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Q9NQL2

- RRAGD_HUMAN

UniProt

Q9NQL2 - RRAGD_HUMAN

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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

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 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
Complete GO annotation...

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
Complete GO annotation...

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. 9 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.
GeneTreeiENSGT00550000074708.
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

        10         20         30         40         50
MSQVLGKPQP QDEDDAEEEE EEDELVGLAD YGDGPDSSDA DPDSGTEEGV
60 70 80 90 100
LDFSDPFSTE VKPRILLMGL RRSGKSSIQK VVFHKMSPNE TLFLESTNKI
110 120 130 140 150
CREDVSNSSF VNFQIWDFPG QIDFFDPTFD YEMIFRGTGA LIFVIDSQDD
160 170 180 190 200
YMEALARLHL TVTRAYKVNT DINFEVFIHK VDGLSDDHKI ETQRDIHQRA
210 220 230 240 250
NDDLADAGLE KIHLSFYLTS IYDHSIFEAF SKVVQKLIPQ LPTLENLLNI
260 270 280 290 300
FISNSGIEKA FLFDVVSKIY IATDSTPVDM QTYELCCDMI DVVIDISCIY
310 320 330 340 350
GLKEDGAGTP YDKESTAIIK LNNTTVLYLK EVTKFLALVC FVREESFERK
360 370 380 390 400
GLIDYNFHCF RKAIHEVFEV RMKVVKSRKV QNRLQKKKRA TPNGTPRVLL
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. 9 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 GC06M090074.
HGNCi HGNC:19903. RRAGD.
MIMi 608268. gene.
neXtProti NX_Q9NQL2.
PharmGKBi PA134957148.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG250062.
GeneTreei ENSGT00550000074708.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 94 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