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Q9Y295 (DRG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Developmentally-regulated GTP-binding protein 1

Short name=DRG-1
Alternative name(s):
Neural precursor cell expressed developmentally down-regulated protein 3
Short name=NEDD-3
Gene names
Name:DRG1
Synonyms:NEDD3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Critical regulator of cell growth under specific conditions. Implicated in differentiation and cell cycle arrest.

Subunit structure

Interacts (via its C-terminal) with TAL1. Interacts with ZC3H15; the interaction forms a polysomal DRG1-DFRP1/ZC3H15 complex which provides protein stability to DRG1 possibly by blocking poly-ubiquitination. Interacts with STK16; the interaction phosphorylates STK16 By similarity. Ref.1 Ref.9 Ref.12

Subcellular location

Cytoplasm. Note: The DRG1-DFRP2/ZC3H15 complex associates with polysomes. Ref.9 Ref.12

Tissue specificity

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. Ref.2

Induction

By androgens.

Post-translational modification

Sumoylated by UBE2I in response to MEKK1-mediated stimuli. Ref.10

Sequence similarities

Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.

Contains 1 OBG-type G (guanine nucleotide-binding) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-719554,EBI-719554
RWDD1Q9H4462EBI-719554,EBI-748952

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 367366Developmentally-regulated GTP-binding protein 1
PRO_0000205424

Regions

Domain65 – 290226OBG-type G
Nucleotide binding71 – 788GTP By similarity
Nucleotide binding117 – 1215GTP By similarity
Nucleotide binding248 – 2514GTP By similarity
Region2 – 1615Required for interaction with STK16
Compositional bias47 – 5610Poly-Gly

Amino acid modifications

Modified residue21N-acetylserine Ref.14
Modified residue1001Phosphothreonine; by STK16 Ref.11

Experimental info

Sequence conflict911V → A in AAH20803. Ref.8

Secondary structure

.................. 367
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y295 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 4A177EA7C8E23005

FASTA36740,542
        10         20         30         40         50         60 
MSSTLAKIAE IEAEMARTQK NKATAHHLGL LKARLAKLRR ELITPKGGGG GGPGEGFDVA 

        70         80         90        100        110        120 
KTGDARIGFV GFPSVGKSTL LSNLAGVYSE VAAYEFTTLT TVPGVIRYKG AKIQLLDLPG 

       130        140        150        160        170        180 
IIEGAKDGKG RGRQVIAVAR TCNLILIVLD VLKPLGHKKI IENELEGFGI RLNSKPPNIG 

       190        200        210        220        230        240 
FKKKDKGGIN LTATCPQSEL DAETVKSILA EYKIHNADVT LRSDATADDL IDVVEGNRVY 

       250        260        270        280        290        300 
IPCIYVLNKI DQISIEELDI IYKVPHCVPI SAHHRWNFDD LLEKIWDYLK LVRIYTKPKG 

       310        320        330        340        350        360 
QLPDYTSPVV LPYSRTTVED FCMKIHKNLI KEFKYALVWG LSVKHNPQKV GKDHTLEDED 


VIQIVKK 

« Hide

References

« Hide 'large scale' references
[1]"SCL binds the human homologue of DRG in vivo."
Zhao X.-F., Aplan P.D.
Biochim. Biophys. Acta 1448:109-114(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TAL1.
[2]"DRG represents a family of two closely related GTP-binding proteins."
Li B., Trueeb B.
Biochim. Biophys. Acta 1491:196-204(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[3]"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.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[6]"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. expand/collapse author list , 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.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Prostate.
[9]"Identification of DRG family regulatory proteins (DFRPs): specific regulation of DRG1 and DRG2."
Ishikawa K., Azuma S., Ikawa S., Semba K., Inoue J.
Genes Cells 10:139-150(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZC3H15, SUBCELLULAR LOCATION.
[10]"Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation."
Jakobs A., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R.
Nucleic Acids Res. 35:E109-E109(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION.
[11]"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.
Structure 16:115-124(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-100, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"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.
Biochem. Biophys. Res. Commun. 390:552-556(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZC3H15 IN THE DRG1-DFRP1/ZC3H15 COMPLEX, SUBCELLULAR LOCATION.
[13]"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.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[15]"Solution structures of the TGS domain of human developmentally-regulated GTP-binding protein 1."
RIKEN structural genomics initiative (RSGI)
Submitted (SEP-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 288-367.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF078103 mRNA. Translation: AAD12240.1.
AJ005940 mRNA. Translation: CAA06775.1.
CR542059 mRNA. Translation: CAG46856.1.
CR456488 mRNA. Translation: CAG30374.1.
BT007237 mRNA. Translation: AAP35901.1.
AK315659 mRNA. Translation: BAG38025.1.
AL096701, AL096702 Genomic DNA. Translation: CAI12876.1.
AL096702, AL096701 Genomic DNA. Translation: CAH71744.1.
CH471095 Genomic DNA. Translation: EAW59976.1.
BC019285 mRNA. Translation: AAH19285.1.
BC020803 mRNA. Translation: AAH20803.1.
CCDSCCDS13897.1.
RefSeqNP_004138.1. NM_004147.3.
UniGeneHs.115242.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EKINMR-A288-367[»]
ProteinModelPortalQ9Y295.
SMRQ9Y295. Positions 2-367.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110810. 24 interactions.
IntActQ9Y295. 11 interactions.
MINTMINT-5006718.
STRING9606.ENSP00000329715.

PTM databases

PhosphoSiteQ9Y295.

Polymorphism databases

DMDM6685390.

Proteomic databases

MaxQBQ9Y295.
PaxDbQ9Y295.
PeptideAtlasQ9Y295.
PRIDEQ9Y295.

Protocols and materials databases

DNASU4733.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331457; ENSP00000329715; ENSG00000185721.
GeneID4733.
KEGGhsa:4733.
UCSCuc003aku.3. human.

Organism-specific databases

CTD4733.
GeneCardsGC22P031795.
HGNCHGNC:3029. DRG1.
HPAHPA001218.
MIM603952. gene.
neXtProtNX_Q9Y295.
PharmGKBPA27483.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1163.
HOGENOMHOG000112078.
HOVERGENHBG000948.
InParanoidQ9Y295.
OMAGNRIYIP.
OrthoDBEOG7PZRXJ.
PhylomeDBQ9Y295.
TreeFamTF105677.

Gene expression databases

ArrayExpressQ9Y295.
BgeeQ9Y295.
CleanExHS_DRG1.
GenevestigatorQ9Y295.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR006074. GTP1-OBG_CS.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR004095. TGS.
IPR012676. TGS-like.
[Graphical view]
PfamPF01926. MMR_HSR1. 1 hit.
PF02824. TGS. 1 hit.
[Graphical view]
PRINTSPR00326. GTP1OBG.
SUPFAMSSF52540. SSF52540. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51710. G_OBG. 1 hit.
PS00905. GTP1_OBG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDRG1. human.
EvolutionaryTraceQ9Y295.
GeneWikiDRG1.
GenomeRNAi4733.
NextBio18246.
PROQ9Y295.
SOURCESearch...

Entry information

Entry nameDRG1_HUMAN
AccessionPrimary (citable) accession number: Q9Y295
Secondary accession number(s): B2RDS8 expand/collapse secondary AC list , Q6FGP8, Q8WW69, Q9UGF2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM