RSN1_YEAST - dbPTM
RSN1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RSN1_YEAST
UniProt AC Q03516
Protein Name Uncharacterized protein RSN1
Gene Name RSN1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 953
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Acts as an osmosensitive calcium-permeable cation channel..
Protein Sequence MNSTNSTNSTTTATSTNTSTQQVVTSLVSNGTIFGVFVIAFLILRIKLKRIYEPKSSFNLINEEKKPEPLPQGVWQWLKPLLKKSDNFVIQQAGLDGYFFLRYLFIIAIYCAVSMSYIFPILLSINASNGNHESGLNQLAYQNVKHRGRYFAHVFCGWIFFWGFLYIIYRELYFYTSMKQAVLASPRYAKKLSSRTVLFQTVPKQYLSEEEFSKLFDGVKRVWIARGSGSIEAMVKARDNMAIQLEGAETKYLKAALKKIKKLNKKSPQLSVSDNIAEYVPDKKRPHHKINKVAKFFFGKKVDTISYIKEELPKLNQKVKALQEDHENSSPFNSVFVEFESQYQAQVAAQITTYHAPLFMTPVYIGIEPSDVVWFNLRMFWWERLGREVSAVSAIVALVILWAFPVAFVGMISNITSLTNEVKWLKFIYKLPKQLLGLLTSLAPTVALAVLMSFLPKFIRGMAITQGAPSKQNVEYFTQQAYFAFQVIQVFLVTTLSSAATSTVTEIVKEPTKAMDLLASNLPKASNFFMSYVILQGLSISSGALLQIVPLILFYVLGAFLDGTVRKKWNRFCGLSSMQWGTAFPVYTNLAVITFSYSIISPLILLFAAVAFFLLYIAYLYNLTYVYQESPDARGIYYPRALFQTIVGIYIGQICLLGLFAVGKGWGPIVLQVIGICVTVLIHLHLSAAFDHLSKVIPVDTMKPLDGVSDTPSFKNIYKGIESTKVKKNTFGANIDMDGIKELPEFPIKKYHKRSESVTEQQVENSIFSENTFEYQFNPANEANADGHAINAENLIEDVPLLADGDTMKIPPAPWWKRFLKPHIYYSYKAVKSRLPEIYGLVDPDERVNDFDISHAYDYPAVSAQCPELWIPRDPFGFSKLLISDVSGVVEMNDENATIDENLKFTLRDVPPPYNDVKDEANGEANGEFDTASKENNPFADPKYKEEESRSAV
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
173PhosphorylationYIIYRELYFYTSMKQ
HHHHHHHHHHHHHHH		6.9827017623
176PhosphorylationYRELYFYTSMKQAVL
HHHHHHHHHHHHHHH		16.6727017623
214UbiquitinationLSEEEFSKLFDGVKR
CCHHHHHHHHCCCEE		59.5023749301
228PhosphorylationRVWIARGSGSIEAMV
EEEEEECCCCHHHHH		24.6623749301
230PhosphorylationWIARGSGSIEAMVKA
EEEECCCCHHHHHHC		20.9627017623
250PhosphorylationIQLEGAETKYLKAAL
EEECCHHHHHHHHHH		25.1827017623
267PhosphorylationIKKLNKKSPQLSVSD
HHHHCCCCCCCCCCC		21.3528889911
295AcetylationHKINKVAKFFFGKKV
HHHCHHHHHHHCCCC		45.7724489116
300UbiquitinationVAKFFFGKKVDTISY
HHHHHHCCCCHHHHH		44.4617644757
301UbiquitinationAKFFFGKKVDTISYI
HHHHHCCCCHHHHHH		45.8017644757
306PhosphorylationGKKVDTISYIKEELP
CCCCHHHHHHHHHHH		23.9328889911
307PhosphorylationKKVDTISYIKEELPK
CCCHHHHHHHHHHHH		16.5028889911
309AcetylationVDTISYIKEELPKLN
CHHHHHHHHHHHHHH		36.5824489116
309UbiquitinationVDTISYIKEELPKLN
CHHHHHHHHHHHHHH		36.5817644757
314UbiquitinationYIKEELPKLNQKVKA
HHHHHHHHHHHHHHH		73.1017644757
703UbiquitinationVIPVDTMKPLDGVSD
CCCCCCCCCCCCCCC		44.5123749301
703AcetylationVIPVDTMKPLDGVSD
CCCCCCCCCCCCCCC		44.5124489116
713PhosphorylationDGVSDTPSFKNIYKG
CCCCCCHHHHHHHHH		51.4421551504
719UbiquitinationPSFKNIYKGIESTKV
HHHHHHHHHHHCCCC		50.0123749301
725UbiquitinationYKGIESTKVKKNTFG
HHHHHCCCCCCCCCC		62.4323749301
727UbiquitinationGIESTKVKKNTFGAN
HHHCCCCCCCCCCCC		41.6917644757
728UbiquitinationIESTKVKKNTFGANI
HHCCCCCCCCCCCCC		65.2923749301
741UbiquitinationNIDMDGIKELPEFPI
CCCCCCCCCCCCCCC		59.7424961812
749UbiquitinationELPEFPIKKYHKRSE
CCCCCCCCCCCCCCC		47.7424961812
750UbiquitinationLPEFPIKKYHKRSES
CCCCCCCCCCCCCCC		53.9917644757
821AcetylationPWWKRFLKPHIYYSY
HHHHHHCCHHHHEHH		31.6624489116
918UbiquitinationPPPYNDVKDEANGEA
CCCCCCCCCCCCCCC		53.3523749301
931PhosphorylationEANGEFDTASKENNP
CCCCCCCCCCCCCCC		37.8425521595
933PhosphorylationNGEFDTASKENNPFA
CCCCCCCCCCCCCCC		42.4625521595
944PhosphorylationNPFADPKYKEEESRS
CCCCCCCCCHHHHHC		29.0819823750
945UbiquitinationPFADPKYKEEESRSA
CCCCCCCCHHHHHCC		65.8523749301
949PhosphorylationPKYKEEESRSAV---
CCCCHHHHHCCC---		34.5119823750
951PhosphorylationYKEEESRSAV-----
CCHHHHHCCC-----		42.5425521595
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 RSN1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RSN1_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 RSN1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIR2_YEASTSIR2genetic
18931302
SLX5_YEASTSLX5genetic
18931302
ELO2_YEASTELO2genetic
27708008
UME6_YEASTUME6genetic
27708008
CP56_YEASTDIT2genetic
27708008
DIT1_YEASTDIT1genetic
27708008
MSN4_YEASTMSN4genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RSN1_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-933, AND MASSSPECTROMETRY.
"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-949, AND MASSSPECTROMETRY.

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