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Q92730 (RND1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho-related GTP-binding protein Rho6
Alternative name(s):
Rho family GTPase 1
Rnd1
Gene names
Name:RND1
Synonyms:RHO6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.7

Subunit structure

Binds GRB7 and PLXNB1. Interacts with UBXD5. Interacts with PLXNA2. Ref.8 Ref.9 Ref.10

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmcytoskeleton Ref.9.

Tissue specificity

Mostly expressed in brain and liver.

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GRB7Q144514EBI-448618,EBI-970191
PLXNB1O431572EBI-448618,EBI-1111488

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 229229Rho-related GTP-binding protein Rho6
PRO_0000198874
Propeptide230 – 2323Removed in mature form By similarity
PRO_0000281226

Regions

Nucleotide binding20 – 278GTP
Nucleotide binding38 – 458GTP
Nucleotide binding67 – 715GTP
Nucleotide binding125 – 1284GTP
Motif42 – 509Effector region Potential

Amino acid modifications

Modified residue2291Cysteine methyl ester By similarity
Lipidation2291S-geranylgeranyl cysteine By similarity

Natural variations

Natural variant441P → R.
Corresponds to variant rs2270577 [ dbSNP | Ensembl ].
VAR_020188

Experimental info

Mutagenesis271T → N: Impairs interaction with UBXD5. Ref.9
Mutagenesis451T → A: Abolishes interaction with UBXD5. Ref.9

Secondary structure

................................. 232
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92730 [UniParc].

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

FASTA23226,056
        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 

« Hide

References

« Hide '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] [Europe PMC] [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]"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. expand/collapse author list , 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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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(2004) [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(2000) [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(2000) [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(2002) [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(2003) [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(2009) [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 (JAN-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 5-200 IN COMPLEX WITH PLXNA2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_055285.1. NM_014470.3.
UniGeneHs.124940.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CLSX-ray2.31A/B5-200[»]
2REXX-ray2.30B/D5-200[»]
3Q3JX-ray1.97B5-200[»]
ProteinModelPortalQ92730.
SMRQ92730. Positions 10-188.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118113. 13 interactions.
IntActQ92730. 5 interactions.
MINTMINT-265539.
STRING9606.ENSP00000308461.

PTM databases

PhosphoSiteQ92730.

Polymorphism databases

DMDM2500182.

Proteomic databases

PaxDbQ92730.
PRIDEQ92730.

Protocols and materials databases

DNASU27289.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309739; ENSP00000308461; ENSG00000172602.
GeneID27289.
KEGGhsa:27289.
UCSCuc001rsn.3. human.

Organism-specific databases

CTD27289.
GeneCardsGC12M049250.
HGNCHGNC:18314. RND1.
MIM609038. gene.
neXtProtNX_Q92730.
PharmGKBPA134972408.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233974.
HOVERGENHBG009351.
InParanoidQ92730.
KOK07531.
OMAVCLNKPS.
PhylomeDBQ92730.
TreeFamTF330887.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
SignaLinkQ92730.

Gene expression databases

ArrayExpressQ92730.
BgeeQ92730.
CleanExHS_RND1.
GenevestigatorQ92730.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ92730.
GeneWikiRnd1.
GenomeRNAi27289.
NextBio50236.
PROQ92730.
SOURCESearch...

Entry information

Entry nameRND1_HUMAN
AccessionPrimary (citable) accession number: Q92730
Secondary accession number(s): A8K9P7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

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