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P52198 (RND2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 RhoN
Alternative name(s):
Rho family GTPase 2
Rho-related GTP-binding protein Rho7
Rnd2
Gene names
Name:RND2
Synonyms:ARHN, RHO7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Interacts with the Rho-GAP domain of RACGAP1. Interacts with UBXD5. Ref.8 Ref.9

Subcellular location

Cytoplasmic vesiclesecretory vesicleacrosome membrane; Lipid-anchor; Cytoplasmic side Potential. Note: Colocalizes with RACGAP1 in Golgi-derived proacrosomal vesicles and the acrosome. Ref.8

Tissue specificity

Highly expressed in testis.

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Fnbp1Q8R5112EBI-1111436,EBI-1111424From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 224224Rho-related GTP-binding protein RhoN
PRO_0000198876
Propeptide225 – 2273Removed in mature form By similarity
PRO_0000281228

Regions

Nucleotide binding14 – 218GTP By similarity
Nucleotide binding61 – 655GTP By similarity
Nucleotide binding119 – 1224GTP By similarity
Motif36 – 449Effector region Potential

Amino acid modifications

Modified residue2241Cysteine methyl ester By similarity
Lipidation2241S-geranylgeranyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
P52198 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: DB2127B97B468F86

FASTA22725,369
        10         20         30         40         50         60 
MEGQSGRCKI VVVGDAECGK TALLQVFAKD AYPGSYVPTV FENYTASFEI DKRRIELNMW 

        70         80         90        100        110        120 
DTSGSSYYDN VRPLAYPDSD AVLICFDISR PETLDSVLKK WQGETQEFCP NAKVVLVGCK 

       130        140        150        160        170        180 
LDMRTDLATL RELSKQRLIP VTHEQGTVLA KQVGAVSYVE CSSRSSERSV RDVFHVATVA 

       190        200        210        220 
SLGRGHRQLR RTDSRRGMQR SAQLSGRPDR GNEGEIHKDR AKSCNLM 

« 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]"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. 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: Thalamus.
[6]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].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11452.1.
RefSeqNP_005431.1. NM_005440.4.
UniGeneHs.603111.

3D structure databases

ProteinModelPortalP52198.
SMRP52198. Positions 7-184.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113810. 8 interactions.
IntActP52198. 1 interaction.
MINTMINT-257912.
STRING9606.ENSP00000225973.

PTM databases

PhosphoSiteP52198.

Polymorphism databases

DMDM2507301.

Proteomic databases

PaxDbP52198.
PRIDEP52198.

Protocols and materials databases

DNASU8153.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000587250; ENSP00000466680; ENSG00000108830.
GeneID8153.
KEGGhsa:8153.
UCSCuc002icn.3. human.

Organism-specific databases

CTD8153.
GeneCardsGC17P041177.
HGNCHGNC:18315. RND2.
MIM601555. gene.
neXtProtNX_P52198.
PharmGKBPA134936989.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233974.
HOVERGENHBG009351.
InParanoidP52198.
KOK07858.
OrthoDBEOG71P2BH.
PhylomeDBP52198.

Gene expression databases

ArrayExpressP52198.
BgeeP52198.
CleanExHS_RND2.
GenevestigatorP52198.

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

GeneWikiRnd2.
GenomeRNAi8153.
NextBio30826.
PROP52198.
SOURCESearch...

Entry information

Entry nameRND2_HUMAN
AccessionPrimary (citable) accession number: P52198
Secondary accession number(s): A8K2D4 expand/collapse secondary AC list , O00690, O00734, Q5U0P6, Q99535
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 126 of the entry and version 2 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

MIM cross-references

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

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM