Rho-related GTP-binding protein Rho6 precursor

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Reviewed, UniProtKB/Swiss-Prot Q92730 (RND1_HUMAN)

Last modified July 7, 2009. Version 94. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Rho-related GTP-binding protein Rho6
Alternative name(s):
    Rho family GTPase 1
    Rnd1

Gene names

Name:	RND1
Synonyms:	RHO6

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	232 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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. Ref.5
Subunit structure	Binds GRB7 and PLXNB1. Interacts with UBXD5. Ref.6 Ref.7 Ref.8
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm › cytoskeleton. Ref.7
Tissue specificity	Mostly expressed in brain and liver.
Sequence similarities	Belongs to the small GTPase superfamily. Rho family.

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Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Prenylation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	actin filament organization Ref.1 Ref.5 Inferred from direct assay. Source: UniProtKB negative regulation of cell adhesion Ref.1 Inferred from direct assay. Source: UniProtKB neuron remodeling Ref.5 Inferred from direct assay. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	adherens junction Ref.1 Inferred from direct assay. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Ref.1 Ref.5 Non-traceable author statement. Source: UniProtKB protein binding Ref.6 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB7	Q14451	2	EBI-448618,EBI-970191

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 229

229

Rho-related GTP-binding protein Rho6

PRO_0000198874

Propeptide

230 – 232

Removed in mature form By similarity

PRO_0000281226

Regions

Nucleotide binding

20 – 27

GTP By similarity

Nucleotide binding

67 – 71

GTP By similarity

Nucleotide binding

125 – 128

GTP By similarity

Motif

42 – 50

Effector region Potential

Amino acid modifications

Modified residue

229

Cysteine methyl ester By similarity

Lipidation

229

S-geranylgeranyl cysteine By similarity

Natural variations

Natural variant

P → R: dbSNP rs2270577.

VAR_020188

Experimental info

Mutagenesis

T → N: Impairs interaction with UBXD5. Ref.7

Mutagenesis

T → A: Abolishes interaction with UBXD5. Ref.7

Secondary structure

232

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q92730-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 9FD56ACB878FBCCA
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FASTA

232

26,056

        10         20         30         40         50         60 
MKERRAPQPV VARCKLVLVG DVQCGKTAML QVLAKDCYPE TYVPTVFENY TACLETEEQR 

        70         80         90        100        110        120 
VELSLWDTSG SPYYDNVRPL CYSDSDAVLL CFDISRPETV DSALKKWRTE ILDYCPSTRV 

       130        140        150        160        170        180 
LLIGCKTDLR TDLSTLMELS HQKQAPISYE QGCAIAKQLG AEIYLEGSAF TSEKSIHSIF 

       190        200        210        220        230 
RTASMLCLNK PSPLPQKSPV RSLSKRLLHL PSRSELISST FKKEKAKSCS IM

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion." Nobes C.D., Lauritzen I., Mattei M.-G., Paris S., Hall A., Chardin P. J. Cell Biol. 141:187-197(1998) [PubMed: 9531558] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Human Rnd1 in carcinogenesis." Tanaka S., Sugimachi K. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Puhl H.L. III, Ikeda S.R., Aronstam R.S. Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"Rnd1, a novel rho family GTPase, induces the formation of neuritic processes in PC12 cells." Aoki J., Katoh H., Mori K., Negishi M. Biochem. Biophys. Res. Commun. 278:604-608(2000) [PubMed: 11095956] [Abstract] Cited for: FUNCTION.
[6]	"Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family." Vayssiere B., Zalcman G., Mahe Y., Mirey G., Ligensa T., Weidner K.M., Chardin P., Camonis J. FEBS Lett. 467:91-96(2000) [PubMed: 10664463] [Abstract] Cited for: INTERACTION WITH GRB7.
[7]	"Socius is a novel Rnd GTPase-interacting protein involved in disassembly of actin stress fibers." Katoh H., Harada A., Mori K., Negishi M. Mol. Cell. Biol. 22:2952-2964(2002) [PubMed: 11940653] [Abstract] Cited for: INTERACTION WITH UBXD5, MUTAGENESIS OF THR-27 AND THR-45, SUBCELLULAR LOCATION.
[8]	"Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF-mediated Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells." Oinuma I., Katoh H., Harada A., Negishi M. J. Biol. Chem. 278:25671-25677(2003) [PubMed: 12730235] [Abstract] Cited for: INTERACTION WITH PLXNB1.

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Cross-references

Sequence databases

Y07923 mRNA. Translation: CAA69228.1.
AB040147 mRNA. Translation: BAB17851.1.
AF498967 mRNA. Translation: AAM21114.1.
BC026356 mRNA. Translation: AAH26356.1.

IPI

IPI00023211.

RefSeq

NP_055285.1.

UniGene

Hs.124940

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CLS	X-ray	2.31	A/B	5-200	[»]
2REX	X-ray	2.30	B/D	5-200	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q92730. 5 interactions.

Proteomic databases

PRIDE

Q92730.

Genome annotation databases

Ensembl

ENSG00000172602. Homo sapiens. [Contig view]

GeneID

27289.

KEGG

hsa:27289.

UCSC

uc001rsn.1. human.

Organism-specific databases

GeneCards

GC12M047537.

H-InvDB

HIX0010770.

HGNC

HGNC:18314. RND1.

MIM

609038. gene.

PharmGKB

PA134972408.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q92730.

HOVERGEN

Q92730.

OMA

Q92730. KSVHSIF.

Gene expression databases

ArrayExpress

Q92730.

Bgee

Q92730.

CleanEx

HS_RND1.

GermOnline

ENSG00000172602. Homo sapiens.

Family and domain databases

InterPro

IPR003578. GTPase_Rho.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR005225. Small_GTP_bd.
[Graphical view]

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00174. RHO. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51420. RHO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

50236.

SOURCE

Search...

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Entry information

Entry name

RND1_HUMAN

Accession

Primary (citable) accession number: Q92730

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	July 7, 2009
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents