LPP (gene)

LPP
Identifiers
Aliases	LPP , LIM domain containing preferred translocation partner in lipoma
External IDs	OMIM: 600700; MGI: 2441849; HomoloGene: 4075; GeneCards: LPP; OMA:LPP - orthologs
Gene location (Human) Chr. Chromosome 3 (human) [1] Band 3q27.3-q28 Start 188,153,284 bp [1] End 188,890,671 bp [1]
Gene location (Mouse) Chr. Chromosome 16 (mouse) [2] Band 16|16 B1 Start 24,393,507 bp [2] End 24,992,578 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in saphenous vein urethra vena cava nipple pylorus tail of epididymis cardia seminal vesicula epithelium of colon superficial temporal artery Top expressed in ascending aorta aortic valve Paneth cell umbilical cord tunica media of zone of aorta endothelial cell of lymphatic vessel conjunctival fornix urinary bladder cervix Ileal epithelium More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding metal ion binding Cellular component cell junction plasma membrane membrane nucleus focal adhesion cytoplasm cytosol stress fiber Biological process cell adhesion biological process cell-cell adhesion Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4026 210126 Ensembl ENSG00000145012 ENSMUSG00000033306 UniProt Q93052 Q8BFW7 RefSeq (mRNA) NM_001167671 NM_001167672 NM_005578 NM_001375455 NM_001375456 NM_001375457 NM_001375458 NM_001375459 NM_001375460 NM_001375461 NM_001375462 NM_001375463 NM_001375464 NM_001375465 NM_001145952 NM_001145954 NM_178665 RefSeq (protein) NP_001161143 NP_001161144 NP_005569 NP_001362384 NP_001362385 NP_001362386 NP_001362387 NP_001362388 NP_001362389 NP_001362390 NP_001362391 NP_001362392 NP_001362393 NP_001362394 NP_001139424 NP_001139426 NP_848780 Location (UCSC) Chr 3: 188.15 – 188.89 Mb Chr 16: 24.39 – 24.99 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Lipoma-preferred partner is a protein that in humans is encoded by the LPP gene. ^{[5] [6]}

Function

Lipoma-preferred partner is a subfamily of LIM domain proteins that are characterized by an N-terminal proline rich region and three C-terminal LIM domains. The encoded protein localizes to the cell periphery in focal adhesions and may be involved in cell-cell adhesion and cell motility. This protein also shuttles through the nucleus and may function as a transcriptional co-activator. This gene is located at the junction of certain disease related chromosomal translocations which result in the expression of fusion proteins that may promote tumor growth. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000145012 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000033306 – 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. Petit MM, Mols R, Schoenmakers EF, Mandahl N, Van de Ven WJ (Feb 1997). "LPP, the preferred fusion partner gene of HMGIC in lipomas, is a novel member of the LIM protein gene family". Genomics. 36 (1): 118–29. doi:10.1006/geno.1996.0432. PMID   8812423.
6. "Entrez Gene: LPP LIM domain containing preferred translocation partner in lipoma".

