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GTP-binding protein Di-Ras1 (Distinct subgroup of the Ras family member 1) (Ras-related inhibitor of cell growth) (Rig) (Small GTP-binding tumor suppressor 1)

 DIRA1_HUMAN             Reviewed;         198 AA.
O95057;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
27-SEP-2017, entry version 146.
RecName: Full=GTP-binding protein Di-Ras1;
AltName: Full=Distinct subgroup of the Ras family member 1;
AltName: Full=Ras-related inhibitor of cell growth;
Short=Rig;
AltName: Full=Small GTP-binding tumor suppressor 1;
Flags: Precursor;
Name=DIRAS1; Synonyms=GBTS1, RIG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], GTPASE ACTIVITY, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=12194967; DOI=10.1074/jbc.M202150200;
Kontani K., Tada M., Ogawa T., Okai T., Saito K., Araki Y., Katada T.;
"Di-Ras, a distinct subgroup of ras family GTPases with unique
biochemical properties.";
J. Biol. Chem. 277:41070-41078(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=12107278; DOI=10.1073/pnas.142193799;
Ellis C.A., Vos M.D., Howell H., Vallecorsa T., Fults D.W.,
Clark G.J.;
"Rig is a novel Ras-related protein and potential neural tumor
suppressor.";
Proc. Natl. Acad. Sci. U.S.A. 99:9876-9881(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Gong L., Wu K.;
"Molecular cloning of GBTS1, a novel gene encoding a small GTP-binding
tumor suppressor.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Cismowski M.J., Kopatz S.A., Aronstam R.S., Sharma S.V.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH GTP ANALOG.
Structural genomics consortium (SGC);
"The crystal structure of the human DiRas1 GTPase in the inactive GDP
bound state.";
Submitted (MAR-2006) to the PDB data bank.
-!- FUNCTION: Displays low GTPase activity and exists predominantly in
the GTP-bound form. {ECO:0000269|PubMed:12194967}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}; Cytoplasmic side {ECO:0000305}.
-!- TISSUE SPECIFICITY: Highly expressed in heart and brain.
{ECO:0000269|PubMed:12107278, ECO:0000269|PubMed:12194967}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Di-Ras
family. {ECO:0000305}.
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EMBL; AB076888; BAC01115.1; -; mRNA.
EMBL; AY056037; AAL23715.1; -; mRNA.
EMBL; AY059641; AAL17968.1; -; mRNA.
EMBL; AY180973; AAO22153.1; -; mRNA.
EMBL; AC006538; AAD13119.1; -; Genomic_DNA.
EMBL; BC030660; AAH30660.1; -; mRNA.
CCDS; CCDS12092.1; -.
RefSeq; NP_660156.1; NM_145173.3.
UniGene; Hs.172753; -.
PDB; 2GF0; X-ray; 1.90 A; A/B/C/D=1-198.
PDBsum; 2GF0; -.
ProteinModelPortal; O95057; -.
SMR; O95057; -.
BioGrid; 127135; 15.
IntAct; O95057; 3.
STRING; 9606.ENSP00000325836; -.
iPTMnet; O95057; -.
PhosphoSitePlus; O95057; -.
BioMuta; DIRAS1; -.
EPD; O95057; -.
MaxQB; O95057; -.
PaxDb; O95057; -.
PeptideAtlas; O95057; -.
PRIDE; O95057; -.
DNASU; 148252; -.
Ensembl; ENST00000323469; ENSP00000325836; ENSG00000176490.
Ensembl; ENST00000585334; ENSP00000468417; ENSG00000176490.
GeneID; 148252; -.
KEGG; hsa:148252; -.
UCSC; uc002lwf.4; human.
CTD; 148252; -.
DisGeNET; 148252; -.
EuPathDB; HostDB:ENSG00000176490.4; -.
GeneCards; DIRAS1; -.
HGNC; HGNC:19127; DIRAS1.
MIM; 607862; gene.
neXtProt; NX_O95057; -.
OpenTargets; ENSG00000176490; -.
PharmGKB; PA134951835; -.
eggNOG; KOG0395; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00860000133678; -.
HOGENOM; HOG000233973; -.
HOVERGEN; HBG009351; -.
InParanoid; O95057; -.
KO; K07840; -.
OMA; LGPIYQL; -.
OrthoDB; EOG091G0SBH; -.
PhylomeDB; O95057; -.
TreeFam; TF313014; -.
EvolutionaryTrace; O95057; -.
GenomeRNAi; 148252; -.
PRO; PR:O95057; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000176490; -.
CleanEx; HS_DIRAS1; -.
ExpressionAtlas; O95057; baseline and differential.
Genevisible; O95057; HS.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras.
PANTHER; PTHR24070; PTHR24070; 1.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51421; RAS; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; GTP-binding;
Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
Reference proteome.
CHAIN 1 195 GTP-binding protein Di-Ras1.
/FTId=PRO_0000191648.
PROPEP 196 198 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000370775.
NP_BIND 17 22 GTP. {ECO:0000244|PDB:2GF0,
ECO:0000305|Ref.7}.
NP_BIND 33 39 GTP. {ECO:0000250|UniProtKB:Q96HU8}.
NP_BIND 61 65 GTP. {ECO:0000250|UniProtKB:Q96HU8}.
NP_BIND 121 125 GTP. {ECO:0000244|PDB:2GF0,
ECO:0000305|Ref.7}.
NP_BIND 151 152 GTP. {ECO:0000250|UniProtKB:Q96HU8}.
MOTIF 36 44 Effector region. {ECO:0000255}.
BINDING 151 151 GTP; via amide nitrogen.
{ECO:0000244|PDB:2GF0,
ECO:0000305|Ref.7}.
MOD_RES 195 195 Cysteine methyl ester. {ECO:0000255}.
LIPID 195 195 S-geranylgeranyl cysteine. {ECO:0000250}.
STRAND 8 14 {ECO:0000244|PDB:2GF0}.
HELIX 20 29 {ECO:0000244|PDB:2GF0}.
STRAND 42 50 {ECO:0000244|PDB:2GF0}.
STRAND 53 61 {ECO:0000244|PDB:2GF0}.
HELIX 64 66 {ECO:0000244|PDB:2GF0}.
HELIX 69 78 {ECO:0000244|PDB:2GF0}.
STRAND 80 87 {ECO:0000244|PDB:2GF0}.
HELIX 91 95 {ECO:0000244|PDB:2GF0}.
HELIX 98 108 {ECO:0000244|PDB:2GF0}.
HELIX 111 113 {ECO:0000244|PDB:2GF0}.
STRAND 116 121 {ECO:0000244|PDB:2GF0}.
HELIX 132 142 {ECO:0000244|PDB:2GF0}.
STRAND 145 148 {ECO:0000244|PDB:2GF0}.
TURN 151 154 {ECO:0000244|PDB:2GF0}.
HELIX 157 167 {ECO:0000244|PDB:2GF0}.
STRAND 169 171 {ECO:0000244|PDB:2GF0}.
SEQUENCE 198 AA; 22329 MW; 32E979AF80BB9A7F CRC64;
MPEQSNDYRV VVFGAGGVGK SSLVLRFVKG TFRDTYIPTI EDTYRQVISC DKSVCTLQIT
DTTGSHQFPA MQRLSISKGH AFILVFSVTS KQSLEELGPI YKLIVQIKGS VEDIPVMLVG
NKCDETQREV DTREAQAVAQ EWKCAFMETS AKMNYNVKEL FQELLTLETR RNMSLNIDGK
RSGKQKRTDR VKGKCTLM


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