Full text data of RASD1
RASD1
(AGS1, DEXRAS1)
[Confidence: low (only semi-automatic identification from reviews)]
Dexamethasone-induced Ras-related protein 1 (Activator of G-protein signaling 1; Flags: Precursor)
Dexamethasone-induced Ras-related protein 1 (Activator of G-protein signaling 1; Flags: Precursor)
UniProt
Q9Y272
ID RASD1_HUMAN Reviewed; 281 AA.
AC Q9Y272; B2R709; B4DFF4; Q9NYB4;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Dexamethasone-induced Ras-related protein 1;
DE AltName: Full=Activator of G-protein signaling 1;
DE Flags: Precursor;
GN Name=RASD1; Synonyms=AGS1, DEXRAS1;
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).
RC TISSUE=Pituitary;
RA Kemppainen R.J.;
RT "Identification of human pituitary Dexras1.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=10673050; DOI=10.1016/S0167-4781(99)00197-9;
RA Tu Y., Wu C.;
RT "Cloning, expression and characterization of a novel human Ras-related
RT protein that is regulated by glucocorticoid hormone.";
RL Biochim. Biophys. Acta 1489:452-456(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=10471929; DOI=10.1038/12867;
RA Cismowski M.J., Takesono A., Ma C., Lizano J.S., Xie X.,
RA Fuernkranz H., Lanier S.M., Duzic E.;
RT "Genetic screens in yeast to identify mammalian nonreceptor modulators
RT of G-protein signaling.";
RL Nat. Biotechnol. 17:878-883(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Cismowski M.J., Xie X., Duzic E.;
RT "Genomic sequence of the human ras-related G-protein activator AGS1.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=12818426; DOI=10.1016/S0167-4781(03)00079-4;
RA Kemppainen R.J., Cox E., Behrend E.N., Brogan M.D., Ammons J.M.;
RT "Identification of a glucocorticoid response element in the 3'-
RT flanking region of the human Dexras1 gene.";
RL Biochim. Biophys. Acta 1627:85-89(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, and Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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).
RN [11]
RP S-NITROSYLATION AT CYS-11, AND MUTAGENESIS OF CYS-11.
RX PubMed=12498886; DOI=10.1016/S1074-5521(02)00293-4;
RA Jaffrey S.R., Fang M., Snyder S.H.;
RT "Nitrosopeptide mapping: a novel methodology reveals s-nitrosylation
RT of dexras1 on a single cysteine residue.";
RL Chem. Biol. 9:1329-1335(2002).
CC -!- FUNCTION: Small GTPase. Negatively regulates the transcription
CC regulation activity of the APBB1/FE65-APP complex via its
CC interaction with APBB1/FE65 (By similarity).
CC -!- SUBUNIT: Forms a ternary complex with CAPON and NOS1. Component of
CC a complex, at least composed of APBB1, RASD1/DEXRAS1 and APP.
CC Interacts with APBB1/FE65 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side (Potential). Cytoplasm, perinuclear region (By similarity).
CC Nucleus (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y272-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y272-2; Sequence=VSP_046431, VSP_046432;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in a variety of tissues including
CC heart, cardiovascular tissues, brain, placenta, lung, liver,
CC skeletal muscle, kidney, pancreas, gastrointestinal and
CC reproductive tissues.
CC -!- INDUCTION: By dexamethasone.
CC -!- PTM: S-nitrosylation stimulates guanine-nucleotide exchange
CC activity.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. RasD family.
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DR EMBL; AF153192; AAD34621.1; -; mRNA.
DR EMBL; AF172846; AAF01364.1; -; mRNA.
DR EMBL; AF069506; AAD34206.1; -; mRNA.
DR EMBL; AF222979; AAG44256.1; -; Genomic_DNA.
DR EMBL; AF262018; AAF72997.1; -; Genomic_DNA.
DR EMBL; AF498923; AAM21071.1; -; mRNA.
DR EMBL; AK294073; BAG57415.1; -; mRNA.
DR EMBL; AK312796; BAG35656.1; -; mRNA.
DR EMBL; AC073621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471196; EAW55705.1; -; Genomic_DNA.
DR EMBL; BC018041; AAH18041.1; -; mRNA.
DR RefSeq; NP_001186918.1; NM_001199989.1.
DR RefSeq; NP_057168.1; NM_016084.4.
DR UniGene; Hs.25829; -.
