NIT3_YEAST - dbPTM
NIT3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NIT3_YEAST
UniProt AC P49954
Protein Name Omega-amidase NIT3 {ECO:0000303|PubMed:28373563}
Gene Name NIT3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 291
Subcellular Localization
Protein Description Has a omega-amidase activity. The role of omega-amidase is to remove potentially toxic intermediates by converting 2-oxoglutaramate and 2-oxosuccinamate to biologically useful 2-oxoglutarate and oxaloacetate, respectively..
Protein Sequence MSASKILSQKIKVALVQLSGSSPDKMANLQRAATFIERAMKEQPDTKLVVLPECFNSPYSTDQFRKYSEVINPKEPSTSVQFLSNLANKFKIILVGGTIPELDPKTDKIYNTSIIFNEDGKLIDKHRKVHLFDVDIPNGISFHESETLSPGEKSTTIDTKYGKFGVGICYDMRFPELAMLSARKGAFAMIYPSAFNTVTGPLHWHLLARSRAVDNQVYVMLCSPARNLQSSYHAYGHSIVVDPRGKIVAEAGEGEEIIYAELDPEVIESFRQAVPLTKQRRFDVYSDVNAH
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
22PhosphorylationLVQLSGSSPDKMANL
EEECCCCCHHHHHHH		40.4123749301
34PhosphorylationANLQRAATFIERAMK
HHHHHHHHHHHHHHH		24.9428889911
47UbiquitinationMKEQPDTKLVVLPEC
HHHCCCCEEEECCCH		46.8223749301
74AcetylationYSEVINPKEPSTSVQ
HHCCCCCCCCCCHHH		77.1924489116
89AcetylationFLSNLANKFKIILVG
HHHHHHHCCEEEEEC		42.2924489116
105AcetylationTIPELDPKTDKIYNT
CCCCCCCCCCCEECE		69.8624489116
110PhosphorylationDPKTDKIYNTSIIFN
CCCCCCEECEEEEEC		20.3727017623
112PhosphorylationKTDKIYNTSIIFNED
CCCCEECEEEEECCC		12.3427017623
121AcetylationIIFNEDGKLIDKHRK
EEECCCCCEEECCCC		55.3724489116
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 NIT3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NIT3_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 NIT3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NIT3_YEASTNIT3physical
12833551
SCC1_YEASTMCD1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
NOT1_YEASTCDC39genetic
27708008
RRP42_YEASTRRP42genetic
27708008
XPO1_YEASTCRM1genetic
27708008
MOB1_YEASTMOB1genetic
27708008
SLN1_YEASTSLN1genetic
27708008
NSE1_YEASTNSE1genetic
27708008
SMC4_YEASTSMC4genetic
27708008
LCB1_YEASTLCB1genetic
27708008
NOG2_YEASTNOG2genetic
27708008
SEC16_YEASTSEC16genetic
27708008
NAB3_YEASTNAB3genetic
27708008
DIM1_YEASTDIM1genetic
27708008
MED10_YEASTNUT2genetic
27708008
2ABA_YEASTCDC55genetic
27453043
DCOR_YEASTSPE1genetic
27453043
BUB1_YEASTBUB1genetic
27453043
VPS1_YEASTVPS1genetic
27453043
DCAM_YEASTSPE2genetic
27453043
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NIT3_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 THR-34, AND MASSSPECTROMETRY.

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