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Q9HB90

- RRAGC_HUMAN

UniProt

Q9HB90 - RRAGC_HUMAN

Protein

Ras-related GTP-binding protein C

Gene

RRAGC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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 bindingi68 – 758GTPBy similarity
    Nucleotide bindingi116 – 1205GTPBy similarity
    Nucleotide bindingi178 – 1814GTPBy similarity

    GO - Molecular functioni

    1. GDP binding Source: UniProtKB
    2. GTPase activity Source: UniProtKB
    3. GTP binding Source: HGNC
    4. magnesium ion binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein heterodimerization activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. cell growth Source: UniProtKB
    3. cellular protein localization Source: UniProtKB
    4. cellular response to amino acid stimulus Source: UniProtKB
    5. GTP catabolic process Source: GOC
    6. RNA splicing Source: UniProtKB
    7. small GTPase mediated signal transduction Source: UniProtKB
    8. transcription, DNA-templated Source: UniProtKB

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related GTP-binding protein C
    Short name:
    Rag C
    Short name:
    RagC
    Alternative name(s):
    GTPase-interacting protein 2
    TIB929
    Gene namesi
    Name:RRAGCImported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:19902. RRAGC.

    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: UniProtKB
    2. intracellular membrane-bounded organelle Source: HPA
    3. lysosome Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Lysosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi75 – 751S → L: Increased RPTOR-binding. 1 Publication
    Mutagenesisi120 – 1201Q → L: Decreased RPTOR-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA134862062.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 399398Ras-related GTP-binding protein CPRO_0000239951Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei96 – 961PhosphothreonineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9HB90.
    PaxDbiQ9HB90.
    PeptideAtlasiQ9HB90.
    PRIDEiQ9HB90.

    PTM databases

    PhosphoSiteiQ9HB90.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9HB90.
    BgeeiQ9HB90.
    CleanExiHS_RRAGC.
    GenevestigatoriQ9HB90.

    Organism-specific databases

    HPAiHPA018247.
    HPA055489.

    Interactioni

    Subunit structurei

    Forms a heterodimer with RRAGA, in a sequence-independent manner, and RRAGB. Heterodimerization stabilizes proteins of the heterodimer. In complex with RRAGA or 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 RRAGB, is negatively regulated by amino acids and prevents interaction with RPTOR.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RRAGAQ7L52311EBI-752390,EBI-752376
    RRAGBQ5VZM24EBI-752390,EBI-993049

    Protein-protein interaction databases

    BioGridi122074. 12 interactions.
    IntActiQ9HB90. 11 interactions.
    MINTiMINT-1451634.
    STRINGi9606.ENSP00000362092.

    Structurei

    Secondary structure

    1
    399
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi63 – 697
    Helixi74 – 829
    Helixi87 – 926
    Beta strandi100 – 1045
    Beta strandi112 – 1165
    Helixi130 – 1356
    Beta strandi138 – 1458
    Helixi151 – 16717
    Beta strandi172 – 1787
    Helixi180 – 1823
    Helixi185 – 20521
    Beta strandi213 – 2186
    Helixi224 – 23512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LLUX-ray1.40A60-237[»]
    ProteinModelPortaliQ9HB90.
    SMRiQ9HB90. Positions 57-367.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HB90.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG250062.
    HOGENOMiHOG000203695.
    HOVERGENiHBG059482.
    InParanoidiQ9HB90.
    KOiK16186.
    OMAiIDYNFIC.
    OrthoDBiEOG7FXZZ8.
    PhylomeDBiQ9HB90.
    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.

    Sequencei

    Sequence statusi: Complete.

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

    Q9HB90-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLQYGAEET PLAGSYGAAD SFPKDFGYGV EEEEEEAAAA GGGVGAGAGG    50
    GCGPGGADSS KPRILLMGLR RSGKSSIQKV VFHKMSPNET LFLESTNKIY 100
    KDDISNSSFV NFQIWDFPGQ MDFFDPTFDY EMIFRGTGAL IYVIDAQDDY 150
    MEALTRLHIT VSKAYKVNPD MNFEVFIHKV DGLSDDHKIE TQRDIHQRAN 200
    DDLADAGLEK LHLSFYLTSI YDHSIFEAFS KVVQKLIPQL PTLENLLNIF 250
    ISNSGIEKAF LFDVVSKIYI ATDSSPVDMQ SYELCCDMID VVIDVSCIYG 300
    LKEDGSGSAY DKESMAIIKL NNTTVLYLKE VTKFLALVCI LREESFERKG 350
    LIDYNFHCFR KAIHEVFEVG VTSHRSCGHQ TSASSLKALT HNGTPRNAI 399
    Length:399
    Mass (Da):44,224
    Last modified:March 1, 2001 - v1
    Checksum:i35B3171253CC69CF
    GO