DR ProteinModelPortal; Q9Y272; -.
DR SMR; Q9Y272; 23-194.
DR IntAct; Q9Y272; 3.
DR MINT; MINT-1437311; -.
DR STRING; 9606.ENSP00000225688; -.
DR PhosphoSite; Q9Y272; -.
DR DMDM; 38258272; -.
DR PaxDb; Q9Y272; -.
DR PRIDE; Q9Y272; -.
DR DNASU; 51655; -.
DR Ensembl; ENST00000225688; ENSP00000225688; ENSG00000108551.
DR Ensembl; ENST00000579152; ENSP00000463388; ENSG00000108551.
DR GeneID; 51655; -.
DR KEGG; hsa:51655; -.
DR UCSC; uc021trg.1; human.
DR CTD; 51655; -.
DR GeneCards; GC17M017397; -.
DR HGNC; HGNC:15828; RASD1.
DR HPA; HPA047896; -.
DR MIM; 605550; gene.
DR neXtProt; NX_Q9Y272; -.
DR PharmGKB; PA34236; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233973; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q9Y272; -.
DR KO; K07843; -.
DR OMA; FYREVEQ; -.
DR OrthoDB; EOG7M0NSN; -.
DR PhylomeDB; Q9Y272; -.
DR GeneWiki; RASD1; -.
DR GenomeRNAi; 51655; -.
DR NextBio; 55626; -.
DR PRO; PR:Q9Y272; -.
DR ArrayExpress; Q9Y272; -.
DR Bgee; Q9Y272; -.
DR CleanEx; HS_RASD1; -.
DR Genevestigator; Q9Y272; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Ensembl.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IEA:Ensembl.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00173; RAS; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
KW GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Nucleus; Prenylation; Reference proteome; S-nitrosylation.
FT CHAIN 1 278 Dexamethasone-induced Ras-related protein
FT 1.
FT /FTId=PRO_0000082717.
FT PROPEP 279 281 Removed in mature form (By similarity).
FT /FTId=PRO_0000281372.
FT NP_BIND 31 38 GTP (By similarity).
FT NP_BIND 78 82 GTP (By similarity).
FT NP_BIND 145 148 GTP (By similarity).
FT MOTIF 53 61 Effector region.
FT MOD_RES 11 11 S-nitrosocysteine.
FT MOD_RES 278 278 Cysteine methyl ester (By similarity).
FT LIPID 278 278 S-farnesyl cysteine (By similarity).
FT VAR_SEQ 96 122 GDVFILVFSLDNRDSFEEVQRLRQQIL -> DPRHQVLPQE
FT QNQGERGRAPGHLRQQG (in isoform 2).
FT /FTId=VSP_046431.
FT VAR_SEQ 123 281 Missing (in isoform 2).
FT /FTId=VSP_046432.
FT MUTAGEN 11 11 C->S: Suppresses NO-induced activation.
FT CONFLICT 118 118 R -> K (in Ref. 5; AAF72997).
SQ SEQUENCE 281 AA; 31642 MW; 06C3C4417E4A69BD CRC64;
MKLAAMIKKM CPSDSELSIP AKNCYRMVIL GSSKVGKTAI VSRFLTGRFE DAYTPTIEDF
HRKFYSIRGE VYQLDILDTS GNHPFPAMRR LSILTGDVFI LVFSLDNRDS FEEVQRLRQQ
ILDTKSCLKN KTKENVDVPL VICGNKGDRD FYREVDQREI EQLVGDDPQR CAYFEISAKK
NSSLDQMFRA LFAMAKLPSE MSPDLHRKVS VQYCDVLHKK ALRNKKLLRA GSGGGGGDPG
DAFGIVAPFA RRPSVHSDLM YIREKASAGS QAKDKERCVI S
//
ID RASD1_HUMAN Reviewed; 281 AA.
AC Q9Y272; B2R709; B4DFF4; Q9NYB4;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Dexamethasone-induced Ras-related protein 1;
DE AltName: Full=Activator of G-protein signaling 1;
DE Flags: Precursor;
GN Name=RASD1; Synonyms=AGS1, DEXRAS1;
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).
RC TISSUE=Pituitary;
RA Kemppainen R.J.;
RT "Identification of human pituitary Dexras1.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=10673050; DOI=10.1016/S0167-4781(99)00197-9;
RA Tu Y., Wu C.;
RT "Cloning, expression and characterization of a novel human Ras-related
RT protein that is regulated by glucocorticoid hormone.";
RL Biochim. Biophys. Acta 1489:452-456(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=10471929; DOI=10.1038/12867;
RA Cismowski M.J., Takesono A., Ma C., Lizano J.S., Xie X.,
RA Fuernkranz H., Lanier S.M., Duzic E.;
RT "Genetic screens in yeast to identify mammalian nonreceptor modulators
RT of G-protein signaling.";
RL Nat. Biotechnol. 17:878-883(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Cismowski M.J., Xie X., Duzic E.;
RT "Genomic sequence of the human ras-related G-protein activator AGS1.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=12818426; DOI=10.1016/S0167-4781(03)00079-4;
RA Kemppainen R.J., Cox E., Behrend E.N., Brogan M.D., Ammons J.M.;
RT "Identification of a glucocorticoid response element in the 3'-
RT flanking region of the human Dexras1 gene.";
RL Biochim. Biophys. Acta 1627:85-89(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, and Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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).
RN [11]
RP S-NITROSYLATION AT CYS-11, AND MUTAGENESIS OF CYS-11.
RX PubMed=12498886; DOI=10.1016/S1074-5521(02)00293-4;
RA Jaffrey S.R., Fang M., Snyder S.H.;
RT "Nitrosopeptide mapping: a novel methodology reveals s-nitrosylation
RT of dexras1 on a single cysteine residue.";
RL Chem. Biol. 9:1329-1335(2002).
CC -!- FUNCTION: Small GTPase. Negatively regulates the transcription
CC regulation activity of the APBB1/FE65-APP complex via its
CC interaction with APBB1/FE65 (By similarity).
CC -!- SUBUNIT: Forms a ternary complex with CAPON and NOS1. Component of
CC a complex, at least composed of APBB1, RASD1/DEXRAS1 and APP.
CC Interacts with APBB1/FE65 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side (Potential). Cytoplasm, perinuclear region (By similarity).
CC Nucleus (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y272-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y272-2; Sequence=VSP_046431, VSP_046432;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in a variety of tissues including
CC heart, cardiovascular tissues, brain, placenta, lung, liver,
CC skeletal muscle, kidney, pancreas, gastrointestinal and
CC reproductive tissues.
CC -!- INDUCTION: By dexamethasone.
CC -!- PTM: S-nitrosylation stimulates guanine-nucleotide exchange
CC activity.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. RasD family.
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DR EMBL; AF153192; AAD34621.1; -; mRNA.
DR EMBL; AF172846; AAF01364.1; -; mRNA.
DR EMBL; AF069506; AAD34206.1; -; mRNA.
DR EMBL; AF222979; AAG44256.1; -; Genomic_DNA.
DR EMBL; AF262018; AAF72997.1; -; Genomic_DNA.
DR EMBL; AF498923; AAM21071.1; -; mRNA.
DR EMBL; AK294073; BAG57415.1; -; mRNA.
DR EMBL; AK312796; BAG35656.1; -; mRNA.
DR EMBL; AC073621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471196; EAW55705.1; -; Genomic_DNA.
DR EMBL; BC018041; AAH18041.1; -; mRNA.
DR RefSeq; NP_001186918.1; NM_001199989.1.
DR RefSeq; NP_057168.1; NM_016084.4.
DR UniGene; Hs.25829; -.
DR ProteinModelPortal; Q9Y272; -.
DR SMR; Q9Y272; 23-194.
DR IntAct; Q9Y272; 3.
DR MINT; MINT-1437311; -.
DR STRING; 9606.ENSP00000225688; -.
DR PhosphoSite; Q9Y272; -.
DR DMDM; 38258272; -.
DR PaxDb; Q9Y272; -.
DR PRIDE; Q9Y272; -.
DR DNASU; 51655; -.
DR Ensembl; ENST00000225688; ENSP00000225688; ENSG00000108551.
DR Ensembl; ENST00000579152; ENSP00000463388; ENSG00000108551.
DR GeneID; 51655; -.
DR KEGG; hsa:51655; -.
DR UCSC; uc021trg.1; human.
DR CTD; 51655; -.
DR GeneCards; GC17M017397; -.
DR HGNC; HGNC:15828; RASD1.
DR HPA; HPA047896; -.
DR MIM; 605550; gene.
DR neXtProt; NX_Q9Y272; -.
