RASD1_HUMAN
ID RASD1_HUMAN Reviewed; 281 AA.
AC Q9Y272; B2R709; B4DFF4; Q9NYB4;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 182.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 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., Fuernkranz H.,
RA Lanier S.M., Duzic E.;
RT "Genetic screens in yeast to identify mammalian nonreceptor modulators of
RT 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'-flanking
RT 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 sequenced by
RT 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., 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 [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., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., 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 the
RT 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., 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 (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 project:
RT 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 of
RT 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 interaction
CC with APBB1/FE65 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a ternary complex with CAPON and NOS1. Component of a
CC complex, at least composed of APBB1, RASD1/DEXRAS1 and APP. Interacts
CC with APBB1/FE65 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y272; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-740818, EBI-11096309;
CC Q9Y272; P05067: APP; NbExp=3; IntAct=EBI-740818, EBI-77613;
CC Q9Y272; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-740818, EBI-10961624;
CC Q9Y272; Q86X02: CDR2L; NbExp=3; IntAct=EBI-740818, EBI-11063830;
CC Q9Y272; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-740818, EBI-3867333;
CC Q9Y272; Q96B26: EXOSC8; NbExp=3; IntAct=EBI-740818, EBI-371922;
CC Q9Y272; P61978: HNRNPK; NbExp=6; IntAct=EBI-740818, EBI-304185;
CC Q9Y272; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-740818, EBI-7060731;
CC Q9Y272; O43390-2: HNRNPR; NbExp=3; IntAct=EBI-740818, EBI-12236340;
CC Q9Y272; O75525: KHDRBS3; NbExp=3; IntAct=EBI-740818, EBI-722504;
CC Q9Y272; O76011: KRT34; NbExp=3; IntAct=EBI-740818, EBI-1047093;
CC Q9Y272; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-740818, EBI-11749135;
CC Q9Y272; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-740818, EBI-10171774;
CC Q9Y272; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-740818, EBI-10172052;
CC Q9Y272; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-740818, EBI-3957672;
CC Q9Y272; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-740818, EBI-3958099;
CC Q9Y272; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-740818, EBI-11962084;
CC Q9Y272; P43243: MATR3; NbExp=6; IntAct=EBI-740818, EBI-352602;
CC Q9Y272; Q99750: MDFI; NbExp=5; IntAct=EBI-740818, EBI-724076;
CC Q9Y272; Q13064: MKRN3; NbExp=3; IntAct=EBI-740818, EBI-2340269;
CC Q9Y272; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-740818, EBI-11522433;
CC Q9Y272; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-740818, EBI-22310682;
CC Q9Y272; Q9NQX1-2: PRDM5; NbExp=3; IntAct=EBI-740818, EBI-12859340;
CC Q9Y272; Q16825: PTPN21; NbExp=3; IntAct=EBI-740818, EBI-2860264;
CC Q9Y272; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-740818, EBI-3437896;
CC Q9Y272; P0DJD3-2: RBMY1A1; NbExp=3; IntAct=EBI-740818, EBI-11994018;
CC Q9Y272; Q15415: RBMY1J; NbExp=6; IntAct=EBI-740818, EBI-8642021;
CC Q9Y272; O94972: TRIM37; NbExp=3; IntAct=EBI-740818, EBI-741602;
CC Q9Y272; O00308: WWP2; NbExp=3; IntAct=EBI-740818, EBI-743923;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Nucleus {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Expressed in a variety of tissues including heart,
CC cardiovascular tissues, brain, placenta, lung, liver, skeletal muscle,
CC kidney, pancreas, gastrointestinal and reproductive tissues.
CC {ECO:0000269|PubMed:10673050, ECO:0000269|PubMed:12818426}.
CC -!- INDUCTION: By dexamethasone. {ECO:0000269|PubMed:10673050}.
CC -!- PTM: S-nitrosylation stimulates guanine-nucleotide exchange activity.
CC {ECO:0000269|PubMed:12498886}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. RasD family.
CC {ECO:0000305}.
