P52198 (RND2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 vesicle › secretory vesicle › acrosome 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.

Ontologies

Keywords
Cellular component	Cytoplasmic vesicle Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	signal transduction Traceable author statement Ref.2. Source: ProtInc small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	acrosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell early endosome Inferred from electronic annotation. Source: Compara
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Fnbp1	Q8R511	2	EBI-1111436,EBI-1111424	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 224	224	Rho-related GTP-binding protein RhoN		PRO_0000198876
	Propeptide	225 – 227	3	Removed in mature form By similarity		PRO_0000281228
Regions
	Nucleotide binding	14 – 21	8	GTP By similarity
	Nucleotide binding	61 – 65	5	GTP By similarity
	Nucleotide binding	119 – 122	4	GTP By similarity
	Motif	36 – 44	9	Effector region Potential
Amino acid modifications
	Modified residue	224	1	Cysteine methyl ester By similarity
	Lipidation	224	1	S-geranylgeranyl cysteine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P52198 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: DB2127B97B468F86	FASTA	227	25,369
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00001436.
RefSeq	NP_005431.1. NM_005440.4.
UniGene	Hs.603111.
3D structure databases
ProteinModelPortal	P52198.
ModBase	Search...
Protein-protein interaction databases
IntAct	P52198. 1 interaction.
MINT	MINT-257912.
STRING	9606.ENSP00000225973.
PTM databases
PhosphoSite	P52198.
Polymorphism databases
DMDM	2507301.
Proteomic databases
PaxDb	P52198.
PRIDE	P52198.
Protocols and materials databases
DNASU	8153.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000587250; ENSP00000466680; ENSG00000108830.
GeneID	8153.
KEGG	hsa:8153.
UCSC	uc002icn.3. human.
Organism-specific databases
CTD	8153.
GeneCards	GC17P041177.
HGNC	HGNC:18315. RND2.
MIM	601555. gene.
neXtProt	NX_P52198.
PharmGKB	PA134936989.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1100.
HOGENOM	HOG000233974.
HOVERGEN	HBG009351.
InParanoid	P52198.
KO	K07858.
OrthoDB	EOG42RD88.
PhylomeDB	P52198.
Gene expression databases
ArrayExpress	P52198.
Bgee	P52198.
CleanEx	HS_RND2.
Genevestigator	P52198.
GermOnline	ENSG00000108830. Homo sapiens.
Family and domain databases
InterPro	IPR027417. P-loop_NTPase. IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003578. Small_GTPase_Rho. [Graphical view]
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00174. RHO. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 1 hit.
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS51420. RHO. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	8153.
NextBio	30826.
SOURCE	Search...

Entry information

Entry name

RND2_HUMAN

Accession

Primary (citable) accession number: P52198
Secondary accession number(s): A8K2D4 , O00690, O00734, Q5U0P6, Q99535

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 1, 1997
Last modified:	May 29, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.