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Protein

Rho-related GTP-binding protein RhoN

Gene

RND2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be specifically involved in neuronal and hepatic functions. Is a C3 toxin-insensitive member of the Rho subfamily (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 218GTPBy similarity
Nucleotide bindingi61 – 655GTPBy similarity
Nucleotide bindingi119 – 1224GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: ProtInc
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • metabolic process Source: GOC
  • positive regulation of collateral sprouting Source: Ensembl
  • signal transduction Source: ProtInc
  • 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 RhoN
Alternative name(s):
Rho family GTPase 2
Rho-related GTP-binding protein Rho7
Rnd2
Gene namesi
Name:RND2
Synonyms:ARHN, RHO7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:18315. RND2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134936989.

Polymorphism and mutation databases

BioMutaiRND2.
DMDMi2507301.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 224224Rho-related GTP-binding protein RhoNPRO_0000198876Add
BLAST
Propeptidei225 – 2273Removed in mature formBy similarityPRO_0000281228

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei224 – 2241Cysteine methyl esterBy similarity
Lipidationi224 – 2241S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiP52198.
PRIDEiP52198.

PTM databases

PhosphoSiteiP52198.

Expressioni

Tissue specificityi

Highly expressed in testis.

Gene expression databases

BgeeiP52198.
CleanExiHS_RND2.
GenevisibleiP52198. HS.

Interactioni

Subunit structurei

Interacts with the Rho-GAP domain of RACGAP1. Interacts with UBXD5.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Fnbp1Q8R5112EBI-1111436,EBI-1111424From a different organism.

Protein-protein interaction databases

BioGridi113810. 9 interactions.
IntActiP52198. 1 interaction.
MINTiMINT-257912.
STRINGi9606.ENSP00000466680.

Structurei

3D structure databases

ProteinModelPortaliP52198.
SMRiP52198. Positions 7-184.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi36 – 449Effector regionSequence Analysis

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP52198.
KOiK07858.
OrthoDBiEOG71P2BH.
PhylomeDBiP52198.

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.

P52198-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGQSGRCKI VVVGDAECGK TALLQVFAKD AYPGSYVPTV FENYTASFEI
60 70 80 90 100
DKRRIELNMW DTSGSSYYDN VRPLAYPDSD AVLICFDISR PETLDSVLKK
110 120 130 140 150
WQGETQEFCP NAKVVLVGCK LDMRTDLATL RELSKQRLIP VTHEQGTVLA
160 170 180 190 200
KQVGAVSYVE CSSRSSERSV RDVFHVATVA SLGRGHRQLR RTDSRRGMQR
210 220
SAQLSGRPDR GNEGEIHKDR AKSCNLM
Length:227
Mass (Da):25,369
Last modified:November 1, 1997 - v2
Checksum:iDB2127B97B468F86
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95456 mRNA. Translation: CAA64726.1.
L78833 Genomic DNA. Translation: AAC37595.1.
AF498968 mRNA. Translation: AAM21115.1.
BT019394 mRNA. Translation: AAV38201.1.
AK290199 mRNA. Translation: BAF82888.1.
CH471152 Genomic DNA. Translation: EAW60920.1.
BC094842 mRNA. Translation: AAH94842.1.
BC104986 mRNA. Translation: AAI04987.1.
BC104990 mRNA. Translation: AAI04991.1.
CCDSiCCDS11452.1.
RefSeqiNP_005431.1. NM_005440.4.
UniGeneiHs.603111.

Genome annotation databases

EnsembliENST00000587250; ENSP00000466680; ENSG00000108830.
GeneIDi8153.
KEGGihsa:8153.
UCSCiuc002icn.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95456 mRNA. Translation: CAA64726.1.
L78833 Genomic DNA. Translation: AAC37595.1.
AF498968 mRNA. Translation: AAM21115.1.
BT019394 mRNA. Translation: AAV38201.1.
AK290199 mRNA. Translation: BAF82888.1.
CH471152 Genomic DNA. Translation: EAW60920.1.
BC094842 mRNA. Translation: AAH94842.1.
BC104986 mRNA. Translation: AAI04987.1.
BC104990 mRNA. Translation: AAI04991.1.
CCDSiCCDS11452.1.
RefSeqiNP_005431.1. NM_005440.4.
UniGeneiHs.603111.

3D structure databases

ProteinModelPortaliP52198.
SMRiP52198. Positions 7-184.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113810. 9 interactions.
IntActiP52198. 1 interaction.
MINTiMINT-257912.
STRINGi9606.ENSP00000466680.

PTM databases

PhosphoSiteiP52198.

Polymorphism and mutation databases

BioMutaiRND2.
DMDMi2507301.

Proteomic databases

PaxDbiP52198.
PRIDEiP52198.

Protocols and materials databases

DNASUi8153.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000587250; ENSP00000466680; ENSG00000108830.
GeneIDi8153.
KEGGihsa:8153.
UCSCiuc002icn.3. human.

Organism-specific databases

CTDi8153.
GeneCardsiGC17P041177.
HGNCiHGNC:18315. RND2.
MIMi601555. gene.
neXtProtiNX_P52198.
PharmGKBiPA134936989.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP52198.
KOiK07858.
OrthoDBiEOG71P2BH.
PhylomeDBiP52198.

Miscellaneous databases

ChiTaRSiRND2. human.
GeneWikiiRnd2.
GenomeRNAii8153.
NextBioi30826.
PROiP52198.
SOURCEiSearch...

Gene expression databases

BgeeiP52198.
CleanExiHS_RND2.
GenevisibleiP52198. HS.

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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Complete genomic sequence and analysis of 117 kb of human DNA containing the gene BRCA1."
    Smith T.M., Lee M.K., Szabo C.I., Jerome N., McEuen M., Taylor M., Hood L., King M.-C.
    Genome Res. 6:1029-1049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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].
  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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "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: Thalamus.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 and Ovary.
  8. "Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male germ cells."
    Naud N., Toure A., Liu J., Pineau C., Morin L., Dorseuil O., Escalier D., Chardin P., Gacon G.
    Biochem. J. 372:105-112(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RACGAP1, SUBCELLULAR LOCATION.
  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.

Entry informationi

Entry nameiRND2_HUMAN
AccessioniPrimary (citable) accession number: P52198
Secondary accession number(s): A8K2D4
, O00690, O00734, Q5U0P6, Q99535
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: June 24, 2015
This is version 133 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. 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.