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P61587

- RND3_HUMAN

UniProt

P61587 - RND3_HUMAN

Protein

Rho-related GTP-binding protein RhoE

Gene

RND3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (24 May 2004)
      Previous versions | rss
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    Functioni

    Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi30 – 378GTPBy similarity
    Nucleotide bindingi77 – 815GTPBy similarity
    Nucleotide bindingi135 – 1384GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: ProtInc
    2. GTP binding Source: ProtInc
    3. protein binding Source: IntAct

    GO - Biological processi

    1. actin cytoskeleton organization Source: ProtInc
    2. cell adhesion Source: ProtInc
    3. GTP catabolic process Source: GOC
    4. small GTPase mediated signal transduction Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho-related GTP-binding protein RhoE
    Alternative name(s):
    Protein MemB
    Rho family GTPase 3
    Rho-related GTP-binding protein Rho8
    Rnd3
    Gene namesi
    Name:RND3
    Synonyms:ARHE, RHO8, RHOE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:671. RND3.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. Golgi membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24953.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 241241Rho-related GTP-binding protein RhoEPRO_0000198878Add
    BLAST
    Propeptidei242 – 2443Removed in mature formBy similarityPRO_0000281230

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei241 – 2411Cysteine methyl esterBy similarity
    Lipidationi241 – 2411S-farnesyl cysteine1 Publication

    Keywords - PTMi

    Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiP61587.
    PaxDbiP61587.
    PRIDEiP61587.

    PTM databases

    PhosphoSiteiP61587.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP61587.
    BgeeiP61587.
    CleanExiHS_RND3.
    GenevestigatoriP61587.

    Interactioni

    Subunit structurei

    Binds ROCK1 By similarity. Interacts with UBXD5.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    YWHABP319462EBI-1111534,EBI-359815
    YWHAZP6310411EBI-1111534,EBI-347088

    Protein-protein interaction databases

    BioGridi106883. 11 interactions.
    IntActiP61587. 5 interactions.
    MINTiMINT-3974781.
    STRINGi9606.ENSP00000263895.

    Structurei

    Secondary structure

    1
    244
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 319
    Helixi36 – 4510
    Beta strandi56 – 6510
    Beta strandi70 – 789
    Helixi82 – 843
    Turni85 – 873
    Helixi88 – 914
    Beta strandi96 – 1038
    Helixi107 – 1159
    Helixi117 – 1248
    Beta strandi129 – 1357
    Helixi137 – 1415
    Helixi143 – 1508
    Turni151 – 1533
    Helixi159 – 16911
    Beta strandi172 – 1765
    Turni179 – 1813
    Helixi183 – 19816

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M7BX-ray2.00A19-200[»]
    2V55X-ray3.70B/D1-200[»]
    4BG6X-ray2.30Q/R232-241[»]
    ProteinModelPortaliP61587.
    SMRiP61587. Positions 22-200.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP61587.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi52 – 609Effector regionSequence Analysis

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rho family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233974.
    HOVERGENiHBG009351.
    InParanoidiP61587.
    KOiK07859.
    OMAiLACINKS.
    OrthoDBiEOG71P2BH.
    PhylomeDBiP61587.
    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.

    P61587-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKERRASQKL SSKSIMDPNQ NVKCKIVVVG DSQCGKTALL HVFAKDCFPE    50
    NYVPTVFENY TASFEIDTQR IELSLWDTSG SPYYDNVRPL SYPDSDAVLI 100
    CFDISRPETL DSVLKKWKGE IQEFCPNTKM LLVGCKSDLR TDVSTLVELS 150
    NHRQTPVSYD QGANMAKQIG AATYIECSAL QSENSVRDIF HVATLACVNK 200
    TNKNVKRNKS QRATKRISHM PSRPELSAVA TDLRKDKAKS CTVM 244
    Length:244
    Mass (Da):27,368
    Last modified:May 24, 2004 - v1
    Checksum:iDD2D4021CD42BACC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95282 mRNA. Translation: CAA64603.1.
    X97758 mRNA. Translation: CAA66352.1.
    AF498969 mRNA. Translation: AAM21116.1.
    BT006769 mRNA. Translation: AAP35415.1.
    CH471058 Genomic DNA. Translation: EAX11524.1.
    CH471058 Genomic DNA. Translation: EAX11526.1.
    BC012513 mRNA. Translation: AAH12513.1.
    S82240 mRNA. Translation: AAB47133.1.
    CCDSiCCDS2190.1.
    RefSeqiNP_001241667.1. NM_001254738.1.
    NP_005159.1. NM_005168.4.
    UniGeneiHs.6838.
    Hs.713765.

    Genome annotation databases

    EnsembliENST00000263895; ENSP00000263895; ENSG00000115963.
    ENST00000375734; ENSP00000364886; ENSG00000115963.
    GeneIDi390.
    KEGGihsa:390.
    UCSCiuc002txe.3. human.

    Polymorphism databases

    DMDMi47606459.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95282 mRNA. Translation: CAA64603.1 .
    X97758 mRNA. Translation: CAA66352.1 .
    AF498969 mRNA. Translation: AAM21116.1 .
    BT006769 mRNA. Translation: AAP35415.1 .
    CH471058 Genomic DNA. Translation: EAX11524.1 .
    CH471058 Genomic DNA. Translation: EAX11526.1 .
    BC012513 mRNA. Translation: AAH12513.1 .
    S82240 mRNA. Translation: AAB47133.1 .
    CCDSi CCDS2190.1.
    RefSeqi NP_001241667.1. NM_001254738.1.
    NP_005159.1. NM_005168.4.
    UniGenei Hs.6838.
    Hs.713765.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M7B X-ray 2.00 A 19-200 [» ]
    2V55 X-ray 3.70 B/D 1-200 [» ]
    4BG6 X-ray 2.30 Q/R 232-241 [» ]
    ProteinModelPortali P61587.
    SMRi P61587. Positions 22-200.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106883. 11 interactions.
    IntActi P61587. 5 interactions.
    MINTi MINT-3974781.
    STRINGi 9606.ENSP00000263895.

    PTM databases

    PhosphoSitei P61587.

    Polymorphism databases

    DMDMi 47606459.

    Proteomic databases

    MaxQBi P61587.
    PaxDbi P61587.
    PRIDEi P61587.

    Protocols and materials databases

    DNASUi 390.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263895 ; ENSP00000263895 ; ENSG00000115963 .
    ENST00000375734 ; ENSP00000364886 ; ENSG00000115963 .
    GeneIDi 390.
    KEGGi hsa:390.
    UCSCi uc002txe.3. human.

    Organism-specific databases

    CTDi 390.
    GeneCardsi GC02M151324.
    HGNCi HGNC:671. RND3.
    MIMi 602924. gene.
    neXtProti NX_P61587.
    PharmGKBi PA24953.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233974.
    HOVERGENi HBG009351.
    InParanoidi P61587.
    KOi K07859.
    OMAi LACINKS.
    OrthoDBi EOG71P2BH.
    PhylomeDBi P61587.
    TreeFami TF330887.

    Miscellaneous databases

    EvolutionaryTracei P61587.
    GeneWikii Rnd3.
    GenomeRNAii 390.
    NextBioi 1627.
    PROi P61587.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61587.
    Bgeei P61587.
    CleanExi HS_RND3.
    Genevestigatori P61587.

    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: Spleen.
    2. "memB, a progression marker of human melanoma cell lines, encodes a member of a rho-related family."
      van Groningen J.J.M., Van Rijk A.A.F., Bloemers H.P.J., Swart G.W.M.
      Submitted (SEP-2004) 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: Placenta.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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: Kidney.
    7. "Identification of a novel human Rho protein with unusual properties: GTPase deficiency and in vivo farnesylation."
      Foster R., Hu K.-Q., Lu Y., Nolan K.M., Thissen J., Settleman J.
      Mol. Cell. Biol. 16:2689-2699(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-244, CHARACTERIZATION, ISOPRENYLATION AT CYS-241.
      Tissue: Fetal brain.
    8. "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.
    9. "Crystal structure of Rnd3/RhoE: functional implications."
      Fiegen D., Blumenstein L., Stege P., Vetter I.R., Ahmadian M.R.
      FEBS Lett. 525:100-104(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-200 IN COMPLEX WITH GTP.

    Entry informationi

    Entry nameiRND3_HUMAN
    AccessioniPrimary (citable) accession number: P61587
    Secondary accession number(s): D3DP95, P52199
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: May 24, 2004
    Last modified: October 1, 2014
    This is version 113 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 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3