NGL3_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NGL3_YEAST
• UniProt AC: Q03210
• Protein Name: Probable RNA exonuclease NGL3
• Gene Name: NGL3
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 505
• Protein Sequence: MDSQVEGKISPSQKESSSTSGLVSPSEDGPAHQKIHRDQLSVDQIKKIREERAQKRQVRRNSLISQGKDPDFPTPDLQFIERPFLPINHDNSKGLTPATIQVTQDSLDVKIMTYNTLAQTLIRRDFFPESGPALKWHKRSKVLVHELKKYRPDVVSLQEVDYNELNFWQENFHKLGFDVIFKRHEGKTHGLLVAWNNKKFQLDNDWMLDYDNILAGNVISARTRTKNIALIISLYFKGITDSSSRGIIVANTHLFWHPFGVFERLRQSYLVLQKIQEIKACSKYNGWHSLLMGDFNTEPEEPPYLAITKRPLILKGPIRAMVECSLAYRYSKKRNGEESDQDDEECDEKSRGEGHSDQPQNPKPESFTATKEEKALVNQLVALHNSLHVKGVSLYGIGYGKVHPENANGSHGEPGLSNWANTWCGLLDYIFYIEGDHNQDTRQKEPLNAFEGNNNVKIIGYLRMPCAQEMPKHSQPFEGEYASDHISLMCQIRLFFGGEKVHSLK

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
10	Phosphorylation	SQVEGKISPSQKESS CCCCCCCCCCCCCCC	23.22	29136822
12	Phosphorylation	VEGKISPSQKESSST CCCCCCCCCCCCCCC	47.28	29136822
16	Phosphorylation	ISPSQKESSSTSGLV CCCCCCCCCCCCCCC	36.30	29136822
24	Phosphorylation	SSTSGLVSPSEDGPA CCCCCCCCCCCCCHH	27.96	29136822
62	Phosphorylation	KRQVRRNSLISQGKD HHHHHHHHHHHCCCC	25.85	17287358
65	Phosphorylation	VRRNSLISQGKDPDF HHHHHHHHCCCCCCC	37.87	24961812
74	Phosphorylation	GKDPDFPTPDLQFIE CCCCCCCCCCCCEEE	29.45	28889911
96	Phosphorylation	HDNSKGLTPATIQVT CCCCCCCCCCEEEEE	21.39	29136822
99	Phosphorylation	SKGLTPATIQVTQDS CCCCCCCEEEEECCC	17.10	29136822
103	Phosphorylation	TPATIQVTQDSLDVK CCCEEEEECCCCCEE	15.41	29136822
106	Phosphorylation	TIQVTQDSLDVKIMT EEEEECCCCCEEEEC	19.36	29136822
339	Phosphorylation	KKRNGEESDQDDEEC HHCCCCCCCCCHHHH	35.95	29136822

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

Oops, there are no upstream regulatory protein records of NGL3_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NGL3_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 NGL3_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATG15_YEAST	ATG15	genetic	20093466
ATG9_YEAST	ATG9	genetic	20093466
SPT3_YEAST	SPT3	genetic	20093466
YJQ3_YEAST	YJL163C	genetic	20093466
RS21B_YEAST	RPS21B	genetic	20093466
RS10A_YEAST	RPS10A	genetic	20093466
VPS10_YEAST	PEP1	genetic	27708008
AIM4_YEAST	AIM4	genetic	27708008
ATG12_YEAST	ATG12	genetic	27708008
MGR1_YEAST	MGR1	genetic	27708008
ATG9_YEAST	ATG9	genetic	27708008
CP56_YEAST	DIT2	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-62, AND MASSSPECTROMETRY.
PubMed: 18407956

"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND MASSSPECTROMETRY.
PubMed: 17287358