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Q93052

- LPP_HUMAN

UniProt

Q93052 - LPP_HUMAN

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Protein

Lipoma-preferred partner

Gene

LPP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei371 – 3722Breakpoint for translocation to form HMGA2-LPP
Sitei470 – 4712Breakpoint for translocation to form HMGA2-LPP and KMT2A/MLL1-LPP

GO - Molecular functioni

  1. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoma-preferred partner
Alternative name(s):
LIM domain-containing preferred translocation partner in lipoma
Gene namesi
Name:LPP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:6679. LPP.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. focal adhesion Source: UniProtKB
  3. nucleus Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi610 – 6101T → A: Abolishes binding to SCRIB. 1 Publication
Mutagenesisi612 – 6121L → A: Abolishes binding to SCRIB. 1 Publication

Organism-specific databases

PharmGKBiPA30440.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 612612Lipoma-preferred partnerPRO_0000075832Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081N6-acetyllysineBy similarity
Modified residuei244 – 2441PhosphotyrosineBy similarity
Modified residuei301 – 3011PhosphotyrosineBy similarity
Modified residuei333 – 3331Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ93052.
PaxDbiQ93052.
PeptideAtlasiQ93052.
PRIDEiQ93052.

PTM databases

PhosphoSiteiQ93052.

Expressioni

Tissue specificityi

Expressed in a wide variety of tissues but no or very low expression in brain and peripheral leukocytes.2 Publications

Gene expression databases

BgeeiQ93052.
CleanExiHS_LPP.
ExpressionAtlasiQ93052. baseline and differential.
GenevestigatoriQ93052.

Organism-specific databases

HPAiHPA011133.
HPA017342.

Interactioni

Subunit structurei

Interacts with VASP, with PDZ domains of SCRIB and with ACTN1/alpha-actinin.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LASP1Q148473EBI-718388,EBI-742828

Protein-protein interaction databases

BioGridi110208. 42 interactions.
IntActiQ93052. 6 interactions.
MINTiMINT-5005514.
STRINGi9606.ENSP00000318089.

Structurei

3D structure databases

ProteinModelPortaliQ93052.
SMRiQ93052. Positions 382-580.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini414 – 47360LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini474 – 53461LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini535 – 60369LIM zinc-binding 3PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi41 – 370330Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the zyxin/ajuba family.Curated
Contains 3 LIM zinc-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiNOG279196.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000220910.
HOVERGENiHBG093602.
InParanoidiQ93052.
KOiK16676.
OMAiQPKGGHT.
OrthoDBiEOG7992Q6.
PhylomeDBiQ93052.
TreeFamiTF320310.

Family and domain databases

Gene3Di2.10.110.10. 3 hits.
InterProiIPR028771. LPP.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR24207:SF0. PTHR24207:SF0. 1 hit.
PfamiPF00412. LIM. 3 hits.
[Graphical view]
SMARTiSM00132. LIM. 3 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q93052-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSHPSWLPPK STGEPLGHVP ARMETTHSFG NPSISVSTQQ PPKKFAPVVA
60 70 80 90 100
PKPKYNPYKQ PGGEGDFLPP PPPPLDDSSA LPSISGNFPP PPPLDEEAFK
110 120 130 140 150
VQGNPGGKTL EERRSSLDAE IDSLTSILAD LECSSPYKPR PPQSSTGSTA
160 170 180 190 200
SPPVSTPVTG HKRMVIPNQP PLTATKKSTL KPQPAPQAGP IPVAPIGTLK
210 220 230 240 250
PQPQPVPASY TTASTSSRPT FNVQVKSAQP SPHYMAAPSS GQIYGSGPQG
260 270 280 290 300
YNTQPVPVSG QCPPPSTRGG MDYAYIPPPG LQPEPGYGYA PNQGRYYEGY
310 320 330 340 350
YAAGPGYGGR NDSDPTYGQQ GHPNTWKREP GYTPPGAGNQ NPPGMYPVTG
360 370 380 390 400
PKKTYITDPV SAPCAPPLQP KGGHSGQLGP SSVAPSFRPE DELEHLTKKM
410 420 430 440 450
LYDMENPPAD EYFGRCARCG ENVVGEGTGC TAMDQVFHVD CFTCIICNNK
460 470 480 490 500
LRGQPFYAVE KKAYCEPCYI NTLEQCNVCS KPIMERILRA TGKAYHPHCF
510 520 530 540 550
TCVMCHRSLD GIPFTVDAGG LIHCIEDFHK KFAPRCSVCK EPIMPAPGQE
560 570 580 590 600
ETVRIVALDR DFHVHCYRCE DCGGLLSEGD NQGCYPLDGH ILCKTCNSAR
610
IRVLTAKAST DL
Length:612
Mass (Da):65,746
Last modified:February 1, 1997 - v1
Checksum:i439CE0101FDE4DDD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti146 – 1461T → A.
Corresponds to variant rs35417432 [ dbSNP | Ensembl ].
VAR_050150
Natural varianti259 – 2591S → P.
Corresponds to variant rs35940579 [ dbSNP | Ensembl ].
VAR_050151
Natural varianti346 – 3461Y → H.
Corresponds to variant rs7645635 [ dbSNP | Ensembl ].
VAR_034070

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49957 mRNA. Translation: AAC50738.1.
U49968
, 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.
CCDSiCCDS3291.1.
RefSeqiNP_001161143.1. NM_001167671.2.
NP_005569.1. NM_005578.4.
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.
UniGeneiHs.720220.

Genome annotation databases

EnsembliENST00000616304; ENSP00000482472; ENSG00000145012.
ENST00000617246; ENSP00000478901; ENSG00000145012.
GeneIDi4026.
KEGGihsa:4026.
UCSCiuc003frs.2. human.

Polymorphism databases

DMDMi74751663.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49957 mRNA. Translation: AAC50738.1 .
U49968
, 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.
CCDSi CCDS3291.1.
RefSeqi NP_001161143.1. NM_001167671.2.
NP_005569.1. NM_005578.4.
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.
UniGenei Hs.720220.

3D structure databases

ProteinModelPortali Q93052.
SMRi Q93052. Positions 382-580.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110208. 42 interactions.
IntActi Q93052. 6 interactions.
MINTi MINT-5005514.
STRINGi 9606.ENSP00000318089.

PTM databases

PhosphoSitei Q93052.

Polymorphism databases

DMDMi 74751663.

Proteomic databases

MaxQBi Q93052.
PaxDbi Q93052.
PeptideAtlasi Q93052.
PRIDEi Q93052.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000616304 ; ENSP00000482472 ; ENSG00000145012 .
ENST00000617246 ; ENSP00000478901 ; ENSG00000145012 .
GeneIDi 4026.
KEGGi hsa:4026.
UCSCi uc003frs.2. human.

Organism-specific databases

CTDi 4026.
GeneCardsi GC03P187871.
HGNCi HGNC:6679. LPP.
HPAi HPA011133.
HPA017342.
MIMi 600700. gene.
neXtProti NX_Q93052.
PharmGKBi PA30440.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG279196.
GeneTreei ENSGT00760000119039.
HOGENOMi HOG000220910.
HOVERGENi HBG093602.
InParanoidi Q93052.
KOi K16676.
OMAi QPKGGHT.
OrthoDBi EOG7992Q6.
PhylomeDBi Q93052.
TreeFami TF320310.

Miscellaneous databases

ChiTaRSi LPP. human.
GeneWikii LPP_(gene).
GenomeRNAii 4026.
NextBioi 15786.
PROi Q93052.
SOURCEi Search...

Gene expression databases

Bgeei Q93052.
CleanExi HS_LPP.
ExpressionAtlasi Q93052. baseline and differential.
Genevestigatori Q93052.

Family and domain databases

Gene3Di 2.10.110.10. 3 hits.
InterProi IPR028771. LPP.
IPR001781. Znf_LIM.
[Graphical view ]
PANTHERi PTHR24207:SF0. PTHR24207:SF0. 1 hit.
Pfami PF00412. LIM. 3 hits.
[Graphical view ]
SMARTi SM00132. LIM. 3 hits.
[Graphical view ]
PROSITEi PS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLPP_HUMAN
AccessioniPrimary (citable) accession number: Q93052
Secondary accession number(s): A1L4L6, D3DNV6, Q8NFX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: February 1, 1997
Last modified: October 29, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3