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Protein

Rho-related GTP-binding protein Rho6

Gene

RND1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lacks intrinsic GTPase activity. Has a low affinity for GDP, and constitutively binds GTP. Controls rearrangements of the actin cytoskeleton. Induces the Rac-dependent neuritic process formation in part by disruption of the cortical actin filaments. Causes the formation of many neuritic processes from the cell body with disruption of the cortical actin filaments.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi20 – 27GTP8
Nucleotide bindingi38 – 45GTP8
Nucleotide bindingi67 – 71GTP5
Nucleotide bindingi125 – 128GTP4

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • receptor binding Source: UniProtKB

GO - Biological processi

  • actin filament organization Source: UniProtKB
  • negative regulation of cell adhesion Source: UniProtKB
  • neuron remodeling Source: UniProtKB
  • small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000172602-MONOMER.
ReactomeiR-HSA-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-HSA-416550. Sema4D mediated inhibition of cell attachment and migration.
R-HSA-416572. Sema4D induced cell migration and growth-cone collapse.
SignaLinkiQ92730.
SIGNORiQ92730.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho-related GTP-binding protein Rho6
Alternative name(s):
Rho family GTPase 1
Rnd1
Gene namesi
Name:RND1
Synonyms:RHO6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:18314. RND1.

Subcellular locationi

GO - Cellular componenti

  • adherens junction Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi27T → N: Impairs interaction with UBXD5. 1 Publication1
Mutagenesisi45T → A: Abolishes interaction with UBXD5. 1 Publication1

Organism-specific databases

DisGeNETi27289.
OpenTargetsiENSG00000172602.
PharmGKBiPA134972408.

Polymorphism and mutation databases

BioMutaiRND1.
DMDMi2500182.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001988741 – 229Rho-related GTP-binding protein Rho6Add BLAST229
PropeptideiPRO_0000281226230 – 232Removed in mature formBy similarity3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei229Cysteine methyl esterBy similarity1
Lipidationi229S-geranylgeranyl cysteineBy similarity1

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiQ92730.
PRIDEiQ92730.

PTM databases

iPTMnetiQ92730.
PhosphoSitePlusiQ92730.

Expressioni

Tissue specificityi

Mostly expressed in brain and liver.

Gene expression databases

BgeeiENSG00000172602.
CleanExiHS_RND1.
ExpressionAtlasiQ92730. baseline and differential.
GenevisibleiQ92730. HS.

Interactioni

Subunit structurei

Binds GRB7 and PLXNB1. Interacts with UBXD5. Interacts with PLXNA2.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GRB7Q144514EBI-448618,EBI-970191
PLXNB1O431572EBI-448618,EBI-1111488

GO - Molecular functioni

  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi118113. 13 interactors.
DIPiDIP-36741N.
IntActiQ92730. 5 interactors.
MINTiMINT-265539.
STRINGi9606.ENSP00000308461.

Structurei

Secondary structure

1232
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 12Combined sources3
Beta strandi14 – 19Combined sources6
Helixi26 – 35Combined sources10
Beta strandi46 – 55Combined sources10
Beta strandi60 – 68Combined sources9
Helixi72 – 74Combined sources3
Turni75 – 77Combined sources3
Helixi78 – 81Combined sources4
Beta strandi86 – 93Combined sources8
Helixi98 – 104Combined sources7
Helixi106 – 114Combined sources9
Beta strandi118 – 125Combined sources8
Helixi127 – 131Combined sources5
Helixi133 – 141Combined sources9
Helixi149 – 159Combined sources11
Beta strandi162 – 166Combined sources5
Turni169 – 171Combined sources3
Helixi173 – 188Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CLSX-ray2.31A/B5-200[»]
2REXX-ray2.30B/D5-200[»]
3Q3JX-ray1.97B5-200[»]
ProteinModelPortaliQ92730.
SMRiQ92730.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92730.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi42 – 50Effector regionSequence analysis9

