ECM3_YEAST - dbPTM
ECM3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECM3_YEAST
UniProt AC Q99252
Protein Name Protein ECM3
Gene Name ECM3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 613
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description May be involved in cell wall organization and biogenesis..
Protein Sequence MTHITLGQAIWASVRPIIKIYLIIGVGFGLCKMNILTVQATRSISDIVLTILLPCLSFNKIVANIEDNDIKDVGIICLTSVILFATGLGFAFIVRSVLPVPKRWRGGILAGGMFPNISDLPIAYLQSMDQGFIFTEAEGEKGVANVIIFLAMFLICVFNLGGFRLIENDFHYKGDDDEENTLTNDDSAQQPTQPIEGNSSSSSNQDILKEPNESTVPNSSQASYISEKNKKEKTELSVPKPTHTAPPAIDDRSSNSSAVVSIDSITHSLRTNHVDAQSVSELNDPTYRTRSQPIAYTTESRTSHVHNNRRNSITGSLRSIDMRELPAEGMSDLIREYSNVDQYGRRRKSSISSQGAPSVLQADGTISPNLTRTSTLQRVKTSNLTRIITSDATVSKKDIETSGSSLPKWLQKFPLTKFFVFFLKNCLRPCSMAVILALIIAFIPWVKALFVTTSNTPKIKQAPDNAPALTFIMDFTSYVGAASVPFGLILLGATLGRLKIGKLYPGFWKSAVVLVFLRQCIMPIFGVLWCDRLVKAGWLNWENDKMLLFVTAITWNLPTMTTLIYFTASYTPEDETEPVQMECTSFFLMLQYPLMVVSLPFLVSYFIKVQMKL
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
220PhosphorylationESTVPNSSQASYISE
CCCCCCCHHHHHHCC		36.0821551504
224PhosphorylationPNSSQASYISEKNKK
CCCHHHHHHCCCCCC		16.1021551504
226PhosphorylationSSQASYISEKNKKEK
CHHHHHHCCCCCCCC		33.9921551504
231UbiquitinationYISEKNKKEKTELSV
HHCCCCCCCCCCCCC		74.0617644757
233UbiquitinationSEKNKKEKTELSVPK
CCCCCCCCCCCCCCC		57.0617644757
240UbiquitinationKTELSVPKPTHTAPP
CCCCCCCCCCCCCCC		61.4617644757
254PhosphorylationPAIDDRSSNSSAVVS
CCCCCCCCCCCEEEE		41.4428889911
271PhosphorylationSITHSLRTNHVDAQS
HHCCHHHCCCCCCCH		34.6622369663
278PhosphorylationTNHVDAQSVSELNDP
CCCCCCCHHHHHCCC		29.3622369663
280PhosphorylationHVDAQSVSELNDPTY
CCCCCHHHHHCCCCC		41.4328889911
289PhosphorylationLNDPTYRTRSQPIAY
HCCCCCCCCCCCEEE		25.0230377154
291PhosphorylationDPTYRTRSQPIAYTT
CCCCCCCCCCEEEEC		39.4321082442
300PhosphorylationPIAYTTESRTSHVHN
CEEEECCCCCCCCCC		38.4719779198
303PhosphorylationYTTESRTSHVHNNRR
EECCCCCCCCCCCCC		23.5419779198
312PhosphorylationVHNNRRNSITGSLRS
CCCCCCCCCCCCCCE		21.5125533186
314PhosphorylationNNRRNSITGSLRSID
CCCCCCCCCCCCEEC		22.1229136822
316PhosphorylationRRNSITGSLRSIDMR
CCCCCCCCCCEECHH		16.3829136822
319PhosphorylationSITGSLRSIDMRELP
CCCCCCCEECHHHCC		28.3819684113
331PhosphorylationELPAEGMSDLIREYS
HCCCCCCHHHHHHHC		39.8728152593
337PhosphorylationMSDLIREYSNVDQYG
CHHHHHHHCCHHHHC		8.8319779198
338PhosphorylationSDLIREYSNVDQYGR
HHHHHHHCCHHHHCH		26.1425533186
348UbiquitinationDQYGRRRKSSISSQG
HHHCHHCHHCCCCCC		46.9017644757
349PhosphorylationQYGRRRKSSISSQGA
HHCHHCHHCCCCCCC		30.9627214570
350PhosphorylationYGRRRKSSISSQGAP
HCHHCHHCCCCCCCC		29.5323749301
352PhosphorylationRRRKSSISSQGAPSV
HHCHHCCCCCCCCCC		20.6821440633
353PhosphorylationRRKSSISSQGAPSVL
HCHHCCCCCCCCCCC		30.8521440633
358PhosphorylationISSQGAPSVLQADGT
CCCCCCCCCCCCCCC		34.6228889911
365PhosphorylationSVLQADGTISPNLTR
CCCCCCCCCCCCCCC		20.8728889911
367PhosphorylationLQADGTISPNLTRTS
CCCCCCCCCCCCCCC		13.9421440633
371PhosphorylationGTISPNLTRTSTLQR
CCCCCCCCCCCCCEE		38.2421551504
381PhosphorylationSTLQRVKTSNLTRII
CCCEEHHHCCCEEEE		21.7128889911
385PhosphorylationRVKTSNLTRIITSDA
EHHHCCCEEEEECCC		24.8724961812
389PhosphorylationSNLTRIITSDATVSK
CCCEEEEECCCCCCH		20.4122890988
390PhosphorylationNLTRIITSDATVSKK
CCEEEEECCCCCCHH		18.1622890988
393PhosphorylationRIITSDATVSKKDIE
EEEECCCCCCHHHHC		30.2424961812
395PhosphorylationITSDATVSKKDIETS
EECCCCCCHHHHCCC		29.6328889911
396UbiquitinationTSDATVSKKDIETSG
ECCCCCCHHHHCCCC		50.5623749301
397UbiquitinationSDATVSKKDIETSGS
CCCCCCHHHHCCCCC		57.3317644757
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 ECM3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ECM3_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 ECM3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BFR1_YEASTBFR1genetic
16269340
PHO86_YEASTPHO86genetic
16269340
BUG1_YEASTBUG1genetic
16269340
LAG1_YEASTLAG1physical
16093310
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
SMD1_YEASTSMD1genetic
27708008
UTP9_YEASTUTP9genetic
27708008
MOB1_YEASTMOB1genetic
27708008
NU192_YEASTNUP192genetic
27708008
KTHY_YEASTCDC8genetic
27708008
SEC22_YEASTSEC22genetic
27708008
RU1C_YEASTYHC1genetic
27708008
BET5_YEASTBET5genetic
27708008
ROT1_YEASTROT1genetic
27708008
SEC63_YEASTSEC63genetic
27708008
MYO2_YEASTMYO2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ECM3_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-278; SER-280; SER-291;SER-338 AND SER-353, AND MASS SPECTROMETRY.

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