DR PharmGKB; PA34236; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233973; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q9Y272; -.
DR KO; K07843; -.
DR OMA; FYREVEQ; -.
DR OrthoDB; EOG7M0NSN; -.
DR PhylomeDB; Q9Y272; -.
DR GeneWiki; RASD1; -.
DR GenomeRNAi; 51655; -.
DR NextBio; 55626; -.
DR PRO; PR:Q9Y272; -.
DR ArrayExpress; Q9Y272; -.
DR Bgee; Q9Y272; -.
DR CleanEx; HS_RASD1; -.
DR Genevestigator; Q9Y272; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Ensembl.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IEA:Ensembl.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00173; RAS; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
KW GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Nucleus; Prenylation; Reference proteome; S-nitrosylation.
FT CHAIN 1 278 Dexamethasone-induced Ras-related protein
FT 1.
FT /FTId=PRO_0000082717.
FT PROPEP 279 281 Removed in mature form (By similarity).
FT /FTId=PRO_0000281372.
FT NP_BIND 31 38 GTP (By similarity).
FT NP_BIND 78 82 GTP (By similarity).
FT NP_BIND 145 148 GTP (By similarity).
FT MOTIF 53 61 Effector region.
FT MOD_RES 11 11 S-nitrosocysteine.
FT MOD_RES 278 278 Cysteine methyl ester (By similarity).
FT LIPID 278 278 S-farnesyl cysteine (By similarity).
FT VAR_SEQ 96 122 GDVFILVFSLDNRDSFEEVQRLRQQIL -> DPRHQVLPQE
FT QNQGERGRAPGHLRQQG (in isoform 2).
FT /FTId=VSP_046431.
FT VAR_SEQ 123 281 Missing (in isoform 2).
FT /FTId=VSP_046432.
FT MUTAGEN 11 11 C->S: Suppresses NO-induced activation.
FT CONFLICT 118 118 R -> K (in Ref. 5; AAF72997).
SQ SEQUENCE 281 AA; 31642 MW; 06C3C4417E4A69BD CRC64;
MKLAAMIKKM CPSDSELSIP AKNCYRMVIL GSSKVGKTAI VSRFLTGRFE DAYTPTIEDF
HRKFYSIRGE VYQLDILDTS GNHPFPAMRR LSILTGDVFI LVFSLDNRDS FEEVQRLRQQ
ILDTKSCLKN KTKENVDVPL VICGNKGDRD FYREVDQREI EQLVGDDPQR CAYFEISAKK
NSSLDQMFRA LFAMAKLPSE MSPDLHRKVS VQYCDVLHKK ALRNKKLLRA GSGGGGGDPG
DAFGIVAPFA RRPSVHSDLM YIREKASAGS QAKDKERCVI S
//
MIM
605550
*RECORD*
*FIELD* NO
605550
*FIELD* TI
*605550 RAS PROTEIN, DEXAMETHASONE-INDUCED, 1; RASD1
;;DEXAMETHASONE-INDUCED RAS PROTEIN 1; DEXRAS1
read more*FIELD* TX
CLONING
Using differential display, Kemppainen and Behrend (1998) identified
Dexras1, a novel RAS superfamily gene induced by dexamethasone in AtT-20
cells (mouse-derived corticotroph tumor cells). The deduced 280-amino
acid mouse protein shares highest homology (36% identity) with human
RAP2B (179541). Northern blot analysis of mouse tissues detected
expression of Dexras1 in brain, heart, kidney, and liver.
By yeast 2-hybrid screening of a lung cDNA library with the third SH3
domain of NCK2 (604930) as bait, Tu and Wu (1999) isolated a cDNA
encoding RASD1, which they called DEXRAS1. The deduced 281-amino acid
protein, which is 98% identical to the mouse protein, contains a P loop,
guanine base-binding loops, and a C-terminal farnesylation site.
SDS-PAGE analysis detected a 33-kD protein, close to the predicted size.
Northern blot analysis revealed ubiquitous expression of a 5.0-kb RASD1
transcript, with highest levels in heart. Dexamethasone exposure
upregulated RASD1 expression.
