ID DRG1_HUMAN Reviewed; 367 AA.
AC Q9Y295; B2RDS8; Q6FGP8; Q8WW69; Q9UGF2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 205.
DE RecName: Full=Developmentally-regulated GTP-binding protein 1;
DE Short=DRG-1;
DE AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 3;
DE Short=NEDD-3;
DE AltName: Full=Translation factor GTPase DRG1;
DE Short=TRAFAC GTPase DRG1;
DE EC=3.6.5.- {ECO:0000305|PubMed:29915238};
GN Name=DRG1 {ECO:0000303|PubMed:29915238, ECO:0000312|HGNC:HGNC:3029};
GN Synonyms=NEDD3;
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], AND INTERACTION WITH TAL1.
RX PubMed=9824680; DOI=10.1016/s0167-4889(98)00129-3;
RA Zhao X.-F., Aplan P.D.;
RT "SCL binds the human homologue of DRG in vivo.";
RL Biochim. Biophys. Acta 1448:109-114(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10760581; DOI=10.1016/s0167-4781(00)00025-7;
RA Li B., Trueeb B.;
RT "DRG represents a family of two closely related GTP-binding proteins.";
RL Biochim. Biophys. Acta 1491:196-204(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Prostate;
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 [9]
RP INTERACTION WITH ZC3H15, AND SUBCELLULAR LOCATION.
RX PubMed=15676025; DOI=10.1111/j.1365-2443.2005.00825.x;
RA Ishikawa K., Azuma S., Ikawa S., Semba K., Inoue J.;
RT "Identification of DRG family regulatory proteins (DFRPs): specific
RT regulation of DRG1 and DRG2.";
RL Genes Cells 10:139-150(2005).
RN [10]
RP SUMOYLATION.
RX PubMed=17709345; DOI=10.1093/nar/gkm617;
RA Jakobs A., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R.;
RT "Ubc9 fusion-directed SUMOylation identifies constitutive and inducible
RT SUMOylation.";
RL Nucleic Acids Res. 35:E109-E109(2007).
RN [11]
RP PHOSPHORYLATION AT THR-100, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP INTERACTION WITH STK16.
RX PubMed=18184589; DOI=10.1016/j.str.2007.10.026;
RA Eswaran J., Bernad A., Ligos J.M., Guinea B., Debreczeni J.E., Sobott F.,
RA Parker S.A., Najmanovich R., Turk B.E., Knapp S.;
RT "Structure of the human protein kinase MPSK1 reveals an atypical activation
RT loop architecture.";
RL Structure 16:115-124(2008).
RN [12]
RP INTERACTION WITH ZC3H15 IN THE DRG1-DFRP1/ZC3H15 COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19819225; DOI=10.1016/j.bbrc.2009.10.003;
RA Ishikawa K., Akiyama T., Ito K., Semba K., Inoue J.;
RT "Independent stabilizations of polysomal Drg1/Dfrp1 complex and non-
RT polysomal Drg2/Dfrp2 complex in mammalian cells.";
RL Biochem. Biophys. Res. Commun. 390:552-556(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, MUTAGENESIS OF THR-100, AND DOMAIN.
RX PubMed=23711155; DOI=10.1111/febs.12356;
RA Perez-Arellano I., Spinola-Amilibia M., Bravo J.;
RT "Human Drg1 is a potassium-dependent GTPase enhanced by Lerepo4.";
RL FEBS J. 280:3647-3657(2013).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP FUNCTION, INTERACTION WITH MICROTUBULES, AND DOMAIN.
RX PubMed=28855639; DOI=10.1038/s41598-017-10088-5;
RA Schellhaus A.K., Moreno-Andres D., Chugh M., Yokoyama H., Moschopoulou A.,
RA De S., Bono F., Hipp K., Schaeffer E., Antonin W.;
RT "Developmentally Regulated GTP binding protein 1 (DRG1) controls
RT microtubule dynamics.";
RL Sci. Rep. 7:9996-9996(2017).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-22, INTERACTION WITH
RP JMJD7, CATALYTIC ACTIVITY, AND HYDROXYLATION AT LYS-22.
