true
2000-05-30
2024-03-27
205
DRG1_HUMAN
SCL binds the human homologue of DRG in vivo.
Zhao X.-F.
Aplan P.D.
doi:10.1016/s0167-4889(98)00129-3
1998
Biochim. Biophys. Acta
1448
109-114
NUCLEOTIDE SEQUENCE [MRNA]
INTERACTION WITH TAL1
DRG represents a family of two closely related GTP-binding proteins.
Li B.
Trueeb B.
doi:10.1016/s0167-4781(00)00025-7
2000
Biochim. Biophys. Acta
1491
196-204
NUCLEOTIDE SEQUENCE [MRNA]
TISSUE SPECIFICITY
A genome annotation-driven approach to cloning the human ORFeome.
Collins J.E.
Wright C.L.
Edwards C.A.
Davis M.P.
Grinham J.A.
Cole C.G.
Goward M.E.
Aguado B.
Mallya M.
Mokrab Y.
Huckle E.J.
Beare D.M.
Dunham I.
doi:10.1186/gb-2004-5-10-r84
2004
Genome Biol.
5
R84.1-R84.11
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
Cloning of human full-length CDSs in BD Creator(TM) system donor vector.
Kalnine N.
Chen X.
Rolfs A.
Halleck A.
Hines L.
Eisenstein S.
Koundinya M.
Raphael J.
Moreira D.
Kelley T.
LaBaer J.
Lin Y.
Phelan M.
Farmer A.
2003-05
EMBL/GenBank/DDBJ
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
Complete sequencing and characterization of 21,243 full-length human cDNAs.
Ota T.
Suzuki Y.
Nishikawa T.
Otsuki T.
Sugiyama T.
Irie R.
Wakamatsu A.
Hayashi K.
Sato H.
Nagai K.
Kimura K.
Makita H.
Sekine M.
Obayashi M.
Nishi T.
Shibahara T.
Tanaka T.
Ishii S.
Yamamoto J.
Saito K.
Kawai Y.
Isono Y.
Nakamura Y.
Nagahari K.
Murakami K.
Yasuda T.
Iwayanagi T.
Wagatsuma M.
Shiratori A.
Sudo H.
Hosoiri T.
Kaku Y.
Kodaira H.
Kondo H.
Sugawara M.
Takahashi M.
Kanda K.
Yokoi T.
Furuya T.
Kikkawa E.
Omura Y.
Abe K.
Kamihara K.
Katsuta N.
Sato K.
Tanikawa M.
Yamazaki M.
Ninomiya K.
Ishibashi T.
Yamashita H.
Murakawa K.
Fujimori K.
Tanai H.
Kimata M.
Watanabe M.
Hiraoka S.
Chiba Y.
Ishida S.
Ono Y.
Takiguchi S.
Watanabe S.
Yosida M.
Hotuta T.
Kusano J.
Kanehori K.
Takahashi-Fujii A.
Hara H.
Tanase T.-O.
Nomura Y.
Togiya S.
Komai F.
Hara R.
Takeuchi K.
Arita M.
Imose N.
Musashino K.
Yuuki H.
Oshima A.
Sasaki N.
Aotsuka S.
Yoshikawa Y.
Matsunawa H.
Ichihara T.
Shiohata N.
Sano S.
Moriya S.
Momiyama H.
Satoh N.
Takami S.
Terashima Y.
Suzuki O.
Nakagawa S.
Senoh A.
Mizoguchi H.
Goto Y.
Shimizu F.
Wakebe H.
Hishigaki H.
Watanabe T.
Sugiyama A.
Takemoto M.
Kawakami B.
Yamazaki M.'
Watanabe K.
Kumagai A.
Itakura S.
Fukuzumi Y.
Fujimori Y.
Komiyama M.
Tashiro H.
Tanigami A.
Fujiwara T.
Ono T.
Yamada K.
Fujii Y.
Ozaki K.
Hirao M.
Ohmori Y.
Kawabata A.
Hikiji T.
Kobatake N.
Inagaki H.
