NMA1_YEAST - dbPTM
NMA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NMA1_YEAST
UniProt AC Q06178
Protein Name Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 {ECO:0000305}
Gene Name NMA1 {ECO:0000303|PubMed:11884393}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 401
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate to form deamido-NAD(+) (NaAD). Key enzyme in both de novo and salvage pathways for NAD(+) biosynthesis. Predominantly acts in the salvage pathways via NMN..
Protein Sequence MDPTRAPDFKPPSADEELIPPPDPESKIPKSIPIIPYVLADANSSIDAPFNIKRKKKHPKHHHHHHHSRKEGNDKKHQHIPLNQDDFQPLSAEVSSEDDDADFRSKERYGSDSTTESETRGVQKYQIADLEEVPHGIVRQARTLEDYEFPSHRLSKKLLDPNKLPLVIVACGSFSPITYLHLRMFEMALDAISEQTRFEVIGGYYSPVSDNYQKQGLAPSYHRVRMCELACERTSSWLMVDAWESLQPSYTRTAKVLDHFNHEINIKRGGVATVTGEKIGVKIMLLAGGDLIESMGEPNVWADADLHHILGNYGCLIVERTGSDVRSFLLSHDIMYEHRRNILIIKQLIYNDISSTKVRLFIRRAMSVQYLLPNSVIRYIQEHRLYVDQTEPVKQVLGNKE
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----MDPTRAPDFKP
----CCCCCCCCCCC		34.8929136822
10UbiquitinationPTRAPDFKPPSADEE
CCCCCCCCCCCCCCC		64.5022106047
13PhosphorylationAPDFKPPSADEELIP
CCCCCCCCCCCCCCC		57.8029136822
44PhosphorylationYVLADANSSIDAPFN
EEECCCCCCCCCCCC		30.3221440633
45PhosphorylationVLADANSSIDAPFNI
EECCCCCCCCCCCCC		25.0523749301
91PhosphorylationQDDFQPLSAEVSSED
CCCCCCCCCCCCCCC		29.1217330950
95PhosphorylationQPLSAEVSSEDDDAD
CCCCCCCCCCCCCCC		21.3717330950
96PhosphorylationPLSAEVSSEDDDADF
CCCCCCCCCCCCCCC		50.6617330950
105PhosphorylationDDDADFRSKERYGSD
CCCCCCCCHHHHCCC		38.5719823750
109PhosphorylationDFRSKERYGSDSTTE
CCCCHHHHCCCCCCH		23.2925521595
111PhosphorylationRSKERYGSDSTTESE
CCHHHHCCCCCCHHH		21.3222369663
113PhosphorylationKERYGSDSTTESETR
HHHHCCCCCCHHHHC		38.6420377248
114PhosphorylationERYGSDSTTESETRG
HHHCCCCCCHHHHCC		39.3020377248
115PhosphorylationRYGSDSTTESETRGV
HHCCCCCCHHHHCCC		41.2720377248
117PhosphorylationGSDSTTESETRGVQK
CCCCCCHHHHCCCEE		42.0220377248
119PhosphorylationDSTTESETRGVQKYQ
CCCCHHHHCCCEEEE		41.8423749301
124UbiquitinationSETRGVQKYQIADLE
HHHCCCEEEEECCHH		36.3923749301
124AcetylationSETRGVQKYQIADLE
HHHCCCEEEEECCHH		36.3924489116
143PhosphorylationGIVRQARTLEDYEFP
HHHHHCCCCCCCCCC		37.2023749301
370PhosphorylationRRAMSVQYLLPNSVI
HHHHCHHHHCCHHHH		14.1928132839
394UbiquitinationVDQTEPVKQVLGNKE
CCCCCCHHHHHCCCC		45.4617644757
400UbiquitinationVKQVLGNKE------
HHHHHCCCC------		64.1017644757
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 NMA1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NMA1_YEAST !!
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 NMA1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NMA2_YEASTNMA2physical
11283351
NMA2_YEASTNMA2physical
10688190
NMA1_YEASTNMA1physical
10688190
NMA1_YEASTNMA1physical
11283351
NMA2_YEASTNMA2physical
18719252
NMA1_YEASTNMA1physical
18719252
SMT3_YEASTSMT3physical
18719252
NMA2_YEASTNMA2genetic
18408719
REI1_YEASTREI1genetic
20093466
NMA2_YEASTNMA2genetic
20093466
RS27B_YEASTRPS27Bgenetic
20093466
MRT4_YEASTMRT4genetic
20093466
TKT1_YEASTTKL1genetic
20093466
NMA2_YEASTNMA2physical
20826334
NMA2_YEASTNMA2genetic
21623372
ACON2_YEASTACO2genetic
21623372
PFKA1_YEASTPFK1genetic
21623372
ARO1_YEASTARO1genetic
21623372
THDH_YEASTILV1genetic
21623372
NMA1_YEASTNMA1physical
22615397
REI1_YEASTREI1genetic
27708008
NMA2_YEASTNMA2genetic
27708008
MRT4_YEASTMRT4genetic
27708008
KAR3_YEASTKAR3genetic
27708008
UBC9_HUMANUBE2Iphysical
27107014
NMNA1_HUMANNMNAT1physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NMA1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-95 AND SER-96,AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; SER-95 AND SER-96,AND MASS SPECTROMETRY.

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