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiQ92730.
KOiK07531.
OMAiHEQGSAM.
OrthoDBiEOG091G0M4M.
PhylomeDBiQ92730.
TreeFamiTF330887.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q92730-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKERRAPQPV VARCKLVLVG DVQCGKTAML QVLAKDCYPE TYVPTVFENY
60 70 80 90 100
TACLETEEQR VELSLWDTSG SPYYDNVRPL CYSDSDAVLL CFDISRPETV
110 120 130 140 150
DSALKKWRTE ILDYCPSTRV LLIGCKTDLR TDLSTLMELS HQKQAPISYE
160 170 180 190 200
QGCAIAKQLG AEIYLEGSAF TSEKSIHSIF RTASMLCLNK PSPLPQKSPV
210 220 230
RSLSKRLLHL PSRSELISST FKKEKAKSCS IM
Length:232
Mass (Da):26,056
Last modified:February 1, 1997 - v1
Checksum:i9FD56ACB878FBCCA
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02018844P → R.Corresponds to variant rs2270577dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07923 mRNA. Translation: CAA69228.1.
AB040147 mRNA. Translation: BAB17851.1.
AF498967 mRNA. Translation: AAM21114.1.
AK292762 mRNA. Translation: BAF85451.1.
CH471111 Genomic DNA. Translation: EAW58019.1.
BC026356 mRNA. Translation: AAH26356.1.
CCDSiCCDS8771.1.
RefSeqiNP_055285.1. NM_014470.3.
UniGeneiHs.124940.

Genome annotation databases

EnsembliENST00000309739; ENSP00000308461; ENSG00000172602.
GeneIDi27289.
KEGGihsa:27289.
UCSCiuc001rsn.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07923 mRNA. Translation: CAA69228.1.
AB040147 mRNA. Translation: BAB17851.1.
AF498967 mRNA. Translation: AAM21114.1.
AK292762 mRNA. Translation: BAF85451.1.
CH471111 Genomic DNA. Translation: EAW58019.1.
BC026356 mRNA. Translation: AAH26356.1.
CCDSiCCDS8771.1.
RefSeqiNP_055285.1. NM_014470.3.
UniGeneiHs.124940.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CLSX-ray2.31A/B5-200[»]
2REXX-ray2.30B/D5-200[»]
3Q3JX-ray1.97B5-200[»]
ProteinModelPortaliQ92730.
SMRiQ92730.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118113. 13 interactors.
DIPiDIP-36741N.
IntActiQ92730. 5 interactors.
MINTiMINT-265539.
STRINGi9606.ENSP00000308461.

PTM databases

iPTMnetiQ92730.
PhosphoSitePlusiQ92730.

Polymorphism and mutation databases

BioMutaiRND1.
DMDMi2500182.

Proteomic databases

PaxDbiQ92730.
PRIDEiQ92730.

Protocols and materials databases

DNASUi27289.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309739; ENSP00000308461; ENSG00000172602.
GeneIDi27289.
KEGGihsa:27289.
UCSCiuc001rsn.4. human.

Organism-specific databases

CTDi27289.
DisGeNETi27289.
GeneCardsiRND1.
HGNCiHGNC:18314. RND1.
MIMi609038. gene.
neXtProtiNX_Q92730.
OpenTargetsiENSG00000172602.
PharmGKBiPA134972408.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiQ92730.
KOiK07531.
OMAiHEQGSAM.
OrthoDBiEOG091G0M4M.
PhylomeDBiQ92730.
TreeFamiTF330887.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000172602-MONOMER.
ReactomeiR-HSA-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-HSA-416550. Sema4D mediated inhibition of cell attachment and migration.
R-HSA-416572. Sema4D induced cell migration and growth-cone collapse.
SignaLinkiQ92730.
SIGNORiQ92730.

Miscellaneous databases

EvolutionaryTraceiQ92730.
GeneWikiiRnd1.
GenomeRNAii27289.
PROiQ92730.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000172602.
CleanExiHS_RND1.
ExpressionAtlasiQ92730. baseline and differential.
GenevisibleiQ92730. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRND1_HUMAN
AccessioniPrimary (citable) accession number: Q92730
Secondary accession number(s): A8K9P7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: November 2, 2016
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.