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Q6IAA8

- LTOR1_HUMAN

UniProt

Q6IAA8 - LTOR1_HUMAN

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Protein

Ragulator complex protein LAMTOR1

Gene
LAMTOR1, C11orf59, PDRO, PP7157
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. LAMTOR1 is directly responsible for anchoring the Ragulator complex to membranes. Also required for late endosomes/lysosomes biogenesis it may regulate both the recycling of receptors through endosomes and the MAPK signaling pathway through recruitment of some of its components to late endosomes. May be involved in cholesterol homeostasis regulating LDL uptake and cholesterol release from late endosomes/lysosomes. May also play a role in RHOA activation.4 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB

GO - Biological processi

  1. cell growth Source: UniProtKB
  2. cellular protein localization Source: UniProtKB
  3. cellular response to amino acid stimulus Source: UniProtKB
  4. cholesterol homeostasis Source: UniProtKB
  5. endosome localization Source: UniProtKB
  6. endosome organization Source: UniProtKB
  7. lysosome localization Source: UniProtKB
  8. lysosome organization Source: UniProtKB
  9. positive regulation of MAPK cascade Source: UniProtKB
  10. positive regulation of TOR signaling Source: UniProtKB
  11. regulation of cholesterol efflux Source: UniProtKB
  12. regulation of cholesterol esterification Source: UniProtKB
  13. regulation of cholesterol import Source: UniProtKB
  14. regulation of GTPase activity Source: GOC
  15. regulation of receptor recycling Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ragulator complex protein LAMTOR1
Alternative name(s):
Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1
Lipid raft adaptor protein p18
Protein associated with DRMs and endosomes
p27Kip1-releasing factor from RhoA
Short name:
p27RF-Rho
Gene namesi
Name:LAMTOR1
Synonyms:C11orf59, PDRO
ORF Names:PP7157
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:26068. LAMTOR1.

Subcellular locationi

Late endosome membrane; Lipid-anchor; Cytoplasmic side. Lysosome membrane; Lipid-anchor; Cytoplasmic side. Cell membrane 2 Publications

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. Golgi apparatus Source: HPA
  3. intracellular membrane-bounded organelle Source: HPA
  4. late endosome membrane Source: UniProtKB
  5. lysosomal membrane Source: UniProtKB-SubCell
  6. lysosome Source: UniProtKB
  7. membrane raft Source: UniProtKB
  8. plasma membrane Source: HPA
  9. Ragulator complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Lysosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485354.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed Reviewed prediction
Chaini2 – 161160Ragulator complex protein LAMTOR1PRO_0000274292Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine Reviewed prediction
Modified residuei27 – 271Phosphoserine1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiQ6IAA8.
PaxDbiQ6IAA8.
PeptideAtlasiQ6IAA8.
PRIDEiQ6IAA8.

PTM databases

PhosphoSiteiQ6IAA8.

Expressioni

Inductioni

Down-regulated by cholesterol (at protein level).1 Publication

Gene expression databases

ArrayExpressiQ6IAA8.
BgeeiQ6IAA8.
CleanExiHS_C11orf59.
GenevestigatoriQ6IAA8.

Organism-specific databases

HPAiHPA002997.

Interactioni

Subunit structurei

Part of the Ragulator complex composed of LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5. LAMTOR4 and LAMTOR5 form a heterodimer that interacts, through LAMTOR1, with a LAMTOR2, LAMTOR3 heterodimer. The Ragulator complex interacts with both the mTORC1 complex and heterodimers constituted of the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD; regulated by amino acid availability. Interacts with LAMTOR2 and LAMTOR3; the interaction is direct. Interacts with RRAGB and RRAGD; the interaction is direct indicating that it probably constitutes the main RAG-interacting subunit of the Ragulator complex. Interacts with MMP14. Interacts with CDKN1B; prevents the interaction of CDKN1B with RHOA leaving RHOA in a form accessible to activation by ARHGEF2.3 Publications

Protein-protein interaction databases

BioGridi120336. 16 interactions.
IntActiQ6IAA8. 16 interactions.
MINTiMINT-1372069.
STRINGi9606.ENSP00000278671.

Structurei

3D structure databases

ProteinModelPortaliQ6IAA8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni121 – 16141Interaction with LAMTOR2 and LAMTOR3 By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the LAMTOR1 family.

Phylogenomic databases

eggNOGiNOG73401.
HOVERGENiHBG081218.
InParanoidiQ6IAA8.
OMAiPYSDVQQ.
PhylomeDBiQ6IAA8.
TreeFamiTF323788.