Fang et al. (2000) isolated cDNAs encoding rat Dexras1 following a yeast
2-hybrid screen using the phosphotyrosine-binding domain of the neuronal
nitric oxide synthase (nNOS; 163731) adaptor protein CAPON (NOS1AP;
605551) as bait. Northern blot analysis in rat showed prominent
expression of Dexras1 mRNA in brain, with somewhat lesser levels in
testis and still lower levels in lung. Dexras1 contains a CAAX box,
suggesting that it may be prenylated. Fang et al. (2000) found that
Dexras1 was principally soluble, though a small fraction was detectable
in membrane fractions.
GENE FUNCTION
Fang et al. (2000) identified a selective interaction between CAPON and
DEXRAS1, a brain-enriched membrane of the RAS family of small monomeric
G proteins. Dexras1 was found to be S-nitrosylated by NO donors. Fang et
al. (2000) determined that Dexras1 is activated by NO donors as well as
by NMDA receptor-stimulated NOS in cortical neurons. The importance of
Dexras1 as a physiologic target of nNOS was established by the selective
decrease of Dexras1 activation, but not of Hras (190020) or 4 other RAS
family members, in the brains of mice harboring a targeted genomic
deletion of nNOS. Fang et al. (2000) showed that nNOS, CAPON, and
Dexras1 form a ternary complex that enhances the ability of nNOS to
activate Dexras1. They concluded that their findings identify DEXRAS1 as
a novel physiologic NO effector and suggest that anchoring of nNOS to
specific targets is a mechanism by which NO signaling is enhanced.
MAPPING
The International Radiation Hybrid Consortium mapped the RASD1 gene to
chromosome 17 (TMAP RH78076).
ANIMAL MODEL
Cheng et al. (2004) found that Rasd1-null mice were born at expected
mendelian frequency, were fertile, and appeared healthy. Histologic
analysis revealed no overt structural or morphologic defects in adult
Rasd1 -/- animals, and Rasd1 -/- mice were indistinguishable from
wildtype controls in most tests of behavior. However, Rasd1 deletion
altered circadian rhythms. Loss of Rads1 reduced photic entrainment by
eliminating pertussis-sensitive circadian response to
N-methyl-D-aspartate. In addition, the mutation potentiated nonphotic
responses to neuropeptide Y (NPY; 162640) and unmasked a nonphotic
response to arousal.
*FIELD* RF
1. Cheng, H.-Y. M.; Obrietan, K.; Cain, S. W.; Lee, B. Y.; Agostino,
P. V.; Joza, N. A.; Harrington, M. E.; Ralph, M. R.; Penninger, J.
M.: Dexras1 potentiates photic and suppresses nonphotic responses
of the circadian clock. Neuron 43: 715-728, 2004.
2. Fang, M.; Jaffrey, S. R.; Sawa, A.; Ye, K.; Luo, X.; Snyder, S.
H.: Dexras1: a G protein specifically coupled to neuronal nitric
oxide synthase via CAPON. Neuron 28: 183-193, 2000.
3. Kemppainen, R. J.; Behrend, E. N.: Dexamethasone rapidly induces
a novel Ras superfamily member-related gene in AtT-20 cells. J. Biol.
Chem. 273: 3129-3131, 1998.
4. Tu, Y.; Wu, C.: Cloning, expression and characterization of a
novel human Ras-related protein that is regulated by glucocorticoid
hormone. Biochim. Biophys. Acta 1489: 452-456, 1999.
*FIELD* CN
Patricia A. Hartz - updated: 3/25/2005
Paul J. Converse - updated: 1/17/2002
*FIELD* CD
Ada Hamosh: 1/12/2001
*FIELD* ED
carol: 10/17/2008
mgross: 3/25/2005
mgross: 1/17/2002
mgross: 11/27/2001
mgross: 1/16/2001
mgross: 1/12/2001
*RECORD*
*FIELD* NO
605550
*FIELD* TI
*605550 RAS PROTEIN, DEXAMETHASONE-INDUCED, 1; RASD1
;;DEXAMETHASONE-INDUCED RAS PROTEIN 1; DEXRAS1
read more*FIELD* TX
CLONING
Using differential display, Kemppainen and Behrend (1998) identified
Dexras1, a novel RAS superfamily gene induced by dexamethasone in AtT-20
cells (mouse-derived corticotroph tumor cells). The deduced 280-amino
acid mouse protein shares highest homology (36% identity) with human
RAP2B (179541). Northern blot analysis of mouse tissues detected
expression of Dexras1 in brain, heart, kidney, and liver.
