Reviewed, UniProtKB/Swiss-Prot Q93052 (LPP_HUMAN)

Names and origin

Protein names

Recommended name:
    Lipoma-preferred partner
Alternative name(s):
    LIM domain-containing preferred translocation partner in lipoma

Gene names

Name:

LPP

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	612 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation of gene transcription. May be involved in signal transduction from cell adhesion sites to the nucleus allowing successful integration of signals arising from soluble factors and cell-cell adhesion sites. Also suggested to serve as a scaffold protein upon which distinct protein complexes are assembled in the cytoplasm and in the nucleus. Ref.2 Ref.6
Subunit structure	Interacts with VASP, with PDZ domains of SCRIB and with ACTN1/alpha-actinin. Ref.6 Ref.8 Ref.9 Ref.12
Subcellular location	Nucleus. Cytoplasm. Cell junction. Cell membrane. Note: Found in the nucleus, in the cytoplasm and at cell adhesion sites. Shuttles between the cytoplasm and the nucleus. It has been found in sites of cell adhesion such as cell-to-cell contact and focal adhesion which are membrane attachment sites of cells to the extracellular matrix. Mainly nuclear when fused with HMGA2/HMGIC and MLL. Ref.6 Ref.8
Tissue specificity	Expressed in a wide variety of tissues but no or very low expression in brain and peripheral leukocytes. Ref.6 Ref.1
Involvement in disease	A chromosomal aberration involving LPP is associated with a subclass of benign mesenchymal tumors known as lipomas. Translocation t(3;12)(q27-q28;q13-q15) with HMGA2 is shown in lipomas. A chromosomal aberration involving LPP is associated with pulmonary chondroid hamartomas. Translocation t(3;12)(q27-q28;q14-q15) with HMGA2 is detected in pulmonary chondroid hamartomas. A chromosomal aberration involving LPP is associated with parosteal lipomas. Translocation t(3;12)(q28;q14) with HMGA2 is also shown in one parosteal lipoma. A chromosomal aberration involving LPP is associated with acute monoblastic leukemia. Translocation t(3;11)(q28;q23) with MLL is associated with acute monoblastic leukemia.
Sequence similarities	Belongs to the zyxin/ajuba family. Contains 3 LIM zinc-binding domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Domain	LIM domain Repeat
Ligand	Metal-binding Zinc
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: HPA focal adhesion Inferred from direct assay. Source: HPA nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Ref.12 Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 612	612	Lipoma-preferred partner		PRO_0000075832
Regions
	Domain	414 – 473	60	LIM zinc-binding 1
	Domain	474 – 534	61	LIM zinc-binding 2
	Domain	535 – 603	69	LIM zinc-binding 3
	Compositional bias	41 – 370	330	Pro-rich
Sites
	Site	371 – 372	2	Breakpoint for translocation to form HMGA2-LPP
	Site	470 – 471	2	Breakpoint for translocation to form HMGA2-LPP and MLL-LPP
Amino acid modifications
	Modified residue	116	1	Phosphoserine By similarity
	Modified residue	126	1	Phosphoserine By similarity
	Modified residue	244	1	Phosphotyrosine By similarity
	Modified residue	297	1	Phosphotyrosine Ref.11
	Modified residue	300	1	Phosphotyrosine Ref.11 Ref.14 Ref.20
	Modified residue	301	1	Phosphotyrosine Ref.14 Ref.20 Ref.10 Ref.13 Ref.15
	Modified residue	317	1	Phosphotyrosine Ref.14 Ref.15 Ref.16
	Modified residue	333	1	Phosphothreonine Ref.18
	Modified residue	375	1	Phosphoserine Ref.17
	Modified residue	397	1	Phosphothreonine Ref.17
Natural variations
	Natural variant	146	1	T → A: dbSNP rs35417432.		VAR_050150
	Natural variant	259	1	S → P: dbSNP rs35940579.		VAR_050151
	Natural variant	346	1	Y → H: dbSNP rs7645635.		VAR_034070
Experimental info
	Mutagenesis	610	1	T → A: Abolishes binding to SCRIB.
	Mutagenesis	612	1	L → A: Abolishes binding to SCRIB.

