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O43504

- LTOR5_HUMAN

UniProt

O43504 - LTOR5_HUMAN

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Protein

Ragulator complex protein LAMTOR5

Gene

LAMTOR5

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. When complexed to BIRC5, interferes with apoptosome assembly, preventing recruitment of pro-caspase-9 to oligomerized APAF1, thereby selectively suppressing apoptosis initiated via the mitochondrial/cytochrome c pathway. Down-regulates hepatitis B virus (HBV) replication.2 Publications

GO - Biological processi

  1. cellular response to amino acid stimulus Source: UniProtKB
  2. negative regulation of apoptotic process Source: UniProtKB
  3. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  4. positive regulation of GTPase activity Source: GOC
  5. positive regulation of TOR signaling Source: UniProtKB
  6. protein localization to lysosome Source: UniProtKB
  7. regulation of cell size Source: UniProtKB
  8. response to virus Source: ProtInc
  9. viral genome replication Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ragulator complex protein LAMTOR5
Alternative name(s):
Hepatitis B virus X-interacting protein
Short name:
HBV X-interacting protein
Short name:
HBX-interacting protein
Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5
Gene namesi
Name:LAMTOR5
Synonyms:HBXIP, XIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:17955. LAMTOR5.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. lysosome Source: UniProtKB
  3. Ragulator complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lysosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121T → A: No change. 1 Publication
Mutagenesisi36 – 361T → A: No interaction with XABX14-154 (truncated form of HBX). 1 Publication

Organism-specific databases

PharmGKBiPA29211.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9191Ragulator complex protein LAMTOR5PRO_0000066007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO43504.
PaxDbiO43504.
PRIDEiO43504.

PTM databases

PhosphoSiteiO43504.

Expressioni

Tissue specificityi

Highly expressed in skeletal and cardiac muscle, followed by pancreas, kidney, liver, brain, placenta and lung. Elevated levels in both cancerous and non-cancerous liver tissue of patients with chronic HBV infection compared with hepatic tissue without HBV infection.

Gene expression databases

BgeeiO43504.
CleanExiHS_HBXIP.
ExpressionAtlasiO43504. baseline and differential.
GenevestigatoriO43504.

Organism-specific databases

HPAiHPA006812.

Interactioni

Subunit structurei

Homodimer (Probable). 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 phosphorylated BIRC5; the resulting complex binds pro-caspase-9, as well as active caspase-9, but much less efficiently. Interacts with SUPV3L1. Interacts with hepatitis B virus (HBV) oncoprotein HBX C-terminus.4 PublicationsCurated

Protein-protein interaction databases

BioGridi115796. 19 interactions.
IntActiO43504. 50 interactions.
MINTiMINT-1389550.
STRINGi9606.ENSP00000256644.

Structurei

Secondary structure

1
91
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 139Combined sources
Beta strandi18 – 247Combined sources
Beta strandi30 – 356Combined sources
Helixi39 – 413Combined sources
Helixi42 – 5413Combined sources
Beta strandi65 – 695Combined sources
Beta strandi72 – 798Combined sources
Beta strandi82 – 887Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MS6X-ray2.08A1-91[»]
3MSHX-ray1.51A1-91[»]
ProteinModelPortaliO43504.
SMRiO43504. Positions 1-91.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43504.

Family & Domainsi

Sequence similaritiesi

Belongs to the LAMTOR5 family.Curated

Phylogenomic databases

eggNOGiNOG84672.
GeneTreeiENSGT00390000006247.
HOGENOMiHOG000045746.
HOVERGENiHBG010343.
InParanoidiO43504.
KOiK16344.
OrthoDBiEOG7FNCBP.
PhylomeDBiO43504.
TreeFamiTF324433.

Family and domain databases

InterProiIPR024135. HBXIP.
[Graphical view]
PANTHERiPTHR13342. PTHR13342. 1 hit.
PRINTSiPR02092. HEPBVIRUSXIP.

Sequencei

Sequence statusi: Complete.

O43504-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEATLEQHLE DTMKNPSIVG VLCTDSQGLN LGCRGTLSDE HAGVISVLAQ
60 70 80 90
QAAKLTSDPT DIPVVCLESD NGNIMIQKHD GITVAVHKMA S
Length:91
Mass (Da):9,614
Last modified:June 1, 1998 - v1
Checksum:i01D9E762ABC63980
GO

Sequence cautioni

The sequence AAH62619.2 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029890 mRNA. Translation: AAC52032.1.
AY623819 mRNA. Translation: AAV30683.1.
CR456866 mRNA. Translation: CAG33147.1.
CR542130 mRNA. Translation: CAG46927.1.
AL390797 Genomic DNA. Translation: CAH71488.1.
BC062619 mRNA. Translation: AAH62619.2. Different initiation.
RefSeqiNP_006393.2. NM_006402.2.
UniGeneiHs.439815.

