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Q93052 (LPP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length612 AA.
Sequence statusComplete.
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.8

Subunit structure

Interacts with VASP, with PDZ domains of SCRIB and with ACTN1/alpha-actinin. Ref.8 Ref.10 Ref.11 Ref.14

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 KMT2A/MLL1. Ref.8 Ref.10

Tissue specificity

Expressed in a wide variety of tissues but no or very low expression in brain and peripheral leukocytes. Ref.1 Ref.8

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 KMT2A/MLL1 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
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference 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

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionzinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LASP1Q148473EBI-718388,EBI-742828

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 KMT2A/MLL1-LPP

Amino acid modifications

Modified residue1081N6-acetyllysine By similarity
Modified residue2441Phosphotyrosine By similarity
Modified residue3011Phosphotyrosine By similarity
Modified residue3331Phosphothreonine Ref.17

Natural variations

Natural variant1461T → A.
Corresponds to variant rs35417432 [ dbSNP | Ensembl ].
VAR_050150
Natural variant2591S → P.
Corresponds to variant rs35940579 [ dbSNP | Ensembl ].
VAR_050151
Natural variant3461Y → H.
Corresponds to variant rs7645635 [ dbSNP | Ensembl ].
VAR_034070

Experimental info

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

Sequences

Sequence LengthMass (Da)Tools
Q93052 [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] [Europe PMC] [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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 276-371.
[6]"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] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH HMGA2.
[7]"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] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH HMGA2.
[8]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH VASP.
[9]"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] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
[10]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH VASP AND ACTN1.
[11]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACTN1.
[12]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCRIB, MUTAGENESIS.
[15]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CH471052 Genomic DNA. Translation: EAW78127.1.
CH471052 Genomic DNA. Translation: EAW78128.1.
CH471052 Genomic DNA. Translation: EAW78133.1.
BC130584 mRNA. Translation: AAI30585.1.
AF393503 mRNA. Translation: AAM73685.1. Different termination.
RefSeqNP_001161143.1. NM_001167671.1.
NP_005569.1. NM_005578.3.
XP_005247502.1. XM_005247445.2.
XP_005247503.1. XM_005247446.2.
XP_005247504.1. XM_005247447.2.
XP_005247505.1. XM_005247448.2.
XP_005247507.1. XM_005247450.2.
XP_005247508.1. XM_005247451.2.
XP_005247510.1. XM_005247453.1.
UniGeneHs.720220.

3D structure databases

ProteinModelPortalQ93052.
SMRQ93052. Positions 414-605.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110208. 39 interactions.
IntActQ93052. 6 interactions.
MINTMINT-5005514.
STRING9606.ENSP00000318089.

PTM databases

PhosphoSiteQ93052.

Polymorphism databases

DMDM74751663.

Proteomic databases

PaxDbQ93052.
PeptideAtlasQ93052.
PRIDEQ93052.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312675; ENSP00000318089; ENSG00000145012.
ENST00000543006; ENSP00000438891; ENSG00000145012.
GeneID4026.
KEGGhsa:4026.
UCSCuc003frs.2. human.

Organism-specific databases

CTD4026.
GeneCardsGC03P187871.
HGNCHGNC:6679. LPP.
HPAHPA011133.
HPA017342.
MIM600700. gene.
neXtProtNX_Q93052.
PharmGKBPA30440.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279196.
HOGENOMHOG000220910.
HOVERGENHBG093602.
InParanoidQ93052.
KOK16676.
OMAQPKGGHT.
OrthoDBEOG7992Q6.
PhylomeDBQ93052.
TreeFamTF320310.

Gene expression databases

ArrayExpressQ93052.
BgeeQ93052.
CleanExHS_LPP.
GenevestigatorQ93052.

Family and domain databases

Gene3D2.10.110.10. 3 hits.
InterProIPR028771. LPP.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERPTHR24207:SF0. PTHR24207:SF0. 1 hit.
PfamPF00412. LIM. 3 hits.
[Graphical view]
SMARTSM00132. LIM. 3 hits.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLPP. human.
GeneWikiLPP_(gene).
GenomeRNAi4026.
NextBio15786.
PROQ93052.
SOURCESearch...

Entry information

Entry nameLPP_HUMAN
AccessionPrimary (citable) accession number: Q93052
Secondary accession number(s): A1L4L6, D3DNV6, Q8NFX5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM