Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00730
Entry Name
UniProt Accession
Theoretical PI
8.39
Molecular Weight
28218.27
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Rho-related GTP-binding protein RhoU
Protein Synonyms/Alias
CDC42-like GTPase 1; GTP-binding protein-like 1; Rho GTPase-like protein ARHU; Ryu GTPase; Wnt-1 responsive Cdc42 homolog 1; WRCH-1;
Gene Name
RHOU
Gene Synonyms/Alias
ARHU; GN CDC42L1; GN G28K; GN WRCH1; SB128;
Created Date
18-MAR-2008
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
255
Canonical
KSWWKKYCCFV****
[1]
S-Palmitoylation
256
Canonical
SWWKKYCCFV*****
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Berzat AC, Buss JE, Chenette EJ, Weinbaum CA, Shutes A, Der CJ, Minden A, Cox AD. Transforming activity of the Rho family GTPase, Wrch-1, a Wnt-regulated Cdc42homolog, is dependent on a novel carboxyl-terminal palmitoylation motif. J BiolChem. 2005 Sep 23;280(38):33055-65. Epub 2005 Jul 26.[PMID:16046391]
Functional Description
Acts upstream of PAK1 to regulate the actin cytoskeleton, adhesion turnover and increase cell migration. Stimulates quiescent cells to reenter the cell cycle. Has no detectable GTPase activity but its high intrinsic guanine nucleotide exchange activity suggests it is constitutively GTP- bound. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape.
Sequence Annotation
Nucleotide-binding: 56 63 GTP.
Nucleotide-binding: 103 107 GTP.
Nucleotide-binding: 161 164 GTP.
Protein Length
258 AA.
Protein Sequence
(Canonical)
MPPQQGDPAF PDRCEAPPVP PRRERGGRGG RGPGEPGGRG RAGGAEGRGV KCVLVGDGAV  60
GKTSLVVSYT TNGYPTEYIP TAFDNFSAVV SVDGRPVRLQ LCDTAGQDEF DKLRPLCYTN  120
TDIFLLCFSV VSPSSFQNVS EKWVPEIRCH CPKAPIILVG TQSDLREDVK VLIELDKCKE  180
KPVPEEAAKL CAEEIKAASY IECSALTQKN LKEVFDAAIV AGIQYSDTQQ QPKKSKSRTP  240
DKMKNLSKSW WKKYCCFV                                                258
FASTA
(Canonical)
>LipidDB-9606-00730|Q7L0Q8
MPPQQGDPAFPDRCEAPPVPPRRERGGRGGRGPGEPGGRGRAGGAEGRGVKCVLVGDGAV
GKTSLVVSYTTNGYPTEYIPTAFDNFSAVVSVDGRPVRLQLCDTAGQDEFDKLRPLCYTN
TDIFLLCFSVVSPSSFQNVSEKWVPEIRCHCPKAPIILVGTQSDLREDVKVLIELDKCKE
KPVPEEAAKLCAEEIKAASYIECSALTQKNLKEVFDAAIVAGIQYSDTQQQPKKSKSRTP
DKMKNLSKSWWKKYCCFV
Gene Ontology
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0042995; C:cell projection; IEA:UniProtKB-KW
GO:0005829; C:cytosol; TAS:Reactome
GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; IEA:Ensembl
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl
GO:0007010; P:cytoskeleton organization; IMP:UniProtKB
GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl
GO:0016601; P:Rac protein signal transduction; IEA:Ensembl
GO:0008360; P:regulation of cell shape; IMP:UniProtKB
GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome
GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome
Interpro
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR005225; Small_GTP-bd_dom
InterPro; IPR001806; Small_GTPase
InterPro; IPR003578; Small_GTPase_Rho
Pfam
Pfam; PF00071; Ras;
SMART
SMART; SM00174; RHO;
PROSITE
PROSITE; PS51420; RHO;
PRINTS
PRINTS; PR00449; RASTRNSFRMNG;