RHOU_HUMAN
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 03-AUG-2022, entry version 128.
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},
GN CDC42L1 {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 Wnt-
RT 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}.
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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; Q7L0Q8; -.
DR PeptideAtlas; Q7L0Q8; -.
DR PRIDE; Q7L0Q8; -.
DR ProteomicsDB; 68734; -. [Q7L0Q8-1]
DR ProteomicsDB; 68735; -. [Q7L0Q8-2]
DR Antibodypedia; 34671; 162 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 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; CEKWVPE; -.
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 1075 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 101 other tissues.
DR ExpressionAtlas; Q7L0Q8; baseline and differential.
DR Genevisible; Q7L0Q8; HS.
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; TAS:Reactome.
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:0030036; P:actin cytoskeleton 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 Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
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 S-
FT 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
