RHOJ_HUMAN
ID RHOJ_HUMAN Reviewed; 214 AA.
AC Q9H4E5; Q96KC1;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Rho-related GTP-binding protein RhoJ {ECO:0000305};
DE AltName: Full=Ras-like protein family member 7B;
DE AltName: Full=Tc10-like GTP-binding protein {ECO:0000303|PubMed:10967094};
DE Flags: Precursor;
GN Name=RHOJ;
GN Synonyms=ARHJ, RASL7B, RHOI {ECO:0000303|Ref.2},
GN TCL {ECO:0000303|PubMed:10967094};
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10967094; DOI=10.1074/jbc.m003487200;
RA Vignal E., De Toledo M., Comunale F., Ladopoulou A., Gauthier-Rouviere C.,
RA Blangy A., Fort P.;
RT "Characterization of TCL, a new GTPase of the Rho family related to TC10
RT and Cdc42.";
RL J. Biol. Chem. 275:36457-36464(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Allen M., Halford S., Daniels H., McIntosh B., Kanuga N., Greenwood J.,
RA Carey A.H., Adamson P.;
RT "A novel Rho GTPase (RhoI) induces loss of stress-fibers and results in
RT apical actin reorganization.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=21628409; DOI=10.1182/blood-2010-10-315275;
RA Yuan L., Sacharidou A., Stratman A.N., Le Bras A., Zwiers P.J., Spokes K.,
RA Bhasin M., Shih S.C., Nagy J.A., Molema G., Aird W.C., Davis G.E.,
RA Oettgen P.;
RT "RhoJ is an endothelial cell-restricted Rho GTPase that mediates vascular
RT morphogenesis and is regulated by the transcription factor ERG.";
RL Blood 118:1145-1153(2011).
RN [7]
RP FUNCTION.
RX PubMed=24434213; DOI=10.1016/j.ccr.2013.12.010;
RA Kim C., Yang H., Fukushima Y., Saw P.E., Lee J., Park J.S., Park I.,
RA Jung J., Kataoka H., Lee D., Heo W.D., Kim I., Jon S., Adams R.H.,
RA Nishikawa S., Uemura A., Koh G.Y.;
RT "Vascular RhoJ is an effective and selective target for tumor angiogenesis
RT and vascular disruption.";
RL Cancer Cell 25:102-117(2014).
RN [8]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 17-ASP--LYS-20; 17-ASP-ASP-18;
RP 19-LYS-LYS-20; GLY-30; THR-35 AND GLN-79.
RX PubMed=27660391; DOI=10.1074/jbc.m116.750026;
RA Ackermann K.L., Florke R.R., Reyes S.S., Tader B.R., Hamann M.J.;
RT "TCL/RhoJ plasma membrane localization and nucleotide exchange is
RT coordinately regulated by amino acids within the n terminus and a distal
RT loop region.";
RL J. Biol. Chem. 291:23604-23617(2016).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-3 AND CYS-11, AND
RP MUTAGENESIS OF CYS-3 AND CYS-11.
RX PubMed=30158707; DOI=10.1038/s41586-018-0466-7;
RA Eelen G., Dubois C., Cantelmo A.R., Goveia J., Bruening U., DeRan M.,
RA Jarugumilli G., van Rijssel J., Saladino G., Comitani F., Zecchin A.,
RA Rocha S., Chen R., Huang H., Vandekeere S., Kalucka J., Lange C.,
RA Morales-Rodriguez F., Cruys B., Treps L., Ramer L., Vinckier S.,
RA Brepoels K., Wyns S., Souffreau J., Schoonjans L., Lamers W.H., Wu Y.,
RA Haustraete J., Hofkens J., Liekens S., Cubbon R., Ghesquiere B.,
RA Dewerchin M., Gervasio F.L., Li X., van Buul J.D., Wu X., Carmeliet P.;
RT "Role of glutamine synthetase in angiogenesis beyond glutamine synthesis.";
RL Nature 561:63-69(2018).
CC -!- FUNCTION: Plasma membrane-associated small GTPase specifically involved
CC in angiogenesis (PubMed:21628409, PubMed:24434213, PubMed:30158707).
CC Required for endothelial cell migration during vascular development via
CC its interaction with GLUL (PubMed:30158707). Elicits the formation of
CC F-actin-rich structures, thereby regulating endothelial cell migration
CC (PubMed:30158707). {ECO:0000269|PubMed:21628409,
CC ECO:0000269|PubMed:24434213, ECO:0000269|PubMed:30158707}.
CC -!- SUBUNIT: Interacts with the CRIB domains of proteins such as Pak1 and
CC Was/Wasp (By similarity). Interacts with GLUL (PubMed:30158707).
CC {ECO:0000250|UniProtKB:Q9ER71, ECO:0000269|PubMed:30158707}.
CC -!- INTERACTION:
CC Q9H4E5; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-6285694, EBI-10173507;
CC Q9H4E5; Q86V38: ATN1; NbExp=3; IntAct=EBI-6285694, EBI-11954292;
CC Q9H4E5; O14503: BHLHE40; NbExp=3; IntAct=EBI-6285694, EBI-711810;
CC Q9H4E5; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-6285694, EBI-2548012;
CC Q9H4E5; Q00587: CDC42EP1; NbExp=3; IntAct=EBI-6285694, EBI-744130;
CC Q9H4E5; P02489: CRYAA; NbExp=3; IntAct=EBI-6285694, EBI-6875961;
CC Q9H4E5; P15104: GLUL; NbExp=2; IntAct=EBI-6285694, EBI-746653;
CC Q9H4E5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-6285694, EBI-618309;
CC Q9H4E5; P50222: MEOX2; NbExp=3; IntAct=EBI-6285694, EBI-748397;
CC Q9H4E5; Q13153: PAK1; NbExp=3; IntAct=EBI-6285694, EBI-1307;
CC Q9H4E5; Q13177: PAK2; NbExp=6; IntAct=EBI-6285694, EBI-1045887;
CC Q9H4E5; O75914-2: PAK3; NbExp=3; IntAct=EBI-6285694, EBI-17483970;
CC Q9H4E5; Q9P286: PAK5; NbExp=3; IntAct=EBI-6285694, EBI-741896;
CC Q9H4E5; Q9NQU5: PAK6; NbExp=4; IntAct=EBI-6285694, EBI-1053685;
CC Q9H4E5; Q9BYG5: PARD6B; NbExp=6; IntAct=EBI-6285694, EBI-295391;
CC Q9H4E5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-6285694, EBI-5235340;
CC Q9H4E5; Q99909: SSX3; NbExp=4; IntAct=EBI-6285694, EBI-10295431;
CC Q9H4E5; Q15642: TRIP10; NbExp=3; IntAct=EBI-6285694, EBI-739936;
CC Q9H4E5; O00401: WASL; NbExp=6; IntAct=EBI-6285694, EBI-957615;
CC Q9H4E5; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-6285694, EBI-743265;
CC Q9H4E5-1; P15104: GLUL; NbExp=2; IntAct=EBI-20738368, EBI-746653;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27660391,
CC ECO:0000269|PubMed:30158707}; Lipid-anchor
CC {ECO:0000269|PubMed:30158707}; Cytoplasmic side {ECO:0000305}.
CC Note=Localization to the plasma membrane is regulated by GLUL.
CC {ECO:0000269|PubMed:30158707}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H4E5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H4E5-2; Sequence=VSP_007231;
CC -!- TISSUE SPECIFICITY: Specifically expressed in endothelial cells in
CC different tissues, such as brain, heart, lung and liver.
CC {ECO:0000269|PubMed:21628409}.
CC -!- INDUCTION: Expression is regulated by the transcription factor ERG.
CC {ECO:0000269|PubMed:21628409}.
CC -!- PTM: Palmitoylated; regulates localization to the plasma membrane and
CC may be mediated by GLUL. {ECO:0000269|PubMed:30158707}.
CC -!- MISCELLANEOUS: [Isoform 2]: Could be created by usage of an unusual
CC splicing donor site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55013.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ276567; CAC06611.1; -; mRNA.
DR EMBL; AF309563; AAL09440.1; -; mRNA.
DR EMBL; AK027278; BAB55013.1; ALT_FRAME; mRNA.
DR EMBL; AK027351; BAB55055.1; -; mRNA.
DR EMBL; AF498977; AAM21124.1; -; mRNA.
DR EMBL; BC062575; AAH62575.1; -; mRNA.
DR CCDS; CCDS9757.1; -. [Q9H4E5-1]
DR RefSeq; NP_065714.1; NM_020663.4. [Q9H4E5-1]
DR AlphaFoldDB; Q9H4E5; -.
DR SMR; Q9H4E5; -.
DR BioGRID; 121499; 621.
DR IntAct; Q9H4E5; 27.
DR MINT; Q9H4E5; -.
DR STRING; 9606.ENSP00000316729; -.
DR iPTMnet; Q9H4E5; -.
DR PhosphoSitePlus; Q9H4E5; -.
DR SwissPalm; Q9H4E5; -.
DR BioMuta; RHOJ; -.
DR DMDM; 24418646; -.
DR jPOST; Q9H4E5; -.
DR MassIVE; Q9H4E5; -.
DR MaxQB; Q9H4E5; -.
DR PaxDb; Q9H4E5; -.
DR PeptideAtlas; Q9H4E5; -.
DR PRIDE; Q9H4E5; -.
DR ProteomicsDB; 80825; -. [Q9H4E5-1]
DR ProteomicsDB; 80826; -. [Q9H4E5-2]
DR Antibodypedia; 160; 354 antibodies from 26 providers.
DR DNASU; 57381; -.
DR Ensembl; ENST00000316754.8; ENSP00000316729.3; ENSG00000126785.13. [Q9H4E5-1]
DR GeneID; 57381; -.
DR KEGG; hsa:57381; -.
DR MANE-Select; ENST00000316754.8; ENSP00000316729.3; NM_020663.5; NP_065714.1.
DR UCSC; uc001xgb.3; human. [Q9H4E5-1]
DR CTD; 57381; -.
DR DisGeNET; 57381; -.
DR GeneCards; RHOJ; -.
DR HGNC; HGNC:688; RHOJ.
DR HPA; ENSG00000126785; Low tissue specificity.
DR MIM; 607653; gene.
DR neXtProt; NX_Q9H4E5; -.
DR OpenTargets; ENSG00000126785; -.
DR PharmGKB; PA24981; -.
DR VEuPathDB; HostDB:ENSG00000126785; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000159098; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q9H4E5; -.
DR OMA; YILIGTQ; -.
DR PhylomeDB; Q9H4E5; -.
DR TreeFam; TF101109; -.
DR PathwayCommons; Q9H4E5; -.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR SignaLink; Q9H4E5; -.
DR BioGRID-ORCS; 57381; 8 hits in 1070 CRISPR screens.
DR ChiTaRS; RHOJ; human.
DR GeneWiki; RHOJ; -.
DR GenomeRNAi; 57381; -.
DR Pharos; Q9H4E5; Tbio.
DR PRO; PR:Q9H4E5; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9H4E5; protein.
DR Bgee; ENSG00000126785; Expressed in tendon of biceps brachii and 160 other tissues.
DR ExpressionAtlas; Q9H4E5; baseline and differential.
DR Genevisible; Q9H4E5; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0032488; P:Cdc42 protein signal transduction; IBA:GO_Central.
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:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0010594; P:regulation of endothelial cell migration; IMP:UniProtKB.
DR GO; GO:1903670; P:regulation of sprouting angiogenesis; IMP:UniProtKB.
DR GO; GO:0061299; P:retina vasculature morphogenesis in camera-type eye; IEA:Ensembl.
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 Alternative splicing; Angiogenesis; Cell membrane; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Palmitate;
KW Prenylation; Reference proteome.
FT CHAIN 1..211
FT /note="Rho-related GTP-binding protein RhoJ"
FT /id="PRO_0000198869"
FT PROPEP 212..214
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000281220"
FT MOTIF 50..58
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 31..36
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 46..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 75..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 177..178
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT MOD_RES 211
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:30158707"
FT LIPID 11
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:30158707"
FT LIPID 211
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT VAR_SEQ 113..134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007231"
FT MUTAGEN 3
FT /note="C->A: Impaired localization to the plasma membrane."
FT /evidence="ECO:0000269|PubMed:30158707"
FT MUTAGEN 11
FT /note="C->A: Impaired localization to the plasma membrane."
FT /evidence="ECO:0000269|PubMed:30158707"
FT MUTAGEN 17..20
FT /note="DEKK->AAAA: Impaired localization to the plasma
FT membrane."
FT /evidence="ECO:0000269|PubMed:27660391"
FT MUTAGEN 17..18
FT /note="DE->AA: Does not affect localization to the plasma
FT membrane."
FT /evidence="ECO:0000269|PubMed:27660391"
FT MUTAGEN 19..20
FT /note="KK->AA: Impaired localization to the plasma
FT membrane."
FT /evidence="ECO:0000269|PubMed:27660391"
FT MUTAGEN 30
FT /note="G->V: Causes constitutive activation."
FT /evidence="ECO:0000269|PubMed:27660391"
FT MUTAGEN 35
FT /note="T->N: Dominant negative mutant."
FT /evidence="ECO:0000269|PubMed:27660391"
FT MUTAGEN 79
FT /note="Q->L: Causes constitutive activation."
FT /evidence="ECO:0000269|PubMed:27660391"
FT CONFLICT 3
FT /note="C -> R (in Ref. 3; BAB55013)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 23821 MW; AAD2E2CED036F48C CRC64;
MNCKEGTDSS CGCRGNDEKK MLKCVVVGDG AVGKTCLLMS YANDAFPEEY VPTVFDHYAV
TVTVGGKQHL LGLYDTAGQE DYNQLRPLSY PNTDVFLICF SVVNPASYHN VQEEWVPELK
DCMPHVPYVL IGTQIDLRDD PKTLARLLYM KEKPLTYEHG VKLAKAIGAQ CYLECSALTQ
KGLKAVFDEA ILTIFHPKKK KKRCSEGHSC CSII
