Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00370
Entry Name
UniProt Accession
Theoretical PI
5.55
Molecular Weight
22171.16
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Ras-related protein Rab-1B
Protein Synonyms/Alias
Gene Name
RAB1B
Gene Synonyms/Alias
Created Date
19-SEP-2002
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
200
Canonical
VKPAGGGCC******
[1][2]
S-Geranylgeranylation
201
Canonical
KPAGGGCC*******
[1][2]
S-Geranylgeranylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Overmeyer JH, Wilson AL, Maltese WA. Membrane targeting of a Rab GTPase thatfails to associate with Rab escort protein (REP) or guanine nucleotidedissociation inhibitor (GDI). J Biol Chem. 2001 Jun 8;276(23):20379-86. Epub 2001Mar 16.[PMID:11389151]
[2] Wilson AL, Sheridan KM, Erdman RA, Maltese WA. Prenylation of a Rab1B mutantwith altered GTPase activity is impaired in cell-free systems but not in intactmammalian cells. Biochem J. 1996 Sep 15;318 ( Pt 3):1007-14.[PMID:8836150]
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. RAB1B regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum.
Sequence Annotation
Nucleotide-binding: 15 22 GTP.
Nucleotide-binding: 63 67 GTP.
Nucleotide-binding: 121 124 GTP.
Region: 64 83 Switch 2 region; required for interactionwith REP1/CHM.
Motif: 37 45 Effector region.
Modified residue: 1 1 N-acetylmethionine.
Modified residue: 76 76 O-(2-cholinephosphoryl)serine; byLegionella AnkX.
Modified residue: 77 77 O-AMP-tyrosine; by Legionella DrrA.
Modified residue: 201 201 Cysteine methyl ester.
Protein Length
201 AA.
Protein Sequence
(Canonical)
MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DTYTESYIST IGVDFKIRTI ELDGKTIKLQ  60
IWDTAGQERF RTITSSYYRG AHGIIVVYDV TDQESYANVK QWLQEIDRYA SENVNKLLVG  120
NKSDLTTKKV VDNTTAKEFA DSLGIPFLET SAKNATNVEQ AFMTMAAEIK KRMGPGAASG  180
GERPNLKIDS TPVKPAGGGC C                                            201
FASTA
(Canonical)
>LipidDB-9606-00370|Q9H0U4
MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQ
IWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVG
NKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQAFMTMAAEIKKRMGPGAASG
GERPNLKIDSTPVKPAGGGCC
Gene Ontology
GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Ensembl
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005794; C:Golgi apparatus; IDA:LIFEdb
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0005739; C:mitochondrion; IEA:Ensembl
GO:0005525; F:GTP binding; IDA:UniProtKB
GO:0006888; P:ER to Golgi vesicle-mediated transport; IGI:UniProtKB
GO:1903020; P:positive regulation of glycoprotein metabolic process; IGI:UniProtKB
GO:0015031; P:protein transport; IEA:UniProtKB-KW
GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro
GO:0019068; P:virion assembly; IGI: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;