Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9615-00436
Entry Name
UniProt Accession
Theoretical PI
5.93
Molecular Weight
22677.75
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Ras-related protein Rab-1A
Protein Synonyms/Alias
Gene Name
RAB1A
Gene Synonyms/Alias
RAB1;
Created Date
16-AUG-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
204
Canonical
VKQSGGGCC******
[1]
S-Geranylgeranylation
205
Canonical
KQSGGGCC*******
[1]
S-Geranylgeranylation
Organism
Canis familiaris (Dog) (Canis lupus familiaris)
NCBI Taxa ID
9615
Reference
[1] Khosravi-Far R, Lutz RJ, Cox AD, Conroy L, Bourne JR, Sinensky M, Balch WE,Buss JE, Der CJ. Isoprenoid modification of rab proteins terminating in CC or CXCmotifs. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6264-8.[PMID:1648736]
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 sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB1A regulates vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment and on to the cell surface, and plays a role in IL-8 and growth hormone secretion. Regulates the level of CASR present at the cell membrane. Plays a role in cell adhesion and cell migration, via its role in protein trafficking. Plays a role in autophagosome assembly and cellular defense reactions against pathogenic bacteria. Plays a role in microtubule-dependent protein transport by early endosomes and in anterograde melanosome transport.
Sequence Annotation
Nucleotide-binding: 18 26 GTP.
Nucleotide-binding: 36 43 GTP.
Nucleotide-binding: 66 70 GTP.
Nucleotide-binding: 124 127 GTP.
Nucleotide-binding: 154 156 GTP.
Motif: 40 48 Effector region.
Modified residue: 2 2 N-acetylserine.
Modified residue: 79 79 O-(2-cholinephosphoryl)serine.
Protein Length
205 AA.
Protein Sequence
(Canonical)
MSSMNPEYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI RTIELDGKTI  60
KLQIWDTAGQ ERFRTITSSY YRGAHGIIVV YDVTDQESFN NVKQWLQEID RYASENVNKL  120
LVGNKCDLTT KKVVDYTTAK EFADSLGIPF LETSAKNATN VEQSFMTMAA EIKKRMGPGA  180
TAGGAEKSNV KIQSTPVKQS GGGCC                                        205
FASTA
(Canonical)
>LipidDB-9615-00436|P62822
MSSMNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTI
KLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESFNNVKQWLQEIDRYASENVNKL
LVGNKCDLTTKKVVDYTTAKEFADSLGIPFLETSAKNATNVEQSFMTMAAEIKKRMGPGA
TAGGAEKSNVKIQSTPVKQSGGGCC
Gene Ontology
GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW
GO:0005768; C:endosome; IEA:UniProtKB-KW
GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; ISS:UniProtKB
GO:0000045; P:autophagic vacuole assembly; ISS:UniProtKB
GO:0006914; P:autophagy; ISS:UniProtKB
GO:0016477; P:cell migration; ISS:UniProtKB
GO:0042742; P:defense response to bacterium; ISS:UniProtKB
GO:0006897; P:endocytosis; ISS:UniProtKB
GO:0006888; P:ER to Golgi vesicle-mediated transport; ISS:UniProtKB
GO:0030252; P:growth hormone secretion; ISS:UniProtKB
GO:0006184; P:GTP catabolic process; ISS:UniProtKB
GO:0072606; P:interleukin-8 secretion; ISS:UniProtKB
GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro
GO:0047496; P:vesicle transport along microtubule; ISS:UniProtKB
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;