Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00842
Entry Name
UniProt Accession
Theoretical PI
5.65
Molecular Weight
20824.79
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Ras-related protein Rap-1b
Protein Synonyms/Alias
GTP-binding protein smg p21B;
Gene Name
RAP1B
Gene Synonyms/Alias
OK/SW-cl.11;
Created Date
10-MAY-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
181
Canonical
KARKKSSCQLL****
[1]
S-Geranylgeranylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Kawata M, Farnsworth CC, Yoshida Y, Gelb MH, Glomset JA, Takai Y.Posttranslationally processed structure of the human platelet protein smg p21B:evidence for geranylgeranylation and carboxyl methylation of the C-terminalcysteine. Proc Natl Acad Sci U S A. 1990 Nov;87(22):8960-4.[PMID:2123345]
Functional Description
GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays a role in the establishment of basal endothelial barrier function.
Sequence Annotation
Nucleotide-binding: 10 18 GTP.
Nucleotide-binding: 57 61 GTP.
Nucleotide-binding: 116 119 GTP.
Nucleotide-binding: 147 149 GTP.
Region: 25 67 Interaction with KRIT1.
Motif: 32 40 Effector region.
Modified residue: 39 39 ADP-ribosylserine; by botulinum toxin.
Modified residue: 179 179 Phosphoserine; by PKA.
Modified residue: 181 181 Cysteine methyl ester.
Protein Length
184 AA.
Protein Sequence
(Canonical)
MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDAQQ CMLEILDTAG  60
TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI LRVKDTDDVP MILVGNKCDL  120
EDERVVGKEQ GQNLARQWNN CAFLESSAKS KINVNEIFYD LVRQINRKTP VPGKARKKSS  180
CQLL                                                               184
FASTA
(Canonical)
>LipidDB-9606-00842|P61224
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAG
TEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDL
EDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINRKTPVPGKARKKSS
CQLL
Gene Ontology
GO:0005911; C:cell-cell junction; IDA:UniProtKB
GO:0005829; C:cytosol; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005622; C:intracellular; IDA:LIFEdb
GO:0005811; C:lipid particle; IDA:UniProtKB
GO:0016020; C:membrane; TAS:UniProtKB
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0019003; F:GDP binding; IDA:UniProtKB
GO:0005525; F:GTP binding; IDA:UniProtKB
GO:0003924; F:GTPase activity; IDA:UniProtKB
GO:0032403; F:protein complex binding; IDA:MGI
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0008283; P:cell proliferation; IEA:Ensembl
GO:0071320; P:cellular response to cAMP; IDA:UniProtKB
GO:0006112; P:energy reserve metabolic process; TAS:Reactome
GO:0061028; P:establishment of endothelial barrier; IMP:UniProtKB
GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IEA:Ensembl
GO:2000301; P:negative regulation of synaptic vesicle exocytosis; IEA:Ensembl
GO:0030168; P:platelet activation; TAS:Reactome
GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl
GO:0032486; P:Rap protein signal transduction; IMP:UniProtKB
GO:1901888; P:regulation of cell junction assembly; IMP:UniProtKB
GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB
GO:0050796; P:regulation of insulin secretion; TAS:Reactome
GO:0044281; P:small molecule metabolic process; TAS:Reactome
Interpro
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR005225; Small_GTP-bd_dom
InterPro; IPR001806; Small_GTPase
InterPro; IPR020849; Small_GTPase_Ras
Pfam
Pfam; PF00071; Ras;
SMART
SMART; SM00173; RAS;
PROSITE
PROSITE; PS51421; RAS;
PRINTS
PRINTS; PR00449; RASTRNSFRMNG;