Ikema Y.
Okamoto S.
Okitani R.
Kawakami T.
Noguchi S.
Itoh T.
Shigeta K.
Senba T.
Matsumura K.
Nakajima Y.
Mizuno T.
Morinaga M.
Sasaki M.
Togashi T.
Oyama M.
Hata H.
Watanabe M.'
Komatsu T.
Mizushima-Sugano J.
Satoh T.
Shirai Y.
Takahashi Y.
Nakagawa K.
Okumura K.
Nagase T.
Nomura N.
Kikuchi H.
Masuho Y.
Yamashita R.
Nakai K.
Yada T.
Nakamura Y.'
Ohara O.
Isogai T.
Sugano S.
doi:10.1038/ng1285
2004
Nat. Genet.
36
40-45
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
Testis
The DNA sequence of human chromosome 22.
Dunham I.
Hunt A.R.
Collins J.E.
Bruskiewich R.
Beare D.M.
Clamp M.
Smink L.J.
Ainscough R.
Almeida J.P.
Babbage A.K.
Bagguley C.
Bailey J.
Barlow K.F.
Bates K.N.
Beasley O.P.
Bird C.P.
Blakey S.E.
Bridgeman A.M.
Buck D.
Burgess J.
Burrill W.D.
Burton J.
Carder C.
Carter N.P.
Chen Y.
Clark G.
Clegg S.M.
Cobley V.E.
Cole C.G.
Collier R.E.
Connor R.
Conroy D.
Corby N.R.
Coville G.J.
Cox A.V.
Davis J.
Dawson E.
Dhami P.D.
Dockree C.
Dodsworth S.J.
Durbin R.M.
Ellington A.G.
Evans K.L.
Fey J.M.
Fleming K.
French L.
Garner A.A.
Gilbert J.G.R.
Goward M.E.
Grafham D.V.
Griffiths M.N.D.
Hall C.
Hall R.E.
Hall-Tamlyn G.
Heathcott R.W.
Ho S.
Holmes S.
Hunt S.E.
Jones M.C.
Kershaw J.
Kimberley A.M.
King A.
Laird G.K.
Langford C.F.
Leversha M.A.
Lloyd C.
Lloyd D.M.
Martyn I.D.
Mashreghi-Mohammadi M.
Matthews L.H.
Mccann O.T.
Mcclay J.
Mclaren S.
McMurray A.A.
Milne S.A.
Mortimore B.J.
Odell C.N.
Pavitt R.
Pearce A.V.
Pearson D.
Phillimore B.J.C.T.
Phillips S.H.
Plumb R.W.
Ramsay H.
Ramsey Y.
Rogers L.
Ross M.T.
Scott C.E.
Sehra H.K.
Skuce C.D.
Smalley S.
Smith M.L.
Soderlund C.
Spragon L.
Steward C.A.
Sulston J.E.
Swann R.M.
Vaudin M.
Wall M.
Wallis J.M.
Whiteley M.N.
Willey D.L.
Williams L.
Williams S.A.
Williamson H.
Wilmer T.E.
Wilming L.
Wright C.L.
Hubbard T.
Bentley D.R.
Beck S.
Rogers J.
Shimizu N.
Minoshima S.
Kawasaki K.
Sasaki T.
Asakawa S.
Kudoh J.
Shintani A.
Shibuya K.
Yoshizaki Y.
Aoki N.
Mitsuyama S.
Roe B.A.
Chen F.
Chu L.
Crabtree J.
Deschamps S.
Do A.
Do T.
Dorman A.
Fang F.
Fu Y.
Hu P.
Hua A.
Kenton S.
Lai H.
Lao H.I.
Lewis J.
Lewis S.
Lin S.-P.
Loh P.
Malaj E.
Nguyen T.
Pan H.
Phan S.
Qi S.
Qian Y.
Ray L.
Ren Q.
Shaull S.
Sloan D.
Song L.
Wang Q.
Wang Y.
Wang Z.
White J.
Willingham D.
Wu H.
Yao Z.
Zhan M.
Zhang G.
Chissoe S.
Murray J.
Miller N.
Minx P.
Fulton R.
Johnson D.
Bemis G.
Bentley D.
Bradshaw H.
Bourne S.
Cordes M.
Du Z.
Fulton L.
Goela D.
Graves T.
Hawkins J.
Hinds K.
Kemp K.
Latreille P.
Layman D.
Ozersky P.
Rohlfing T.
Scheet P.
Walker C.
Wamsley A.
Wohldmann P.
Pepin K.
Nelson J.
Korf I.
Bedell J.A.
Hillier L.W.
Mardis E.
Waterston R.
Wilson R.
Emanuel B.S.
Shaikh T.
Kurahashi H.
Saitta S.
Budarf M.L.
McDermid H.E.
Johnson A.
Wong A.C.C.
Morrow B.E.
Edelmann L.
Kim U.J.
Shizuya H.
Simon M.I.
Dumanski J.P.
Peyrard M.
Kedra D.
Seroussi E.
Fransson I.
Tapia I.
Bruder C.E.
O'Brien K.P.
Wilkinson P.
Bodenteich A.
Hartman K.
Hu X.
Khan A.S.
Lane L.
Tilahun Y.
Wright H.
doi:10.1038/990031
1999
Nature
402
489-495
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
Mural R.J.
Istrail S.
Sutton G.G.
Florea L.
Halpern A.L.
Mobarry C.M.
Lippert R.
Walenz B.
Shatkay H.
Dew I.
Miller J.R.
Flanigan M.J.
Edwards N.J.
Bolanos R.
Fasulo D.
Halldorsson B.V.
Hannenhalli S.
Turner R.
Yooseph S.
Lu F.
Nusskern D.R.
Shue B.C.
Zheng X.H.
Zhong F.
Delcher A.L.
Huson D.H.
Kravitz S.A.
Mouchard L.
Reinert K.
Remington K.A.
Clark A.G.
Waterman M.S.
Eichler E.E.
Adams M.D.
Hunkapiller M.W.
Myers E.W.
Venter J.C.
2005-07
EMBL/GenBank/DDBJ
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team
doi:10.1101/gr.2596504
2004
Genome Res.
14
2121-2127
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
Lung
Prostate
Identification of DRG family regulatory proteins (DFRPs): specific regulation of DRG1 and DRG2.
Ishikawa K.
Azuma S.
Ikawa S.
Semba K.
Inoue J.
doi:10.1111/j.1365-2443.2005.00825.x
2005
Genes Cells
10
139-150
INTERACTION WITH ZC3H15
SUBCELLULAR LOCATION
Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation.
Jakobs A.
Himstedt F.
Funk M.
Korn B.
Gaestel M.
Niedenthal R.
doi:10.1093/nar/gkm617
2007
Nucleic Acids Res.
35
E109
SUMOYLATION
Structure of the human protein kinase MPSK1 reveals an atypical activation loop architecture.
Eswaran J.
Bernad A.
Ligos J.M.
Guinea B.
Debreczeni J.E.
Sobott F.
Parker S.A.
Najmanovich R.
Turk B.E.
Knapp S.
doi:10.1016/j.str.2007.10.026
2008
Structure
16
115-124
PHOSPHORYLATION AT THR-100
IDENTIFICATION BY MASS SPECTROMETRY
INTERACTION WITH STK16
Independent stabilizations of polysomal Drg1/Dfrp1 complex and non-polysomal Drg2/Dfrp2 complex in mammalian cells.
Ishikawa K.
Akiyama T.
Ito K.
Semba K.
Inoue J.
doi:10.1016/j.bbrc.2009.10.003
2009
Biochem. Biophys. Res. Commun.
390
552-556
INTERACTION WITH ZC3H15 IN THE DRG1-DFRP1/ZC3H15 COMPLEX
SUBCELLULAR LOCATION
Initial characterization of the human central proteome.
Burkard T.R.
Planyavsky M.
Kaupe I.
Breitwieser F.P.
Buerckstuemmer T.
