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Reviewed, UniProtKB/Swiss-Prot Q93052 (LPP_HUMAN)

Last modified November 3, 2009. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lipoma-preferred partner
Alternative name(s):
    LIM domain-containing preferred translocation partner in lipoma
Gene names
Name: LPP
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length612 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 processCell adhesion
   Cellular componentCell junction
Cell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityChromosomal rearrangement
Polymorphism
   DomainLIM domain
Repeat
   LigandMetal-binding
Zinc
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from direct assay. Source: HPA

focal adhesion

Inferred from direct assay. Source: HPA

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 612612Lipoma-preferred partner
PRO_0000075832

Regions

Domain414 – 47360LIM zinc-binding 1
Domain474 – 53461LIM zinc-binding 2
Domain535 – 60369LIM zinc-binding 3
Compositional bias41 – 370330Pro-rich

Sites

Site371 – 3722Breakpoint for translocation to form HMGA2-LPP
Site470 – 4712Breakpoint for translocation to form HMGA2-LPP and MLL-LPP

Amino acid modifications

Modified residue1161Phosphoserine By similarity
Modified residue1261Phosphoserine By similarity
Modified residue2441Phosphotyrosine By similarity
Modified residue2971Phosphotyrosine Ref.11
Modified residue3001Phosphotyrosine Ref.11 Ref.14 Ref.20
Modified residue3011Phosphotyrosine Ref.14 Ref.20 Ref.10 Ref.13 Ref.15
Modified residue3171Phosphotyrosine Ref.14 Ref.15 Ref.16
Modified residue3331Phosphothreonine Ref.18
Modified residue3751Phosphoserine Ref.17
Modified residue3971Phosphothreonine Ref.17

Natural variations

Natural variant1461T → A: dbSNP rs35417432.
VAR_050150
Natural variant2591S → P: dbSNP rs35940579.
VAR_050151
Natural variant3461Y → H: dbSNP rs7645635.
VAR_034070

Experimental info

Mutagenesis6101T → A: Abolishes binding to SCRIB.
Mutagenesis6121L → A: Abolishes binding to SCRIB.

Sequences

Sequence LengthMass (Da)Tools
Q93052-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 439CE0101FDE4DDD

FASTA61265,746
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.

Cross-references

Sequence databases

U49957 mRNA. Translation: AAC50738.1.
U49968 expand/collapse EMBL AC list , 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.
IPIIPI00023704.
RefSeqNP_005569.1.
UniGeneHs.444362

3D structure databases

HSSPHSSP built from PDB template 1B8T based on UniProtKB P32965.
SMRQ93052. Positions 468-533.
ModBaseSearch...

Protein-protein interaction databases

IntActQ93052. 3 interactions.
STRINGQ93052.

PTM databases

PhosphoSiteQ93052.

Proteomic databases

PeptideAtlasQ93052.
PRIDEQ93052.

Genome annotation databases

EnsemblENST00000312675; 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]
GeneID4026.
KEGGhsa:4026.
UCSCuc003frs.1. human.

Organism-specific databases

CTD4026.
GeneCardsGC03P189413.
H-InvDBHIX0003943.
HGNCHGNC:6679. LPP.
HPAHPA011133.
HPA017342.
MIM600700. gene.
PharmGKBPA24730.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ93052.
HOVERGENQ93052.
OMAPLTATKK.

Gene expression databases

ArrayExpressQ93052.
BgeeQ93052.
CleanExHS_LPP.
GenevestigatorQ93052.

Family and domain databases

InterProIPR001781. Znf_LIM.
[Graphical view]
Gene3DG3DSA:2.10.110.10. Znf_LIM. 2 hits.
PfamPF00412. LIM. 3 hits.
[Graphical view]
ProDomPD000094. LIM. 3 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00132. LIM. 3 hits.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio15786.
SOURCESearch...

Entry information

Entry nameLPP_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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List of human entries with polymorphisms or disease mutations

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Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents