ID RHOU_HUMAN Reviewed; 258 AA. AC Q7L0Q8; B1AKN1; Q59FE9; Q8TDQ2; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 137. DE RecName: Full=Rho-related GTP-binding protein RhoU; DE AltName: Full=CDC42-like GTPase 1; DE AltName: Full=GTP-binding protein-like 1; DE AltName: Full=Rho GTPase-like protein ARHU; DE AltName: Full=Ryu GTPase; DE AltName: Full=Wnt-1 responsive Cdc42 homolog 1; DE Short=WRCH-1; GN Name=RHOU {ECO:0000312|HGNC:HGNC:17794}; GN Synonyms=ARHU {ECO:0000312|EMBL:BAB86361.1}, CDC42L1 GN {ECO:0000312|EMBL:AAL54874.1}, G28K {ECO:0000312|EMBL:BAB18638.1}, GN WRCH1 {ECO:0000312|EMBL:AAK83340.1}; ORFNames=SB128; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK83340.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND RP MUTAGENESIS OF THR-63 AND GLN-107. RX PubMed=11459829; DOI=10.1101/gad.894301; RA Tao W., Pennica D., Xu L., Kalejta R.F., Levine A.J.; RT "Wrch-1, a novel member of the Rho gene family that is regulated by RT Wnt-1."; RL Genes Dev. 15:1796-1807(2001). RN [2] {ECO:0000305, ECO:0000312|EMBL:BAB86361.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=11894124; RA Kirikoshi H., Katoh M.; RT "Expression of WRCH1 in human cancer and down-regulation of WRCH1 by beta- RT estradiol in MCF-7 cells."; RL Int. J. Oncol. 20:777-783(2002). RN [3] {ECO:0000305, ECO:0000312|EMBL:BAB18638.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=14731133; DOI=10.1111/j.1440-1746.2004.03298.x; RA Daigo Y., Takayama I., Ponder B.A.J., Caldas C., Ward S.M., Sanders K.M., RA Fujino M.A.; RT "Novel human, mouse and Xenopus genes encoding a member of the RAS RT superfamily of low-molecular-weight GTP-binding proteins and its RT downregulation in W/WV mouse jejunum."; RL J. Gastroenterol. Hepatol. 19:211-217(2004). RN [4] {ECO:0000312|EMBL:ABD48870.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=16751668; DOI=10.1534/genetics.106.055715; RA Bubb K.L., Bovee D., Buckley D., Haugen E., Kibukawa M., Paddock M., RA Palmieri A., Subramanian S., Zhou Y., Kaul R., Green P., Olson M.V.; RT "Scan of human genome reveals no new loci under ancient balancing RT selection."; RL Genetics 173:2165-2177(2006). RN [5] {ECO:0000305, ECO:0000312|EMBL:AAL54874.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Zhang J.S., Smith D.I., Urrutia R.; RT "A novel GTPase homologous to CDC42."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000305, ECO:0000312|EMBL:AAL54874.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Ikeda W., Nakanishi H., Takai Y.; RT "Ryu: a new member of Rho family."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000305, ECO:0000312|EMBL:AAL54874.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Zhang W., Wan T., Li N., He L., Chen T., Cao X.; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000305, ECO:0000312|EMBL:BAF82660.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hippocampus {ECO:0000312|EMBL:BAF82660.1}; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [9] {ECO:0000305, ECO:0000312|EMBL:AAL54874.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [11] {ECO:0000305, ECO:0000312|EMBL:AAL54874.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [12] {ECO:0000305, ECO:0000312|EMBL:AAH40076.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain {ECO:0000312|EMBL:AAH40076.