AMPD1_HUMAN - dbPTM
AMPD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMPD1_HUMAN
UniProt AC P23109
Protein Name AMP deaminase 1
Gene Name AMPD1
Organism Homo sapiens (Human).
Sequence Length 780
Subcellular Localization
Protein Description AMP deaminase plays a critical role in energy metabolism..
Protein Sequence MNVRIFYSVSQSPHSLLSLLFYCAILESRISATMPLFKLPAEEKQIDDAMRNFAEKVFASEVKDEGGRQEISPFDVDEICPISHHEMQAHIFHLETLSTSTEARRKKRFQGRKTVNLSIPLSETSSTKLSHIDEYISSSPTYQTVPDFQRVQITGDYASGVTVEDFEIVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEAWVANESFYPVFTPPVKKGEDPFRTDNLPENLGYHLKMKDGVVYVYPNEAAVSKDEPKPLPYPNLDTFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKELFAKLKMHPYDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWSKLSSWFVCNRIHCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKHITGFDSVDDESKHSGHMFSSKSPKPQEWTLEKNPSYTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADDISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTNVAQIRMAYRYETWCYELNLIAEGLKSTE
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
28PhosphorylationFYCAILESRISATMP
HHHHHHHHHHHCCCC		31.3129759185
31PhosphorylationAILESRISATMPLFK
HHHHHHHHCCCCCCC		19.3129759185
33PhosphorylationLESRISATMPLFKLP
HHHHHHCCCCCCCCC		16.7229759185
56UbiquitinationAMRNFAEKVFASEVK
HHHHHHHHHHHHHHC		38.94-
63UbiquitinationKVFASEVKDEGGRQE
HHHHHHHCCCCCCCC		46.11-
113UbiquitinationKKRFQGRKTVNLSIP
HHHHCCCCEEEEECC		64.74-
114PhosphorylationKRFQGRKTVNLSIPL
HHHCCCCEEEEECCC		17.1726437602
118PhosphorylationGRKTVNLSIPLSETS
CCCEEEEECCCCCCC		19.5626437602
138PhosphorylationHIDEYISSSPTYQTV
HHHHHHHCCCCCCCC		30.6726657352
171UbiquitinationEDFEIVCKGLYRALC
HHHHHHHHHHHHHHH		40.85-
186UbiquitinationIREKYMQKSFQRFPK
HHHHHHHHHHHHCCC		36.39-
187PhosphorylationREKYMQKSFQRFPKT
HHHHHHHHHHHCCCC		15.1029759185
197UbiquitinationRFPKTPSKYLRNIDG
HCCCCHHHHHHCCCC		49.89-
230PhosphorylationKGEDPFRTDNLPENL
CCCCCCCCCCCCCCC		29.6226437602
239PhosphorylationNLPENLGYHLKMKDG
CCCCCCCEEEEECCC		13.7226437602
249PhosphorylationKMKDGVVYVYPNEAA
EECCCEEEECCCCCC		7.58-
291PhosphorylationIAQGPVKTYTHRRLK
HHCCCCCCCHHHHHH		33.6121082442
298UbiquitinationTYTHRRLKFLSSKFQ
CCHHHHHHHHHHHHH		42.31-
302PhosphorylationRRLKFLSSKFQVHQM
HHHHHHHHHHHHHHH		39.3721082442
354UbiquitinationHLLRFIKKSYQIDAD
HHHHHHHHHHCCCCC		49.97-
354AcetylationHLLRFIKKSYQIDAD
HHHHHHHHHHCCCCC		49.9711793975
355PhosphorylationLLRFIKKSYQIDADR
HHHHHHHHHCCCCCC		19.7826437602
356PhosphorylationLRFIKKSYQIDADRV
HHHHHHHHCCCCCCE		20.5426437602
366PhosphorylationDADRVVYSTKEKNLT
CCCCEEEEHHHCCCC		22.7626437602
367PhosphorylationADRVVYSTKEKNLTL
CCCEEEEHHHCCCCH		26.0726437602
368UbiquitinationDRVVYSTKEKNLTLK
CCEEEEHHHCCCCHH		61.83-
375UbiquitinationKEKNLTLKELFAKLK
HHCCCCHHHHHHHHC		47.32-
407UbiquitinationQTFQRFDKFNDKYNP
HHHHHHHHCCCCCCC		43.27-
451UbiquitinationGADLVEAKYQHAEPR
CHHHHHHHHHCCCCC		31.75-
452PhosphorylationADLVEAKYQHAEPRL
HHHHHHHHHCCCCCC		16.7526437602
460PhosphorylationQHAEPRLSIYGRSPD
HCCCCCCEECCCCHH		18.2922673903
462PhosphorylationAEPRLSIYGRSPDEW
CCCCCEECCCCHHHH		11.7822673903
465PhosphorylationRLSIYGRSPDEWSKL
CCEECCCCHHHHHHH		32.1322673903
471UbiquitinationRSPDEWSKLSSWFVC
CCHHHHHHHHHCEEE		54.16-
474PhosphorylationDEWSKLSSWFVCNRI
HHHHHHHHCEEECCC		34.66-
558PhosphorylationHSGHMFSSKSPKPQE
CCCCCCCCCCCCCCC		26.3626437602
576PhosphorylationEKNPSYTYYAYYMYA
CCCCCHHHEEEEHHH		4.28153695
580PhosphorylationSYTYYAYYMYANIMV
CHHHEEEEHHHHHHH		3.88153699
626PhosphorylationFMIADDISHGLNLKK
HHHHHHHHCCCCCCC		20.63108417803
662PhosphorylationNNSLFLEYAKNPFLD
CCCHHHHHHCCHHHH		25.6423879269
691AcetylationPMQFHFTKEPLMEEY
CCCCCCCCCHHHHHH		57.297683069
732UbiquitinationISHEEKVKFLGDNYL
CCHHHHCHHCCCCCC		46.03-
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 AMPD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMPD1_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 AMPD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AMPD1_HUMAN !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AMPD1_HUMAN

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Related Literatures of Post-Translational Modification

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