Bennett K.L.
Superti-Furga G.
Colinge J.
doi:10.1186/1752-0509-5-17
2011
BMC Syst. Biol.
5
17
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
Van Damme P.
Lasa M.
Polevoda B.
Gazquez C.
Elosegui-Artola A.
Kim D.S.
De Juan-Pardo E.
Demeyer K.
Hole K.
Larrea E.
Timmerman E.
Prieto J.
Arnesen T.
Sherman F.
Gevaert K.
Aldabe R.
doi:10.1073/pnas.1210303109
2012
Proc. Natl. Acad. Sci. U.S.A.
109
12449-12454
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
Human Drg1 is a potassium-dependent GTPase enhanced by Lerepo4.
Perez-Arellano I.
Spinola-Amilibia M.
Bravo J.
doi:10.1111/febs.12356
2013
FEBS J.
280
3647-3657
FUNCTION
CATALYTIC ACTIVITY
BIOPHYSICOCHEMICAL PROPERTIES
ACTIVITY REGULATION
MUTAGENESIS OF THR-100
DOMAIN
N-terminome analysis of the human mitochondrial proteome.
Vaca Jacome A.S.
Rabilloud T.
Schaeffer-Reiss C.
Rompais M.
Ayoub D.
Lane L.
Bairoch A.
Van Dorsselaer A.
Carapito C.
doi:10.1002/pmic.201400617
2015
Proteomics
15
2519-2524
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
Developmentally Regulated GTP binding protein 1 (DRG1) controls microtubule dynamics.
Schellhaus A.K.
Moreno-Andres D.
Chugh M.
Yokoyama H.
Moschopoulou A.
De S.
Bono F.
Hipp K.
Schaeffer E.
Antonin W.
doi:10.1038/s41598-017-10088-5
2017
Sci. Rep.
7
9996
FUNCTION
INTERACTION WITH MICROTUBULES
DOMAIN
The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases.
Markolovic S.
Zhuang Q.
Wilkins S.E.
Eaton C.D.
Abboud M.I.
Katz M.J.
McNeil H.E.
Lesniak R.K.
Hall C.
Struwe W.B.
Konietzny R.
Davis S.
Yang M.
Ge W.
Benesch J.L.P.
Kessler B.M.
Ratcliffe P.J.
Cockman M.E.
Fischer R.
Wappner P.
Chowdhury R.
Coleman M.L.
Schofield C.J.
doi:10.1038/s41589-018-0071-y
2018
Nat. Chem. Biol.
14
688-695
FUNCTION
SUBCELLULAR LOCATION
MUTAGENESIS OF LYS-22
INTERACTION WITH JMJD7
CATALYTIC ACTIVITY
HYDROXYLATION AT LYS-22
Solution structures of the TGS domain of human developmentally-regulated GTP-binding protein 1.
RIKEN structural genomics initiative (RSGI)
2007-09
PDB
STRUCTURE BY NMR OF 288-367
A=288-367
356
52
1 site, 1 O-linked glycan (1 site)
263 antibodies from 28 providers
human
DRG1
Tissue enhanced (testis)
gene
Eukaryota
Protein hydroxylation
175 hits in 1140 CRISPR screens
human
Tbio
Protein
Expressed in left testis and 208 other cell types or tissues
baseline and differential
DRG
TGS_DRG1
Beta-grasp_dom_sf
DRG
G_OBG
GTP-bd
GTP-binding_2
GTP1-OBG_CS
P-loop_NTPase
Small_GTP-bd_dom
TGS
TGS-like
small_GTP
DEVELOPMENTALLY-REGULATED GTP-BINDING PROTEIN 1
DEVELOPMENTALLY-REGULATED GTP-BINDING PROTEIN 2
MMR_HSR1
MMR_HSR1_Xtn
TGS
GTP1OBG
P-loop containing nucleoside triphosphate hydrolases
TGS-like
G_OBG
GTP1_OBG
TGS
HS
Developmentally-regulated GTP-binding protein 1
DRG-1
Neural precursor cell expressed developmentally down-regulated protein 3
NEDD-3
Translation factor GTPase DRG1
TRAFAC GTPase DRG1
3.6.5.-
DRG1
NEDD3
Catalyzes the conversion of GTP to GDP through hydrolysis of the gamma-phosphate bond in GTP (PubMed:29915238, PubMed:23711155). Appears to have an intrinsic GTPase activity that is stimulated by ZC3H15/DFRP1 binding likely by increasing the affinity for the potassium ions (PubMed:23711155). When hydroxylated at C-3 of 'Lys-22' by JMJD7, may bind to RNA and play a role in translation (PubMed:19819225, PubMed:29915238). Binds to microtubules and promotes microtubule polymerization and stability that are required for mitotic spindle assembly during prophase to anaphase transition. GTPase activity is not necessary for these microtubule-related functions (PubMed:28855639).
