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Q9Y2Q5

- LTOR2_HUMAN

UniProt

Q9Y2Q5 - LTOR2_HUMAN

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Protein
Ragulator complex protein LAMTOR2
Gene
LAMTOR2, MAPBPIP, ROBLD3, HSPC003
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. Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2.2 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. activation of MAPKK activity Source: Ensembl
  2. cell growth Source: UniProtKB
  3. cellular protein localization Source: UniProtKB
  4. cellular response to amino acid stimulus Source: UniProtKB
  5. positive regulation of TOR signaling Source: UniProtKB
  6. regulation of GTPase activity Source: GOC
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ragulator complex protein LAMTOR2
Alternative name(s):
Endosomal adaptor protein p14
Late endosomal/lysosomal Mp1-interacting protein
Late endosomal/lysosomal adaptor and MAPK and MTOR activator 2
Mitogen-activated protein-binding protein-interacting protein
Short name:
MAPBP-interacting protein
Roadblock domain-containing protein 3
Gene namesi
Name:LAMTOR2
Synonyms:MAPBPIP, ROBLD3
ORF Names:HSPC003
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:29796. LAMTOR2.

Subcellular locationi

Late endosome membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Lysosome membrane; Peripheral membrane protein; Cytoplasmic side By similarity 1 Publication

GO - Cellular componenti

  1. Ragulator complex Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. late endosome Source: UniProtKB
  4. lysosomal membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Lysosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Immunodeficiency due to defect in MAPBP-interacting protein (ID-MAPBPIP) [MIM:610798]: This form of primary immunodeficiency syndrome includes congenital neutropenia, partial albinism, short stature and B-cell and cytotoxic T-cell deficiency.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Organism-specific databases

MIMi610798. phenotype.
Orphaneti90023. Primary immunodeficiency syndrome due to p14 deficiency.
PharmGKBiPA164725527.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 125125Ragulator complex protein LAMTOR2
PRO_0000220960Add
BLAST

Proteomic databases

MaxQBiQ9Y2Q5.
PaxDbiQ9Y2Q5.
PRIDEiQ9Y2Q5.

2D gel databases

OGPiQ9Y2Q5.

PTM databases

PhosphoSiteiQ9Y2Q5.

Expressioni

Gene expression databases

BgeeiQ9Y2Q5.
GenevestigatoriQ9Y2Q5.

Organism-specific databases

HPAiHPA004126.

Interactioni

Subunit structurei

Interacts with MAPK1 and MAP2K1 By similarity. 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 LAMTOR1 and LAMTOR3; the interaction is direct.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LAMTOR3Q9UHA47EBI-2643704,EBI-1038192

Protein-protein interaction databases

BioGridi118783. 12 interactions.
IntActiQ9Y2Q5. 10 interactions.
MINTiMINT-5003178.
STRINGi9606.ENSP00000357288.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2Q5.
SMRiQ9Y2Q5. Positions 1-125.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 7014Required for location at endosomes By similarity
Add
BLAST

Sequence similaritiesi

Belongs to the GAMAD family.

Phylogenomic databases

eggNOGiNOG237668.
HOVERGENiHBG004518.
OMAiIDCECGH.
OrthoDBiEOG77DJ8B.
PhylomeDBiQ9Y2Q5.
TreeFamiTF313929.

Family and domain databases

InterProiIPR004942. Dynein_light-rel.
[Graphical view]
PfamiPF03259. Robl_LC7. 1 hit.
[Graphical view]
SMARTiSM00960. Robl_LC7. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y2Q5-1) [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

MLRPKALTQV LSQANTGGVQ STLLLNNEGS LLAYSGYGDT DARVTAAIAS    50
NIWAAYDRNG NQAFNEDNLK FILMDCMEGR VAITRVANLL LCMYAKETVG 100
FGMLKAKAQA LVQYLEEPLT QVAAS 125
Length:125
Mass (Da):13,508
Last modified:November 1, 1999 - v1
Checksum:i69599211C2CBC03D
GO
Isoform 2 (identifier: Q9Y2Q5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     109-125: QALVQYLEEPLTQVAAS → VCGTDLCSPSAGPGFGAVPGGAPHPSGGILTALVEAGVRKEK

Note: No experimental confirmation available.

Show »
Length:150
Mass (Da):15,609
Checksum:iD45D4B887C721086
GO
Isoform 3 (identifier: Q9Y2Q5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     78-107: Missing.