Sequences

	Sequence		Length	Mass (Da)
	Q93052-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 439CE0101FDE4DDD	FASTA	612	65,746
	10 20 30 40 50 60 MSHPSWLPPK STGEPLGHVP ARMETTHSFG NPSISVSTQQ PPKKFAPVVA PKPKYNPYKQ 70 80 90 100 110 120 PGGEGDFLPP PPPPLDDSSA LPSISGNFPP PPPLDEEAFK VQGNPGGKTL EERRSSLDAE 130 140 150 160 170 180 IDSLTSILAD LECSSPYKPR PPQSSTGSTA SPPVSTPVTG HKRMVIPNQP PLTATKKSTL 190 200 210 220 230 240 KPQPAPQAGP IPVAPIGTLK PQPQPVPASY TTASTSSRPT FNVQVKSAQP SPHYMAAPSS 250 260 270 280 290 300 GQIYGSGPQG YNTQPVPVSG QCPPPSTRGG MDYAYIPPPG LQPEPGYGYA PNQGRYYEGY 310 320 330 340 350 360 YAAGPGYGGR NDSDPTYGQQ GHPNTWKREP GYTPPGAGNQ NPPGMYPVTG PKKTYITDPV 370 380 390 400 410 420 SAPCAPPLQP KGGHSGQLGP SSVAPSFRPE DELEHLTKKM LYDMENPPAD EYFGRCARCG 430 440 450 460 470 480 ENVVGEGTGC TAMDQVFHVD CFTCIICNNK LRGQPFYAVE KKAYCEPCYI NTLEQCNVCS 490 500 510 520 530 540 KPIMERILRA TGKAYHPHCF TCVMCHRSLD GIPFTVDAGG LIHCIEDFHK KFAPRCSVCK 550 560 570 580 590 600 EPIMPAPGQE ETVRIVALDR DFHVHCYRCE DCGGLLSEGD NQGCYPLDGH ILCKTCNSAR 610 IRVLTAKAST DL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"LPP, the preferred fusion partner gene of HMGIC in lipomas, is a novel member of the LIM protein gene family." Petit M.M.R., Mols R., Schoenmakers E.F., Mandahl N., Van de Ven W.J.M. Genomics 36:118-129(1996) [PubMed: 8812423] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CHROMOSOMAL TRANSLOCATION WITH HMGA2, TISSUE SPECIFICITY. Tissue: Small intestine.
[2]	"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], FUNCTION.
[3]	"A novel LPP fusion gene indicates the crucial role of truncated LPP proteins in lipomas and pulmonary chondroid hamartomas." Lemke I., Rogalla P., Bullerdiek J. Cytogenet. Cell Genet. 95:153-156(2001) [PubMed: 12063392] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 276-371.
[4]	"Expression of reciprocal fusion transcripts of the HMGIC and LPP genes in parosteal lipoma." Petit M.M., Swarts S., Bridge J.A., Van de Ven W.J.M. Cancer Genet. Cytogenet. 106:18-23(1998) [PubMed: 9772904] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH HMGA2.
[5]	"An identical HMGIC-LPP fusion transcript is consistently expressed in pulmonary chondroid hamartomas with t(3;12)(q27-28;q14-15)." Rogalla P., Lemke I., Kazmierczak B., Bullerdiek J. Genes Chromosomes Cancer 29:363-366(2000) [PubMed: 11066083] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH HMGA2.
[6]	"LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity." Petit M.M., Fradelizi J., Golsteyn R.M., Ayoubi T.A., Menichi B., Louvard D., Van de Ven W.J.M., Friederich E. Mol. Biol. Cell 11:117-129(2000) [PubMed: 10637295] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH VASP.
[7]	"Human LPP gene is fused to MLL in a secondary acute leukemia with a t(3;11) (q28;q23)." Daheron L., Veinstein A., Brizard F., Drabkin H., Lacotte L., Guilhot F., Larsen C.J., Brizard A., Roche J. Genes Chromosomes Cancer 31:382-389(2001) [PubMed: 11433529] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH MLL.
[8]	"The focal adhesion and nuclear targeting capacity of the LIM-containing lipoma-preferred partner (LPP) protein." Petit M.M., Meulemans S.M., Van de Ven W.J.M. J. Biol. Chem. 278:2157-2168(2003) [PubMed: 12441356] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH VASP AND ACTN1.
[9]	"The lipoma preferred partner LPP interacts with alpha-actinin." Li B., Zhuang L., Reinhard M., Trueb B. J. Cell Sci. 116:1359-1366(2003) [PubMed: 12615977] [Abstract] Cited for: INTERACTION WITH ACTN1.
[10]	"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry." Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C. Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed: 12522270] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-301, MASS SPECTROMETRY.
