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Protein

Ragulator complex protein LAMTOR2

Gene

LAMTOR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 - Biological processi

  • activation of MAPKK activity Source: Ensembl
  • cell growth Source: UniProtKB
  • cellular protein localization Source: UniProtKB
  • cellular response to amino acid stimulus Source: UniProtKB
  • positive regulation of GTPase activity Source: GOC
  • positive regulation of TOR signaling Source: UniProtKB
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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:29796. LAMTOR2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • late endosome Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • Ragulator complex 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)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionThis form of primary immunodeficiency syndrome includes congenital neutropenia, partial albinism, short stature and B-cell and cytotoxic T-cell deficiency.

See also OMIM:610798

Organism-specific databases

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

Polymorphism and mutation databases

BioMutaiLAMTOR2.
DMDMi12585246.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 125125Ragulator complex protein LAMTOR2PRO_0000220960Add
BLAST

Proteomic databases

MaxQBiQ9Y2Q5.
PaxDbiQ9Y2Q5.
PRIDEiQ9Y2Q5.

2D gel databases

OGPiQ9Y2Q5.

PTM databases

PhosphoSiteiQ9Y2Q5.

Expressioni

Gene expression databases

BgeeiQ9Y2Q5.
GenevisibleiQ9Y2Q5. HS.

Organism-specific databases

HPAiHPA004126.

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 (PubMed:20381137, PubMed:22980980). 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 (PubMed:20381137, PubMed:22980980). The Ragulator complex interacts with SLC38A9; the probable amino acid sensor (PubMed:25561175, PubMed:25567906). Interacts with LAMTOR1 and LAMTOR3; the interaction is direct. Interacts with MAPK1 and MAP2K1 (By similarity).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LAMTOR3Q9UHA413EBI-2643704,EBI-1038192

Protein-protein interaction databases

BioGridi118783. 20 interactions.
IntActiQ9Y2Q5. 11 interactions.
MINTiMINT-5003178.
STRINGi9606.ENSP00000357288.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2Q5.
SMRiQ9Y2Q5. Positions 1-125.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 7014Required for location at endosomesBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the GAMAD family.Curated

Phylogenomic databases

eggNOGiNOG237668.
GeneTreeiENSGT00390000006100.
HOGENOMiHOG000007645.
HOVERGENiHBG004518.
InParanoidiQ9Y2Q5.
OMAiYEKHGRN.
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. AlignAdd to basket

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

        10         20         30         40         50
MLRPKALTQV LSQANTGGVQ STLLLNNEGS LLAYSGYGDT DARVTAAIAS
60 70 80 90 100
NIWAAYDRNG NQAFNEDNLK FILMDCMEGR VAITRVANLL LCMYAKETVG
110 120
FGMLKAKAQA LVQYLEEPLT QVAAS
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. 1 PublicationVSP_040980Add
BLAST
Alternative sequencei109 – 12517QALVQ…QVAAS → VCGTDLCSPSAGPGFGAVPG GAPHPSGGILTALVEAGVRK EK in isoform 2. CuratedVSP_036543Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
GeneIDi28956.
KEGGihsa:28956.
UCSCiuc001fnb.3. human. [Q9Y2Q5-1]
uc010pgy.1. human. [Q9Y2Q5-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

MAPBPIPbase

ROBLD3 mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9Y2Q5.
SMRiQ9Y2Q5. Positions 1-125.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118783. 20 interactions.
IntActiQ9Y2Q5. 11 interactions.
MINTiMINT-5003178.
STRINGi9606.ENSP00000357288.

PTM databases

PhosphoSiteiQ9Y2Q5.

Polymorphism and mutation databases

BioMutaiLAMTOR2.
DMDMi12585246.

2D gel databases

OGPiQ9Y2Q5.

Proteomic databases

MaxQBiQ9Y2Q5.
PaxDbiQ9Y2Q5.
PRIDEiQ9Y2Q5.

Protocols and materials databases

DNASUi28956.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi28956.
GeneCardsiGC01P156025.
HGNCiHGNC:29796. LAMTOR2.
HPAiHPA004126.
MIMi610389. gene.
610798. phenotype.
neXtProtiNX_Q9Y2Q5.
Orphaneti90023. Primary immunodeficiency syndrome due to p14 deficiency.
PharmGKBiPA164725527.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG237668.
GeneTreeiENSGT00390000006100.
HOGENOMiHOG000007645.
HOVERGENiHBG004518.
InParanoidiQ9Y2Q5.
OMAiYEKHGRN.
OrthoDBiEOG77DJ8B.
PhylomeDBiQ9Y2Q5.
TreeFamiTF313929.

Miscellaneous databases

ChiTaRSiLAMTOR2. human.
GenomeRNAii28956.
NextBioi51776.
PROiQ9Y2Q5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2Q5.
GenevisibleiQ9Y2Q5. HS.

Family and domain databases

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

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.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. Cited for: SUBUNIT.
  12. Cited for: SUBUNIT.

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: July 22, 2015
This is version 126 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.