Q7L0Q8 (RHOU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho-related GTP-binding protein RhoU

Alternative name(s):
CDC42-like GTPase 1
GTP-binding protein-like 1
Rho GTPase-like protein ARHU
Ryu GTPase
Wnt-1 responsive Cdc42 homolog 1
Short name=WRCH-1

Gene names

Name:	RHOU
Synonyms:	ARHU, CDC42L1, G28K, WRCH1
ORF Names:	SB128

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts upstream of PAK1 to regulate the actin cytoskeleton, adhesion turnover and increase cell migration. Stimulates quiescent cells to reenter the cell cycle. Has no detectable GTPase activity but its high intrinsic guanine nucleotide exchange activity suggests it is constitutively GTP-bound. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. Ref.1 Ref.14 Ref.15 Ref.16 Ref.17
Cofactor	Magnesium. Ref.14
Subunit structure	Interacts with PAK3. Interacts with ARHGAP30 in a GTP-independent manner. In its GTP-loaded conformation, interacts with ARHGAP31. Interacts with PTK2B/PYK2. Ref.15 Ref.16 Ref.18
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane; Lipid-anchor. Cell junction › focal adhesion. Cell projection › podosome. Note: Localizes to podosomes in SRC-transformed cells. Ref.13 Ref.14 Ref.15 Ref.16
Tissue specificity	Ubiquitously expressed in all tissues examined. Expressed at high levels in the stomach, small intestine, brain, skeletal muscle and placenta. Ref.1 Ref.3
Post-translational modification	Tyrosine phosphorylated by SRC in response to PTK2B/PYK2 activation. Ref.16
Sequence similarities	Belongs to the small GTPase superfamily. Rho family. Ref.14

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cell projection Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of cell shape Inferred from mutant phenotype Ref.17. Source: UniProtKB regulation of small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell projection Inferred from electronic annotation. Source: UniProtKB-KW cytosol Traceable author statement. Source: Reactome focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell podosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.16. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK2	O43639	4	EBI-1638043,EBI-713635
PTK2B	Q14289	4	EBI-1638043,EBI-298640

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.7 Ref.8 Ref.12 (identifier: Q7L0Q8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 Ref.9 (identifier: Q7L0Q8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.
     62-66: KTSLV → MTNIG

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 258

258

Rho-related GTP-binding protein RhoU

PRO_0000326435

Regions

Nucleotide binding

56 – 63

8

GTP Ref.1

Nucleotide binding

103 – 107

5

GTP By similarity Ref.1

Nucleotide binding

161 – 164

4

GTP UniProtKB P61586

Compositional bias

26 – 61

36

Gly-rich

Amino acid modifications

Lipidation

256

1

S-palmitoyl cysteine Ref.13 Ref.14

Natural variations

Alternative sequence

1 – 61

61

Missing in isoform 2. Ref.9

VSP_052732

Alternative sequence

62 – 66

5

KTSLV → MTNIG in isoform 2. Ref.9

VSP_052733

Natural variant

121

1

T → A.
Corresponds to variant rs3820264 [ dbSNP | Ensembl ].

VAR_051975

Experimental info

Mutagenesis

63

1

T → N: Loss of GTP-binding and localization to focal adhesions. No effect on ARHGAP30-binding. Ref.1 Ref.15 Ref.18

Mutagenesis

80

1

P → G: No effect on ARHGAP30-binding. Ref.18

Mutagenesis

81

1

T → S: Loss of binding to PAK3; when associated with A-83 and C-86. Ref.15

Mutagenesis

83

1

F → A: Loss of binding to PAK3; when associated with S-81 and C-86. Ref.15 Ref.18

Mutagenesis

83

1

F → G: Loss of ARHGAP30-binding. Ref.15 Ref.18

Mutagenesis

86

1

F → C: Loss of PAK3-binding; when associated with S-81 and A-83. No effect on ARHGAP30-binding. Ref.15 Ref.18

Mutagenesis

107

1

Q → L: Constitutively active. Results in increased rates of stress fiber dissolution and cell migration. No effect on ARHGAP30-binding. Ref.1 Ref.15 Ref.18

Mutagenesis

255

1

C → S: No effect on subcellular location. Ref.13

Mutagenesis

256

1

C → S: Loss of subcellular location to plasma and intracellular membranes. Ref.13

Sequence conflict

1 – 13

13

MPPQQ…AFPDR → QLLPTATLRGGGAVGPGPAS PRPQA in BAD92748. Ref.7

Sequence conflict

71

1

T → P in AAL99390. Ref.2

Secondary structure

1

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258

Helix Strand Turn

Details...