[11]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-297 AND TYR-300, MASS SPECTROMETRY. Tissue: T-cell.
[12]	"The tumor suppressor Scrib interacts with the zyxin-related protein LPP, which shuttles between cell adhesion sites and the nucleus." Petit M.M.R., Meulemans S.M.P., Alen P., Ayoubi T.A.Y., Jansen E., Van de Ven W.J.M. BMC Cell Biol. 6:1-1(2005) [PubMed: 15649318] [Abstract] Cited for: INTERACTION WITH SCRIB, MUTAGENESIS.
[13]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-301, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-300; TYR-301 AND TYR-317, MASS SPECTROMETRY.
[15]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-301 AND TYR-317, MASS SPECTROMETRY. Tissue: T-cell.
[16]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-317, MASS SPECTROMETRY.
[17]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375 AND THR-397, MASS SPECTROMETRY.
[18]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, MASS SPECTROMETRY.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-300 AND TYR-301, MASS SPECTROMETRY. Tissue: Mammary epithelium.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBLGenBankDDBJ	U49957 mRNA. Translation: AAC50738.1. U49968 , U49960, U49961, U49962, U49963, U49964, U49965, U49966, U49967 Genomic DNA. Translation: AAC50739.1. CR457074 mRNA. Translation: CAG33355.1. AF393503 mRNA. Translation: AAM73685.1. Different termination.
IPI	IPI00023704.
RefSeq	NP_005569.1.
UniGene	Hs.444362
3D structure databases
HSSP	HSSP built from PDB template 1B8T based on UniProtKB P32965.
SMR	Q93052. Positions 468-533.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q93052. 3 interactions.
STRING	Q93052.
PTM databases
PhosphoSite	Q93052.
Proteomic databases
PeptideAtlas	Q93052.
PRIDE	Q93052.
Genome annotation databases
Ensembl	ENST00000312675; ENSP00000318089; ENSG00000145012; Homo sapiens. [Genome view] ENST00000414139; ENSP00000392667; ENSG00000145012; Homo sapiens. [Genome view] ENST00000415906; ENSP00000393008; ENSG00000145012; Homo sapiens. [Genome view] ENST00000416784; ENSP00000410340; ENSG00000145012; Homo sapiens. [Genome view] ENST00000420410; ENSP00000405138; ENSG00000145012; Homo sapiens. [Genome view] ENST00000426274; ENSP00000397017; ENSG00000145012; Homo sapiens. [Genome view] ENST00000430340; ENSP00000397166; ENSG00000145012; Homo sapiens. [Genome view] ENST00000443217; ENSP00000404679; ENSG00000145012; Homo sapiens. [Genome view] ENST00000448637; ENSP00000393602; ENSG00000145012; Homo sapiens. [Genome view] ENST00000454789; ENSP00000394257; ENSG00000145012; Homo sapiens. [Genome view] ENST00000457242; ENSP00000403825; ENSG00000145012; Homo sapiens. [Genome view]
GeneID	4026.
KEGG	hsa:4026.
UCSC	uc003frs.1. human.
Organism-specific databases
CTD	4026.
GeneCards	GC03P189413.
H-InvDB	HIX0003943.
HGNC	HGNC:6679. LPP.
HPA	HPA011133. HPA017342.
MIM	600700. gene.
PharmGKB	PA24730.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q93052.
HOVERGEN	Q93052.
OMA	PLTATKK.
Gene expression databases
ArrayExpress	Q93052.
Bgee	Q93052.
CleanEx	HS_LPP.
Genevestigator	Q93052.
Family and domain databases
InterPro	IPR001781. Znf_LIM. [Graphical view]
Gene3D	G3DSA:2.10.110.10. Znf_LIM. 2 hits.
Pfam	PF00412. LIM. 3 hits. [Graphical view]
ProDom	PD000094. LIM. 3 hits. [Graphical view] [Entries sharing at least one domain]
SMART	SM00132. LIM. 3 hits. [Graphical view]
PROSITE	PS00478. LIM_DOMAIN_1. 2 hits. PS50023. LIM_DOMAIN_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	15786.
SOURCE	Search...

Entry information

Entry name

LPP_HUMAN

Accession

Primary (citable) accession number: Q93052
Secondary accession number(s): Q8NFX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	February 1, 1997
Last modified:	November 3, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.