RX PubMed=29915238; DOI=10.1038/s41589-018-0071-y;
RA Markolovic S., Zhuang Q., Wilkins S.E., Eaton C.D., Abboud M.I., Katz M.J.,
RA McNeil H.E., Lesniak R.K., Hall C., Struwe W.B., Konietzny R., Davis S.,
RA Yang M., Ge W., Benesch J.L.P., Kessler B.M., Ratcliffe P.J., Cockman M.E.,
RA Fischer R., Wappner P., Chowdhury R., Coleman M.L., Schofield C.J.;
RT "The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC
RT GTPases.";
RL Nat. Chem. Biol. 14:688-695(2018).
RN [19]
RP STRUCTURE BY NMR OF 288-367.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the TGS domain of human developmentally-regulated
RT GTP-binding protein 1.";
RL Submitted (SEP-2007) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the conversion of GTP to GDP through hydrolysis of
CC the gamma-phosphate bond in GTP (PubMed:29915238, PubMed:23711155).
CC Appears to have an intrinsic GTPase activity that is stimulated by
CC ZC3H15/DFRP1 binding likely by increasing the affinity for the
CC potassium ions (PubMed:23711155). When hydroxylated at C-3 of 'Lys-22'
CC by JMJD7, may bind to RNA and play a role in translation
CC (PubMed:19819225, PubMed:29915238). Binds to microtubules and promotes
CC microtubule polymerization and stability that are required for mitotic
CC spindle assembly during prophase to anaphase transition. GTPase
CC activity is not necessary for these microtubule-related functions
CC (PubMed:28855639). {ECO:0000269|PubMed:19819225,
CC ECO:0000269|PubMed:23711155, ECO:0000269|PubMed:28855639,
CC ECO:0000269|PubMed:29915238}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:29915238};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000269|PubMed:29915238};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:23711155};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:23711155};
CC -!- ACTIVITY REGULATION: The GTPase activity is enhanced by potassium ions
CC as well as by DFRP1 binding. {ECO:0000269|PubMed:23711155}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for GTP {ECO:0000269|PubMed:23711155};
CC Vmax=3.59 nmol/min/mg enzyme {ECO:0000269|PubMed:23711155};
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:23711155};
CC Temperature dependence:
CC Optimum temperature is 42 degrees Celsius.
CC {ECO:0000269|PubMed:23711155};
CC -!- SUBUNIT: Interacts (via its C-terminal) with TAL1. Interacts with
CC DFRP1/ZC3H15; this interaction prevents DRG1 poly-ubiquitination and
CC degradation by the proteasome. DRG1-ZC3H15/DFRP1 complex co-sediments
CC with polysomes (PubMed:19819225). Interacts with STK16
CC (PubMed:18184589). Interacts with JMJD7 (PubMed:29915238). Associates
CC with microtubules either in an immobile or diffusive manner; in vitro
CC binds to tubulin lacking the negatively charged C-terminal domain
CC (PubMed:28855639). {ECO:0000269|PubMed:18184589,
CC ECO:0000269|PubMed:19819225, ECO:0000269|PubMed:28855639,
CC ECO:0000269|PubMed:29915238}.
CC -!- INTERACTION:
CC Q9Y295; P13569: CFTR; NbExp=9; IntAct=EBI-719554, EBI-349854;
CC Q9Y295; P38432: COIL; NbExp=3; IntAct=EBI-719554, EBI-945751;
CC Q9Y295; Q9Y295: DRG1; NbExp=2; IntAct=EBI-719554, EBI-719554;
CC Q9Y295; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-719554, EBI-739832;
CC Q9Y295; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-719554, EBI-16439278;
CC Q9Y295; Q8IXK0: PHC2; NbExp=4; IntAct=EBI-719554, EBI-713786;
CC Q9Y295; Q9H446: RWDD1; NbExp=8; IntAct=EBI-719554, EBI-748952;
CC Q9Y295; P12757: SKIL; NbExp=3; IntAct=EBI-719554, EBI-2902468;
CC Q9Y295; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-719554, EBI-2212028;
CC Q9Y295; O75716: STK16; NbExp=3; IntAct=EBI-719554, EBI-749295;
CC Q9Y295; Q8WU90: ZC3H15; NbExp=9; IntAct=EBI-719554, EBI-1042636;
CC Q9Y295; Q9WH76: M; Xeno; NbExp=3; IntAct=EBI-719554, EBI-10823897;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29915238}. Cytoplasm
CC {ECO:0000269|PubMed:15676025, ECO:0000269|PubMed:19819225,
CC ECO:0000269|PubMed:29915238}. Note=The DRG1-ZC3H15/DFRP1 complex
CC associates with polysomes.
