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Q9HB90

- RRAGC_HUMAN

UniProt

Q9HB90 - RRAGC_HUMAN

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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

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 – 758GTP By similarityBy similarity
Nucleotide bindingi116 – 1205GTP By similarity
Nucleotide bindingi178 – 1814GTP By similarityBy 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
Complete GO annotation...

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:RRAGC
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.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. intracellular membrane-bounded organelle Source: HPA
  3. lysosome Source: UniProtKB
  4. nucleus Source: UniProtKB
Complete GO annotation...

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 – 961Phosphothreonine By 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.

Miscellaneous databases

EvolutionaryTraceiQ9HB90.

Family & Domainsi

Sequence similaritiesi

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061A → S in AAG45221. 1 Publication

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

« Hide 'large scale' publications
  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: Lymph.
  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: Ovary.
  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: July 9, 2014
This is version 103 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

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