AMPD_SCHPO - dbPTM
AMPD_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMPD_SCHPO
UniProt AC P50998
Protein Name AMP deaminase
Gene Name ada1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 831
Subcellular Localization Cytoplasm .
Protein Description AMP deaminase plays a critical role in energy metabolism..
Protein Sequence MNMEQEDDQVPAVAAETVPLKRYVTNPGANRDEEVAAAPSSQDTPYFDYAYERSLRHQDAKFLAMNGTQNGRDGLPSKSPRRPSVSASTVRNSDDVNHSKAGPGSGKLLNDTLQSKISSIHMPHVQQGDNAVVSSVGGPETDPGNMETTDPLFSDELAEIYLSIHKCMDMRHKYIRVSLQGELDNPIDDDSWIIYPDCKEGEDDTGLFNFADCKIPGIENEMEYHMDHQGIFQVYENDSAYIAGTPSFHIPTIRDYYIDLEFLLSASSDGPSKSFSFRRLQYLEGRWNMYMLLNEYQELADTKKVPHRDFYNVRKVDTHVHHSALANQKHLLRFIKAKLRKCPNEKVIWRDGKFLTLQEVFDSLKLTSYDLSIDTLDMHAHTDTFHRFDKFNLKYNPIGESRLRTIFLKTDNDINGRYLAELTKEVFTDLRTQKYQMAEYRISIYGRNREEWDKLAAWIIDNELFSPNVRWLIQVPRLYDVYKKSGIVETFEEVVRNVFEPLFEVTKDPRTHPKLHVFLQRVIGFDSVDDESKPERRTFRKFPYPKHWDINLNPPYSYWLYYMYANMTSLNSWRKIRGFNTFVLRPHCGEAGDTDHLASAFLLSHGINHGILLRKVPFLQYLWYLDQIPIAMSPLSNNALFLAYDKNPFLTYFKRGLNVSLSTDDPLQFAFTREPLIEEYAVAAQIYKLSAVDMCELARNSVLQSGFERQLKERWLGVDFQDIDRTNVPIIRLAYRALTLTQEIALVNKHVQPSKHPSNHDLEELIHKYDAMTGTSDPLSASPRTNDATISSRLSLHDGHDHGAFFPGLSVISERRRRKDSMASSSQDLKD
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
25PhosphorylationVPLKRYVTNPGANRD
CCCEEEECCCCCCCC		27.1129996109
40PhosphorylationEEVAAAPSSQDTPYF
HHHHCCCCCCCCCCH		35.5929996109
41PhosphorylationEVAAAPSSQDTPYFD
HHHCCCCCCCCCCHH		30.8929996109
44PhosphorylationAAPSSQDTPYFDYAY
CCCCCCCCCCHHHHH		16.5529996109
77PhosphorylationNGRDGLPSKSPRRPS
CCCCCCCCCCCCCCC		51.3025720772
79PhosphorylationRDGLPSKSPRRPSVS
CCCCCCCCCCCCCCC		28.1628889911
84PhosphorylationSKSPRRPSVSASTVR
CCCCCCCCCCCHHCC		27.2228889911
86PhosphorylationSPRRPSVSASTVRNS
CCCCCCCCCHHCCCC		22.3429996109
88PhosphorylationRRPSVSASTVRNSDD
CCCCCCCHHCCCCCC		21.6729996109
89PhosphorylationRPSVSASTVRNSDDV
CCCCCCHHCCCCCCC		24.1725720772
93PhosphorylationSASTVRNSDDVNHSK
CCHHCCCCCCCCCCC		25.3228889911
99PhosphorylationNSDDVNHSKAGPGSG
CCCCCCCCCCCCCCC		20.9928889911
105PhosphorylationHSKAGPGSGKLLNDT
CCCCCCCCCHHCHHH		35.5725720772
758PhosphorylationVQPSKHPSNHDLEEL
CCCCCCCCCCCHHHH		46.6628889911
773PhosphorylationIHKYDAMTGTSDPLS
HHHHHHCCCCCCCCC		38.7428889911
776PhosphorylationYDAMTGTSDPLSASP
HHHCCCCCCCCCCCC		38.2828889911
780PhosphorylationTGTSDPLSASPRTND
CCCCCCCCCCCCCCC		31.8928889911
782PhosphorylationTSDPLSASPRTNDAT
CCCCCCCCCCCCCCC		16.1328889911
791PhosphorylationRTNDATISSRLSLHD
CCCCCCHHHCEECCC		12.6828889911
795PhosphorylationATISSRLSLHDGHDH
CCHHHCEECCCCCCC		23.6528889911
821PhosphorylationERRRRKDSMASSSQD
HHHHHHHHHCCCCCC		21.2029996109
824PhosphorylationRRKDSMASSSQDLKD
HHHHHHCCCCCCCCC		23.1424763107
825PhosphorylationRKDSMASSSQDLKD-
HHHHHCCCCCCCCC-		23.6021712547
826PhosphorylationKDSMASSSQDLKD--
HHHHCCCCCCCCC--		25.8124763107
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_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMPD_SCHPO !!
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_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPT7_SCHPOspt7physical
21642955
NGG1_SCHPOngg1physical
21642955
TAF5_SCHPOtaf5physical
21642955
SPT8_SCHPOspt8physical
21642955
SPT20_SCHPOspt20physical
21642955
GCN5_SCHPOgcn5physical
21642955
UBP8_SCHPOubp8physical
21642955
AMPD_SCHPOada1physical
21642955
TAF6_SCHPOtaf6physical
21642955
ADA2_SCHPOada2physical
21642955
TAF12_SCHPOtaf12physical
21642955
SGF73_SCHPOsgf73physical
21642955
SPT3_SCHPOspt3physical
21642955
SGF29_SCHPOsgf29physical
21642955
TAF10_SCHPOtaf10physical
21642955
TAF9_SCHPOtaf9physical
21642955
SGF11_SCHPOsgf11physical
21642955
SUS1_SCHPOsus1physical
21642955
RUVB2_SCHPOrvb2physical
21642955
RUVB1_SCHPOrvb1physical
21642955
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AMPD_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-84; SER-758;SER-776; SER-780 AND SER-782, AND MASS SPECTROMETRY.

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