Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-559292-01017
Entry Name
UniProt Accession
Theoretical PI
5.17
Molecular Weight
23214.25
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
GTP-binding protein YPT1
Protein Synonyms/Alias
Protein YP2; Rab GTPase YPT1; Transport GTPase YPT1;
Gene Name
YPT1
Gene Synonyms/Alias
YP2; YFL038C;
Created Date
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
205
Canonical
LTNTGGGCC******
[1]
S-Geranylgeranylation
206
Canonical
TNTGGGCC*******
[1]
S-Geranylgeranylation
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
NCBI Taxa ID
559292
Reference
[1] Yoo JS, Grabowski R, Xing L, Trepte HH, Schmitt HD, Gallwitz D. Functionalimplications of genetic interactions between genes encoding small GTPasesinvolved in vesicular transport in yeast. Mol Gen Genet. 1999 Feb;261(1):80-91.[PMID:10071213]
Functional Description
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. YPT1 regulates the trafficking of secretory vesicles from the endoplasmic reticulum (ER) to the Golgi. 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. Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum. Also involved in the recycling of membrane proteins.
Sequence Annotation
Nucleotide-binding: 15 22 GTP.
Nucleotide-binding: 63 67 GTP.
Nucleotide-binding: 121 124 GTP.
Region: 63 80 Interaction with GDI1.
Region: 189 195 Interaction with GDI1.
Motif: 37 45 Effector region.
Modified residue: 1 1 N-acetylmethionine.
Modified residue: 172 172 Phosphoserine.
Modified residue: 174 174 Phosphoserine.
Protein Length
206 AA.
Protein Sequence
(Canonical)
MNSEYDYLFK LLLIGNSGVG KSCLLLRFSD DTYTNDYIST IGVDFKIKTV ELDGKTVKLQ  60
IWDTAGQERF RTITSSYYRG SHGIIIVYDV TDQESFNGVK MWLQEIDRYA TSTVLKLLVG  120
NKCDLKDKRV VEYDVAKEFA DANKMPFLET SALDSTNVED AFLTMARQIK ESMSQQNLNE  180
TTQKKEDKGN VNLKGQSLTN TGGGCC                                       206
FASTA
(Canonical)
>LipidDB-559292-01017|P01123
MNSEYDYLFKLLLIGNSGVGKSCLLLRFSDDTYTNDYISTIGVDFKIKTVELDGKTVKLQ
IWDTAGQERFRTITSSYYRGSHGIIIVYDVTDQESFNGVKMWLQEIDRYATSTVLKLLVG
NKCDLKDKRVVEYDVAKEFADANKMPFLETSALDSTNVEDAFLTMARQIKESMSQQNLNE
TTQKKEDKGNVNLKGQSLTNTGGGCC
Gene Ontology
GO:0031410; C:cytoplasmic vesicle; IDA:SGD
GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD
GO:0000139; C:Golgi membrane; IDA:SGD
GO:0005795; C:Golgi stack; IDA:SGD
GO:0000407; C:pre-autophagosomal structure; IDA:SGD
GO:0005802; C:trans-Golgi network; IDA:SGD
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; IDA:SGD
GO:0000149; F:SNARE binding; IDA:SGD
GO:0090114; P:COPII-coated vesicle budding; IMP:SGD
GO:0032258; P:CVT pathway; IMP:SGD
GO:0034498; P:early endosome to Golgi transport; IMP:SGD
GO:0032456; P:endocytic recycling; IMP:SGD
GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:SGD
GO:0048194; P:Golgi vesicle budding; IGI:SGD
GO:0048211; P:Golgi vesicle docking; IMP:SGD
GO:0006184; P:GTP catabolic process; IDA:GOC
GO:0016236; P:macroautophagy; IMP:SGD
GO:1990261; P:pre-mRNA catabolic process; IMP:SGD
GO:0006461; P:protein complex assembly; IDA:SGD
GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; IMP:SGD
GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IMP:SGD
GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro
GO:0035494; P:SNARE complex disassembly; IMP:SGD
Interpro
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR005225; Small_GTP-bd_dom
InterPro; IPR001806; Small_GTPase
InterPro; IPR003579; Small_GTPase_Rab_type
Pfam
Pfam; PF00071; Ras;
SMART
SMART; SM00175; RAB;
PROSITE
PROSITE; PS51419; RAB;
PRINTS
PRINTS; PR00449; RASTRNSFRMNG;