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Q9NQL2

- RRAGD_HUMAN

UniProt

Q9NQL2 - RRAGD_HUMAN

Protein

Ras-related GTP-binding protein D

Gene

RRAGD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Guanine nucleotide-binding protein forming heterodimeric Rag complexes required for the amino acid-induced relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. This is a crucial step in the activation of the TOR signaling cascade by amino acids.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi69 – 779GTP
    Nucleotide bindingi117 – 1215GTP
    Nucleotide bindingi179 – 1824GTP

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein heterodimerization activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein localization Source: UniProtKB
    2. cellular response to amino acid stimulus Source: UniProtKB
    3. positive regulation of TOR signaling Source: UniProtKB

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related GTP-binding protein D
    Short name:
    Rag D
    Short name:
    RagD
    Gene namesi
    Name:RRAGDImported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:19903. RRAGD.

    Subcellular locationi

    Cytoplasm. Nucleus. Lysosome
    Note: Predominantly cytoplasmic. May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state of associated RRAGA.

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. lysosome Source: UniProtKB
    3. nucleus Source: HGNC

    Keywords - Cellular componenti

    Cytoplasm, Lysosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi76 – 761S → L: Increased RPTOR-binding. 1 Publication
    Mutagenesisi121 – 1211Q → L: Decreased RPTOR-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA134957148.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 400400Ras-related GTP-binding protein DPRO_0000239953Add
    BLAST

    Proteomic databases

    MaxQBiQ9NQL2.
    PaxDbiQ9NQL2.
    PRIDEiQ9NQL2.

    PTM databases

    PhosphoSiteiQ9NQL2.

    Expressioni

    Gene expression databases

    BgeeiQ9NQL2.
    CleanExiHS_RRAGD.
    GenevestigatoriQ9NQL2.

    Interactioni

    Subunit structurei

    Forms a heterodimer with RRAGA in a sequence-independent manner and RRAGB. Heterodimerization stabilizes RRAG proteins. In complex with RRAGB, interacts with RPTOR; this interaction is particularly efficient with GTP-loaded RRAGB and GDP-loaded RRAGC. Interacts with NOL8. Interacts with SH3BP4; the interaction with this negative regulator is most probably direct, preferentially occurs with the inactive GDP-bound form of RRAGD and is negatively regulated by amino acids.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LARSQ9P2J513EBI-992949,EBI-356077
    RRAGAQ7L5237EBI-992949,EBI-752376
    RRAGBQ5VZM27EBI-992949,EBI-993049

    Protein-protein interaction databases

    BioGridi121848. 8 interactions.
    IntActiQ9NQL2. 7 interactions.
    STRINGi9606.ENSP00000358423.

    Structurei

    Secondary structure

    1
    400
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi64 – 707
    Helixi75 – 8410
    Helixi88 – 936
    Beta strandi101 – 1055
    Beta strandi113 – 1175
    Helixi131 – 1366
    Beta strandi138 – 1469
    Helixi152 – 16817
    Beta strandi173 – 1797
    Helixi181 – 1833
    Helixi188 – 20619
    Beta strandi214 – 2196
    Helixi225 – 23511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Q3FX-ray2.10A/B60-239[»]
    ProteinModelPortaliQ9NQL2.
    SMRiQ9NQL2. Positions 61-367.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NQL2.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GTR/RAG GTP-binding protein family.Curated

    Phylogenomic databases

    eggNOGiNOG250062.
    HOGENOMiHOG000203695.
    HOVERGENiHBG059482.
    InParanoidiQ9NQL2.
    KOiK16186.
    OMAiNFEIFIH.
    OrthoDBiEOG7FXZZ8.
    PhylomeDBiQ9NQL2.
    TreeFamiTF300659.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR006762. Gtr1_RagA.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR11259. PTHR11259. 1 hit.
    PfamiPF04670. Gtr1_RagA. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q9NQL2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSQVLGKPQP QDEDDAEEEE EEDELVGLAD YGDGPDSSDA DPDSGTEEGV    50
    LDFSDPFSTE VKPRILLMGL RRSGKSSIQK VVFHKMSPNE TLFLESTNKI 100
    CREDVSNSSF VNFQIWDFPG QIDFFDPTFD YEMIFRGTGA LIFVIDSQDD 150
    YMEALARLHL TVTRAYKVNT DINFEVFIHK VDGLSDDHKI ETQRDIHQRA 200
    NDDLADAGLE KIHLSFYLTS IYDHSIFEAF SKVVQKLIPQ LPTLENLLNI 250
    FISNSGIEKA FLFDVVSKIY IATDSTPVDM QTYELCCDMI DVVIDISCIY 300
    GLKEDGAGTP YDKESTAIIK LNNTTVLYLK EVTKFLALVC FVREESFERK 350
    GLIDYNFHCF RKAIHEVFEV RMKVVKSRKV QNRLQKKKRA TPNGTPRVLL 400
    Length:400
    Mass (Da):45,588
    Last modified:October 1, 2000 - v1
    Checksum:i96FF0854B11AA1BC
    GO
    Isoform 21 Publication (identifier: Q9NQL2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-151: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:249
    Mass (Da):28,611
    Checksum:i4A6435D188BE8283
    GO

    Sequence cautioni

    The sequence AAH03088.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 151151Missing in isoform 2. 1 PublicationVSP_052078Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF272036 mRNA. Translation: AAG32663.1.
    AK289799 mRNA. Translation: BAF82488.1.
    AL138717 Genomic DNA. Translation: CAB99361.1.
    AL138717 Genomic DNA. Translation: CAB99362.1.
    CH471051 Genomic DNA. Translation: EAW48554.1.
    AL137502 mRNA. Translation: CAB70775.2.
    BC003088 mRNA. Translation: AAH03088.1. Different initiation.
    CCDSiCCDS5022.1. [Q9NQL2-1]
    PIRiT46254.
    RefSeqiNP_067067.1. NM_021244.4. [Q9NQL2-1]
    UniGeneiHs.31712.