The GTPase activity is enhanced by potassium ions as well as by DFRP1 binding.
0.25 mM for GTP
3.59 nmol/min/mg enzyme
Optimum pH is 8-9.
Optimum temperature is 42 degrees Celsius.
Interacts (via its C-terminal) with TAL1. Interacts with DFRP1/ZC3H15; this interaction prevents DRG1 poly-ubiquitination and degradation by the proteasome. DRG1-ZC3H15/DFRP1 complex co-sediments with polysomes (PubMed:19819225). Interacts with STK16 (PubMed:18184589). Interacts with JMJD7 (PubMed:29915238). Associates with microtubules either in an immobile or diffusive manner; in vitro binds to tubulin lacking the negatively charged C-terminal domain (PubMed:28855639).
The DRG1-ZC3H15/DFRP1 complex associates with polysomes.
High levels in skeletal muscle, heart, and kidney. Intermediate levels in liver, placenta and brain. Low levels in colon, thymus, spleen, small intestine, lung and leukocytes.
By androgens.
The ThrRS, GTPase, SpoT (TGS) domain is not necessary for GTP binding nor for the GTPase activity. It appears to play a regulatory role favoring GTP hydrolysis mediated by DFRP1/ZC3H15.
Sumoylated by UBE2I in response to MEKK1-mediated stimuli.
Phosphorylated at Thr-100 by STK16.
Hydroxylated (with S stereochemistry) at C-3 of Lys-22 by JMJD7; this modification hinders trypsin-catalyzed proteolysis in vitro.
Polyubiquitinated; this modification induces proteolytic degradation and is impaired by interaction with ZC3H15.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.
Removed
1
Developmentally-regulated GTP-binding protein 1
40411
2
367
OBG-type G
65
290
TGS
366
Required for interaction with STK16
16
71
78
98
117
121
248
251
N-acetylserine
(3S)-3-hydroxylysine
22
Phosphothreonine; by STK16
100
Impairs JMJD7-mediated hydroxylation.
A
Reduces the GTPase activity.
D
A
91
291
296
305
307
309
312
318
325
330
332
333
340
343
350
358
362
364
false
9
false
3
false
2
false
3
false
3
false
4
false
8
false
3
false
3
false
3
false
9
true
3
DRG1
CFTR
COIL
LNX1
MEOX2
PHC2
RWDD1
SKIL
SSX2IP
STK16
ZC3H15
M
1999-11-01
1
40542
a44e221ff599622e2095f0bbc03b1d3d
MSSTLAKIAEIEAEMARTQKNKATAHHLGLLKARLAKLRRELITPKGGGGGGPGEGFDVAKTGDARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNLILIVLDVLKPLGHKKIIENELEGFGIRLNSKPPNIGFKKKDKGGINLTATCPQSELDAETVKSILAEYKIHNADVTLRSDATADDLIDVVEGNRVYIPCIYVLNKIDQISIEELDIIYKVPHCVPISAHHRWNFDDLLEKIWDYLKLVRIYTKPKGQLPDYTSPVVLPYSRTTVEDFCMKIHKNLIKEFKYALVWGLSVKHNPQKVGKDHTLEDEDVIQIVKK
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true