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Q9HB90 (RRAGC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related GTP-binding protein C

Short name=Rag C
Short name=RagC
Alternative name(s):
GTPase-interacting protein 2
TIB929
Gene names
Name:RRAGC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Subunit structure

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. Ref.2 Ref.6 Ref.7 Ref.11

Subcellular location

Cytoplasm. Nucleus. Lysosome. Note: Predominantly cytoplasmic. May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state of associated RRAGA. Ref.2 Ref.8

Sequence similarities

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

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RRAGAQ7L52311EBI-752390,EBI-752376
RRAGBQ5VZM24EBI-752390,EBI-993049

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 399398Ras-related GTP-binding protein C
PRO_0000239951

Regions

Nucleotide binding68 – 758GTP By similarity UniProtKB P53290
Nucleotide binding116 – 1205GTP By similarity
Nucleotide binding178 – 1814GTP By similarity UniProtKB P53290

Amino acid modifications

Modified residue21N-acetylserine Ref.9
Modified residue21Phosphoserine Ref.9
Modified residue961Phosphothreonine By similarity

Experimental info

Mutagenesis751S → L: Increased RPTOR-binding. Ref.7
Mutagenesis1201Q → L: Decreased RPTOR-binding. Ref.7
Sequence conflict2061A → S in AAG45221. Ref.1

Secondary structure

........................... 399
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9HB90 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 35B3171253CC69CF

FASTA39944,224
        10         20         30         40         50         60 
MSLQYGAEET PLAGSYGAAD SFPKDFGYGV EEEEEEAAAA GGGVGAGAGG GCGPGGADSS 

        70         80         90        100        110        120 
KPRILLMGLR RSGKSSIQKV VFHKMSPNET LFLESTNKIY KDDISNSSFV NFQIWDFPGQ 

       130        140        150        160        170        180 
MDFFDPTFDY EMIFRGTGAL IYVIDAQDDY MEALTRLHIT VSKAYKVNPD MNFEVFIHKV 

       190        200        210        220        230        240 
DGLSDDHKIE TQRDIHQRAN DDLADAGLEK LHLSFYLTSI YDHSIFEAFS KVVQKLIPQL 

       250        260        270        280        290        300 
PTLENLLNIF ISNSGIEKAF LFDVVSKIYI ATDSSPVDMQ SYELCCDMID VVIDVSCIYG 

       310        320        330        340        350        360 
LKEDGSGSAY DKESMAIIKL NNTTVLYLKE VTKFLALVCI LREESFERKG LIDYNFHCFR 

       370        380        390 
KAIHEVFEVG VTSHRSCGHQ TSASSLKALT HNGTPRNAI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001258780.1. NM_001271851.1.
NP_071440.1. NM_022157.3.
UniGeneHs.532461.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LLUX-ray1.40A60-237[»]
ProteinModelPortalQ9HB90.
SMRQ9HB90. Positions 57-367.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122074. 12 interactions.
IntActQ9HB90. 11 interactions.
MINTMINT-1451634.
STRING9606.ENSP00000362092.

PTM databases

PhosphoSiteQ9HB90.

Polymorphism databases

DMDM74752776.

Proteomic databases

PaxDbQ9HB90.
PeptideAtlasQ9HB90.
PRIDEQ9HB90.

Protocols and materials databases

DNASU64121.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373001; ENSP00000362092; ENSG00000116954.
GeneID64121.
KEGGhsa:64121.
UCSCuc001ccq.3. human.

Organism-specific databases

CTD64121.
GeneCardsGC01M039303.
HGNCHGNC:19902. RRAGC.
HPAHPA018247.
HPA055489.
MIM608267. gene.
neXtProtNX_Q9HB90.
PharmGKBPA134862062.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG250062.
HOGENOMHOG000203695.
HOVERGENHBG059482.
InParanoidQ9HB90.
KOK16186.
OMAIDYNFIC.
OrthoDBEOG7FXZZ8.
PhylomeDBQ9HB90.
TreeFamTF300659.

Gene expression databases

ArrayExpressQ9HB90.
BgeeQ9HB90.
CleanExHS_RRAGC.
GenevestigatorQ9HB90.

Family and domain databases

InterProIPR006762. Gtr1_RagA.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11259. PTHR11259. 1 hit.
PfamPF04670. Gtr1_RagA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRRAGC. human.
EvolutionaryTraceQ9HB90.
GeneWikiRRAGC.
GenomeRNAi64121.
NextBio65996.
PROQ9HB90.
SOURCESearch...

Entry information

Entry nameRRAGC_HUMAN
AccessionPrimary (citable) accession number: Q9HB90
Secondary accession number(s): Q9H202, Q9H8Q8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: March 1, 2001
Last modified: March 19, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM