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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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 278GTP
Nucleotide bindingi38 – 458GTP
Nucleotide bindingi67 – 715GTP
Nucleotide bindingi125 – 1284GTP

GO - Molecular functioni

  1. GTPase activity Source: UniProtKB
  2. GTP binding Source: UniProtKB-KW
  3. receptor binding Source: UniProtKB

GO - Biological processi

  1. actin filament organization Source: UniProtKB
  2. axon guidance Source: Reactome
  3. metabolic process Source: GOC
  4. negative regulation of cell adhesion Source: UniProtKB
  5. neuron remodeling Source: UniProtKB
  6. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_19266. Sema4D mediated inhibition of cell attachment and migration.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_19279. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
SignaLinkiQ92730.

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
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:18314. RND1.

Subcellular locationi

Cell membrane 1 Publication; Lipid-anchor 1 Publication; Cytoplasmic side 1 Publication. Cytoplasmcytoskeleton 1 Publication

GO - Cellular componenti

  1. adherens junction Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-SubCell
  3. cytosol Source: Reactome
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271T → N: Impairs interaction with UBXD5. 1 Publication
Mutagenesisi45 – 451T → A: Abolishes interaction with UBXD5. 1 Publication

Organism-specific databases

PharmGKBiPA134972408.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 229229Rho-related GTP-binding protein Rho6PRO_0000198874Add
BLAST
Propeptidei230 – 2323Removed in mature formBy similarityPRO_0000281226

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei229 – 2291Cysteine methyl esterBy similarity
Lipidationi229 – 2291S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiQ92730.
PRIDEiQ92730.

PTM databases

PhosphoSiteiQ92730.

Expressioni

Tissue specificityi

Mostly expressed in brain and liver.

Gene expression databases

BgeeiQ92730.
CleanExiHS_RND1.
ExpressionAtlasiQ92730. baseline and differential.
GenevestigatoriQ92730.

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

Protein-protein interaction databases

BioGridi118113. 13 interactions.
IntActiQ92730. 5 interactions.
MINTiMINT-265539.
STRINGi9606.ENSP00000308461.

Structurei

Secondary structure

1
232
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 196Combined sources
Helixi26 – 3510Combined sources
Beta strandi46 – 5510Combined sources
Beta strandi60 – 689Combined sources
Helixi72 – 743Combined sources
Turni75 – 773Combined sources
Helixi78 – 814Combined sources
Beta strandi86 – 938Combined sources
Helixi98 – 1047Combined sources
Helixi106 – 1149Combined sources
Beta strandi118 – 1258Combined sources
Helixi127 – 1315Combined sources
Helixi133 – 1419Combined sources
Helixi149 – 15911Combined sources
Beta strandi162 – 1665Combined sources
Turni169 – 1713Combined sources
Helixi173 – 18816Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CLSX-ray2.31A/B5-200[»]
2REXX-ray2.30B/D5-200[»]
3Q3JX-ray1.97B5-200[»]
SMRiQ92730. Positions 10-188.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92730.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi42 – 509Effector regionSequence Analysis

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiQ92730.
KOiK07531.
OMAiIFRMASM.
PhylomeDBiQ92730.
TreeFamiTF330887.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441P → R.
Corresponds to variant rs2270577 [ dbSNP | Ensembl ].
VAR_020188

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.3. human.

Polymorphism databases

DMDMi2500182.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2CLSX-ray2.31A/B5-200[»]
2REXX-ray2.30B/D5-200[»]
3Q3JX-ray1.97B5-200[»]
SMRiQ92730. Positions 10-188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118113. 13 interactions.
IntActiQ92730. 5 interactions.
MINTiMINT-265539.
STRINGi9606.ENSP00000308461.

PTM databases

PhosphoSiteiQ92730.

Polymorphism databases

DMDMi2500182.

Proteomic databases

PaxDbiQ92730.
PRIDEiQ92730.

Protocols and materials databases

DNASUi27289.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309739; ENSP00000308461; ENSG00000172602.
GeneIDi27289.
KEGGihsa:27289.
UCSCiuc001rsn.3. human.

Organism-specific databases

CTDi27289.
GeneCardsiGC12M049250.
HGNCiHGNC:18314. RND1.
MIMi609038. gene.
neXtProtiNX_Q92730.
PharmGKBiPA134972408.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiQ92730.
KOiK07531.
OMAiIFRMASM.
PhylomeDBiQ92730.
TreeFamiTF330887.

Enzyme and pathway databases

ReactomeiREACT_19266. Sema4D mediated inhibition of cell attachment and migration.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_19279. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
SignaLinkiQ92730.

Miscellaneous databases

EvolutionaryTraceiQ92730.
GeneWikiiRnd1.
GenomeRNAii27289.
NextBioi50236.
PROiQ92730.
SOURCEiSearch...

Gene expression databases

BgeeiQ92730.
CleanExiHS_RND1.
ExpressionAtlasiQ92730. baseline and differential.
GenevestigatoriQ92730.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Human Rnd1 in carcinogenesis."
    Tanaka S., Sugimachi K.
    Submitted (FEB-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 (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  7. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRB7.
  9. "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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBXD5, MUTAGENESIS OF THR-27 AND THR-45, SUBCELLULAR LOCATION.
  10. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLXNB1.
  11. "Structure and function of the intracellular region of the plexin-B1 transmembrane receptor."
    Tong Y., Hota P.K., Penachioni J.Y., Hamaneh M.B., Kim S., Alviani R.S., Shen L., He H., Tempel W., Tamagnone L., Park H.W., Buck M.
    J. Biol. Chem. 284:35962-35972(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 5-200 IN COMPLEX WITH GDP AND PLXNB1.
  12. "Crystal structure of plexin A2 RBD in complex with RND1."
    Structural genomics consortium (SGC)
    Submitted (DEC-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 5-200 IN COMPLEX WITH PLXNA2.

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: April 1, 2015
This is version 148 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

External Data

Dasty 3

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 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.