Genome annotation databases

EnsembliENST00000256644; ENSP00000256644; ENSG00000134248.
ENST00000602318; ENSP00000473439; ENSG00000134248.
ENST00000614544; ENSP00000480529; ENSG00000134248.
GeneIDi10542.
KEGGihsa:10542.
UCSCiuc001dzr.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029890 mRNA. Translation: AAC52032.1 .
AY623819 mRNA. Translation: AAV30683.1 .
CR456866 mRNA. Translation: CAG33147.1 .
CR542130 mRNA. Translation: CAG46927.1 .
AL390797 Genomic DNA. Translation: CAH71488.1 .
BC062619 mRNA. Translation: AAH62619.2 . Different initiation.
RefSeqi NP_006393.2. NM_006402.2.
UniGenei Hs.439815.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3MS6 X-ray 2.08 A 1-91 [» ]
3MSH X-ray 1.51 A 1-91 [» ]
ProteinModelPortali O43504.
SMRi O43504. Positions 1-91.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115796. 19 interactions.
IntActi O43504. 50 interactions.
MINTi MINT-1389550.
STRINGi 9606.ENSP00000256644.

PTM databases

PhosphoSitei O43504.

Proteomic databases

MaxQBi O43504.
PaxDbi O43504.
PRIDEi O43504.

Protocols and materials databases

DNASUi 10542.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256644 ; ENSP00000256644 ; ENSG00000134248 .
ENST00000602318 ; ENSP00000473439 ; ENSG00000134248 .
ENST00000614544 ; ENSP00000480529 ; ENSG00000134248 .
GeneIDi 10542.
KEGGi hsa:10542.
UCSCi uc001dzr.3. human.

Organism-specific databases

CTDi 10542.
GeneCardsi GC01M110944.
H-InvDB HIX0029151.
HGNCi HGNC:17955. LAMTOR5.
HPAi HPA006812.
MIMi 608521. gene.
neXtProti NX_O43504.
PharmGKBi PA29211.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG84672.
GeneTreei ENSGT00390000006247.
HOGENOMi HOG000045746.
HOVERGENi HBG010343.
InParanoidi O43504.
KOi K16344.
OrthoDBi EOG7FNCBP.
PhylomeDBi O43504.
TreeFami TF324433.

Miscellaneous databases

EvolutionaryTracei O43504.
GeneWikii HBXIP.
GenomeRNAii 10542.
NextBioi 39997.
PROi O43504.
SOURCEi Search...

Gene expression databases

Bgeei O43504.
CleanExi HS_HBXIP.
ExpressionAtlasi O43504. baseline and differential.
Genevestigatori O43504.

Family and domain databases

InterProi IPR024135. HBXIP.
[Graphical view ]
PANTHERi PTHR13342. PTHR13342. 1 hit.
PRINTSi PR02092. HEPBVIRUSXIP.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a novel hepatitis B virus x binding protein that inhibits viral replication."
    Melegari M., Scaglioni P.P., Wands J.R.
    J. Virol. 72:1737-1743(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS.
    Tissue: Liver.
  2. "Clone of human uterus hepatitis B virus x interacting protein (HBXIP) gene."
    Zhang X., Ye L., Shi Z.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Uterus.
  3. "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].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "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].
  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].
    Tissue: Colon.
  7. Bienvenut W.V., Quadroni M.
    Submitted (JUL-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-14, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Melanoma.
  8. "HBXIP functions as a cofactor of survivin in apoptosis suppression."
    Marusawa H., Matsuzawa S., Welsh K., Zou H., Armstrong R., Tamm I., Reed J.C.
    EMBO J. 22:2729-2740(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS SUPPRESSION, INTERACTION WITH BIRC5, SUBCELLULAR LOCATION.
  9. "Human ATP-dependent RNA/DNA helicase hSuv3p interacts with the cofactor of survivin HBXIP."
    Minczuk M., Mroczek S., Pawlak S.D., Stepien P.P.
    FEBS J. 272:5008-5019(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUPV3L1, SUBCELLULAR LOCATION.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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, SUBCELLULAR LOCATION.
  14. "Structural characterization of HBXIP: the protein that interacts with the anti-apoptotic protein survivin and the oncogenic viral protein HBx."
    Garcia-Saez I., Lacroix F.B., Blot D., Gabel F., Skoufias D.A.
    J. Mol. Biol. 405:331-340(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiLTOR5_HUMAN
AccessioniPrimary (citable) accession number: O43504
Secondary accession number(s): Q6IBD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: November 26, 2014
This is version 116 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

Miscellaneous

Suppression of caspase activation by the BIRC5/HBXIP complex is increased in the presence of HBX.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3