NMA2_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NMA2_YEAST
• UniProt AC: P53204
• Protein Name: Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 {ECO:0000305}
• Gene Name: NMA2 {ECO:0000303|PubMed:11884393}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 395
• Subcellular Localization: Nucleus .
• Protein Description: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. [PubMed: 12597897 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 (By similarity Predominantly acts in the salvage pathways via NMN]
• Protein Sequence: MDPTKAPDFKPPQPNEELQPPPDPTHTIPKSGPIVPYVLADYNSSIDAPFNLDIYKTLSSRKKNANSSNRMDHIPLNTSDFQPLSRDVSSEEESEGQSNGIDATLQDVTMTGNLGVLKSQIADLEEVPHTIVRQARTIEDYEFPVHRLTKKLQDPEKLPLIIVACGSFSPITYLHLRMFEMALDDINEQTRFEVVGGYFSPVSDNYQKRGLAPAYHRVRMCELACERTSSWLMVDAWESLQSSYTRTAKVLDHFNHEINIKRGGIMTVDGEKMGVKIMLLAGGDLIESMGEPHVWADSDLHHILGNYGCLIVERTGSDVRSFLLSHDIMYEHRRNILIIKQLIYNDISSTKVRLFIRRGMSVQYLLPNSVIRYIQEYNLYINQSEPVKQVLDSKE

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
78	Phosphorylation	MDHIPLNTSDFQPLS CCCCCCCCCCCCCCC	37.04	22369663
79	Phosphorylation	DHIPLNTSDFQPLSR CCCCCCCCCCCCCCC	35.04	22369663
85	Phosphorylation	TSDFQPLSRDVSSEE CCCCCCCCCCCCCHH	32.87	22369663
89	Phosphorylation	QPLSRDVSSEEESEG CCCCCCCCCHHHHHH	36.00	28889911
90	Phosphorylation	PLSRDVSSEEESEGQ CCCCCCCCHHHHHHH	49.20	28889911
94	Phosphorylation	DVSSEEESEGQSNGI CCCCHHHHHHHCCCC	50.75	19779198
98	Phosphorylation	EEESEGQSNGIDATL HHHHHHHCCCCCCEE	48.13	19779198
137	Phosphorylation	TIVRQARTIEDYEFP HHHHHCCCHHCCCCC	31.56	28889911
157	Ubiquitination	KKLQDPEKLPLIIVA HHCCCHHHCCEEEEE	61.87	22106047
261	Acetylation	FNHEINIKRGGIMTV CCCCEEEECCCEEEE	40.27	24489116

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of NMA2_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NMA2_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NMA2_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NMA2_YEAST	NMA2	physical	10688190
NMA1_YEAST	NMA1	physical	10688190
NMA1_YEAST	NMA1	physical	16554755
NMA1_YEAST	NMA1	physical	11283351
NMA1_YEAST	NMA1	genetic	21623372
ACON_YEAST	ACO1	genetic	21623372
ERG2_YEAST	ERG2	genetic	21623372
THDH_YEAST	ILV1	genetic	21623372
UAP1_YEAST	QRI1	genetic	27708008
CDC48_YEAST	CDC48	genetic	27708008
RPB1_YEAST	RPO21	genetic	27708008
SEC31_YEAST	SEC31	genetic	27708008
SNU56_YEAST	SNU56	genetic	27708008
TFB1_YEAST	TFB1	genetic	27708008
COG3_YEAST	COG3	genetic	27708008
ACT_YEAST	ACT1	genetic	27708008
RPB2_YEAST	RPB2	genetic	27708008

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-85, AND MASSSPECTROMETRY.
PubMed: 18407956

"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-85, AND MASSSPECTROMETRY.
PubMed: 17330950