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Q9Y295

- DRG1_HUMAN

UniProt

Q9Y295 - DRG1_HUMAN

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
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    4. transcription factor binding Source: ProtInc

    GO - Biological processi

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

    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-SubCell
    2. membrane Source: UniProtKB
    3. polysome Source: UniProtKB

    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

    ArrayExpressiQ9Y295.
    BgeeiQ9Y295.
    CleanExiHS_DRG1.
    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. 23 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 – 2966
    Beta strandi305 – 3073
    Beta strandi309 – 3124
    Helixi318 – 3258
    Turni330 – 3323
    Beta strandi333 – 3408
    Beta strandi343 – 3508
    Beta strandi358 – 3625
    Beta strandi364 – 3663

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MSSTLAKIAE IEAEMARTQK NKATAHHLGL LKARLAKLRR ELITPKGGGG    50
    GGPGEGFDVA KTGDARIGFV GFPSVGKSTL LSNLAGVYSE VAAYEFTTLT 100
    TVPGVIRYKG AKIQLLDLPG IIEGAKDGKG RGRQVIAVAR TCNLILIVLD 150
    VLKPLGHKKI IENELEGFGI RLNSKPPNIG FKKKDKGGIN LTATCPQSEL 200
    DAETVKSILA EYKIHNADVT LRSDATADDL IDVVEGNRVY IPCIYVLNKI 250
    DQISIEELDI IYKVPHCVPI SAHHRWNFDD LLEKIWDYLK LVRIYTKPKG 300
    QLPDYTSPVV LPYSRTTVED FCMKIHKNLI KEFKYALVWG LSVKHNPQKV 350
    GKDHTLEDED VIQIVKK 367
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 23 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.
    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

    ArrayExpressi Q9Y295.
    Bgeei Q9Y295.
    CleanExi HS_DRG1.
    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

    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: October 1, 2014
    This is version 135 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