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Protein

Lipoma-preferred partner homolog

Gene

Lpp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

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 homolog
Gene namesi
Name:Lpp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:2441849. Lpp.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity. Cell junction By similarity
Note: Found in the nucleus, in the cytoplasm and at cell adhesion sites.By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. focal adhesion Source: MGI
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 613613Lipoma-preferred partner homologPRO_0000075833Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei109 – 1091N6-acetyllysine1 Publication
Modified residuei245 – 2451Phosphotyrosine2 Publications
Modified residuei302 – 3021Phosphotyrosine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8BFW7.
PaxDbiQ8BFW7.
PRIDEiQ8BFW7.

PTM databases

PhosphoSiteiQ8BFW7.

Expressioni

Gene expression databases

BgeeiQ8BFW7.
GenevestigatoriQ8BFW7.

Interactioni

Subunit structurei

Interacts with VASP, with PDZ domains of SCRIB and with ACTN1/alpha-actinin.By similarity

Protein-protein interaction databases

BioGridi229132. 2 interactions.
IntActiQ8BFW7. 5 interactions.
MINTiMINT-4111189.

Structurei

3D structure databases

ProteinModelPortaliQ8BFW7.
SMRiQ8BFW7. Positions 383-581.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini415 – 47460LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini475 – 53561LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini536 – 60469LIM zinc-binding 3PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi41 – 390350Pro-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.
HOVERGENiHBG093602.
InParanoidiQ8BFW7.
KOiK16676.
OMAiRNDSDPA.
OrthoDBiEOG7992Q6.
PhylomeDBiQ8BFW7.
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]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8BFW7-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSHPSWLPPK STGEPLGHVP ARMETTHSFG NPSISVSTQQ PPKKYAPVVA
60 70 80 90 100
PKPKYNPYKQ PGGEGDLLPP PPPPLEDPGT IPPGPGHFPP PPPLDEGAFK
110 120 130 140 150
VQQGNPGGKT LEERRSSLDA EIDSLTSILA DLECSSPYKP RPPQGSASSI
160 170 180 190 200
ASPPVSTPVT GHKRMVIPQQ PPLTATKKSA TKPQPAPQAA PIPVTPIGTL
210 220 230 240 250
KPQPQPVPAS YTTASTSSRP TFNVQVKSAQ PSPHYMAGPS SGQIYGPGPR
260 270 280 290 300
GYNNQPVPVS GQCPPPPTCV GTDYAYIPPS GHPPESGYGY TSNQGRYYEP
310 320 330 340 350
YYAAGPSYGG RSEGDTAYGQ QVQPNTWKRE AAYAPPASGN QNHPGMYPVS
360 370 380 390 400
GPKKTYITDP VSAPCAPPLQ PKGGYPGPMG PPSIPPSFRP EDELEHLTKK
410 420 430 440 450
MLYDMENPPA DDYFGRCARC GENVVGEGTG CTAMDQVFHV DCFTCIVCDV
460 470 480 490 500
KLRGQPFYAV EKKAYCEPCY INTLEQCSVC SKPIMERILR ATGKAYHPHC
510 520 530 540 550
FTCVMCHRSL DGIPFTVDAC GLIHCIEDFH KKFAPRCSVC KEPIMPAPGQ
560 570 580 590 600
EETVRIVALD RDFHVHCYRC EDCGGLLSEG DNQGCYPLDG HILCKTCNSA
610
RIRVLTAKAS TDL
Length:613
Mass (Da):65,891
Last modified:March 1, 2003 - v1
Checksum:iE34BE2EF2A3B7126
GO
Isoform 2 (identifier: Q8BFW7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     145-152: GSASSIAS → VGTSHSAA
     153-613: Missing.

Note: No experimental confirmation available.

Show »
Length:152
Mass (Da):16,071
Checksum:i2D25715A6A8CD79A
GO
Isoform 3 (identifier: Q8BFW7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     102-102: Missing.
     145-152: GSASSIAS → VGTSHSAA
     153-613: Missing.

