ASNS1_YEAST - dbPTM
ASNS1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASNS1_YEAST
UniProt AC P49089
Protein Name Asparagine synthetase [glutamine-hydrolyzing] 1
Gene Name ASN1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 572
Subcellular Localization
Protein Description
Protein Sequence MCGIFAAFRHEDVHRYKPKALQLSKRIRHRGPDWSGNAIKNSTIFVHERLAIVGVESGAQPITSSDGEYMLCVNGEIYNHIQLREECADYEFGTLSDCEPIIPMYLKHDIDAPKYLDGMFAWTLYDAKQDRIVAARDPIGITTLYMGRSSASPKTVYFASELKCLTDDCDTITAFPPGHVYDSKTDKITRYFTPDWLDEKRIPSTPIDYMAIRHSLEKAVRKRLMAEVPYGVLLSGGLDSSLIASIAARETAKATNDVEPSTYDSKARHLAGIDDDGKLHTAGWTSLHSFAIGLPNAPDLQAARKVAKFIGSIHHEHTFTLQEGLDALDDVIYHLETYDVTTIRASTPMFLLSRKIKAQGVKMVLSGEGSDEIFGGYLYFAQAPSAAEFHTESVQRVKNLHLADCLRANKSTMAWGLEARVPFLDREFLQLCMNIDPNEKMIKPKEGRIEKYILRKAFDTTGEPDAKPYLPEEILWRQKEQFSDGVGYSWIDGLKDTAEAVISDEMFASPKAEWGSDIPTTKEAFWYRLKFDALFPQKTVADTVMRWIPKADWGCAEDPSGRYAQIHEKHIE
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
17UbiquitinationHEDVHRYKPKALQLS
CCHHHHHCCHHHHHH		39.7422817900
19UbiquitinationDVHRYKPKALQLSKR
HHHHHCCHHHHHHHH		58.5422817900
40UbiquitinationDWSGNAIKNSTIFVH
CCCCCCCCCCEEEEE		42.3022817900
96PhosphorylationDYEFGTLSDCEPIIP
CCCCCCHHCCCCCHH		39.8027017623
115PhosphorylationHDIDAPKYLDGMFAW
CCCCCCHHHCCCCCE		14.6827017623
154UbiquitinationGRSSASPKTVYFASE
CCCCCCCCCEEEEEE		48.4023749301
154AcetylationGRSSASPKTVYFASE
CCCCCCCCCEEEEEE		48.4024489116
193PhosphorylationDKITRYFTPDWLDEK
CEEEECCCCHHHCCC		16.0521440633
200AcetylationTPDWLDEKRIPSTPI
CCHHHCCCCCCCCCC		56.1224489116
204PhosphorylationLDEKRIPSTPIDYMA
HCCCCCCCCCCCHHH		44.4322369663
205PhosphorylationDEKRIPSTPIDYMAI
CCCCCCCCCCCHHHH		20.9322369663
218UbiquitinationAIRHSLEKAVRKRLM
HHHHHHHHHHHHHHH		58.4323749301
218AcetylationAIRHSLEKAVRKRLM
HHHHHHHHHHHHHHH		58.4324489116
253UbiquitinationIAARETAKATNDVEP
HHHHHHHHHCCCCCC		64.2623749301
261PhosphorylationATNDVEPSTYDSKAR
HCCCCCCCCCCCCCH		26.5422369663
262PhosphorylationTNDVEPSTYDSKARH
CCCCCCCCCCCCCHH		41.9022369663
263PhosphorylationNDVEPSTYDSKARHL
CCCCCCCCCCCCHHC		23.6623749301
265PhosphorylationVEPSTYDSKARHLAG
CCCCCCCCCCHHCCC		20.1522369663
266UbiquitinationEPSTYDSKARHLAGI
CCCCCCCCCHHCCCC		46.6823749301
266AcetylationEPSTYDSKARHLAGI
CCCCCCCCCHHCCCC		46.6825381059
281PhosphorylationDDDGKLHTAGWTSLH
CCCCCEECCCCCEEC		36.9819795423
285PhosphorylationKLHTAGWTSLHSFAI
CEECCCCCEECCHHC		22.0919795423
286PhosphorylationLHTAGWTSLHSFAIG
EECCCCCEECCHHCC		19.9919795423
289PhosphorylationAGWTSLHSFAIGLPN
CCCCEECCHHCCCCC		22.9719795423
347PhosphorylationVTTIRASTPMFLLSR
CCEEEECCCHHHHHH		20.1428889911