Family and domain databases

InterProiIPR026310. LAMTOR1-like.
IPR028209. LAMTOR1/MEH1.
[Graphical view]
PANTHERiPTHR13401. PTHR13401. 1 hit.
PfamiPF15454. LAMTOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q6IAA8-1 [UniParc]FASTAAdd to Basket

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MGCCYSSENE DSDQDREERK LLLDPSSPPT KALNGAEPNY HSLPSARTDE    50
QALLSSILAK TASNIIDVSA ADSQGMEQHE YMDRARQYST RLAVLSSSLT 100
HWKKLPPLPS LTSQPHQVLA SEPIPFSDLQ QVSRIAAYAY SALSQIRVDA 150
KEELVVQFGI P 161
Length:161
Mass (Da):17,745
Last modified:February 6, 2007 - v2
Checksum:i610CC6C548356051
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti73 – 731S → L.
Corresponds to variant rs1053443 [ dbSNP | Ensembl ].
VAR_030250

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501E → V in CAG33528. 1 Publication
Sequence conflicti60 – 601K → R in AAL55767. 1 Publication
Sequence conflicti69 – 691S → P in CAG33528. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF289583 mRNA. Translation: AAL55767.1.
CR457247 mRNA. Translation: CAG33528.1.
AK000632 mRNA. Translation: BAA91297.1.
BC001706 mRNA. Translation: AAH01706.1.
CCDSiCCDS8209.1.
RefSeqiNP_060377.1. NM_017907.2.
UniGeneiHs.731528.

Genome annotation databases

EnsembliENST00000278671; ENSP00000278671; ENSG00000149357.
GeneIDi55004.
KEGGihsa:55004.
UCSCiuc001ort.3. human.

Polymorphism databases

DMDMi125863645.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF289583 mRNA. Translation: AAL55767.1 .
CR457247 mRNA. Translation: CAG33528.1 .
AK000632 mRNA. Translation: BAA91297.1 .
BC001706 mRNA. Translation: AAH01706.1 .
CCDSi CCDS8209.1.
RefSeqi NP_060377.1. NM_017907.2.
UniGenei Hs.731528.

3D structure databases

ProteinModelPortali Q6IAA8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120336. 16 interactions.
IntActi Q6IAA8. 16 interactions.
MINTi MINT-1372069.
STRINGi 9606.ENSP00000278671.

PTM databases

PhosphoSitei Q6IAA8.

Polymorphism databases

DMDMi 125863645.

Proteomic databases

MaxQBi Q6IAA8.
PaxDbi Q6IAA8.
PeptideAtlasi Q6IAA8.
PRIDEi Q6IAA8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000278671 ; ENSP00000278671 ; ENSG00000149357 .
GeneIDi 55004.
KEGGi hsa:55004.
UCSCi uc001ort.3. human.

Organism-specific databases

CTDi 55004.
GeneCardsi GC11M071809.
H-InvDB HIX0009905.
HGNCi HGNC:26068. LAMTOR1.
HPAi HPA002997.
MIMi 613510. gene.
neXtProti NX_Q6IAA8.
PharmGKBi PA143485354.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG73401.
HOVERGENi HBG081218.
InParanoidi Q6IAA8.
OMAi PYSDVQQ.
PhylomeDBi Q6IAA8.
TreeFami TF323788.

Miscellaneous databases

GenomeRNAii 55004.
NextBioi 58336.
PROi Q6IAA8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q6IAA8.
Bgeei Q6IAA8.
CleanExi HS_C11orf59.
Genevestigatori Q6IAA8.

Family and domain databases

InterProi IPR026310. LAMTOR1-like.
IPR028209. LAMTOR1/MEH1.
[Graphical view ]
PANTHERi PTHR13401. PTHR13401. 1 hit.
Pfami PF15454. LAMTOR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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].
  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: Skin.
  5. Bienvenut W.V.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 48-60 AND 135-147, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "A novel protein associated with membrane-type 1 matrix metalloproteinase binds p27(kip1) and regulates RhoA activation, actin remodeling, and matrigel invasion."
    Hoshino D., Tomari T., Nagano M., Koshikawa N., Seiki M.
    J. Biol. Chem. 284:27315-27326(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MMP14 AND CDKN1B.
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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, IDENTIFICATION IN RAGULATOR COMPLEX, INTERACTION WITH RRAGB AND RRAGD.
  12. "Pdro, a protein associated with late endosomes and lysosomes and implicated in cellular cholesterol homeostasis."
    Guillaumot P., Luquain C., Malek M., Huber A.L., Brugiere S., Garin J., Grunwald D., Regnier D., Petrilli V., Lefai E., Manie S.N.
    PLoS ONE 5:E10977-E10977(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY CHOLESTEROL.
  13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Ragulator is a GEF for the Rag GTPases that signal amino acid levels to mTORC1."
    Bar-Peled L., Schweitzer L.D., Zoncu R., Sabatini D.M.
    Cell 150:1196-1208(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MTORC1 SIGNALING, IDENTIFICATION IN RAGULATOR COMPLEX, INTERACTION WITH MTORC1 COMPLEX AND RAG GTPASES.

Entry informationi

Entry nameiLTOR1_HUMAN
AccessioniPrimary (citable) accession number: Q6IAA8
Secondary accession number(s): Q8WZ09, Q9NWT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: February 6, 2007
Last modified: September 3, 2014
This is version 83 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families
  6. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

External Data

Dasty 3