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Protein

Lipoma-preferred partner

Gene

LPP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SIGNORiQ93052.

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
Proteomesi
  • UP000005640 Componenti: 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

  • cytoplasm Source: HPA
  • focal adhesion Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB-SubCell
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

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

Organism-specific databases

MalaCardsiLPP.
PharmGKBiPA30440.

Polymorphism and mutation databases

BioMutaiLPP.
DMDMi74751663.

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 residuei116 – 1161PhosphoserineBy similarity
Modified residuei151 – 1511PhosphoserineBy similarity
Modified residuei244 – 2441PhosphotyrosineBy similarity
Modified residuei301 – 3011PhosphotyrosineBy similarity
Cross-linki327 – 327Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei333 – 3331PhosphothreonineCombined sources
Modified residuei375 – 3751PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ93052.
MaxQBiQ93052.
PaxDbiQ93052.
PeptideAtlasiQ93052.
PRIDEiQ93052.

PTM databases

iPTMnetiQ93052.
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

BgeeiENSG00000145012.
CleanExiHS_LPP.
ExpressionAtlasiQ93052. baseline and differential.
GenevisibleiQ93052. HS.

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. 55 interactions.
IntActiQ93052. 13 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

eggNOGiKOG1701. Eukaryota.
ENOG410Y3GP. LUCA.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000220910.
HOVERGENiHBG093602.
InParanoidiQ93052.
KOiK16676.
OMAiRNDSDPA.
OrthoDBiEOG091G085F.
PhylomeDBiQ93052.
TreeFamiTF320310.

Family and domain databases

Gene3Di2.10.110.10. 3 hits.
InterProiIPR028771. LPP.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR24207:SF0. PTHR24207:SF0. 2 hits.
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_005247503.1. XM_005247446.4.
XP_005247507.1. XM_005247450.4.
XP_005247508.1. XM_005247451.4.
XP_005247510.1. XM_005247453.2.
XP_011511122.1. XM_011512820.2.
XP_011511129.1. XM_011512827.2.
XP_011511130.1. XM_011512828.2.
XP_011511133.1. XM_011512831.2.
XP_011511135.1. XM_011512833.2.
XP_011511136.1. XM_011512834.2.
UniGeneiHs.720220.

Genome annotation databases

EnsembliENST00000617246; ENSP00000478901; ENSG00000145012.
GeneIDi4026.
KEGGihsa:4026.
UCSCiuc032sne.1. human.

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.
CCDSiCCDS3291.1.
RefSeqiNP_001161143.1. NM_001167671.2.
NP_005569.1. NM_005578.4.
XP_005247503.1. XM_005247446.4.
XP_005247507.1. XM_005247450.4.
XP_005247508.1. XM_005247451.4.
XP_005247510.1. XM_005247453.2.
XP_011511122.1. XM_011512820.2.
XP_011511129.1. XM_011512827.2.
XP_011511130.1. XM_011512828.2.
XP_011511133.1. XM_011512831.2.
XP_011511135.1. XM_011512833.2.
XP_011511136.1. XM_011512834.2.
UniGeneiHs.720220.

3D structure databases

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

Protein-protein interaction databases

BioGridi110208. 55 interactions.
IntActiQ93052. 13 interactions.
MINTiMINT-5005514.
STRINGi9606.ENSP00000318089.

PTM databases

iPTMnetiQ93052.
PhosphoSiteiQ93052.

Polymorphism and mutation databases

BioMutaiLPP.
DMDMi74751663.

Proteomic databases

EPDiQ93052.
MaxQBiQ93052.
PaxDbiQ93052.
PeptideAtlasiQ93052.
PRIDEiQ93052.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000617246; ENSP00000478901; ENSG00000145012.
GeneIDi4026.
KEGGihsa:4026.
UCSCiuc032sne.1. human.

Organism-specific databases

CTDi4026.
GeneCardsiLPP.
HGNCiHGNC:6679. LPP.
HPAiHPA011133.
HPA017342.
MalaCardsiLPP.
MIMi600700. gene.
neXtProtiNX_Q93052.
PharmGKBiPA30440.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1701. Eukaryota.
ENOG410Y3GP. LUCA.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000220910.
HOVERGENiHBG093602.
InParanoidiQ93052.
KOiK16676.
OMAiRNDSDPA.
OrthoDBiEOG091G085F.
PhylomeDBiQ93052.
TreeFamiTF320310.

Enzyme and pathway databases

SIGNORiQ93052.

Miscellaneous databases

ChiTaRSiLPP. human.
GeneWikiiLPP_(gene).
GenomeRNAii4026.
PROiQ93052.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000145012.
CleanExiHS_LPP.
ExpressionAtlasiQ93052. baseline and differential.
GenevisibleiQ93052. HS.

Family and domain databases

Gene3Di2.10.110.10. 3 hits.
InterProiIPR028771. LPP.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR24207:SF0. PTHR24207:SF0. 2 hits.
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]
ProtoNetiSearch...

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: September 7, 2016
This is version 146 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.