Beta strand

50 – 55

6

Helix

62 – 70

9

Beta strand

82 – 92

11

Beta strand

95 – 103

9

Beta strand

111 – 113

3

Helix

114 – 118

5

Beta strand

122 – 129

8

Helix

133 – 141

9

Helix

143 – 150

8

Beta strand

152 – 154

3

Beta strand

156 – 161

6

Helix

163 – 167

5

Helix

169 – 176

8

Turn

177 – 179

3

Helix

185 – 195

11

Beta strand

198 – 202

5

Turn

205 – 207

3

Helix

211 – 226

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: D90059DE82288B97	FASTA	258	28,218
	10 20 30 40 50 60 MPPQQGDPAF PDRCEAPPVP PRRERGGRGG RGPGEPGGRG RAGGAEGRGV KCVLVGDGAV 70 80 90 100 110 120 GKTSLVVSYT TNGYPTEYIP TAFDNFSAVV SVDGRPVRLQ LCDTAGQDEF DKLRPLCYTN 130 140 150 160 170 180 TDIFLLCFSV VSPSSFQNVS EKWVPEIRCH CPKAPIILVG TQSDLREDVK VLIELDKCKE 190 200 210 220 230 240 KPVPEEAAKL CAEEIKAASY IECSALTQKN LKEVFDAAIV AGIQYSDTQQ QPKKSKSRTP 250 DKMKNLSKSW WKKYCCFV
	Isoform 2 [UniParc]. Checksum: CAE1A9715F8B7D0B	FASTA	197	22,164
	10 20 30 40 50 60 MTNIGVSYTT NGYPTEYIPT AFDNFSAVVS VDGRPVRLQL CDTAGQDEFD KLRPLCYTNT 70 80 90 100 110 120 DIFLLCFSVV SPSSFQNVSE KWVPEIRCHC PKAPIILVGT QSDLREDVKV LIELDKCKEK 130 140 150 160 170 180 PVPEEAAKLC AEEIKAASYI ECSALTQKNL KEVFDAAIVA GIQYSDTQQQ PKKSKSRTPD 190 KMKNLSKSWW KKYCCFV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Wrch-1, a novel member of the Rho gene family that is regulated by Wnt-1." Tao W., Pennica D., Xu L., Kalejta R.F., Levine A.J. Genes Dev. 15:1796-1807(2001) [PubMed: 11459829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF THR-63 AND GLN-107.
[2]	"Expression of WRCH1 in human cancer and down-regulation of WRCH1 by beta-estradiol in MCF-7 cells." Kirikoshi H., Katoh M. Int. J. Oncol. 20:777-783(2002) [PubMed: 11894124] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Novel human, mouse and xenopus genes encoding a member of the RAS superfamily of low-molecular-weight GTP-binding proteins and its downregulation in W/WV mouse jejunum." Daigo Y., Takayama I., Ponder B.A.J., Caldas C., Ward S.M., Sanders K.M., Fujino M.A. J. Gastroenterol. Hepatol. 19:211-217(2004) [PubMed: 14731133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[4]	"Scan of human genome reveals no new loci under ancient balancing selection." Bubb K.L., Bovee D., Buckley D., Haugen E., Kibukawa M., Paddock M., Palmieri A., Subramanian S., Zhou Y., Kaul R., Green P., Olson M.V. Genetics 173:2165-2177(2006) [PubMed: 16751668] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"A novel GTPase homologous to CDC42." Zhang J.S., Smith D.I., Urrutia R. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]	"Ryu: a new member of Rho family." Ikeda W., Nakanishi H., Takai Y. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]	Zhang W., Wan T., Li N., He L., Chen T., Cao X. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[8]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Hippocampus.
[9]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[10]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	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].
[12]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[13]	"Transforming activity of the Rho family GTPase, Wrch-1, a Wnt-regulated Cdc42 homolog, is dependent on a novel carboxyl-terminal palmitoylation motif." Berzat A.C., Buss J.E., Chenette E.J., Weinbaum C.A., Shutes A., Der C.J., Minden A., Cox A.D. J. Biol. Chem. 280:33055-33065(2005) [PubMed: 16046391] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-255 AND CYS-256, PALMITOYLATION AT CYS-256.
[14]	"Biochemical analyses of the Wrch atypical Rho family GTPases." Shutes A., Berzat A.C., Chenette E.J., Cox A.D., Der C.J. Methods Enzymol. 406:11-26(2006) [PubMed: 16472646] [Abstract] Cited for: FUNCTION, COFACTOR, SUBCELLULAR LOCATION, GTP-BINDING, PALMITOYLATION.
[15]	"Identification of a bipartite focal adhesion localization signal in RhoU/Wrch-1, a Rho family GTPase that regulates cell adhesion and migration." Ory S., Brazier H., Blangy A. Biol. Cell 99:701-716(2007) [PubMed: 17620058] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PAK3, MUTAGENESIS OF THR-63; THR-81; PHE-83; PHE-86 AND GLN-107.
[16]	"The atypical Rho GTPase Wrch1 collaborates with the nonreceptor tyrosine kinases Pyk2 and Src in regulating cytoskeletal dynamics." Ruusala A., Aspenstrom P. Mol. Cell. Biol. 28:1802-1814(2008) [PubMed: 18086875] [Abstract] Cited for: INTERACTION WITH PTK2B/PYK2, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[17]	"Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration." Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J. BMC Biol. 9:54-54(2011) [PubMed: 21834987] [Abstract] Cited for: FUNCTION.
[18]	"ARHGAP30 is a Wrch-1-interacting protein involved in actin dynamics and cell adhesion." Naji L., Pacholsky D., Aspenstrom P. Biochem. Biophys. Res. Commun. 409:96-102(2011) [PubMed: 21565175] [Abstract] Cited for: INTERACTION WITH ARHGAP30 AND ARHGAP31, MUTAGENESIS OF THR-63; PRO-80; PHE-83; PHE-86 AND GLN-107.
[19]	"The crystal structure of RHOUA in the GDP-bound state." Structural genomics consortium (SGC) Submitted (JUN-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 32-230 IN COMPLEX WITH GDP AND MAGNESIUM IONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF378087 mRNA. Translation: AAK83340.1.
AB074878 mRNA. Translation: BAB86361.1.
AB051826 mRNA. Translation: BAB18638.1.
DQ384420 Genomic DNA. Translation: ABD48870.1.
DQ384421 Genomic DNA. Translation: ABD48871.1.
DQ384422 Genomic DNA. Translation: ABD48872.1.
DQ384423 Genomic DNA. Translation: ABD48873.1.
DQ384424 Genomic DNA. Translation: ABD48874.1.
DQ384425 Genomic DNA. Translation: ABD48875.1.
AF211836 mRNA. Translation: AAL54874.1.
AF282258 mRNA. Translation: AAG46058.1.
AF251701 mRNA. Translation: AAL99390.1.
AK289971 mRNA. Translation: BAF82660.1.
AB209511 mRNA. Translation: BAD92748.1.
AL096776 Genomic DNA. Translation: CAC00584.1.
CH471098 Genomic DNA. Translation: EAW69885.1.
BC040076 mRNA. Translation: AAH40076.1.