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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 CCDS; CCDS11185.1; -. [Q9Y272-1]
DR CCDS; CCDS58519.1; -. [Q9Y272-2]
DR RefSeq; NP_001186918.1; NM_001199989.1. [Q9Y272-2]
DR RefSeq; NP_057168.1; NM_016084.4. [Q9Y272-1]
DR AlphaFoldDB; Q9Y272; -.
DR SMR; Q9Y272; -.
DR BioGRID; 119662; 38.
DR IntAct; Q9Y272; 32.
DR MINT; Q9Y272; -.
DR STRING; 9606.ENSP00000225688; -.
DR iPTMnet; Q9Y272; -.
DR PhosphoSitePlus; Q9Y272; -.
DR BioMuta; RASD1; -.
DR DMDM; 38258272; -.
DR MassIVE; Q9Y272; -.
DR PaxDb; Q9Y272; -.
DR PeptideAtlas; Q9Y272; -.
DR PRIDE; Q9Y272; -.
DR Antibodypedia; 25457; 81 antibodies from 21 providers.
DR DNASU; 51655; -.
DR Ensembl; ENST00000225688.4; ENSP00000225688.3; ENSG00000108551.5. [Q9Y272-1]
DR Ensembl; ENST00000579152.1; ENSP00000463388.1; ENSG00000108551.5. [Q9Y272-2]
DR GeneID; 51655; -.
DR KEGG; hsa:51655; -.
DR MANE-Select; ENST00000225688.4; ENSP00000225688.3; NM_016084.5; NP_057168.1.
DR UCSC; uc002gri.4; human. [Q9Y272-1]
DR CTD; 51655; -.
DR DisGeNET; 51655; -.
DR GeneCards; RASD1; -.
DR HGNC; HGNC:15828; RASD1.
DR HPA; ENSG00000108551; Tissue enhanced (pituitary).
DR MIM; 605550; gene.
DR neXtProt; NX_Q9Y272; -.
DR OpenTargets; ENSG00000108551; -.
DR PharmGKB; PA34236; -.
DR VEuPathDB; HostDB:ENSG00000108551; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000161274; -.
DR HOGENOM; CLU_041217_9_3_1; -.
DR InParanoid; Q9Y272; -.
DR OMA; FYREVEP; -.
DR OrthoDB; 1398885at2759; -.
DR PhylomeDB; Q9Y272; -.
DR TreeFam; TF316238; -.
DR PathwayCommons; Q9Y272; -.
DR SignaLink; Q9Y272; -.
DR BioGRID-ORCS; 51655; 17 hits in 1073 CRISPR screens.
DR ChiTaRS; RASD1; human.
DR GeneWiki; RASD1; -.
DR GenomeRNAi; 51655; -.
DR Pharos; Q9Y272; Tbio.
DR PRO; PR:Q9Y272; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y272; protein.
DR Bgee; ENSG00000108551; Expressed in pericardium and 175 other tissues.
DR Genevisible; Q9Y272; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016529; C:sarcoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
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-templated; IEA:Ensembl.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 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; Cytoplasm; GTP-binding; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Nucleus; Prenylation;
KW Reference proteome; S-nitrosylation.
FT CHAIN 1..278
FT /note="Dexamethasone-induced Ras-related protein 1"
FT /id="PRO_0000082717"
FT PROPEP 279..281
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281372"
FT MOTIF 53..61
FT /note="Effector region"
FT BINDING 31..38
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 78..82
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 145..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:12498886"
FT MOD_RES 278
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 278
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 96..122
FT /note="GDVFILVFSLDNRDSFEEVQRLRQQIL -> DPRHQVLPQEQNQGERGRAPG
FT HLRQQG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046431"
FT VAR_SEQ 123..281
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046432"
FT MUTAGEN 11
FT /note="C->S: Suppresses NO-induced activation."
FT /evidence="ECO:0000269|PubMed:12498886"
FT CONFLICT 118
FT /note="R -> K (in Ref. 5; AAF72997)"
FT /evidence="ECO:0000305"
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
