Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01187
Entry Name
UniProt Accession
Theoretical PI
4.87
Molecular Weight
20744.76
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Ras-related protein Rap-2c
Protein Synonyms/Alias
Gene Name
RAP2C
Gene Synonyms/Alias
Created Date
10-MAY-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
176
Canonical
LPEKQDQCCTTCVVQ
[1]
S-Palmitoylation
177
Canonical
PEKQDQCCTTCVVQ*
[1]
S-Palmitoylation
180
Canonical
QDQCCTTCVVQ****
[2]
S-Geranylgeranylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
[2] Chan LN, Hart C, Guo L, Nyberg T, Davies BS, Fong LG, Young SG, Agnew BJ,Tamanoi F. A novel approach to tag and identify geranylgeranylated proteins.Electrophoresis. 2009 Oct;30(20):3598-606. doi: 10.1002/elps.200900259. PubMedPMID: 19784953; PubMed Central PMCID: PMC2855049.[PMID:19784953]
Functional Description
Small GTP-binding protein which cycles between a GDP- bound inactive and a GTP-bound active form. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May play a role in SRE-mediated gene transcription.
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 VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG  60
TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI VRVKRYEKVP LILVGNKVDL  120
EPEREVMSSE GRALAQEWGC PFMETSAKSK SMVDELFAEI VRQMNYSSLP EKQDQCCTTC  180
VVQ                                                                183
MREYKVVVLG SGGVGKSALT VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG  60
TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI VRVKRYEKVP LILVGNKVDL  120
EPEREVMSSE GRALAQEWGC PFMETSAKSK SMVDELFAEI VRQMNYSSLP EKQDQCCTTC  180
VVQ                                                                183
FASTA
(Canonical)
>LipidDB-9606-01187|Q9Y3L5
MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAG
TEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIVRVKRYEKVPLILVGNKVDL
EPEREVMSSEGRALAQEWGCPFMETSAKSKSMVDELFAEIVRQMNYSSLPEKQDQCCTTC
VVQ
MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAG
TEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIVRVKRYEKVPLILVGNKVDL
EPEREVMSSEGRALAQEWGCPFMETSAKSKSMVDELFAEIVRQMNYSSLPEKQDQCCTTC
VVQ
Gene Ontology
GO:0005737; C:cytoplasm; IDA:UniProt
GO:0005829; C:cytosol; IEA:Ensembl
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005886; C:plasma membrane; IDA:UniProt
GO:0055038; C:recycling endosome membrane; ISS:UniProtKB
GO:0019003; F:GDP binding; IDA:UniProt
GO:0005525; F:GTP binding; IDA:UniProt
GO:0003713; F:transcription coactivator activity; IDA:UniProt
GO:0006184; P:GTP catabolic process; IEA:InterPro
GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB
GO:0031954; P:positive regulation of protein autophosphorylation; ISS:UniProtKB
GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB
GO:0061097; P:regulation of protein tyrosine kinase activity; ISS:UniProtKB
GO:2001141; P:regulation of RNA biosynthetic process; IDA:GOC
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;