DIRA2_HUMAN
ID DIRA2_HUMAN Reviewed; 199 AA.
AC Q96HU8; B3KVM2;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=GTP-binding protein Di-Ras2;
DE AltName: Full=Distinct subgroup of the Ras family member 2;
DE Flags: Precursor;
GN Name=DIRAS2;
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], GTPASE ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12194967; DOI=10.1074/jbc.m202150200;
RA Kontani K., Tada M., Ogawa T., Okai T., Saito K., Araki Y., Katada T.;
RT "Di-Ras, a distinct subgroup of ras family GTPases with unique biochemical
RT properties.";
RL J. Biol. Chem. 277:41070-41078(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 5-176 IN COMPLEX WITH GTP ANALOG.
RG Structural genomics consortium (SGC);
RT "Crystal structure of DIRAS2.";
RL Submitted (DEC-2005) to the PDB data bank.
CC -!- FUNCTION: Displays low GTPase activity and exists predominantly in the
CC GTP-bound form. {ECO:0000269|PubMed:12194967}.
CC -!- INTERACTION:
CC Q96HU8; P52306-5: RAP1GDS1; NbExp=3; IntAct=EBI-911391, EBI-12832744;
CC Q96HU8; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-911391, EBI-10226430;
CC Q96HU8; Q9H3U1: UNC45A; NbExp=3; IntAct=EBI-911391, EBI-1048763;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC {ECO:0000269|PubMed:12194967}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Di-Ras family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB076889; BAC01116.1; -; mRNA.
DR EMBL; AK122986; BAG53834.1; -; mRNA.
DR EMBL; AL353619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62780.1; -; Genomic_DNA.
DR EMBL; BC008065; AAH08065.1; -; mRNA.
DR CCDS; CCDS6687.1; -.
DR RefSeq; NP_060064.2; NM_017594.4.
DR PDB; 2ERX; X-ray; 1.65 A; A/B=5-176.
DR PDB; 6NAZ; X-ray; 3.08 A; A=1-61, A=83-199.
DR PDBsum; 2ERX; -.
DR PDBsum; 6NAZ; -.
DR AlphaFoldDB; Q96HU8; -.
DR SMR; Q96HU8; -.
DR BioGRID; 120143; 13.
DR IntAct; Q96HU8; 12.
DR MINT; Q96HU8; -.
DR STRING; 9606.ENSP00000364919; -.
DR GlyGen; Q96HU8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96HU8; -.
DR PhosphoSitePlus; Q96HU8; -.
DR BioMuta; DIRAS2; -.
DR DMDM; 62286631; -.
DR EPD; Q96HU8; -.
DR jPOST; Q96HU8; -.
DR MassIVE; Q96HU8; -.
DR MaxQB; Q96HU8; -.
DR PaxDb; Q96HU8; -.
DR PeptideAtlas; Q96HU8; -.
DR PRIDE; Q96HU8; -.
DR ProteomicsDB; 76787; -.
DR Antibodypedia; 28067; 137 antibodies from 22 providers.
DR DNASU; 54769; -.
DR Ensembl; ENST00000375765.5; ENSP00000364919.3; ENSG00000165023.7.
DR GeneID; 54769; -.
DR KEGG; hsa:54769; -.
DR MANE-Select; ENST00000375765.5; ENSP00000364919.3; NM_017594.5; NP_060064.2.
DR UCSC; uc004aqx.2; human.
DR CTD; 54769; -.
DR DisGeNET; 54769; -.
DR GeneCards; DIRAS2; -.
DR HGNC; HGNC:19323; DIRAS2.
DR HPA; ENSG00000165023; Group enriched (brain, retina).
DR MIM; 607863; gene.
DR neXtProt; NX_Q96HU8; -.
DR OpenTargets; ENSG00000165023; -.
DR PharmGKB; PA134958969; -.
DR VEuPathDB; HostDB:ENSG00000165023; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000158196; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q96HU8; -.
DR OMA; CKETNGA; -.
DR OrthoDB; 1218505at2759; -.
DR PhylomeDB; Q96HU8; -.
DR TreeFam; TF313014; -.
DR PathwayCommons; Q96HU8; -.
DR SignaLink; Q96HU8; -.
DR BioGRID-ORCS; 54769; 11 hits in 1069 CRISPR screens.
DR ChiTaRS; DIRAS2; human.
DR EvolutionaryTrace; Q96HU8; -.
DR GenomeRNAi; 54769; -.
DR Pharos; Q96HU8; Tbio.
DR PRO; PR:Q96HU8; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q96HU8; protein.
DR Bgee; ENSG00000165023; Expressed in cerebellar vermis and 130 other tissues.
DR ExpressionAtlas; Q96HU8; baseline and differential.
DR Genevisible; Q96HU8; HS.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; Phosphoprotein; Prenylation;
KW Reference proteome.
FT CHAIN 1..196
FT /note="GTP-binding protein Di-Ras2"
FT /id="PRO_0000191650"
FT PROPEP 197..199
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370777"
FT MOTIF 36..44
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:2ERX"
FT BINDING 33..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:2ERX"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:2ERX"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:2ERX"
FT BINDING 152..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:2ERX"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PR73"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PR73"
FT MOD_RES 196
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 196
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:2ERX"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:2ERX"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:6NAZ"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:2ERX"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:2ERX"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:2ERX"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:2ERX"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:2ERX"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:2ERX"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:2ERX"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:2ERX"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:2ERX"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:2ERX"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:2ERX"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:2ERX"
SQ SEQUENCE 199 AA; 22485 MW; 429D17026CC3EADC CRC64;
MPEQSNDYRV AVFGAGGVGK SSLVLRFVKG TFRESYIPTV EDTYRQVISC DKSICTLQIT
DTTGSHQFPA MQRLSISKGH AFILVYSITS RQSLEELKPI YEQICEIKGD VESIPIMLVG
NKCDESPSRE VQSSEAEALA RTWKCAFMET SAKLNHNVKE LFQELLNLEK RRTVSLQIDG
KKSKQQKRKE KLKGKCVIM
