ASNS2_YEAST - dbPTM
ASNS2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASNS2_YEAST
UniProt AC P49090
Protein Name Asparagine synthetase [glutamine-hydrolyzing] 2
Gene Name ASN2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 572
Subcellular Localization
Protein Description
Protein Sequence MCGIFAAFKHEDIHNFKPKALQLSKKIRHRGPDWSGNAVMNSTIFVHERLAIVGLDSGAQPITSADGEYMLGVNGEIYNHIQLREMCSDYKFQTFSDCEPIIPLYLEHDIDAPKYLDGMFAFCLYDSKKDRIVAARDPIGVVTLYMGRSSQSPETVYFASELKCLTDVCDSIISFPPGHVYDSETDKITRYFTPDWLDEKRIPSTPVDYHAIRHSLEKAVRKRLMAEVPYGVLLSGGLDSSLIAAIAARETEKANADANEDNNVDEKQLAGIDDQGHLHTSGWSRLHSFAIGLPNAPDLQAARKVAKFIGSIHHEHTFTLQEGLDALDDVIYHLETYDVTTIRASTPMFLLSRKIKAQGVKMVLSGEGSDEIFGGYLYFAQAPSAAEFHTESVQRVKNLHLADCLRANKSTMAWGLEARVPFLDKDFLQLCMNIDPNEKMIKPKEGRIEKYILRKAFDTTDEPDVKPYLPEEILWRQKEQFSDGVGYSWIDGLRDTAERAISDAMFANPKADWGDDIPTTKEAYWYRLKFDAWFPQKTAADTVMRWIPKADWGCAEDPSGRYAKIHEKHVSA
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
17AcetylationHEDIHNFKPKALQLS
CHHHHCCCHHHHHHH		51.4222865919
19AcetylationDIHNFKPKALQLSKK
HHHCCCHHHHHHHHH		63.4224489116
24PhosphorylationKPKALQLSKKIRHRG
CHHHHHHHHHHHHCC		20.9521126336
91AcetylationREMCSDYKFQTFSDC
HHHHCCCCCCCCCCC		35.6725381059
91UbiquitinationREMCSDYKFQTFSDC
HHHHCCCCCCCCCCC		35.6723749301
96PhosphorylationDYKFQTFSDCEPIIP
CCCCCCCCCCCCCHH		44.7521440633
166PhosphorylationASELKCLTDVCDSII
HHHHHHHHHHHHHHH		35.5427017623
171PhosphorylationCLTDVCDSIISFPPG
HHHHHHHHHHCCCCC		19.3927017623
181PhosphorylationSFPPGHVYDSETDKI
CCCCCCCCCCCCCCE		14.2127017623
193PhosphorylationDKITRYFTPDWLDEK
CCEEECCCCHHHCCC		16.0521440633
200AcetylationTPDWLDEKRIPSTPV
CCHHHCCCCCCCCCC		56.1224489116
204PhosphorylationLDEKRIPSTPVDYHA
HCCCCCCCCCCCHHH		42.8622369663
205PhosphorylationDEKRIPSTPVDYHAI
CCCCCCCCCCCHHHH		23.2122369663
209PhosphorylationIPSTPVDYHAIRHSL
CCCCCCCHHHHHHHH		8.0623749301
218UbiquitinationAIRHSLEKAVRKRLM
HHHHHHHHHHHHHHH		58.4323749301
253UbiquitinationIAARETEKANADANE
HHHHHHHHHCCCCCC		55.1223749301
267AcetylationEDNNVDEKQLAGIDD
CCCCCCHHHHCCCCC		46.2624489116
346PhosphorylationVTTIRASTPMFLLSR
CCEEEECCCHHHHHH		20.1428889911
352PhosphorylationSTPMFLLSRKIKAQG
CCCHHHHHHHHHHCC		33.4028889911
397UbiquitinationTESVQRVKNLHLADC
HHHHHHHHCCCHHHH		56.8523749301
411PhosphorylationCLRANKSTMAWGLEA
HHHCCCCHHHCCCEE		16.7121440633
450UbiquitinationPKEGRIEKYILRKAF
CCCCHHHHHHHHHHC		34.9122817900
455UbiquitinationIEKYILRKAFDTTDE
HHHHHHHHHCCCCCC		50.3823749301
466AcetylationTTDEPDVKPYLPEEI
CCCCCCCCCCCCHHH		35.0124489116
482PhosphorylationWRQKEQFSDGVGYSW
HHCHHHCCCCCCCHH		32.9022369663
487PhosphorylationQFSDGVGYSWIDGLR
HCCCCCCCHHHHHHH		9.8322369663
488PhosphorylationFSDGVGYSWIDGLRD
CCCCCCCHHHHHHHH		16.1822369663
502PhosphorylationDTAERAISDAMFANP
HHHHHHHHHHHHCCC		20.5223749301
529UbiquitinationEAYWYRLKFDAWFPQ
HEEEEEEEECCCCCC		32.0023749301
529AcetylationEAYWYRLKFDAWFPQ
HEEEEEEEECCCCCC		32.0024489116
549UbiquitinationTVMRWIPKADWGCAE
HHHHHCCCCCCCCCC		50.2523749301
564AcetylationDPSGRYAKIHEKHVS
CCCCCCCCCHHCCCC		35.3425381059
568AcetylationRYAKIHEKHVSA---
CCCCCHHCCCCC---		34.8325381059
571PhosphorylationKIHEKHVSA------
CCHHCCCCC------		28.1623749301
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 ASNS2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASNS2_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 ASNS2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
URA7_YEASTURA7physical
16554755
PWP1_YEASTPWP1physical
16554755
ACE2_YEASTACE2genetic
20093466
ASNS1_YEASTASN1genetic
21623372
LGE1_YEASTLGE1genetic
27708008
EF1G_HUMANEEF1Gphysical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ASNS2_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-204 AND THR-205, ANDMASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204 AND THR-205, ANDMASS SPECTROMETRY.
"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-204 AND THR-205, ANDMASS SPECTROMETRY.

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