    Genome annotation databases

    EnsembliENST00000359203; ENSP00000352131; ENSG00000025039. [Q9NQL2-2]
    ENST00000369415; ENSP00000358423; ENSG00000025039. [Q9NQL2-1]
    GeneIDi58528.
    KEGGihsa:58528.
    UCSCiuc003pnd.4. human. [Q9NQL2-1]

    Polymorphism databases

    DMDMi74752904.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF272036 mRNA. Translation: AAG32663.1 .
    AK289799 mRNA. Translation: BAF82488.1 .
    AL138717 Genomic DNA. Translation: CAB99361.1 .
    AL138717 Genomic DNA. Translation: CAB99362.1 .
    CH471051 Genomic DNA. Translation: EAW48554.1 .
    AL137502 mRNA. Translation: CAB70775.2 .
    BC003088 mRNA. Translation: AAH03088.1 . Different initiation.
    CCDSi CCDS5022.1. [Q9NQL2-1 ]
    PIRi T46254.
    RefSeqi NP_067067.1. NM_021244.4. [Q9NQL2-1 ]
    UniGenei Hs.31712.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Q3F X-ray 2.10 A/B 60-239 [» ]
    ProteinModelPortali Q9NQL2.
    SMRi Q9NQL2. Positions 61-367.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121848. 8 interactions.
    IntActi Q9NQL2. 7 interactions.
    STRINGi 9606.ENSP00000358423.

    PTM databases

    PhosphoSitei Q9NQL2.

    Polymorphism databases

    DMDMi 74752904.

    Proteomic databases

    MaxQBi Q9NQL2.
    PaxDbi Q9NQL2.
    PRIDEi Q9NQL2.

    Protocols and materials databases

    DNASUi 58528.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359203 ; ENSP00000352131 ; ENSG00000025039 . [Q9NQL2-2 ]
    ENST00000369415 ; ENSP00000358423 ; ENSG00000025039 . [Q9NQL2-1 ]
    GeneIDi 58528.
    KEGGi hsa:58528.
    UCSCi uc003pnd.4. human. [Q9NQL2-1 ]

    Organism-specific databases

    CTDi 58528.
    GeneCardsi GC06M090131.
    HGNCi HGNC:19903. RRAGD.
    MIMi 608268. gene.
    neXtProti NX_Q9NQL2.
    PharmGKBi PA134957148.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG250062.
    HOGENOMi HOG000203695.
    HOVERGENi HBG059482.
    InParanoidi Q9NQL2.
    KOi K16186.
    OMAi NFEIFIH.
    OrthoDBi EOG7FXZZ8.
    PhylomeDBi Q9NQL2.
    TreeFami TF300659.

    Miscellaneous databases

    EvolutionaryTracei Q9NQL2.
    GenomeRNAii 58528.
    NextBioi 65098.
    PROi Q9NQL2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NQL2.
    CleanExi HS_RRAGD.
    Genevestigatori Q9NQL2.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR006762. Gtr1_RagA.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR11259. PTHR11259. 1 hit.
    Pfami PF04670. Gtr1_RagA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B."
      Sekiguchi T., Hirose E., Nakashima N., Ii M., Nishimoto T.
      J. Biol. Chem. 276:7246-7257(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RRAGA AND RRAGB, SUBCELLULAR LOCATION, GTP-BINDING.
    2. "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] (ISOFORM 1).
      Tissue: Brain.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-49 (ISOFORM 1).
      Tissue: Amygdala.
    6. "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] OF 20-400 (ISOFORM 1).
      Tissue: LungImported.
    7. "A novel human nucleolar protein, Nop132, binds to the G proteins, RRAG A/C/D."
      Sekiguchi T., Todaka Y., Wang Y., Hirose E., Nakashima N., Nishimoto T.
      J. Biol. Chem. 279:8343-8350(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NOL8 AND RRAGA.
    8. "The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1."
      Sancak Y., Peterson T.R., Shaul Y.D., Lindquist R.A., Thoreen C.C., Bar-Peled L., Sabatini D.M.
      Science 320:1496-1501(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RPTOR, MUTAGENESIS OF SER-76 AND GLN-121.
    9. "Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids."
      Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., Sabatini D.M.
      Cell 141:290-303(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "SH3BP4 is a negative regulator of amino acid-Rag GTPase-mTORC1 signaling."
      Kim Y.M., Stone M., Hwang T.H., Kim Y.G., Dunlevy J.R., Griffin T.J., Kim D.H.
      Mol. Cell 46:833-846(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SH3BP4.
    11. "Crystal structure of human Ras-related GTP-binding D."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 60-239 IN COMPLEX WITH GTP ANALOG.

    Entry informationi

    Entry nameiRRAGD_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQL2
    Secondary accession number(s): A8K184, Q7L8F9, Q9NPG0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2006
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 93 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 6
      Human chromosome 6: 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