353PhosphorylationSTPMFLLSRKIKAQG
CCCHHHHHHHHHHCC		33.4028889911
398UbiquitinationTESVQRVKNLHLADC
HHHHHHHHCCCHHHH		56.8523749301
412PhosphorylationCLRANKSTMAWGLEA
HHHCCCCHHHHCCCC		16.7121440633
451AcetylationPKEGRIEKYILRKAF
CCCCHHHHHHHHHHH		34.9124489116
451UbiquitinationPKEGRIEKYILRKAF
CCCCHHHHHHHHHHH		34.9122817900
456UbiquitinationIEKYILRKAFDTTGE
HHHHHHHHHHCCCCC		50.3823749301
467AcetylationTTGEPDAKPYLPEEI
CCCCCCCCCCCCHHH		41.3924489116
467UbiquitinationTTGEPDAKPYLPEEI
CCCCCCCCCCCCHHH		41.3923749301
479AcetylationEEILWRQKEQFSDGV
HHHHHHCHHHCCCCC		44.9324489116
497PhosphorylationWIDGLKDTAEAVISD
HHCCHHHHHHHHHCH		25.4719823750
503PhosphorylationDTAEAVISDEMFASP
HHHHHHHCHHHHCCC		22.4019823750
509PhosphorylationISDEMFASPKAEWGS
HCHHHHCCCCCCCCC		18.7022369663
516PhosphorylationSPKAEWGSDIPTTKE
CCCCCCCCCCCCHHH		33.1828889911
530AcetylationEAFWYRLKFDALFPQ
HHHHHHHHHCCCCCC		32.0024489116
530UbiquitinationEAFWYRLKFDALFPQ
HHHHHHHHHCCCCCC		32.0023749301
539PhosphorylationDALFPQKTVADTVMR
CCCCCCCCHHHHHHH		18.7122369663
550UbiquitinationTVMRWIPKADWGCAE
HHHHHCCCCCCCCCC		50.2523749301
550AcetylationTVMRWIPKADWGCAE
HHHHHCCCCCCCCCC		50.2524489116
569AcetylationRYAQIHEKHIE----
CCCCHHHHHCC----		35.4022865919
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 ASNS1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASNS1_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 ASNS1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASNS2_YEASTASN2genetic
8951815
ASNS2_YEASTASN2genetic
17284612
ASNS2_YEASTASN2genetic
18408719
ASNS2_YEASTASN2genetic
16941010
LRP1_YEASTLRP1genetic
20093466
MGA2_YEASTMGA2genetic
20093466
GPT2_YEASTGPT2genetic
20093466
YNO6_YEASTYNL146Wgenetic
20093466
OCA2_YEASTOCA2genetic
20093466
ATP23_YEASTATP23genetic
20093466
RS28A_YEASTRPS28Agenetic
20093466
SYSM_YEASTDIA4genetic
21623372
QCR8_YEASTQCR8genetic
21623372
STT3_YEASTSTT3genetic
27708008
MED6_YEASTMED6genetic
27708008
CDC11_YEASTCDC11genetic
27708008
SEC22_YEASTSEC22genetic
27708008
SNF1_YEASTSNF1genetic
27708008
LRP1_YEASTLRP1genetic
27708008
MGA2_YEASTMGA2genetic
27708008
DCOR_YEASTSPE1genetic
27708008
IRS4_YEASTIRS4genetic
27708008
YNO6_YEASTYNL146Wgenetic
27708008
RS28A_YEASTRPS28Agenetic
27708008
PNG1_YEASTPNG1genetic
27708008
PMP1_YEASTPMP1physical
26404137
CEP55_HUMANCEP55physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ASNS1_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; THR-205; SER-265AND SER-509, AND MASS 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 MASSSPECTROMETRY.

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