Further reading

• Schoenmakers EF, Wanschura S, Mols R, et al. (1995). "Recurrent rearrangements in the high mobility group protein gene, HMGI-C, in benign mesenchymal tumours". Nat. Genet. 10 (4): 436–44. doi:10.1038/ng0895-436. PMID   7670494. S2CID   29935721.
• Petit MM, Swarts S, Bridge JA, Van de Ven WJ (1998). "Expression of reciprocal fusion transcripts of the HMGIC and LPP genes in parosteal lipoma". Cancer Genet. Cytogenet. 106 (1): 18–23. doi:10.1016/S0165-4608(98)00038-7. PMID   9772904.
• Petit MM, Fradelizi J, Golsteyn RM, et al. (2000). "LPP, an Actin Cytoskeleton Protein Related to Zyxin, Harbors a Nuclear Export Signal and Transcriptional Activation Capacity". Mol. Biol. Cell. 11 (1): 117–29. doi:10.1091/mbc.11.1.117. PMC   14761 . PMID   10637295.
• Rogalla P, Lemke I, Kazmierczak B, Bullerdiek J (2001). "An identical HMGIC-LPP fusion transcript is consistently expressed in pulmonary chondroid hamartomas with t(3;12)(q27-28;q14-15)". Genes Chromosomes Cancer. 29 (4): 363–6. doi:10.1002/1098-2264(2000)9999:9999<1::AID-GCC1043>3.0.CO;2-N. PMID   11066083. S2CID   35883889.
• Harrington JJ, Sherf B, Rundlett S, et al. (2001). "Creation of genome-wide protein expression libraries using random activation of gene expression". Nat. Biotechnol. 19 (5): 440–5. doi:10.1038/88107. PMID   11329013. S2CID   25064683.
• Dahéron L, Veinstein A, Brizard F, et al. (2001). "Human LPP gene is fused to MLL in a secondary acute leukemia with a t(3;11) (q28;q23)". Genes Chromosomes Cancer. 31 (4): 382–9. doi: 10.1002/gcc.1157 . PMID   11433529. S2CID   32921978.
• Lemke I, Rogalla P, Bullerdiek J (2002). "A novel LPP fusion gene indicates the crucial role of truncated LPP proteins in lipomas and pulmonary chondroid hamartomas". Cytogenet. Cell Genet. 95 (3–4): 153–6. doi:10.1159/000059338. PMID   12063392. S2CID   42951388.
• Petit MM, Meulemans SM, Van de Ven WJ (2003). "The focal adhesion and nuclear targeting capacity of the LIM-containing lipoma-preferred partner (LPP) protein". J. Biol. Chem. 278 (4): 2157–68. doi: 10.1074/jbc.M206106200 . PMID   12441356.
• Lemke I, Rogalla P, Grundmann F, et al. (2003). "Expression of the HMGA2-LPP fusion transcript in only 1 of 61 karyotypically normal pulmonary chondroid hamartomas". Cancer Genet. Cytogenet. 138 (2): 160–4. doi:10.1016/S0165-4608(02)00595-2. PMID   12505264.
• Salomon AR, Ficarro SB, Brill LM, et al. (2003). "Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry". Proc. Natl. Acad. Sci. U.S.A. 100 (2): 443–8. Bibcode:2003PNAS..100..443S. doi: 10.1073/pnas.2436191100 . PMC   141014 . PMID   12522270.
• Li B, Zhuang L, Reinhard M, Trueb B (2003). "The lipoma preferred partner LPP interacts with alpha-actinin". J. Cell Sci. 116 (Pt 7): 1359–66. doi: 10.1242/jcs.00309 . PMID   12615977.
• Gorenne I, Nakamoto RK, Phelps CP, et al. (2003). "LPP, a LIM protein highly expressed in smooth muscle". Am. J. Physiol., Cell Physiol. 285 (3): C674–85. doi:10.1152/ajpcell.00608.2002. PMID   12760907.
• Brill LM, Salomon AR, Ficarro SB, et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID   15144186.
• Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID   15592455. S2CID   7200157.
• Petit MM, Meulemans SM, Alen P, et al. (2006). "The tumor suppressor Scrib interacts with the zyxin-related protein LPP, which shuttles between cell adhesion sites and the nucleus". BMC Cell Biol. 6 (1): 1. doi: 10.1186/1471-2121-6-1 . PMC   546208 . PMID   15649318.
• Zhang Y, Wolf-Yadlin A, Ross PL, et al. (2005). "Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules". Mol. Cell. Proteomics. 4 (9): 1240–50. doi: 10.1074/mcp.M500089-MCP200 . PMID   15951569.
• Tao WA, Wollscheid B, O'Brien R, et al. (2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". Nat. Methods. 2 (8): 591–8. doi:10.1038/nmeth776. PMID   16094384. S2CID   20475874.
• von Ahsen I, Rogalla P, Bullerdiek J (2006). "Expression patterns of the LPP-HMGA2 fusion transcript in pulmonary chondroid hamartomas with t(3;12)(q27 approximately 28;q14 approximately 15)". Cancer Genet. Cytogenet. 163 (1): 68–70. doi:10.1016/j.cancergencyto.2005.02.023. PMID   16271958.
• Kubo T, Matsui Y, Goto T, et al. (2006). "Overexpression of HMGA2-LPP fusion transcripts promotes expression of the alpha 2 type XI collagen gene". Biochem. Biophys. Res. Commun. 340 (2): 476–81. doi:10.1016/j.bbrc.2005.12.042. PMID   16375854.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.