPFAHYP CCCCCCCCCCCCCCC | 54.27 | 23776212 | |
291 | Phosphorylation | NTEPFAHYPQGKSDH CCCCCCCCCCCCCCC | 8.20 | 23776212 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AMPD_ARATH !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
STLP2_ARATH | STL2P | physical | 16543243 | |
CD48A_ARATH | CDC48 | physical | 16543243 | |
AMPD_ARATH | FAC1 | physical | 16543243 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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. |