Show »
Length:95
Mass (Da):10,242
Checksum:i13ADB9F75E3E9E8C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei78 – 10730Missing in isoform 3.
VSP_040980Add
BLAST
Alternative sequencei109 – 12517QALVQ…QVAAS → VCGTDLCSPSAGPGFGAVPG GAPHPSGGILTALVEAGVRK EK in isoform 2.
VSP_036543Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF070659 mRNA. Translation: AAD20965.1.
AK307086 mRNA. No translation available.
AL355388 Genomic DNA. Translation: CAH72635.1.
AL355388 Genomic DNA. Translation: CAH72636.1.
AL355388 Genomic DNA. Translation: CAH72637.1.
BC024190 mRNA. Translation: AAH24190.1.
CCDSiCCDS1128.1. [Q9Y2Q5-1]
CCDS44243.1. [Q9Y2Q5-3]
RefSeqiNP_001138736.1. NM_001145264.1. [Q9Y2Q5-3]
NP_054736.1. NM_014017.3. [Q9Y2Q5-1]
UniGeneiHs.632483.

Genome annotation databases

EnsembliENST00000368302; ENSP00000357285; ENSG00000116586. [Q9Y2Q5-2]
ENST00000368304; ENSP00000357287; ENSG00000116586. [Q9Y2Q5-3]
ENST00000368305; ENSP00000357288; ENSG00000116586. [Q9Y2Q5-1]
GeneIDi28956.
KEGGihsa:28956.
UCSCiuc001fnb.3. human. [Q9Y2Q5-1]
uc010pgy.1. human. [Q9Y2Q5-3]

Polymorphism databases

DMDMi12585246.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

MAPBPIPbase

ROBLD3 mutation db

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF070659 mRNA. Translation: AAD20965.1 .
AK307086 mRNA. No translation available.
AL355388 Genomic DNA. Translation: CAH72635.1 .
AL355388 Genomic DNA. Translation: CAH72636.1 .
AL355388 Genomic DNA. Translation: CAH72637.1 .
BC024190 mRNA. Translation: AAH24190.1 .
CCDSi CCDS1128.1. [Q9Y2Q5-1 ]
CCDS44243.1. [Q9Y2Q5-3 ]
RefSeqi NP_001138736.1. NM_001145264.1. [Q9Y2Q5-3 ]
NP_054736.1. NM_014017.3. [Q9Y2Q5-1 ]
UniGenei Hs.632483.

3D structure databases

ProteinModelPortali Q9Y2Q5.
SMRi Q9Y2Q5. Positions 1-125.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118783. 12 interactions.
IntActi Q9Y2Q5. 10 interactions.
MINTi MINT-5003178.
STRINGi 9606.ENSP00000357288.

PTM databases

PhosphoSitei Q9Y2Q5.

Polymorphism databases

DMDMi 12585246.

2D gel databases

OGPi Q9Y2Q5.

Proteomic databases

MaxQBi Q9Y2Q5.
PaxDbi Q9Y2Q5.
PRIDEi Q9Y2Q5.

Protocols and materials databases

DNASUi 28956.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368302 ; ENSP00000357285 ; ENSG00000116586 . [Q9Y2Q5-2 ]
ENST00000368304 ; ENSP00000357287 ; ENSG00000116586 . [Q9Y2Q5-3 ]
ENST00000368305 ; ENSP00000357288 ; ENSG00000116586 . [Q9Y2Q5-1 ]
GeneIDi 28956.
KEGGi hsa:28956.
UCSCi uc001fnb.3. human. [Q9Y2Q5-1 ]
uc010pgy.1. human. [Q9Y2Q5-3 ]

Organism-specific databases

CTDi 28956.
GeneCardsi GC01P156025.
HGNCi HGNC:29796. LAMTOR2.
HPAi HPA004126.
MIMi 610389. gene.
610798. phenotype.
neXtProti NX_Q9Y2Q5.
Orphaneti 90023. Primary immunodeficiency syndrome due to p14 deficiency.
PharmGKBi PA164725527.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG237668.
HOVERGENi HBG004518.
OMAi IDCECGH.
OrthoDBi EOG77DJ8B.
PhylomeDBi Q9Y2Q5.
TreeFami TF313929.

Miscellaneous databases

GenomeRNAii 28956.
NextBioi 51776.
PROi Q9Y2Q5.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y2Q5.
Genevestigatori Q9Y2Q5.

Family and domain databases

InterProi IPR004942. Dynein_light-rel.
[Graphical view ]
Pfami PF03259. Robl_LC7. 1 hit.
[Graphical view ]
SMARTi SM00960. Robl_LC7. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  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 3).
  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] (ISOFORM 1).
    Tissue: Lung.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Placenta.
  6. "A novel human primary immunodeficiency syndrome caused by deficiency of the endosomal adaptor protein p14."
    Bohn G., Allroth A., Brandes G., Thiel J., Glocker E., Schaeffer A.A., Rathinam C., Taub N., Teis D., Zeidler C., Dewey R.A., Geffers R., Buer J., Huber L.A., Welte K., Grimbacher B., Klein C.
    Nat. Med. 13:38-45(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN IMMUNODEFICIENCY DUE TO DEFECT IN MAPBP-INTERACTING PROTEIN.
  7. "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.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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 nameiLTOR2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2Q5
Secondary accession number(s): Q5VY97, Q5VY98, Q5VY99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 115 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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