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Q93052

- LPP_HUMAN

UniProt

Q93052 - LPP_HUMAN

Protein

Lipoma-preferred partner

Gene

LPP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW

    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: HPA
    3. nucleus Source: UniProtKB-SubCell
    4. plasma membrane Source: UniProtKB-SubCell

    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

    ArrayExpressiQ93052.
    BgeeiQ93052.
    CleanExiHS_LPP.
    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.
    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

    MSHPSWLPPK STGEPLGHVP ARMETTHSFG NPSISVSTQQ PPKKFAPVVA    50
    PKPKYNPYKQ PGGEGDFLPP PPPPLDDSSA LPSISGNFPP PPPLDEEAFK 100
    VQGNPGGKTL EERRSSLDAE IDSLTSILAD LECSSPYKPR PPQSSTGSTA 150
    SPPVSTPVTG HKRMVIPNQP PLTATKKSTL KPQPAPQAGP IPVAPIGTLK 200
    PQPQPVPASY TTASTSSRPT FNVQVKSAQP SPHYMAAPSS GQIYGSGPQG 250
    YNTQPVPVSG QCPPPSTRGG MDYAYIPPPG LQPEPGYGYA PNQGRYYEGY 300
    YAAGPGYGGR NDSDPTYGQQ GHPNTWKREP GYTPPGAGNQ NPPGMYPVTG 350
    PKKTYITDPV SAPCAPPLQP KGGHSGQLGP SSVAPSFRPE DELEHLTKKM 400
    LYDMENPPAD EYFGRCARCG ENVVGEGTGC TAMDQVFHVD CFTCIICNNK 450
    LRGQPFYAVE KKAYCEPCYI NTLEQCNVCS KPIMERILRA TGKAYHPHCF 500
    TCVMCHRSLD GIPFTVDAGG LIHCIEDFHK KFAPRCSVCK EPIMPAPGQE 550
    ETVRIVALDR DFHVHCYRCE DCGGLLSEGD NQGCYPLDGH ILCKTCNSAR 600
    IRVLTAKAST DL 612
    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:
    EMBL
    GenBank
    DDBJ
    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_001167671.1.
    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.
    UniGeneiHs.720220.

    Genome annotation databases

    EnsembliENST00000312675; ENSP00000318089; ENSG00000145012.
    ENST00000543006; ENSP00000438891; 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:
    EMBL
    GenBank
    DDBJ
    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_001167671.1.
    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.
    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 ENST00000312675 ; ENSP00000318089 ; ENSG00000145012 .
    ENST00000543006 ; ENSP00000438891 ; 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.
    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

    ArrayExpressi Q93052.
    Bgeei Q93052.
    CleanExi HS_LPP.
    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

    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 1, 2014
    This is version 128 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