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [13] {ECO:0000305} RP SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-255 AND CYS-256, AND RP PALMITOYLATION AT CYS-256. RX PubMed=16046391; DOI=10.1074/jbc.m507362200; RA Berzat A.C., Buss J.E., Chenette E.J., Weinbaum C.A., Shutes A., Der C.J., RA Minden A., Cox A.D.; RT "Transforming activity of the Rho family GTPase, Wrch-1, a Wnt-regulated RT Cdc42 homolog, is dependent on a novel carboxyl-terminal palmitoylation RT motif."; RL J. Biol. Chem. 280:33055-33065(2005). RN [14] {ECO:0000305} RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, GTP-BINDING, AND PALMITOYLATION. RX PubMed=16472646; DOI=10.1016/s0076-6879(06)06002-2; RA Shutes A., Berzat A.C., Chenette E.J., Cox A.D., Der C.J.; RT "Biochemical analyses of the Wrch atypical Rho family GTPases."; RL Methods Enzymol. 406:11-26(2006). RN [15] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PAK3, AND MUTAGENESIS OF RP THR-63; THR-81; PHE-83; PHE-86 AND GLN-107. RX PubMed=17620058; DOI=10.1042/bc20070058; RA Ory S., Brazier H., Blangy A.; RT "Identification of a bipartite focal adhesion localization signal in RT RhoU/Wrch-1, a Rho family GTPase that regulates cell adhesion and RT migration."; RL Biol. Cell 99:701-716(2007). RN [16] RP INTERACTION WITH PTK2B/PYK2, FUNCTION, SUBCELLULAR LOCATION, AND RP PHOSPHORYLATION. RX PubMed=18086875; DOI=10.1128/mcb.00201-07; RA Ruusala A., Aspenstrom P.; RT "The atypical Rho GTPase Wrch1 collaborates with the nonreceptor tyrosine RT kinases Pyk2 and Src in regulating cytoskeletal dynamics."; RL Mol. Cell. Biol. 28:1802-1814(2008). RN [17] RP FUNCTION. RX PubMed=21834987; DOI=10.1186/1741-7007-9-54; RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.; RT "Identification and characterization of a set of conserved and new RT regulators of cytoskeletal organisation, cell morphology and migration."; RL BMC Biol. 9:54-54(2011). RN [18] RP INTERACTION WITH ARHGAP30 AND ARHGAP31, AND MUTAGENESIS OF THR-63; PRO-80; RP PHE-83; PHE-86 AND GLN-107. RX PubMed=21565175; DOI=10.1016/j.bbrc.2011.04.116; RA Naji L., Pacholsky D., Aspenstrom P.; RT "ARHGAP30 is a Wrch-1-interacting protein involved in actin dynamics and RT cell adhesion."; RL Biochem. Biophys. Res. Commun. 409:96-102(2011). RN [19] {ECO:0000305, ECO:0000312|EMBL:AAL54874.1} RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 32-230 IN COMPLEX WITH GDP AND RP MAGNESIUM IONS. RG Structural genomics consortium (SGC); RT "The crystal structure of RHOUA in the GDP-bound state."; RL Submitted (JUN-2007) to the PDB data bank. CC -!- FUNCTION: Acts upstream of PAK1 to regulate the actin cytoskeleton, CC adhesion turnover and increase cell migration. Stimulates quiescent CC cells to reenter the cell cycle. Has no detectable GTPase activity but CC its high intrinsic guanine nucleotide exchange activity suggests it is CC constitutively GTP-bound. Plays a role in the regulation of cell CC morphology and cytoskeletal organization. Required in the control of CC cell shape. {ECO:0000269|PubMed:11459829, ECO:0000269|PubMed:16472646, CC ECO:0000269|PubMed:17620058, ECO:0000269|PubMed:18086875, CC ECO:0000269|PubMed:21834987}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:16472646}; CC -!- SUBUNIT: Interacts with PAK3. Interacts with ARHGAP30 in a GTP- CC independent manner. In its GTP-loaded conformation, interacts with CC ARHGAP31. Interacts with PTK2B/PYK2. {ECO:0000269|PubMed:17620058, CC ECO:0000269|PubMed:18086875, ECO:0000269|PubMed:21565175, CC ECO:0000269|Ref.19}. CC -!- INTERACTION: CC Q7L0Q8; Q7Z6I6: ARHGAP30; NbExp=2; IntAct=EBI-1638043, EBI-2814810; CC Q7L0Q8; Q7Z6I6-2: ARHGAP30; NbExp=3; IntAct=EBI-1638043, EBI-26970905; CC Q7L0Q8; O43639: NCK2; NbExp=6; IntAct=EBI-1638043, EBI-713635; CC Q7L0Q8; Q13153-2: PAK1; NbExp=2; IntAct=EBI-1638043, EBI-1019502; CC Q7L0Q8; Q14289: PTK2B; NbExp=4; IntAct=EBI-1638043, EBI-298640; CC Q7L0Q8; A6X8Z5: Arhgap31; Xeno; NbExp=2; IntAct=EBI-1638043, EBI-4325995; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16046391, CC ECO:0000269|PubMed:16472646, ECO:0000269|PubMed:17620058}; Lipid-anchor CC {ECO:0000269|PubMed:16046391, ECO:0000269|PubMed:16472646, CC ECO:0000269|PubMed:17620058}; Cytoplasmic side CC {ECO:0000269|PubMed:16046391, ECO:0000269|PubMed:16472646, CC ECO:0000269|PubMed:17620058}. Golgi apparatus membrane CC {ECO:0000269|PubMed:16046391, ECO:0000269|PubMed:16472646, CC ECO:0000269|PubMed:17620058}; Lipid-anchor CC {ECO:0000269|PubMed:16046391, ECO:0000269|PubMed:16472646, CC ECO:0000269|PubMed:17620058}. Cell junction, focal adhesion CC {ECO:0000269|PubMed:16046391, ECO:0000269|PubMed:16472646, CC ECO:0000269|PubMed:17620058}. Cell projection, podosome CC {ECO:0000269|PubMed:16046391, ECO:0000269|PubMed:16472646, CC ECO:0000269|PubMed:17620058}. Note=Localizes to podosomes in SRC- CC transformed cells. {ECO:0000269|PubMed:16046391, CC ECO:0000269|PubMed:16472646, ECO:0000269|PubMed:17620058}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1 {ECO:0000269|PubMed:11459829, ECO:0000269|PubMed:11894124, CC ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:14731133, CC ECO:0000269|PubMed:15489334, ECO:0000269|Ref.5, ECO:0000269|Ref.6}; CC IsoId=Q7L0Q8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7L0Q8-2; Sequence=VSP_052732, VSP_052733; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined. CC Expressed at high levels in the stomach, small intestine, brain, CC skeletal muscle and placenta. {ECO:0000269|PubMed:11459829, CC ECO:0000269|PubMed:14731133}. CC -!- PTM: Tyrosine phosphorylated by SRC in response to PTK2B/PYK2 CC activation. {ECO:0000269|PubMed:18086875}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CC {ECO:0000269|PubMed:16472646}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF378087; AAK83340.1; -; mRNA. DR EMBL; AB074878; BAB86361.1; -; mRNA. DR EMBL; AB051826; BAB18638.1; -; mRNA. DR EMBL; DQ384420; ABD48870.1; -; Genomic_DNA. DR EMBL; DQ384421; ABD48871.1; -; Genomic_DNA. DR EMBL; DQ384422; ABD48872.1; -; Genomic_DNA. DR EMBL; DQ384423; ABD48873.1; -; Genomic_DNA. DR EMBL; DQ384424; ABD48874.1; -; Genomic_DNA. DR EMBL; DQ384425; ABD48875.1; -; Genomic_DNA. DR EMBL; AF211836; AAL54874.1; -; mRNA. DR EMBL; AF282258; AAG46058.1; -; mRNA. DR EMBL; AF251701; AAL99390.1; -; mRNA. DR EMBL; AK289971; BAF82660.1; -; mRNA. DR EMBL; AB209511; BAD92748.1; -; mRNA. DR EMBL; AL096776; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471098; EAW69885.1; -; Genomic_DNA. DR EMBL; BC040076; AAH40076.1; -; mRNA. DR CCDS; CCDS1575.1; -. [Q7L0Q8-1] DR RefSeq; NP_067028.1; NM_021205.5. [Q7L0Q8-1] DR PDB; 2Q3H; X-ray; 1.73 A; A=32-230. DR PDBsum; 2Q3H; -. DR AlphaFoldDB; Q7L0Q8; -. DR SMR; Q7L0Q8; -. DR BioGRID; 121812; 508. DR IntAct; Q7L0Q8; 9. DR MINT; Q7L0Q8; -. DR STRING; 9606.ENSP00000355652; -. DR iPTMnet; Q7L0Q8; -. DR PhosphoSitePlus; Q7L0Q8; -. DR SwissPalm; Q7L0Q8; -. DR BioMuta; RHOU; -. DR DMDM; 172046189; -. DR EPD; Q7L0Q8; -. DR MassIVE; Q7L0Q8; -. DR PaxDb; 9606-ENSP00000355652; -. DR PeptideAtlas; Q7L0Q8; -. DR ProteomicsDB; 68734; -. [Q7L0Q8-1] DR ProteomicsDB; 68735; -. [Q7L0Q8-2] DR Antibodypedia; 34671; 187 antibodies from 25 providers. DR DNASU; 58480; -. DR Ensembl; ENST00000366691.4; ENSP00000355652.3; ENSG00000116574.6. [Q7L0Q8-1] DR Ensembl; ENST00000646945.2; ENSP00000494673.1; ENSG00000284984.2. [Q7L0Q8-1] DR GeneID; 58480; -. DR KEGG; hsa:58480; -. DR MANE-Select; ENST00000366691.4; ENSP00000355652.3; NM_021205.6; NP_067028.1. DR UCSC; uc001htf.3; human. [Q7L0Q8-1] DR AGR; HGNC:17794; -. DR CTD; 58480; -. DR DisGeNET; 58480; -. DR GeneCards; RHOU; -. DR HGNC; HGNC:17794; RHOU. DR HPA; ENSG00000116574; Low tissue specificity. DR MIM; 606366; gene. DR neXtProt; NX_Q7L0Q8; -. DR OpenTargets; ENSG00000116574; -. DR PharmGKB; PA38246; -. DR VEuPathDB; HostDB:ENSG00000116574; -. DR eggNOG; KOG0393; Eukaryota. DR GeneTree; ENSGT00940000156644; -. DR HOGENOM; CLU_041217_21_7_1; -. DR InParanoid; Q7L0Q8; -. DR OMA; PEIHKHA; -. DR OrthoDB; 20499at2759; -. DR PhylomeDB; Q7L0Q8; -. DR TreeFam; TF321839; -. DR PathwayCommons; Q7L0Q8; -. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR Reactome; R-HSA-9013420; RHOU GTPase cycle. DR SignaLink; Q7L0Q8; -. DR SIGNOR; Q7L0Q8; -. DR BioGRID-ORCS; 58480; 10 hits in 1153 CRISPR screens. DR ChiTaRS; RHOU; human. DR EvolutionaryTrace; Q7L0Q8; -. DR GenomeRNAi; 58480; -. DR Pharos; Q7L0Q8; Tbio. DR PRO; PR:Q7L0Q8; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q7L0Q8; Protein. DR Bgee; ENSG00000116574; Expressed in corpus callosum and 103 other cell types or tissues. DR ExpressionAtlas; Q7L0Q8; baseline and differential. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0010008; C:endosome membrane; TAS:Reactome. DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IBA:GO_Central. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central. DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central. DR GO; GO:0032488; P:Cdc42 protein signal transduction; IBA:GO_Central. DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB. DR GO; GO:0006897; P:endocytosis; IBA:GO_Central. DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl. DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL. DR GO; GO:0016601; P:Rac protein signal transduction; IEA:Ensembl. DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB. DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome. DR CDD; cd04130; Wrch_1; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR InterPro; IPR003578; Small_GTPase_Rho. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR24072; RHO FAMILY GTPASE; 1. DR PANTHER; PTHR24072:SF148; RHO-RELATED GTP-BINDING PROTEIN RHOU; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51420; RHO; 1. DR Genevisible; Q7L0Q8; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell junction; Cell membrane; KW Cell projection; Golgi apparatus; GTP-binding; Lipoprotein; Magnesium; KW Membrane; Metal-binding; Nucleotide-binding; Palmitate; Phosphoprotein; KW Reference proteome. FT CHAIN 1..258 FT /note="Rho-related GTP-binding protein RhoU" FT /id="PRO_0000326435" FT REGION 1..45 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 56..63 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:11459829" FT BINDING 103..107 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 161..164 