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P61588

- RND3_MOUSE

UniProt

P61588 - RND3_MOUSE

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Protein

Rho-related GTP-binding protein RhoE

Gene
Rnd3, Arhe, Rhoe
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 378GTP By similarity
Nucleotide bindingi77 – 815GTP By similarity
Nucleotide bindingi135 – 1384GTP By similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. protein binding Source: IntAct

GO - Biological processi

  1. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Rho-related GTP-binding protein RhoE
Alternative name(s):
Rho family GTPase 3
Rnd3
Gene namesi
Name:Rnd3
Synonyms:Arhe, Rhoe
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1921444. Rnd3.

Subcellular locationi

Golgi apparatus membrane; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 241241Rho-related GTP-binding protein RhoEPRO_0000198879Add
BLAST
Propeptidei242 – 2443Removed in mature form By similarityPRO_0000281231

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei241 – 2411Cysteine methyl ester By similarity
Lipidationi241 – 2411S-farnesyl cysteine By similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PRIDEiP61588.

PTM databases

PhosphoSiteiP61588.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiP61588.
BgeeiP61588.
CleanExiMM_RND3.
GenevestigatoriP61588.

Interactioni

Subunit structurei

Interacts with UBXD5 By similarity. Binds ROCK1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ARHGAP5Q130172EBI-6930266,EBI-7237884From a different organism.
Rock1P703357EBI-6930266,EBI-989293
YWHABP319465EBI-6930266,EBI-359815From a different organism.
YWHAEP622582EBI-6930266,EBI-356498From a different organism.
YWHAGP619812EBI-6930266,EBI-359832From a different organism.
YWHAHQ049172EBI-6930266,EBI-306940From a different organism.
YWHAQP273482EBI-6930266,EBI-359854From a different organism.
YWHAZP631043EBI-6930266,EBI-347088From a different organism.

Protein-protein interaction databases

IntActiP61588. 9 interactions.

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 319
Helixi36 – 4510
Beta strandi56 – 7823
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 – 19917

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GWNX-ray2.10A/C16-200[»]
ProteinModelPortaliP61588.
SMRiP61588. Positions 22-200.

Miscellaneous databases

EvolutionaryTraceiP61588.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi52 – 609Effector region Reviewed prediction

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00700000104387.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP61588.
KOiK07859.
OMAiLACINKS.
OrthoDBiEOG71P2BH.
PhylomeDBiP61588.
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.

P61588-1 [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
AK011442 mRNA. Translation: BAB27622.1.
AK035195 mRNA. Translation: BAC28975.1.
BC009002 mRNA. Translation: AAH09002.1.
CCDSiCCDS16028.1.
RefSeqiNP_083086.1. NM_028810.2.
UniGeneiMm.46497.

Genome annotation databases

EnsembliENSMUST00000017288; ENSMUSP00000017288; ENSMUSG00000017144.
GeneIDi74194.
KEGGimmu:74194.
UCSCiuc008jqf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK011442 mRNA. Translation: BAB27622.1 .
AK035195 mRNA. Translation: BAC28975.1 .
BC009002 mRNA. Translation: AAH09002.1 .
CCDSi CCDS16028.1.
RefSeqi NP_083086.1. NM_028810.2.
UniGenei Mm.46497.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GWN X-ray 2.10 A/C 16-200 [» ]
ProteinModelPortali P61588.
SMRi P61588. Positions 22-200.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P61588. 9 interactions.

PTM databases

PhosphoSitei P61588.

Proteomic databases

PRIDEi P61588.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000017288 ; ENSMUSP00000017288 ; ENSMUSG00000017144 .
GeneIDi 74194.
KEGGi mmu:74194.
UCSCi uc008jqf.1. mouse.

Organism-specific databases

CTDi 390.
MGIi MGI:1921444. Rnd3.

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00700000104387.
HOGENOMi HOG000233974.
HOVERGENi HBG009351.
InParanoidi P61588.
KOi K07859.
OMAi LACINKS.
OrthoDBi EOG71P2BH.
PhylomeDBi P61588.
TreeFami TF330887.

Miscellaneous databases

EvolutionaryTracei P61588.
NextBioi 1627.
PROi P61588.
SOURCEi Search...

Gene expression databases

ArrayExpressi P61588.
Bgeei P61588.
CleanExi MM_RND3.
Genevestigatori P61588.

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

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  2. "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].
  3. "RhoE binds to ROCK I and inhibits downstream signaling."
    Riento K., Guasch R.M., Garg R., Jin B., Ridley A.J.
    Mol. Cell. Biol. 23:4219-4229(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ROCK1, SUBCELLULAR LOCATION.
  4. "Crystal structure of the core domain of RhoE/Rnd3: a constitutively activated small G protein."
    Garavini H., Riento K., Phelan J.P., McAlister M.S., Ridley A.J., Keep N.H.
    Biochemistry 41:6303-6310(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 14-200.

Entry informationi

Entry nameiRND3_MOUSE
AccessioniPrimary (citable) accession number: P61588
Secondary accession number(s): P52199, Q6ZWS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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