Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00840
Entry Name
UniProt Accession
Theoretical PI
4.73
Molecular Weight
20504.36
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Ras-related protein Rap-2b
Protein Synonyms/Alias
Gene Name
RAP2B
Gene Synonyms/Alias
Created Date
10-MAY-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
176
Canonical
QPNGDEGCCSACVIL
[1]
S-Palmitoylation
177
Canonical
PNGDEGCCSACVIL*
[1]
S-Palmitoylation
180
Canonical
DEGCCSACVIL****
[2]
S-Geranylgeranylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Canobbio I, Trionfini P, Guidetti GF, Balduini C, Torti M. Targeting of thesmall GTPase Rap2b, but not Rap1b, to lipid rafts is promoted by palmitoylationat Cys176 and Cys177 and is required for efficient protein activation in humanplatelets. Cell Signal. 2008 Sep;20(9):1662-70. doi:10.1016/j.cellsig.2008.05.016. Epub 2008 Jun 7.[PMID:18582561]
[2] Farrell FX, Yamamoto K, Lapetina EG. Prenyl group identification of rap2proteins: a ras superfamily member other than ras that is farnesylated. BiochemJ. 1993 Jan 15;289 ( Pt 2):349-55.[PMID:8424780]
Functional Description
Small GTP-binding protein which cycles between a GDP- bound inactive and a GTP-bound active form. Involved in EGFR and CHRM3 signaling pathways through stimulation of PLCE1. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May regulate membrane vesiculation in red blood cells.
Sequence Annotation
Nucleotide-binding: 10 17 GTP.
Nucleotide-binding: 57 61 GTP.
Nucleotide-binding: 116 119 GTP.
Motif: 32 40 Effector region.
Modified residue: 180 180 Cysteine methyl ester.
Protein Length
183 AA.
Protein Sequence
(Canonical)
MREYKVVVLG SGGVGKSALT VQFVTGSFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG  60
TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI IRVKRYERVP MILVGNKVDL  120
EGEREVSYGE GKALAEEWSC PFMETSAKNK ASVDELFAEI VRQMNYAAQP NGDEGCCSAC  180
VIL                                                                183
MREYKVVVLG SGGVGKSALT VQFVTGSFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG  60
TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI IRVKRYERVP MILVGNKVDL  120
EGEREVSYGE GKALAEEWSC PFMETSAKNK ASVDELFAEI VRQMNYAAQP NGDEGCCSAC  180
VIL                                                                183
FASTA
(Canonical)
>LipidDB-9606-00840|P61225
MREYKVVVLGSGGVGKSALTVQFVTGSFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAG
TEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYERVPMILVGNKVDL
EGEREVSYGEGKALAEEWSCPFMETSAKNKASVDELFAEIVRQMNYAAQPNGDEGCCSAC
VIL
MREYKVVVLGSGGVGKSALTVQFVTGSFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAG
TEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYERVPMILVGNKVDL
EGEREVSYGEGKALAEEWSCPFMETSAKNKASVDELFAEIVRQMNYAAQPNGDEGCCSAC
VIL
Gene Ontology
GO:0005829; C:cytosol; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0016020; C:membrane; IMP:UniProtKB
GO:0045121; C:membrane raft; IMP:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0055038; C:recycling endosome membrane; ISS:UniProtKB
GO:0019003; F:GDP binding; IDA:UniProt
GO:0005525; F:GTP binding; IDA:UniProtKB
GO:0006184; P:GTP catabolic process; IEA:InterPro
GO:0030336; P:negative regulation of cell migration; IEA:Ensembl
GO:0030168; P:platelet activation; IDA:UniProtKB
GO:0070527; P:platelet aggregation; IDA:UniProtKB
GO:0031954; P:positive regulation of protein autophosphorylation; IEA:Ensembl
GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB
GO:0061097; P:regulation of protein tyrosine kinase activity; ISS:UniProtKB
GO:0007165; P:signal transduction; TAS:ProtInc
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;