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT LIPID 256 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:16046391" FT VAR_SEQ 1..61 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.7" FT /id="VSP_052732" FT VAR_SEQ 62..66 FT /note="KTSLV -> MTNIG (in isoform 2)" FT /evidence="ECO:0000303|Ref.7" FT /id="VSP_052733" FT VARIANT 121 FT /note="T -> A (in dbSNP:rs3820264)" FT /id="VAR_051975" FT MUTAGEN 63 FT /note="T->N: Loss of GTP-binding and localization to focal FT adhesions. No effect on ARHGAP30-binding." FT /evidence="ECO:0000269|PubMed:11459829, FT ECO:0000269|PubMed:17620058, ECO:0000269|PubMed:21565175" FT MUTAGEN 80 FT /note="P->G: No effect on ARHGAP30-binding." FT /evidence="ECO:0000269|PubMed:21565175" FT MUTAGEN 81 FT /note="T->S: Loss of binding to PAK3; when associated with FT A-83 and C-86." FT /evidence="ECO:0000269|PubMed:17620058" FT MUTAGEN 83 FT /note="F->A: Loss of binding to PAK3; when associated with FT S-81 and C-86." FT /evidence="ECO:0000269|PubMed:17620058, FT ECO:0000269|PubMed:21565175" FT MUTAGEN 83 FT /note="F->G: Loss of ARHGAP30-binding." FT /evidence="ECO:0000269|PubMed:17620058, FT ECO:0000269|PubMed:21565175" FT MUTAGEN 86 FT /note="F->C: Loss of PAK3-binding; when associated with FT S-81 and A-83. No effect on ARHGAP30-binding." FT /evidence="ECO:0000269|PubMed:17620058, FT ECO:0000269|PubMed:21565175" FT MUTAGEN 107 FT /note="Q->L: Constitutively active. Results in increased FT rates of stress fiber dissolution and cell migration. No FT effect on ARHGAP30-binding." FT /evidence="ECO:0000269|PubMed:11459829, FT ECO:0000269|PubMed:17620058, ECO:0000269|PubMed:21565175" FT MUTAGEN 255 FT /note="C->S: No effect on subcellular location." FT /evidence="ECO:0000269|PubMed:16046391" FT MUTAGEN 256 FT /note="C->S: Loss of subcellular location to plasma and FT intracellular membranes." FT /evidence="ECO:0000269|PubMed:16046391" FT CONFLICT 1..13 FT /note="MPPQQGDPAFPDR -> QLLPTATLRGGGAVGPGPASPRPQA (in Ref. FT 7; BAD92748)" FT /evidence="ECO:0000305" FT CONFLICT 71 FT /note="T -> P (in Ref. 2; AAL99390)" FT /evidence="ECO:0000305" FT STRAND 50..55 FT /evidence="ECO:0007829|PDB:2Q3H" FT HELIX 62..70 FT /evidence="ECO:0007829|PDB:2Q3H" FT STRAND 82..92 FT /evidence="ECO:0007829|PDB:2Q3H" FT STRAND 95..103 FT /evidence="ECO:0007829|PDB:2Q3H" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:2Q3H" FT HELIX 114..118 FT /evidence="ECO:0007829|PDB:2Q3H" FT STRAND 122..129 FT /evidence="ECO:0007829|PDB:2Q3H" FT HELIX 133..141 FT /evidence="ECO:0007829|PDB:2Q3H" FT HELIX 143..150 FT /evidence="ECO:0007829|PDB:2Q3H" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:2Q3H" FT STRAND 156..161 FT /evidence="ECO:0007829|PDB:2Q3H" FT HELIX 163..167 FT /evidence="ECO:0007829|PDB:2Q3H" FT HELIX 169..176 FT /evidence="ECO:0007829|PDB:2Q3H" FT TURN 177..179 FT /evidence="ECO:0007829|PDB:2Q3H" FT HELIX 185..195 FT /evidence="ECO:0007829|PDB:2Q3H" FT STRAND 198..202 FT /evidence="ECO:0007829|PDB:2Q3H" FT TURN 205..207 FT /evidence="ECO:0007829|PDB:2Q3H" FT HELIX 211..226 FT /evidence="ECO:0007829|PDB:2Q3H" SQ SEQUENCE 258 AA; 28218 MW; D90059DE82288B97 CRC64; MPPQQGDPAF PDRCEAPPVP PRRERGGRGG RGPGEPGGRG RAGGAEGRGV KCVLVGDGAV GKTSLVVSYT TNGYPTEYIP TAFDNFSAVV SVDGRPVRLQ LCDTAGQDEF DKLRPLCYTN TDIFLLCFSV VSPSSFQNVS EKWVPEIRCH CPKAPIILVG TQSDLREDVK VLIELDKCKE KPVPEEAAKL CAEEIKAASY IECSALTQKN LKEVFDAAIV AGIQYSDTQQ QPKKSKSRTP DKMKNLSKSW WKKYCCFV //