RTN1_YEAST - dbPTM
RTN1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RTN1_YEAST
UniProt AC Q04947
Protein Name Reticulon-like protein 1
Gene Name RTN1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 295
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MSASAQHSQAQQQQQQKSCNCDLLLWRNPVQTGKYFGGSLLALLILKKVNLITFFLKVAYTILFTTGSIEFVSKLFLGQGLITKYGPKECPNIAGFIKPHIDEALKQLPVFQAHIRKTVFAQVPKHTFKTAVALFLLHKFFSWFSIWTIVFVADIFTFTLPVIYHSYKHEIDATVAQGVEISKQKTQEFSQMACEKTKPYLDKVESKLGPISNLVKSKTAPVSSTAGPQTASTSKLAADVPLEPESKAYTSSAQVMPEVPQHEPSTTQEFNVDELSNELKKSTKNLQNELEKNNA
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
2Phosphorylation------MSASAQHSQ
------CCHHHHHHH		30.8224909858
4Phosphorylation----MSASAQHSQAQ
----CCHHHHHHHHH		22.5822369663
8PhosphorylationMSASAQHSQAQQQQQ
CCHHHHHHHHHHHHH		18.3522369663
18PhosphorylationQQQQQQKSCNCDLLL
HHHHHHHCCCCCEEE		13.2628889911
84AcetylationLGQGLITKYGPKECP
CCCCHHHHCCCCCCC		41.0124489116
88AcetylationLITKYGPKECPNIAG
HHHHCCCCCCCCCCH		68.5324489116
98AcetylationPNIAGFIKPHIDEAL
CCCCHHCHHHHHHHH		28.4324489116
125AcetylationTVFAQVPKHTFKTAV
HHHHCCCHHHHHHHH		57.3224489116
185UbiquitinationGVEISKQKTQEFSQM
CCCCCHHHHHHHHHH		56.7823749301
186PhosphorylationVEISKQKTQEFSQMA
CCCCHHHHHHHHHHH		30.7322369663
190PhosphorylationKQKTQEFSQMACEKT
HHHHHHHHHHHHHHC		20.4929734811
196AcetylationFSQMACEKTKPYLDK
HHHHHHHHCHHHHHH		62.8324489116
196UbiquitinationFSQMACEKTKPYLDK
HHHHHHHHCHHHHHH		62.8317644757
198UbiquitinationQMACEKTKPYLDKVE
HHHHHHCHHHHHHHH		42.6117644757
203AcetylationKTKPYLDKVESKLGP
HCHHHHHHHHHHHCH		45.3624489116
203UbiquitinationKTKPYLDKVESKLGP
HCHHHHHHHHHHHCH		45.3617644757
206PhosphorylationPYLDKVESKLGPISN
HHHHHHHHHHCHHHH		35.8522890988
207AcetylationYLDKVESKLGPISNL
HHHHHHHHHCHHHHH		43.9124489116
207UbiquitinationYLDKVESKLGPISNL
HHHHHHHHHCHHHHH		43.9117644757
212PhosphorylationESKLGPISNLVKSKT
HHHHCHHHHHHCCCC		27.5222369663
216AcetylationGPISNLVKSKTAPVS
CHHHHHHCCCCCCCC		49.7724489116
216UbiquitinationGPISNLVKSKTAPVS
CHHHHHHCCCCCCCC		49.7717644757
217PhosphorylationPISNLVKSKTAPVSS
HHHHHHCCCCCCCCC		27.9722369663
218UbiquitinationISNLVKSKTAPVSST
HHHHHCCCCCCCCCC		42.8823749301
219PhosphorylationSNLVKSKTAPVSSTA
HHHHCCCCCCCCCCC		43.2022369663
223PhosphorylationKSKTAPVSSTAGPQT
CCCCCCCCCCCCCCC		22.4022890988
224PhosphorylationSKTAPVSSTAGPQTA
CCCCCCCCCCCCCCC		23.6322890988
225PhosphorylationKTAPVSSTAGPQTAS
CCCCCCCCCCCCCCC		28.2922369663
230PhosphorylationSSTAGPQTASTSKLA
CCCCCCCCCCCCCCC		26.2125521595
232PhosphorylationTAGPQTASTSKLAAD
CCCCCCCCCCCCCCC		36.2822369663
233PhosphorylationAGPQTASTSKLAADV
CCCCCCCCCCCCCCC		27.6722890988
234PhosphorylationGPQTASTSKLAADVP
CCCCCCCCCCCCCCC		24.1522369663
235AcetylationPQTASTSKLAADVPL
CCCCCCCCCCCCCCC		42.0824489116
235UbiquitinationPQTASTSKLAADVPL
CCCCCCCCCCCCCCC		42.0823749301
246PhosphorylationDVPLEPESKAYTSSA
CCCCCCCCCCCCCCC		33.0522369663
249PhosphorylationLEPESKAYTSSAQVM
CCCCCCCCCCCCCCC		15.7621440633
250PhosphorylationEPESKAYTSSAQVMP
CCCCCCCCCCCCCCC		22.5121551504
251PhosphorylationPESKAYTSSAQVMPE
CCCCCCCCCCCCCCC		15.8221440633
252PhosphorylationESKAYTSSAQVMPEV
CCCCCCCCCCCCCCC		18.2130377154
265PhosphorylationEVPQHEPSTTQEFNV
CCCCCCCCCCCCCCH		40.8920377248
266PhosphorylationVPQHEPSTTQEFNVD
CCCCCCCCCCCCCHH		43.1219779198
267PhosphorylationPQHEPSTTQEFNVDE
CCCCCCCCCCCCHHH		30.3620377248
276PhosphorylationEFNVDELSNELKKST
CCCHHHHHHHHHHHH		26.6421082442
280AcetylationDELSNELKKSTKNLQ
HHHHHHHHHHHHHHH		38.2024489116
282PhosphorylationLSNELKKSTKNLQNE
HHHHHHHHHHHHHHH		42.9230377154
283PhosphorylationSNELKKSTKNLQNEL
HHHHHHHHHHHHHHH		32.6030377154
284UbiquitinationNELKKSTKNLQNELE
HHHHHHHHHHHHHHH		63.8523749301
292AcetylationNLQNELEKNNA----
HHHHHHHHHCC----		69.0324489116
292UbiquitinationNLQNELEKNNA----
HHHHHHHHHCC----		69.0323749301
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 RTN1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RTN1_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 RTN1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRA1_YEASTYIP3physical
16002643
YPT1_YEASTYPT1physical
16002643
RTN2_YEASTRTN2physical
16002643
CARP_YEASTPEP4physical
16554755
CARP_YEASTPEP4physical
16429126
SEC6_YEASTSEC6physical
16624861
SCS7_YEASTSCS7genetic
16269340
GET2_YEASTGET2genetic
16269340
ATU2_YEASTCCC2genetic
16269340
DPM1_YEASTDPM1genetic
16269340
MSC2_YEASTMSC2genetic
16269340
MTC4_YEASTMTC4genetic
16269340
PRY1_YEASTPRY1genetic
16269340
CYPD_YEASTCPR5genetic
16269340
SLY41_YEASTSLY41genetic
16269340
CAB5_YEASTCAB5genetic
16269340
OSTB_YEASTWBP1genetic
16269340
COPD_YEASTRET2genetic
16269340
PGA3_YEASTPGA3genetic
16269340
DGK1_YEASTDGK1genetic
16269340
GAS1_YEASTGAS1genetic
16269340
ICE2_YEASTICE2genetic
16269340
SC6B1_YEASTSBH1physical
17699516
RPD3_YEASTRPD3genetic
19547744
SIN3_YEASTSIN3genetic
19547744
RTN1_YEASTRTN1physical
18442980
NUP85_YEASTNUP85genetic
19273614
NU120_YEASTNUP120genetic
19273614
NU145_YEASTNUP145genetic
19273614
PO152_YEASTPOM152genetic
19273614
NUP82_YEASTNUP82genetic
19273614
NU116_YEASTNUP116genetic
19273614
GLE2_YEASTGLE2genetic
19273614
NU188_YEASTNUP188genetic
19273614
SPO7_YEASTSPO7genetic
19273614
NEM1_YEASTNEM1genetic
19273614
POM33_YEASTPOM33physical
20498018
GET2_YEASTGET2genetic
19325107
CYS3_YEASTCYS3genetic
19325107
EOS1_YEASTEOS1genetic
19325107
GET3_YEASTGET3genetic
19325107
VPS54_YEASTVPS54genetic
19325107
NDC1_YEASTNDC1genetic
22798490
BBP1_YEASTBBP1genetic
22798490
MPS2_YEASTMPS2genetic
22798490
LNP_YEASTLNP1genetic
22729086
YOP1_YEASTYOP1genetic
22729086
ENO2_YEASTENO2physical
22940862
HSP71_YEASTSSA1physical
22940862
KPYK1_YEASTCDC19physical
22940862
CARP_YEASTPEP4physical
22940862
HSP7F_YEASTSSE1physical
22940862
RTN1_YEASTRTN1physical
22940862
SSB1_YEASTSSB1physical
22940862
HSP72_YEASTSSA2physical
22940862
RV161_YEASTRVS161genetic
23891562
SEC22_YEASTSEC22genetic
23891562
GET2_YEASTGET2genetic
23891562
ERV46_YEASTERV46genetic
23891562
ICE2_YEASTICE2genetic
23891562
YOP1_YEASTYOP1genetic
20805477
NDC1_YEASTNDC1physical
26041935
LNP_YEASTLNP1genetic
27117666
PEX30_YEASTPEX30physical
27129769
YOP1_YEASTYOP1physical
27129769
PEX29_YEASTPEX29physical
27129769
SCS2_YEASTSCS2physical
27129769
DPM1_YEASTDPM1physical
27129769
YET3_YEASTYET3physical
27129769
ERG6_YEASTERG6physical
27129769
ERG1_YEASTERG1physical
27129769
FDFT_YEASTERG9physical
27129769
CP51_YEASTERG11physical
27129769
NCB5R_YEASTCBR1physical
27129769
NCPR_YEASTNCP1physical
27129769
PRA1_YEASTYIP3physical
27129769
LSP1_YEASTLSP1physical
27129769
PIL1_YEASTPIL1physical
27129769
SEY1_YEASTSEY1physical
27129769
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RTN1_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-186; THR-230; SER-232;SER-234; SER-265; THR-267 AND SER-276, 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 THR-186 AND THR-219, ANDMASS SPECTROMETRY.

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