    Sequence cautioni

    The sequence BAB14548.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti206 – 2061A → S in AAG45221. (PubMed:11145883)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF323609 mRNA. Translation: AAG45221.1.
    AF272035 mRNA. Translation: AAG32662.1.
    AL139260 Genomic DNA. Translation: CAI23049.1.
    BC016668 mRNA. Translation: AAH16668.1.
    AK023373 mRNA. Translation: BAB14548.1. Different initiation.
    CCDSiCCDS430.1.
    RefSeqiNP_001258780.1. NM_001271851.1.
    NP_071440.1. NM_022157.3.
    UniGeneiHs.532461.

    Genome annotation databases

    EnsembliENST00000373001; ENSP00000362092; ENSG00000116954.
    GeneIDi64121.
    KEGGihsa:64121.
    UCSCiuc001ccq.3. human.

    Polymorphism databases

    DMDMi74752776.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF323609 mRNA. Translation: AAG45221.1 .
    AF272035 mRNA. Translation: AAG32662.1 .
    AL139260 Genomic DNA. Translation: CAI23049.1 .
    BC016668 mRNA. Translation: AAH16668.1 .
    AK023373 mRNA. Translation: BAB14548.1 . Different initiation.
    CCDSi CCDS430.1.
    RefSeqi NP_001258780.1. NM_001271851.1.
    NP_071440.1. NM_022157.3.
    UniGenei Hs.532461.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3LLU X-ray 1.40 A 60-237 [» ]
    ProteinModelPortali Q9HB90.
    SMRi Q9HB90. Positions 57-367.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122074. 12 interactions.
    IntActi Q9HB90. 11 interactions.
    MINTi MINT-1451634.
    STRINGi 9606.ENSP00000362092.

    PTM databases

    PhosphoSitei Q9HB90.

    Polymorphism databases

    DMDMi 74752776.

    Proteomic databases

    MaxQBi Q9HB90.
    PaxDbi Q9HB90.
    PeptideAtlasi Q9HB90.
    PRIDEi Q9HB90.

    Protocols and materials databases

    DNASUi 64121.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373001 ; ENSP00000362092 ; ENSG00000116954 .
    GeneIDi 64121.
    KEGGi hsa:64121.
    UCSCi uc001ccq.3. human.

    Organism-specific databases

    CTDi 64121.
    GeneCardsi GC01M039303.
    HGNCi HGNC:19902. RRAGC.
    HPAi HPA018247.
    HPA055489.
    MIMi 608267. gene.
    neXtProti NX_Q9HB90.
    PharmGKBi PA134862062.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG250062.
    HOGENOMi HOG000203695.
    HOVERGENi HBG059482.
    InParanoidi Q9HB90.
    KOi K16186.
    OMAi IDYNFIC.
    OrthoDBi EOG7FXZZ8.
    PhylomeDBi Q9HB90.
    TreeFami TF300659.

    Miscellaneous databases

    ChiTaRSi RRAGC. human.
    EvolutionaryTracei Q9HB90.
    GeneWikii RRAGC.
    GenomeRNAii 64121.
    NextBioi 65996.
    PROi Q9HB90.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HB90.
    Bgeei Q9HB90.
    CleanExi HS_RRAGC.
    Genevestigatori Q9HB90.

    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. "Adenovirus immunoregulatory genes and their cellular targets."
      Horwitz M.S.
      Virology 279:1-8(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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], INTERACTION WITH RRAGA AND RRAGB, SUBCELLULAR LOCATION, GTP-BINDING.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: LymphImported.
    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] OF 266-399.
      Tissue: OvaryImported.
    6. "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.
    7. "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-75 AND GLN-120.
    8. "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.
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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.

    Entry informationi

    Entry nameiRRAGC_HUMAN
    AccessioniPrimary (citable) accession number: Q9HB90
    Secondary accession number(s): Q9H202, Q9H8Q8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2006
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 104 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 1
      Human chromosome 1: 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