Note: No experimental confirmation available.

Show »
Length:151
Mass (Da):15,943
Checksum:i0DEB9F3A114646C1
GO
Isoform 4 (identifier: Q8BFW7-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-125: Missing.
     126-144: TSILADLECSSPYKPRPPQ → MELLGKVGACLKRSTGTLK

Note: No experimental confirmation available.

Show »
Length:488
Mass (Da):52,536
Checksum:i1C6BFA1A10350549
GO
Isoform 5 (identifier: Q8BFW7-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     373-378: GGYPGP → VRNLLT
     379-613: Missing.

Note: No experimental confirmation available.

Show »
Length:378
Mass (Da):39,835
Checksum:i666D0E86F1E394DD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291F → V in BAC32298. (PubMed:16141072)Curated
Sequence conflicti81 – 811I → T in BAC34815. (PubMed:16141072)Curated
Sequence conflicti83 – 831P → S in AAH85321. (PubMed:15489334)Curated
Sequence conflicti133 – 1331E → D in BAC26401. (PubMed:16141072)Curated
Sequence conflicti395 – 3951E → A in BAC34608. (PubMed:16141072)Curated
Sequence conflicti567 – 5671C → R in AAH85321. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 125125Missing in isoform 4. 1 PublicationVSP_016350Add
BLAST
Alternative sequencei102 – 1021Missing in isoform 3. 1 PublicationVSP_016351
Alternative sequencei126 – 14419TSILA…PRPPQ → MELLGKVGACLKRSTGTLK in isoform 4. 1 PublicationVSP_016352Add
BLAST
Alternative sequencei145 – 1528GSASSIAS → VGTSHSAA in isoform 2 and isoform 3. 1 PublicationVSP_016353
Alternative sequencei153 – 613461Missing in isoform 2 and isoform 3. 1 PublicationVSP_016354Add
BLAST
Alternative sequencei373 – 3786GGYPGP → VRNLLT in isoform 5. 1 PublicationVSP_016355
Alternative sequencei379 – 613235Missing in isoform 5. 1 PublicationVSP_016356Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029335 mRNA. Translation: BAC26401.1.
AK029567 mRNA. Translation: BAC26516.1.
AK040643 mRNA. Translation: BAC30654.1.
AK045288 mRNA. Translation: BAC32298.1.
AK045341 mRNA. Translation: BAC32316.1.
AK051345 mRNA. Translation: BAC34608.1.
AK051937 mRNA. Translation: BAC34815.1.
AK054550 mRNA. Translation: BAC35821.1.
AK076989 mRNA. Translation: BAC36552.1.
AK169780 mRNA. Translation: BAE41362.1.
BC085321 mRNA. Translation: AAH85321.1.
CCDSiCCDS28083.1. [Q8BFW7-1]
CCDS49807.1. [Q8BFW7-4]
RefSeqiNP_001139424.1. NM_001145952.1. [Q8BFW7-1]
NP_001139426.1. NM_001145954.1. [Q8BFW7-4]
NP_848780.3. NM_178665.5. [Q8BFW7-1]
XP_006522020.1. XM_006521957.1. [Q8BFW7-1]
UniGeneiMm.209385.
Mm.450045.

Genome annotation databases

EnsembliENSMUST00000038053; ENSMUSP00000036304; ENSMUSG00000033306. [Q8BFW7-1]
ENSMUST00000078988; ENSMUSP00000078005; ENSMUSG00000033306. [Q8BFW7-1]
ENSMUST00000115314; ENSMUSP00000110969; ENSMUSG00000033306. [Q8BFW7-4]
GeneIDi210126.
KEGGimmu:210126.
UCSCiuc007yub.2. mouse. [Q8BFW7-2]
uc007yuc.2. mouse. [Q8BFW7-3]
uc007yud.2. mouse. [Q8BFW7-5]
uc007yue.2. mouse. [Q8BFW7-1]
uc007yuh.2. mouse. [Q8BFW7-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029335 mRNA. Translation: BAC26401.1.
AK029567 mRNA. Translation: BAC26516.1.
AK040643 mRNA. Translation: BAC30654.1.
AK045288 mRNA. Translation: BAC32298.1.
AK045341 mRNA. Translation: BAC32316.1.
AK051345 mRNA. Translation: BAC34608.1.
AK051937 mRNA. Translation: BAC34815.1.
AK054550 mRNA. Translation: BAC35821.1.
AK076989 mRNA. Translation: BAC36552.1.
AK169780 mRNA. Translation: BAE41362.1.
BC085321 mRNA. Translation: AAH85321.1.
CCDSiCCDS28083.1. [Q8BFW7-1]
CCDS49807.1. [Q8BFW7-4]
RefSeqiNP_001139424.1. NM_001145952.1. [Q8BFW7-1]
NP_001139426.1. NM_001145954.1. [Q8BFW7-4]
NP_848780.3. NM_178665.5. [Q8BFW7-1]
XP_006522020.1. XM_006521957.1. [Q8BFW7-1]
UniGeneiMm.209385.
Mm.450045.

3D structure databases

ProteinModelPortaliQ8BFW7.
SMRiQ8BFW7. Positions 383-581.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229132. 2 interactions.
IntActiQ8BFW7. 5 interactions.
MINTiMINT-4111189.

PTM databases

PhosphoSiteiQ8BFW7.

Proteomic databases

MaxQBiQ8BFW7.
PaxDbiQ8BFW7.
PRIDEiQ8BFW7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038053; ENSMUSP00000036304; ENSMUSG00000033306. [Q8BFW7-1]
ENSMUST00000078988; ENSMUSP00000078005; ENSMUSG00000033306. [Q8BFW7-1]
ENSMUST00000115314; ENSMUSP00000110969; ENSMUSG00000033306. [Q8BFW7-4]
GeneIDi210126.
KEGGimmu:210126.
UCSCiuc007yub.2. mouse. [Q8BFW7-2]
uc007yuc.2. mouse. [Q8BFW7-3]
uc007yud.2. mouse. [Q8BFW7-5]
uc007yue.2. mouse. [Q8BFW7-1]
uc007yuh.2. mouse. [Q8BFW7-4]

Organism-specific databases

CTDi4026.
MGIiMGI:2441849. Lpp.

Phylogenomic databases

eggNOGiNOG279196.
GeneTreeiENSGT00760000119039.
HOVERGENiHBG093602.
InParanoidiQ8BFW7.
KOiK16676.
OMAiRNDSDPA.
OrthoDBiEOG7992Q6.
PhylomeDBiQ8BFW7.
TreeFamiTF320310.

Miscellaneous databases

ChiTaRSiLpp. mouse.
NextBioi372874.
PROiQ8BFW7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BFW7.
GenevestigatoriQ8BFW7.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
    Strain: C57BL/6J and NOD.
    Tissue: Aorta, Embryo, Eye, Head, Ovary, Spinal ganglion, Testis, Thymus and Vein.
  2. "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] (ISOFORM 1).
    Strain: C3H/He.
    Tissue: Mesenchymal stem cell.
  3. "Truncated and chimeric HMGI-C genes induce neoplastic transformation of NIH3T3 murine fibroblasts."
    Fedele M., Berlingieri M.T., Scala S., Chiariotti L., Viglietto G., Rippel V., Bullerdiek J., Santoro M., Fusco A.
    Oncogene 17:413-418(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NEOPLASTIC TRANSFORMATION.
  4. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiLPP_MOUSE
AccessioniPrimary (citable) accession number: Q8BFW7
Secondary accession number(s): Q5U407
, Q8BHI1, Q8BKI0, Q8BKN2, Q8BLF4, Q8BLG3, Q8C101
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: March 1, 2003
Last modified: February 4, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Fusion protein carrying the DNA-binding domains of HMGA2/HMGIC and the LIM domain of LPP causes malignant transformation of NIH3T3 cells.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.