IPI

IPI00009644.
IPI00889079.

RefSeq

NP_067028.1. NM_021205.5.

UniGene

Hs.647774.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Q3H	X-ray	1.73	A	32-230	[»]

ProteinModelPortal

Q7L0Q8.

SMR

Q7L0Q8. Positions 49-227.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q7L0Q8. 5 interactions.

STRING

Q7L0Q8.

PTM databases

PhosphoSite

Q7L0Q8.

Polymorphism databases

DMDM

172046189.

Proteomic databases

PRIDE

Q7L0Q8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000366691; ENSP00000355652; ENSG00000116574.

GeneID

58480.

KEGG

hsa:58480.

UCSC

uc001htf.1. human.

Organism-specific databases

CTD

58480.

GeneCards

GC01P228870.

H-InvDB

HIX0001673.

HGNC

HGNC:17794. RHOU.

MIM

606366. gene.

neXtProt

NX_Q7L0Q8.

PharmGKB

PA38246.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13152.

GeneTree

ENSGT00560000076971.

HOGENOM

HBG745225.

HOVERGEN

HBG009351.

InParanoid

Q7L0Q8.

OMA

EIRRHCP.

OrthoDB

EOG4DFPPJ.

PhylomeDB

Q7L0Q8.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q7L0Q8.

Bgee

Q7L0Q8.

CleanEx

HS_RHOU.

Genevestigator

Q7L0Q8.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]

KO

K07865.

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00174. RHO. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. Small_GTP. 1 hit.

PROSITE

PS51420. RHO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

64926.

SOURCE

Search...

Entry information

Entry name

RHOU_HUMAN

Accession

Primary (citable) accession number: Q7L0Q8
Secondary accession number(s): B1AKN1, Q59FE9, Q8TDQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 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.