CC -!- TISSUE SPECIFICITY: High levels in skeletal muscle, heart, and kidney.
CC Intermediate levels in liver, placenta and brain. Low levels in colon,
CC thymus, spleen, small intestine, lung and leukocytes.
CC {ECO:0000269|PubMed:10760581}.
CC -!- INDUCTION: By androgens.
CC -!- DOMAIN: The ThrRS, GTPase, SpoT (TGS) domain is not necessary for GTP
CC binding nor for the GTPase activity. It appears to play a regulatory
CC role favoring GTP hydrolysis mediated by DFRP1/ZC3H15.
CC {ECO:0000269|PubMed:23711155}.
CC -!- PTM: Sumoylated by UBE2I in response to MEKK1-mediated stimuli.
CC {ECO:0000269|PubMed:17709345}.
CC -!- PTM: Phosphorylated at Thr-100 by STK16. {ECO:0000269|PubMed:18184589}.
CC -!- PTM: Hydroxylated (with S stereochemistry) at C-3 of Lys-22 by JMJD7;
CC this modification hinders trypsin-catalyzed proteolysis in vitro.
CC {ECO:0000269|PubMed:29915238}.
CC -!- PTM: Polyubiquitinated; this modification induces proteolytic
CC degradation and is impaired by interaction with ZC3H15.
CC {ECO:0000250|UniProtKB:P32233}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. {ECO:0000255|PROSITE-ProRule:PRU01047}.
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DR EMBL; AF078103; AAD12240.1; -; mRNA.
DR EMBL; AJ005940; CAA06775.1; -; mRNA.
DR EMBL; CR542059; CAG46856.1; -; mRNA.
DR EMBL; CR456488; CAG30374.1; -; mRNA.
DR EMBL; BT007237; AAP35901.1; -; mRNA.
DR EMBL; AK315659; BAG38025.1; -; mRNA.
DR EMBL; AL096701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL096702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW59976.1; -; Genomic_DNA.
DR EMBL; BC019285; AAH19285.1; -; mRNA.
DR EMBL; BC020803; AAH20803.1; -; mRNA.
DR CCDS; CCDS13897.1; -.
DR RefSeq; NP_004138.1; NM_004147.3.
DR PDB; 2EKI; NMR; -; A=288-367.
DR PDBsum; 2EKI; -.
DR AlphaFoldDB; Q9Y295; -.
DR BMRB; Q9Y295; -.
DR SMR; Q9Y295; -.
DR BioGRID; 110810; 356.
DR IntAct; Q9Y295; 52.
DR MINT; Q9Y295; -.
DR STRING; 9606.ENSP00000329715; -.
DR GlyGen; Q9Y295; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y295; -.
DR MetOSite; Q9Y295; -.
DR PhosphoSitePlus; Q9Y295; -.
DR SwissPalm; Q9Y295; -.
DR BioMuta; DRG1; -.
DR DMDM; 6685390; -.
DR EPD; Q9Y295; -.
DR jPOST; Q9Y295; -.
DR MassIVE; Q9Y295; -.
DR MaxQB; Q9Y295; -.
DR PaxDb; 9606-ENSP00000329715; -.
DR PeptideAtlas; Q9Y295; -.
DR ProteomicsDB; 85703; -.
DR Pumba; Q9Y295; -.
DR Antibodypedia; 238; 263 antibodies from 28 providers.
DR DNASU; 4733; -.
DR Ensembl; ENST00000331457.9; ENSP00000329715.4; ENSG00000185721.13.
DR GeneID; 4733; -.
DR KEGG; hsa:4733; -.
DR MANE-Select; ENST00000331457.9; ENSP00000329715.4; NM_004147.4; NP_004138.1.
DR UCSC; uc003aku.4; human.
DR AGR; HGNC:3029; -.
DR CTD; 4733; -.
DR DisGeNET; 4733; -.
DR GeneCards; DRG1; -.
DR HGNC; HGNC:3029; DRG1.
DR HPA; ENSG00000185721; Tissue enhanced (testis).
DR MIM; 603952; gene.
DR neXtProt; NX_Q9Y295; -.
DR OpenTargets; ENSG00000185721; -.
DR PharmGKB; PA27483; -.
DR VEuPathDB; HostDB:ENSG00000185721; -.
DR eggNOG; KOG1487; Eukaryota.
DR GeneTree; ENSGT00940000153340; -.
DR HOGENOM; CLU_044997_0_0_1; -.
DR InParanoid; Q9Y295; -.
DR OMA; SAKHPGQ; -.
DR OrthoDB; 146471at2759; -.
DR PhylomeDB; Q9Y295; -.
DR TreeFam; TF105677; -.
DR PathwayCommons; Q9Y295; -.
DR Reactome; R-HSA-9629569; Protein hydroxylation.
DR SignaLink; Q9Y295; -.
DR SIGNOR; Q9Y295; -.
DR BioGRID-ORCS; 4733; 175 hits in 1140 CRISPR screens.
DR ChiTaRS; DRG1; human.
DR EvolutionaryTrace; Q9Y295; -.
DR GeneWiki; DRG1; -.
DR GenomeRNAi; 4733; -.
DR Pharos; Q9Y295; Tbio.
DR PRO; PR:Q9Y295; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9Y295; Protein.
DR Bgee; ENSG00000185721; Expressed in left testis and 208 other cell types or tissues.
DR ExpressionAtlas; Q9Y295; baseline and differential.
DR Genevisible; Q9Y295; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0030955; F:potassium ion binding; IDA:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
DR CDD; cd01896; DRG; 1.
DR CDD; cd17230; TGS_DRG1; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 6.10.140.1070; -; 2.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR045001; DRG.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR031662; GTP-binding_2.
DR InterPro; IPR006074; GTP1-OBG_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43127:SF1; DEVELOPMENTALLY-REGULATED GTP-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR43127; DEVELOPMENTALLY-REGULATED GTP-BINDING PROTEIN 2; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF16897; MMR_HSR1_Xtn; 1.
DR Pfam; PF02824; TGS; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS00905; GTP1_OBG; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; GTP-binding; Hydrolase;
KW Hydroxylation; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..367
FT /note="Developmentally-regulated GTP-binding protein 1"
FT /id="PRO_0000205424"
FT DOMAIN 65..290
FT /note="OBG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT DOMAIN 290..366
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228,
FT ECO:0000303|PubMed:23711155"
FT REGION 2..16
FT /note="Required for interaction with STK16"
FT /evidence="ECO:0000269|PubMed:18184589"
FT BINDING 71..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 117..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 248..251
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 22
FT /note="(3S)-3-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:29915238"
FT MOD_RES 100
FT /note="Phosphothreonine; by STK16"
FT /evidence="ECO:0000269|PubMed:18184589"
FT MUTAGEN 22
FT /note="K->A: Impairs JMJD7-mediated hydroxylation."
FT /evidence="ECO:0000269|PubMed:29915238"
FT MUTAGEN 100
FT /note="T->D: Reduces the GTPase activity."
FT /evidence="ECO:0000269|PubMed:23711155"
FT CONFLICT 91
FT /note="V -> A (in Ref. 8; AAH20803)"
FT /evidence="ECO:0000305"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:2EKI"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:2EKI"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:2EKI"
FT HELIX 318..325
FT /evidence="ECO:0007829|PDB:2EKI"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:2EKI"
FT STRAND 333..340
FT /evidence="ECO:0007829|PDB:2EKI"
FT STRAND 343..350
FT /evidence="ECO:0007829|PDB:2EKI"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:2EKI"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:2EKI"
SQ SEQUENCE 367 AA; 40542 MW; 4A177EA7C8E23005 CRC64;
MSSTLAKIAE IEAEMARTQK NKATAHHLGL LKARLAKLRR ELITPKGGGG GGPGEGFDVA
KTGDARIGFV GFPSVGKSTL LSNLAGVYSE VAAYEFTTLT TVPGVIRYKG AKIQLLDLPG
IIEGAKDGKG RGRQVIAVAR TCNLILIVLD VLKPLGHKKI IENELEGFGI RLNSKPPNIG
FKKKDKGGIN LTATCPQSEL DAETVKSILA EYKIHNADVT LRSDATADDL IDVVEGNRVY
IPCIYVLNKI DQISIEELDI IYKVPHCVPI SAHHRWNFDD LLEKIWDYLK LVRIYTKPKG
QLPDYTSPVV LPYSRTTVED FCMKIHKNLI KEFKYALVWG LSVKHNPQKV GKDHTLEDED
VIQIVKK
//