By yeast 2-hybrid screening of a lung cDNA library with the third SH3
domain of NCK2 (604930) as bait, Tu and Wu (1999) isolated a cDNA
encoding RASD1, which they called DEXRAS1. The deduced 281-amino acid
protein, which is 98% identical to the mouse protein, contains a P loop,
guanine base-binding loops, and a C-terminal farnesylation site.
SDS-PAGE analysis detected a 33-kD protein, close to the predicted size.
Northern blot analysis revealed ubiquitous expression of a 5.0-kb RASD1
transcript, with highest levels in heart. Dexamethasone exposure
upregulated RASD1 expression.
Fang et al. (2000) isolated cDNAs encoding rat Dexras1 following a yeast
2-hybrid screen using the phosphotyrosine-binding domain of the neuronal
nitric oxide synthase (nNOS; 163731) adaptor protein CAPON (NOS1AP;
605551) as bait. Northern blot analysis in rat showed prominent
expression of Dexras1 mRNA in brain, with somewhat lesser levels in
testis and still lower levels in lung. Dexras1 contains a CAAX box,
suggesting that it may be prenylated. Fang et al. (2000) found that
Dexras1 was principally soluble, though a small fraction was detectable
in membrane fractions.
GENE FUNCTION
Fang et al. (2000) identified a selective interaction between CAPON and
DEXRAS1, a brain-enriched membrane of the RAS family of small monomeric
G proteins. Dexras1 was found to be S-nitrosylated by NO donors. Fang et
al. (2000) determined that Dexras1 is activated by NO donors as well as
by NMDA receptor-stimulated NOS in cortical neurons. The importance of
Dexras1 as a physiologic target of nNOS was established by the selective
decrease of Dexras1 activation, but not of Hras (190020) or 4 other RAS
family members, in the brains of mice harboring a targeted genomic
deletion of nNOS. Fang et al. (2000) showed that nNOS, CAPON, and
Dexras1 form a ternary complex that enhances the ability of nNOS to
activate Dexras1. They concluded that their findings identify DEXRAS1 as
a novel physiologic NO effector and suggest that anchoring of nNOS to
specific targets is a mechanism by which NO signaling is enhanced.
MAPPING
The International Radiation Hybrid Consortium mapped the RASD1 gene to
chromosome 17 (TMAP RH78076).
ANIMAL MODEL
Cheng et al. (2004) found that Rasd1-null mice were born at expected
mendelian frequency, were fertile, and appeared healthy. Histologic
analysis revealed no overt structural or morphologic defects in adult
Rasd1 -/- animals, and Rasd1 -/- mice were indistinguishable from
wildtype controls in most tests of behavior. However, Rasd1 deletion
altered circadian rhythms. Loss of Rads1 reduced photic entrainment by
eliminating pertussis-sensitive circadian response to
N-methyl-D-aspartate. In addition, the mutation potentiated nonphotic
responses to neuropeptide Y (NPY; 162640) and unmasked a nonphotic
response to arousal.
*FIELD* RF
1. Cheng, H.-Y. M.; Obrietan, K.; Cain, S. W.; Lee, B. Y.; Agostino,
P. V.; Joza, N. A.; Harrington, M. E.; Ralph, M. R.; Penninger, J.
M.: Dexras1 potentiates photic and suppresses nonphotic responses
of the circadian clock. Neuron 43: 715-728, 2004.
2. Fang, M.; Jaffrey, S. R.; Sawa, A.; Ye, K.; Luo, X.; Snyder, S.
H.: Dexras1: a G protein specifically coupled to neuronal nitric
oxide synthase via CAPON. Neuron 28: 183-193, 2000.
3. Kemppainen, R. J.; Behrend, E. N.: Dexamethasone rapidly induces
a novel Ras superfamily member-related gene in AtT-20 cells. J. Biol.
Chem. 273: 3129-3131, 1998.
4. Tu, Y.; Wu, C.: Cloning, expression and characterization of a
novel human Ras-related protein that is regulated by glucocorticoid
hormone. Biochim. Biophys. Acta 1489: 452-456, 1999.
*FIELD* CN
Patricia A. Hartz - updated: 3/25/2005
Paul J. Converse - updated: 1/17/2002
*FIELD* CD
Ada Hamosh: 1/12/2001
*FIELD* ED
carol: 10/17/2008
mgross: 3/25/2005
mgross: 1/17/2002
mgross: 11/27/2001
mgross: 1/16/2001
mgross: 1/12/2001