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LAMTOR5
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3MS6, 3MSH
Identifiers
Aliases	LAMTOR5, HBXIP, XIP, late endosomal/lysosomal adaptor, MAPK and MTOR activator 5
External IDs	OMIM: 608521; MGI: 1915826; HomoloGene: 4668; GeneCards: LAMTOR5; OMA:LAMTOR5 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1p13.3 Start 110,401,249 bp End 110,407,942 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 F2.3 Start 107,186,174 bp End 107,191,398 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in kidney tubule islet of Langerhans palpebral conjunctiva monocyte human kidney apex of heart muscle of thigh left ventricle anterior pituitary glomerulus Top expressed in right kidney yolk sac facial motor nucleus medial ganglionic eminence proximal tubule human kidney endocardial cushion embryo anterior horn of spinal cord embryo More reference expression data BioGPS More reference expression data
Gene ontology Molecular function guanyl-nucleotide exchange factor activity protein binding molecular adaptor activity Cellular component cytoplasm cytosol Ragulator complex lysosomal membrane lysosome Biological process regulation of cell size negative regulation of cysteine-type endopeptidase activity involved in apoptotic process viral genome replication response to virus negative regulation of apoptotic process protein localization to lysosome cellular response to amino acid stimulus positive regulation of TOR signaling regulation of macroautophagy positive regulation of TORC1 signaling Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10542 68576 Ensembl ENSG00000134248 ENSMUSG00000087260 UniProt O43504 Q9D1L9 RefSeq (mRNA) NM_006402 NM_001382293 NM_026774 RefSeq (protein) NP_006393 NP_001369222 NP_006393.2 NP_081050 Location (UCSC) Chr 1: 110.4 – 110.41 Mb Chr 3: 107.19 – 107.19 Mb PubMed search
Wikidata
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Hepatitis B virus X-interacting protein is a protein that in humans is encoded by the HBXIP gene.

This gene encodes a protein that specifically complexes with the C-terminus of hepatitis B virus X protein (HBx). The function of this protein is to negatively regulate HBx activity and thus to alter the replication life cycle of the virus.

Interactions

HBXIP has been shown to interact with NCOA6.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000134248 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000087260 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Melegari M, Scaglioni PP, Wands JR (March 1998). "Cloning and characterization of a novel hepatitis B virus x binding protein that inhibits viral replication". Journal of Virology. 72 (3): 1737–43. doi:10.1128/jvi.72.3.1737-1743.1998. PMC 109461. PMID 9499022.
6. ^ "Entrez Gene: HBXIP hepatitis B virus x interacting protein".
7. Kong HJ, Park MJ, Hong S, Yu HJ, Lee YC, Choi YH, Cheong J (November 2003). "Hepatitis B virus X protein regulates transactivation activity and protein stability of the cancer-amplified transcription coactivator ASC-2". Hepatology. 38 (5): 1258–66. doi:10.1053/jhep.2003.50451. PMID 14578865.

Further reading

• Shamay M, Barak O, Doitsh G, Ben-Dor I, Shaul Y (March 2002). "Hepatitis B virus pX interacts with HBXAP, a PHD finger protein to coactivate transcription". The Journal of Biological Chemistry. 277 (12): 9982–8. doi:10.1074/jbc.M111354200. PMID 11788598.
• Li Y, Lu YY (April 2002). "Applying a highly specific and reproducible cDNA RDA method to clone garlic up-regulated genes in human gastric cancer cells". World Journal of Gastroenterology. 8 (2): 213–6. doi:10.3748/wjg.v8.i2.213. PMC 4658353. PMID 11925594.
• Marusawa H, Matsuzawa S, Welsh K, Zou H, Armstrong R, Tamm I, Reed JC (June 2003). "HBXIP functions as a cofactor of survivin in apoptosis suppression". The EMBO Journal. 22 (11): 2729–40. doi:10.1093/emboj/cdg263. PMC 156760. PMID 12773388.
• Kong HJ, Park MJ, Hong S, Yu HJ, Lee YC, Choi YH, Cheong J (November 2003). "Hepatitis B virus X protein regulates transactivation activity and protein stability of the cancer-amplified transcription coactivator ASC-2". Hepatology. 38 (5): 1258–66. doi:10.1053/jhep.2003.50451. PMID 14578865.
• Lee SH, Park SG, Lim SO, Jung G (June 2005). "The hepatitis B virus X protein up-regulates lymphotoxin alpha expression in hepatocytes". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1741 (1–2): 75–84. doi:10.1016/j.bbadis.2004.10.004. PMID 15955450.
• Lee AT, Ren J, Wong ET, Ban KH, Lee LA, Lee CG (September 2005). "The hepatitis B virus X protein sensitizes HepG2 cells to UV light-induced DNA damage". The Journal of Biological Chemistry. 280 (39): 33525–35. doi:10.1074/jbc.M506628200. PMID 16055925.
• Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
• Minczuk M, Mroczek S, Pawlak SD, Stepien PP (October 2005). "Human ATP-dependent RNA/DNA helicase hSuv3p interacts with the cofactor of survivin HBXIP". The FEBS Journal. 272 (19): 5008–19. doi:10.1111/j.1742-4658.2005.04910.x. PMID 16176273. S2CID 40846992.
• Muroyama R, Kato N, Yoshida H, Otsuka M, Moriyama M, Wang Y, Shao RX, Dharel N, Tanaka Y, Ohta M, Tateishi R, Shiina S, Tatsukawa M, Fukai K, Imazeki F, Yokosuka O, Shiratori Y, Omata M (December 2006). "Nucleotide change of codon 38 in the X gene of hepatitis B virus genotype C is associated with an increased risk of hepatocellular carcinoma". Journal of Hepatology. 45 (6): 805–12. doi:10.1016/j.jhep.2006.07.025. PMID 17050029.
• Chen J, Siddiqui A (June 2007). "Hepatitis B virus X protein stimulates the mitochondrial translocation of Raf-1 via oxidative stress". Journal of Virology. 81 (12): 6757–60. doi:10.1128/JVI.00172-07. PMC 1900104. PMID 17428866.

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