YET1_YEAST - dbPTM
YET1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YET1_YEAST
UniProt AC P35723
Protein Name Endoplasmic reticulum transmembrane protein 1
Gene Name YET1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 206
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi..
Protein Sequence MSLYFTTLFLLLTVEMVMLFIFVLPLPFRIRRGIFSTYNQLTAKQQIKTIIFITGCLVGLLFIDSWKRSQIRVSLYHNDNSGSIGSSAVTPIQALASRAYNQRNMYISGFILYFSICIPTVMSIVKRLVKYQGLINEQEKQKLNKPSSNSKKDSNEADSTKLQEELRKKQISLEGLQKQVKNLEKYFDEKNQPGNVAAAEASKKGN
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
87PhosphorylationNSGSIGSSAVTPIQA
CCCCCCCCCCCHHHH
22.8828889911
97PhosphorylationTPIQALASRAYNQRN
CHHHHHHHHHHHHCC
20.4928889911
130UbiquitinationSIVKRLVKYQGLINE
HHHHHHHHHHCCCCH
36.1323749301
130AcetylationSIVKRLVKYQGLINE
HHHHHHHHHHCCCCH
36.1324489116
147PhosphorylationKQKLNKPSSNSKKDS
HHHHCCCCCCCCCCC
43.7027214570
148PhosphorylationQKLNKPSSNSKKDSN
HHHCCCCCCCCCCCC
54.3627214570
150PhosphorylationLNKPSSNSKKDSNEA
HCCCCCCCCCCCCHH
42.9328889911
161AcetylationSNEADSTKLQEELRK
CCHHHHHHHHHHHHH
52.7224489116
172PhosphorylationELRKKQISLEGLQKQ
HHHHHCCCHHHHHHH
20.2023749301
178AcetylationISLEGLQKQVKNLEK
CCHHHHHHHHHHHHH
63.2024489116
185AcetylationKQVKNLEKYFDEKNQ
HHHHHHHHHHCCCCC
55.1524489116
185SuccinylationKQVKNLEKYFDEKNQ
HHHHHHHHHHCCCCC
55.1523954790
190UbiquitinationLEKYFDEKNQPGNVA
HHHHHCCCCCCCCHH
63.8323749301
190AcetylationLEKYFDEKNQPGNVA
HHHHHCCCCCCCCHH
63.8324489116
202PhosphorylationNVAAAEASKKGN---
CHHHHHHHHCCC---
26.8022369663

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 YET1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YET1_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 YET1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATC3_YEASTDRS2genetic
16269340
PER1_YEASTPER1genetic
16269340
RGP1_YEASTRGP1genetic
16269340
RIC1_YEASTRIC1genetic
16269340
LAC1_YEASTLAC1genetic
16269340
YET3_YEASTYET3physical
20378542
SEC63_YEASTSEC63physical
20378542
SC61A_YEASTSEC61physical
20378542
SEC66_YEASTSEC66physical
20378542
SEC63_YEASTSEC63genetic
20378542
SC61A_YEASTSEC61genetic
20378542
DED1_YEASTDED1physical
22940862
AF9_YEASTYAF9physical
22875988
YP216_YEASTYPL216Wphysical
22875988
CND2_YEASTBRN1genetic
27708008
TECR_YEASTTSC13genetic
27708008
SC61G_YEASTSSS1genetic
27708008
SEC20_YEASTSEC20genetic
27708008
STT3_YEASTSTT3genetic
27708008
GPI10_YEASTGPI10genetic
27708008
CBF3A_YEASTCBF2genetic
27708008
BOS1_YEASTBOS1genetic
27708008
SMC4_YEASTSMC4genetic
27708008
SEC63_YEASTSEC63genetic
27708008
ATC3_YEASTDRS2genetic
27708008
SEC66_YEASTSEC66genetic
27708008
SSH1_YEASTSSH1genetic
27708008
RPN4_YEASTRPN4genetic
27708008
CHO2_YEASTCHO2genetic
27708008
VPS53_YEASTVPS53genetic
27708008
YPT6_YEASTYPT6genetic
27708008
YNN4_YEASTYNL134Cgenetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YET1_YEAST

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Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery.";
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-190, AND MASSSPECTROMETRY.

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