Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  GTP-binding protein YPT1  

UniProtKB / Swiss-Prot ID :  YPT1_YEAST

Gene Name (Synonyms) : 
YPT1, YP2 YFL038C  

Species :  Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). 

Subcellular Localization :  Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Cytoplasm. Note=ER and Golgi when GTP-bound. Cytoplasmic when bound to GDI1. 

Protein Function :  Involved in the trafficking of secretory vesicles from the endoplasmic reticulum (ER) to the Golgi. Regulates correct targeting and tethering of vesicles to target membranes by catalyzing the selective recruitment of proteins required for tethering and fusion onto membranes. Vesicular transport depends on shuttling of YPT1 between membrane and cytosol by GDI1, probably by recycling it to its membrane of origin after a vesicle fusion event. Required for sorting and transport of proteins from the ER through the Golgi compartment. Also involved in the recycling of membrane proteins. 

Protein Sequence MNSEYDYLFKLLLIGNSGVGKSCLLLRFSDDTYTNDYISTIGVDFKIKTVELDGKTVKLQIWDTAGQERF...
Predicted Secondary Structure CCCCCCEEEEEEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCEEEEEEEEEECCEEEEEEEEECCCCHHH...
Protein Variant -
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
1N-acetylmethionine.----MNSEY
----CCCCC
12.89UniProtKB
Link-
17PhosphoserineLIGNSGVGK
EEECCCCCH
29.64SysPTM
Link
17Phosphoserine.LIGNSGVGK
EEECCCCCH
29.64UniProtKB
Link
172PhosphoserineQIKESMSQQ
HHHHCCCCC
20.80SysPTM
Link
172Phosphoserine.QIKESMSQQ
HHHHCCCCC
20.80UniProtKB
Link
174PhosphoserineKESMSQQNL
HHCCCCCCC
37.58SysPTM
Link
174Phosphoserine.KESMSQQNL
HHCCCCCCC
37.58UniProtKB
Link
205S-geranylgeranyl cysteine.TGGGCC
CCCCCC
2.55UniProtKB
Link
206S-geranylgeranyl cysteine.GGGCC
CCCCC
7.65UniProtKB
Link
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
- top -

Disease Reference
Drug Reference
- top -
Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-174, AND MASSSPECTROMETRY.
"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-17; SER-172 AND SER-174,AND MASS SPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures