Entry euk: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   12-APR-2017, entry version 144.
DE   RecName: Full=Rho-related GTP-binding protein RhoJ;
DE   AltName: Full=Ras-like protein family member 7B;
DE   AltName: Full=Tc10-like GTP-binding protein;
DE   Flags: Precursor;
GN   Name=RHOJ; Synonyms=ARHJ, RASL7B, RHOI, TCL;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Gauthier-Rouviere C., Blangy A., Fort P.;
RT   "Characterization of TCL, a new GTPase of the Rho family related to
RT   TC10 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.,
RA   Greenwood J., Carey A.H., Adamson P.;
RT   "A novel Rho GTPase (RhoI) induces loss of stress-fibers and results
RT   in 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT   sequenced by 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: GTP-binding protein with GTPase activity. Elicits the
CC       formation of F-actin-rich structures in fibroblasts and is
CC       involved in the regulation of cell morphology (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the CRIB domains of proteins such as Pak1
CC       and Was/Wasp. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q6UY14-3:ADAMTSL4; NbExp=3; IntAct=EBI-6285694, EBI-10173507;
CC       O14503:BHLHE40; NbExp=3; IntAct=EBI-6285694, EBI-711810;
CC       Q9H2G9:BLZF1; NbExp=3; IntAct=EBI-6285694, EBI-2548012;
CC       Q00587:CDC42EP1; NbExp=3; IntAct=EBI-6285694, EBI-744130;
CC       A4D127:MEOX2; NbExp=3; IntAct=EBI-6285694, EBI-10172134;
CC       Q13177:PAK2; NbExp=5; IntAct=EBI-6285694, EBI-1045887;
CC       Q9NQU5:PAK6; NbExp=3; IntAct=EBI-6285694, EBI-1053685;
CC       Q9BYG5:PARD6B; NbExp=5; IntAct=EBI-6285694, EBI-295391;
CC       Q99909:SSX3; NbExp=4; IntAct=EBI-6285694, EBI-10295431;
CC       Q15642:TRIP10; NbExp=3; IntAct=EBI-6285694, EBI-739936;
CC       O00401:WASL; NbExp=5; IntAct=EBI-6285694, EBI-957615;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
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         Note=No experimental confirmation available. Could be created by
CC         usage of an unusual splicing donor site.;
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB55013.1; Type=Frameshift; Positions=143; 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   UniGene; Hs.656339; -.
DR   ProteinModelPortal; Q9H4E5; -.
DR   SMR; Q9H4E5; -.
DR   BioGrid; 121499; 20.
DR   IntAct; Q9H4E5; 17.
DR   STRING; 9606.ENSP00000316729; -.
DR   iPTMnet; Q9H4E5; -.
DR   PhosphoSitePlus; Q9H4E5; -.
DR   SwissPalm; Q9H4E5; -.
DR   BioMuta; RHOJ; -.
DR   DMDM; 24418646; -.
DR   MaxQB; Q9H4E5; -.
DR   PaxDb; Q9H4E5; -.
DR   PeptideAtlas; Q9H4E5; -.
DR   PRIDE; Q9H4E5; -.
DR   DNASU; 57381; -.
DR   Ensembl; ENST00000316754; ENSP00000316729; ENSG00000126785. [Q9H4E5-1]
DR   GeneID; 57381; -.
DR   KEGG; hsa:57381; -.
DR   UCSC; uc001xgb.3; human. [Q9H4E5-1]
DR   CTD; 57381; -.
DR   DisGeNET; 57381; -.
DR   GeneCards; RHOJ; -.
DR   HGNC; HGNC:688; RHOJ.
DR   HPA; HPA003050; -.
DR   MIM; 607653; gene.
DR   neXtProt; NX_Q9H4E5; -.
DR   OpenTargets; ENSG00000126785; -.
DR   PharmGKB; PA24981; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   eggNOG; COG1100; LUCA.
DR   GeneTree; ENSGT00760000118978; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; Q9H4E5; -.
DR   KO; K07864; -.
DR   OMA; YILIGTQ; -.
DR   OrthoDB; EOG091G0KCM; -.
DR   PhylomeDB; Q9H4E5; -.
DR   TreeFam; TF101109; -.
DR   Reactome; R-HSA-194840; Rho GTPase cycle.
DR   ChiTaRS; RHOJ; human.
DR   GeneWiki; RHOJ; -.
DR   GenomeRNAi; 57381; -.
DR   PRO; PR:Q9H4E5; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   Bgee; ENSG00000126785; -.
DR   CleanEx; HS_RHOJ; -.
DR   ExpressionAtlas; Q9H4E5; baseline and differential.
DR   Genevisible; Q9H4E5; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0061299; P:retina vasculature morphogenesis in camera-type eye; IEA:Ensembl.
DR   GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
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   Pfam; PF00071; Ras; 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; Cell membrane; Cell shape; Complete proteome;
KW   GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW   Prenylation; Reference proteome.
FT   CHAIN         1    211       Rho-related GTP-binding protein RhoJ.
FT                                /FTId=PRO_0000198869.
FT   PROPEP      212    214       Removed in mature form. {ECO:0000250}.
FT                                /FTId=PRO_0000281220.
FT   NP_BIND      28     35       GTP. {ECO:0000250}.
FT   NP_BIND      75     79       GTP. {ECO:0000250}.
FT   NP_BIND     133    136       GTP. {ECO:0000250}.
FT   MOTIF        50     58       Effector region. {ECO:0000255}.
FT   MOD_RES     211    211       Cysteine methyl ester. {ECO:0000250}.
FT   LIPID       211    211       S-farnesyl cysteine. {ECO:0000250}.
FT   VAR_SEQ     113    134       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_007231.
FT   CONFLICT      3      3       C -> R (in Ref. 3; BAB55013).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        23    194       ipfam:Ras [T]
FT   MYHIT        15    194       iprf:RHO [T]
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
//