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DIRA3_HUMAN
ID   DIRA3_HUMAN             Reviewed;         229 AA.
AC   O95661; B3KMP3;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 187.
DE   RecName: Full=GTP-binding protein Di-Ras3;
DE   AltName: Full=Distinct subgroup of the Ras family member 3;
DE   AltName: Full=Rho-related GTP-binding protein RhoI;
DE   Flags: Precursor;
GN   Name=DIRAS3; Synonyms=ARHI, NOEY2, RHOI;
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].
RX   PubMed=9874798; DOI=10.1073/pnas.96.1.214;
RA   Yu Y.H., Xu F.J., Peng H., Fang X., Zhao S., Li Y., Cuevas B., Kuo W.-L.,
RA   Gray J.W., Siciliano M., Mills G.B., Bast R.C. Jr.;
RT   "NOEY2 (ARHI), an imprinted putative tumor suppressor gene in ovarian and
RT   breast carcinomas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:214-219(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11418188; DOI=10.1016/s0167-4781(01)00226-3;
RA   Luo R.Z., Peng H., Xu F., Bao J., Pang Y., Pershad R., Issa J.P.,
RA   Liao W.S., Bast R.C. Jr., Yu Y.;
RT   "Genomic structure and promoter characterization of an imprinted tumor
RT   suppressor gene ARHI.";
RL   Biochim. Biophys. Acta 1519:216-222(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow;
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).
CC   -!- INTERACTION:
CC       O95661; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-6139214, EBI-16439278;
CC       O95661; P40763: STAT3; NbExp=3; IntAct=EBI-6139214, EBI-518675;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in normal ovarian and breast epithelial
CC       cells but not in ovarian and breast cancers.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Di-Ras family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=NOEY2 entry;
CC       URL="https://en.wikipedia.org/wiki/NOEY2";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/DIRAS3ID702ch1p31.html";
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DR   EMBL; U96750; AAD03164.1; -; mRNA.
DR   EMBL; AF202543; AAG35625.1; -; Genomic_DNA.
DR   EMBL; CR541870; CAG46668.1; -; mRNA.
DR   EMBL; CR541892; CAG46690.1; -; mRNA.
DR   EMBL; AK021882; BAG51055.1; -; mRNA.
DR   EMBL; AL157407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX06483.1; -; Genomic_DNA.
DR   EMBL; BC005362; AAH05362.1; -; mRNA.
DR   CCDS; CCDS641.1; -.
DR   RefSeq; NP_004666.1; NM_004675.3.
DR   RefSeq; XP_016858262.1; XM_017002773.1.
DR   PDB; 6NAZ; X-ray; 3.08 A; A=92-112.
DR   PDBsum; 6NAZ; -.
DR   AlphaFoldDB; O95661; -.
DR   SMR; O95661; -.
DR   BioGRID; 114534; 261.
DR   IntAct; O95661; 18.
DR   MINT; O95661; -.
DR   STRING; 9606.ENSP00000360020; -.
DR   iPTMnet; O95661; -.
DR   PhosphoSitePlus; O95661; -.
DR   BioMuta; DIRAS3; -.
DR   MassIVE; O95661; -.
DR   PaxDb; O95661; -.
DR   PeptideAtlas; O95661; -.
DR   PRIDE; O95661; -.
DR   ProteomicsDB; 50981; -.
DR   Antibodypedia; 33414; 179 antibodies from 26 providers.
DR   DNASU; 9077; -.
DR   Ensembl; ENST00000370981.3; ENSP00000360020.1; ENSG00000162595.8.
DR   Ensembl; ENST00000646789.1; ENSP00000495736.1; ENSG00000162595.8.
DR   Ensembl; ENST00000691269.1; ENSP00000509833.1; ENSG00000162595.8.
DR   Ensembl; ENST00000693623.1; ENSP00000510070.1; ENSG00000162595.8.
DR   GeneID; 9077; -.
DR   KEGG; hsa:9077; -.
DR   MANE-Select; ENST00000646789.1; ENSP00000495736.1; NM_004675.5; NP_004666.1.
DR   UCSC; uc001ded.4; human.
DR   CTD; 9077; -.
DR   DisGeNET; 9077; -.
DR   GeneCards; DIRAS3; -.
DR   HGNC; HGNC:687; DIRAS3.
DR   HPA; ENSG00000162595; Tissue enhanced (brain, ovary, pituitary gland).
DR   MIM; 605193; gene.
DR   neXtProt; NX_O95661; -.
DR   OpenTargets; ENSG00000162595; -.
DR   PharmGKB; PA24980; -.
DR   VEuPathDB; HostDB:ENSG00000162595; -.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000164094; -.
DR   HOGENOM; CLU_041217_9_8_1; -.
DR   InParanoid; O95661; -.
DR   OMA; SCFGFKE; -.
DR   OrthoDB; 1218505at2759; -.
DR   PhylomeDB; O95661; -.
DR   TreeFam; TF313014; -.
DR   PathwayCommons; O95661; -.
DR   SignaLink; O95661; -.
DR   BioGRID-ORCS; 9077; 42 hits in 1075 CRISPR screens.
DR   GenomeRNAi; 9077; -.
DR   Pharos; O95661; Tbio.
DR   PRO; PR:O95661; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O95661; protein.
DR   Bgee; ENSG00000162595; Expressed in adenohypophysis and 132 other tissues.
DR   Genevisible; O95661; HS.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
DR   GO; GO:0006349; P:regulation of gene expression by genomic imprinting; TAS:ProtInc.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
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; IPR020849; Small_GTPase_Ras-type.
DR   PANTHER; PTHR24070; PTHR24070; 1.
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   3D-structure; Cell membrane; GTP-binding; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN           1..226
FT                   /note="GTP-binding protein Di-Ras3"
FT                   /id="PRO_0000191654"
FT   PROPEP          227..229
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000370781"
FT   MOTIF           66..74
FT                   /note="Effector region"
FT                   /evidence="ECO:0000255"
FT   BINDING         44..51
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT   BINDING         63..69
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT   BINDING         91..95
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT   BINDING         152..155
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT   BINDING         182..183
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT   MOD_RES         226
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           226
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   HELIX           102..108
FT                   /evidence="ECO:0007829|PDB:6NAZ"
SQ   SEQUENCE   229 AA;  25861 MW;  16AEA60089A91B3F CRC64;
     MGNASFGSKE QKLLKRLRLL PALLILRAFK PHRKIRDYRV VVVGTAGVGK STLLHKWASG
     NFRHEYLPTI ENTYCQLLGC SHGVLSLHIT DSKSGDGNRA LQRHVIARGH AFVLVYSVTK
     KETLEELKAF YELICKIKGN NLHKFPIVLV GNKSDDTHRE VALNDGATCA MEWNCAFMEI
     SAKTDVNVQE LFHMLLNYKK KPTTGLQEPE KKSQMPNTTE KLLDKCIIM
 
 
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