NNRD_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NNRD_YEAST
• UniProt AC: P36059
• Protein Name: ATP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000255|HAMAP-Rule:MF_03157}
• Gene Name: YKL151C
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 337
• Subcellular Localization: Cytoplasm .
• Protein Description: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration..
• Protein Sequence: MLAELSHRELIKLAQKRCIPPLLPKFHKGQSGGRVCIIGGCEDYTGAPYFSANATALMGCDLTHVICEYNAGTVIKSYTPNLMVHPYLRMSNTKLDVDMDEQRKKINSLLDRIHVVVIGPGLGRDPLMLKSIKDIIRYILEKHEGKIPLVIDADGLFLVTQDSEVKEMLKSYPKGRVILTPNVVEFKRLCDAIGKKGDSHSEMGSLIAQELNCIVVEKGQSDKIFSPDSEKDMLTNSEEGSNKRVGGQGDTLTGAISCMLAFSRAMYDFKICEQEEKGESSNDKPLKNWVDYAMLSCYAGCTITRECSRLGFKAKGRAMQTTDLNDRVGEVFAKLFG

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
6	Phosphorylation	--MLAELSHRELIKL --CCCCCCHHHHHHH	16.41	21440633
44	Phosphorylation	IIGGCEDYTGAPYFS EECCCCCCCCCCCCC	5.69	29688323
45	Phosphorylation	IGGCEDYTGAPYFSA ECCCCCCCCCCCCCC	38.91	29688323
49	Phosphorylation	EDYTGAPYFSANATA CCCCCCCCCCCCHHH	15.05	29688323
51	Phosphorylation	YTGAPYFSANATALM CCCCCCCCCCHHHHC	18.12	29688323
55	Phosphorylation	PYFSANATALMGCDL CCCCCCHHHHCCCCC	21.82	29688323
63	Phosphorylation	ALMGCDLTHVICEYN HHCCCCCEEEEEEEC	10.80	29688323
69	Phosphorylation	LTHVICEYNAGTVIK CEEEEEEECCCCCEE	13.10	29688323
73	Phosphorylation	ICEYNAGTVIKSYTP EEEECCCCCEEECCC	19.35	29688323
142	Acetylation	IIRYILEKHEGKIPL HHHHHHHHCCCCCCE	43.44	22865919
172	Phosphorylation	VKEMLKSYPKGRVIL HHHHHHHCCCCCEEE	13.84	27017623
187	Acetylation	TPNVVEFKRLCDAIG CCCHHHHHHHHHHHC	30.84	24489116
231	Acetylation	IFSPDSEKDMLTNSE CCCCCHHHCCCCCCC	53.00	24489116
280	Phosphorylation	EQEEKGESSNDKPLK CCHHCCCCCCCCCCC	43.01	28889911
281	Phosphorylation	QEEKGESSNDKPLKN CHHCCCCCCCCCCCH	44.75	28889911
321	Phosphorylation	AKGRAMQTTDLNDRV ECCCCCCCCCCHHHH	14.81	22369663
322	Phosphorylation	KGRAMQTTDLNDRVG CCCCCCCCCCHHHHH	22.92	22369663

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NNRD_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 NNRD_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MAM33_YEAST	MAM33	physical	16554755
YPQ3_YEAST	RTC2	genetic	27708008
NPL4_YEAST	NPL4	genetic	27708008
STE50_YEAST	STE50	genetic	27708008
ARV1_YEAST	ARV1	genetic	27708008
AIM34_YEAST	AIM34	genetic	27708008
PABC_YEAST	ABZ2	genetic	27708008
VPS21_YEAST	VPS21	genetic	27708008
VPS17_YEAST	VPS17	genetic	27708008
PMA2_YEAST	PMA2	genetic	27708008
SUR1_YEAST	SUR1	genetic	27708008
RL21B_YEAST	RPL21B	genetic	27708008
MGR2_YEAST	MGR2	genetic	27708008
DBP1_YEAST	DBP1	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-6, AND MASSSPECTROMETRY.
PubMed: 18407956