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Q92730

- RND1_HUMAN

UniProt

Q92730 - RND1_HUMAN

Protein

Rho-related GTP-binding protein Rho6

Gene

RND1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    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. protein binding Source: IntAct
    4. receptor binding Source: UniProtKB

    GO - Biological processi

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

    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: 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

    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

    ArrayExpressiQ92730.
    BgeeiQ92730.
    CleanExiHS_RND1.
    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 – 196
    Helixi26 – 3510
    Beta strandi46 – 5510
    Beta strandi60 – 689
    Helixi72 – 743
    Turni75 – 773
    Helixi78 – 814
    Beta strandi86 – 938
    Helixi98 – 1047
    Helixi106 – 1149
    Beta strandi118 – 1258
    Helixi127 – 1315
    Helixi133 – 1419
    Helixi149 – 15911
    Beta strandi162 – 1665
    Turni169 – 1713
    Helixi173 – 18816

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CLSX-ray2.31A/B5-200[»]
    2REXX-ray2.30B/D5-200[»]
    3Q3JX-ray1.97B5-200[»]
    ProteinModelPortaliQ92730.
    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.
    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

    MKERRAPQPV VARCKLVLVG DVQCGKTAML QVLAKDCYPE TYVPTVFENY    50
    TACLETEEQR VELSLWDTSG SPYYDNVRPL CYSDSDAVLL CFDISRPETV 100
    DSALKKWRTE ILDYCPSTRV LLIGCKTDLR TDLSTLMELS HQKQAPISYE 150
    QGCAIAKQLG AEIYLEGSAF TSEKSIHSIF RTASMLCLNK PSPLPQKSPV 200
    RSLSKRLLHL PSRSELISST FKKEKAKSCS IM 232
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS8771.1.
    RefSeqi NP_055285.1. NM_014470.3.
    UniGenei Hs.124940.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    3Q3J X-ray 1.97 B 5-200 [» ]
    ProteinModelPortali Q92730.
    SMRi Q92730. Positions 10-188.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118113. 13 interactions.
    IntActi Q92730. 5 interactions.
    MINTi MINT-265539.
    STRINGi 9606.ENSP00000308461.

    PTM databases

    PhosphoSitei Q92730.

    Polymorphism databases

    DMDMi 2500182.

    Proteomic databases

    PaxDbi Q92730.
    PRIDEi Q92730.

    Protocols and materials databases

    DNASUi 27289.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309739 ; ENSP00000308461 ; ENSG00000172602 .
    GeneIDi 27289.
    KEGGi hsa:27289.
    UCSCi uc001rsn.3. human.

    Organism-specific databases

    CTDi 27289.
    GeneCardsi GC12M049250.
    HGNCi HGNC:18314. RND1.
    MIMi 609038. gene.
    neXtProti NX_Q92730.
    PharmGKBi PA134972408.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233974.
    HOVERGENi HBG009351.
    InParanoidi Q92730.
    KOi K07531.
    OMAi IFRMASM.
    PhylomeDBi Q92730.
    TreeFami TF330887.

    Enzyme and pathway databases

    Reactomei REACT_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.
    SignaLinki Q92730.

    Miscellaneous databases

    EvolutionaryTracei Q92730.
    GeneWikii Rnd1.
    GenomeRNAii 27289.
    NextBioi 50236.
    PROi Q92730.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92730.
    Bgeei Q92730.
    CleanExi HS_RND1.
    Genevestigatori Q92730.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003578. Small_GTPase_Rho.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00174. RHO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51420. RHO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    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: October 1, 2014
    This is version 143 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