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Q9Y295

- DRG1_HUMAN

UniProt

Q9Y295 - DRG1_HUMAN

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Protein

Developmentally-regulated GTP-binding protein 1

Gene

DRG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi71 – 788GTPPROSITE-ProRule annotation
Nucleotide bindingi117 – 1215GTPPROSITE-ProRule annotation
Nucleotide bindingi248 – 2514GTPPROSITE-ProRule annotation

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. transcription factor binding Source: ProtInc

GO - Biological processi

  1. multicellular organismal development Source: ProtInc
  2. transcription, DNA-templated Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:DRG1
Synonyms:NEDD3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:3029. DRG1.

Subcellular locationi

Cytoplasm 2 Publications
Note: The DRG1-DFRP2/ZC3H15 complex associates with polysomes.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. membrane Source: UniProtKB
  3. polysome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27483.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 367366Developmentally-regulated GTP-binding protein 1PRO_0000205424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei100 – 1001Phosphothreonine; by STK161 Publication

Post-translational modificationi

Sumoylated by UBE2I in response to MEKK1-mediated stimuli.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Y295.
PaxDbiQ9Y295.
PeptideAtlasiQ9Y295.
PRIDEiQ9Y295.

PTM databases

PhosphoSiteiQ9Y295.

Expressioni

Tissue specificityi

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.1 Publication

Inductioni

By androgens.

Gene expression databases

BgeeiQ9Y295.
CleanExiHS_DRG1.
ExpressionAtlasiQ9Y295. baseline and differential.
GenevestigatoriQ9Y295.

Organism-specific databases

HPAiHPA001218.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-719554,EBI-719554
RWDD1Q9H4462EBI-719554,EBI-748952

Protein-protein interaction databases

BioGridi110810. 27 interactions.
IntActiQ9Y295. 11 interactions.
MINTiMINT-5006718.
STRINGi9606.ENSP00000329715.

Structurei

Secondary structure

1
367
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi291 – 2966Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi309 – 3124Combined sources
Helixi318 – 3258Combined sources
Turni330 – 3323Combined sources
Beta strandi333 – 3408Combined sources
Beta strandi343 – 3508Combined sources
Beta strandi358 – 3625Combined sources
Beta strandi364 – 3663Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EKINMR-A288-367[»]
ProteinModelPortaliQ9Y295.
SMRiQ9Y295. Positions 2-367.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y295.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 290226OBG-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 1615Required for interaction with STK16Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi47 – 5610Poly-Gly

Sequence similaritiesi

Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.PROSITE-ProRule annotation
Contains 1 OBG-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1163.
GeneTreeiENSGT00550000075013.
HOGENOMiHOG000112078.
HOVERGENiHBG000948.
InParanoidiQ9Y295.
OMAiGNRIYIP.
OrthoDBiEOG7PZRXJ.
PhylomeDBiQ9Y295.
TreeFamiTF105677.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR006074. GTP1-OBG_CS.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR004095. TGS.
IPR012676. TGS-like.
[Graphical view]
PfamiPF01926. MMR_HSR1. 1 hit.
PF02824. TGS. 1 hit.
[Graphical view]
PRINTSiPR00326. GTP1OBG.
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51710. G_OBG. 1 hit.
PS00905. GTP1_OBG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y295-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSTLAKIAE IEAEMARTQK NKATAHHLGL LKARLAKLRR ELITPKGGGG
60 70 80 90 100
GGPGEGFDVA KTGDARIGFV GFPSVGKSTL LSNLAGVYSE VAAYEFTTLT
110 120 130 140 150
TVPGVIRYKG AKIQLLDLPG IIEGAKDGKG RGRQVIAVAR TCNLILIVLD
160 170 180 190 200
VLKPLGHKKI IENELEGFGI RLNSKPPNIG FKKKDKGGIN LTATCPQSEL
210 220 230 240 250
DAETVKSILA EYKIHNADVT LRSDATADDL IDVVEGNRVY IPCIYVLNKI
260 270 280 290 300
DQISIEELDI IYKVPHCVPI SAHHRWNFDD LLEKIWDYLK LVRIYTKPKG
310 320 330 340 350
QLPDYTSPVV LPYSRTTVED FCMKIHKNLI KEFKYALVWG LSVKHNPQKV
360
GKDHTLEDED VIQIVKK
Length:367
Mass (Da):40,542
Last modified:November 1, 1999 - v1
Checksum:i4A177EA7C8E23005
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911V → A in AAH20803. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13897.1.
RefSeqiNP_004138.1. NM_004147.3.
UniGeneiHs.115242.

Genome annotation databases

EnsembliENST00000331457; ENSP00000329715; ENSG00000185721.
GeneIDi4733.
KEGGihsa:4733.
UCSCiuc003aku.3. human.

Polymorphism databases

DMDMi6685390.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS13897.1.
RefSeqi NP_004138.1. NM_004147.3.
UniGenei Hs.115242.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EKI NMR - A 288-367 [» ]
ProteinModelPortali Q9Y295.
SMRi Q9Y295. Positions 2-367.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110810. 27 interactions.
IntActi Q9Y295. 11 interactions.
MINTi MINT-5006718.
STRINGi 9606.ENSP00000329715.

PTM databases

PhosphoSitei Q9Y295.

Polymorphism databases

DMDMi 6685390.

Proteomic databases

MaxQBi Q9Y295.
PaxDbi Q9Y295.
PeptideAtlasi Q9Y295.
PRIDEi Q9Y295.

Protocols and materials databases

DNASUi 4733.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331457 ; ENSP00000329715 ; ENSG00000185721 .
GeneIDi 4733.
KEGGi hsa:4733.
UCSCi uc003aku.3. human.

Organism-specific databases

CTDi 4733.
GeneCardsi GC22P031795.
HGNCi HGNC:3029. DRG1.
HPAi HPA001218.
MIMi 603952. gene.
neXtProti NX_Q9Y295.
PharmGKBi PA27483.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1163.
GeneTreei ENSGT00550000075013.
HOGENOMi HOG000112078.
HOVERGENi HBG000948.
InParanoidi Q9Y295.
OMAi GNRIYIP.
OrthoDBi EOG7PZRXJ.
PhylomeDBi Q9Y295.
TreeFami TF105677.

Miscellaneous databases

ChiTaRSi DRG1. human.
EvolutionaryTracei Q9Y295.
GeneWikii DRG1.
GenomeRNAii 4733.
NextBioi 18246.
PROi Q9Y295.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y295.
CleanExi HS_DRG1.
ExpressionAtlasi Q9Y295. baseline and differential.
Genevestigatori Q9Y295.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR006074. GTP1-OBG_CS.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR004095. TGS.
IPR012676. TGS-like.
[Graphical view ]
Pfami PF01926. MMR_HSR1. 1 hit.
PF02824. TGS. 1 hit.
[Graphical view ]
PRINTSi PR00326. GTP1OBG.
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51710. G_OBG. 1 hit.
PS00905. GTP1_OBG. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. 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.

Entry informationi

Entry nameiDRG1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y295
Secondary accession number(s): B2RDS8
, Q6FGP8, Q8WW69, Q9UGF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: November 26, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3