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Q8BFW7 (LPP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipoma-preferred partner homolog
Gene names
Name:Lpp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length613 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 By similarity.

Subunit structure

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

Subcellular location

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.

Miscellaneous

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

Sequence similarities

Belongs to the zyxin/ajuba family.

Contains 3 LIM zinc-binding domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   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 electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 15465019. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BFW7-1)

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.
Isoform 2 (identifier: Q8BFW7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     145-152: GSASSIAS → VGTSHSAA
     153-613: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8BFW7-3)

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.
Isoform 4 (identifier: Q8BFW7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-125: Missing.
     126-144: TSILADLECSSPYKPRPPQ → MELLGKVGACLKRSTGTLK
Note: No experimental confirmation available.
Isoform 5 (identifier: Q8BFW7-5)

The sequence of this isoform differs from the canonical sequence as follows:
     373-378: GGYPGP → VRNLLT
     379-613: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 613613Lipoma-preferred partner homolog
PRO_0000075833

Regions

Domain415 – 47460LIM zinc-binding 1
Domain475 – 53561LIM zinc-binding 2
Domain536 – 60469LIM zinc-binding 3
Compositional bias41 – 390350Pro-rich

Amino acid modifications

Modified residue1091N6-acetyllysine Ref.7
Modified residue2451Phosphotyrosine Ref.4 Ref.6
Modified residue3021Phosphotyrosine Ref.5

Natural variations

Alternative sequence1 – 125125Missing in isoform 4.
VSP_016350
Alternative sequence1021Missing in isoform 3.
VSP_016351
Alternative sequence126 – 14419TSILA…PRPPQ → MELLGKVGACLKRSTGTLK in isoform 4.
VSP_016352
Alternative sequence145 – 1528GSASSIAS → VGTSHSAA in isoform 2 and isoform 3.
VSP_016353
Alternative sequence153 – 613461Missing in isoform 2 and isoform 3.
VSP_016354
Alternative sequence373 – 3786GGYPGP → VRNLLT in isoform 5.
VSP_016355
Alternative sequence379 – 613235Missing in isoform 5.
VSP_016356

Experimental info

Sequence conflict291F → V in BAC32298. Ref.1
Sequence conflict811I → T in BAC34815. Ref.1
Sequence conflict831P → S in AAH85321. Ref.2
Sequence conflict1331E → D in BAC26401. Ref.1
Sequence conflict3951E → A in BAC34608. Ref.1
Sequence conflict5671C → R in AAH85321. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E34BE2EF2A3B7126

FASTA61365,891
        10         20         30         40         50         60 
MSHPSWLPPK STGEPLGHVP ARMETTHSFG NPSISVSTQQ PPKKYAPVVA PKPKYNPYKQ 

        70         80         90        100        110        120 
PGGEGDLLPP PPPPLEDPGT IPPGPGHFPP PPPLDEGAFK VQQGNPGGKT LEERRSSLDA 

       130        140        150        160        170        180 
EIDSLTSILA DLECSSPYKP RPPQGSASSI ASPPVSTPVT GHKRMVIPQQ PPLTATKKSA 

       190        200        210        220        230        240 
TKPQPAPQAA PIPVTPIGTL KPQPQPVPAS YTTASTSSRP TFNVQVKSAQ PSPHYMAGPS 

       250        260        270        280        290        300 
SGQIYGPGPR GYNNQPVPVS GQCPPPPTCV GTDYAYIPPS GHPPESGYGY TSNQGRYYEP 

       310        320        330        340        350        360 
YYAAGPSYGG RSEGDTAYGQ QVQPNTWKRE AAYAPPASGN QNHPGMYPVS GPKKTYITDP 

       370        380        390        400        410        420 
VSAPCAPPLQ PKGGYPGPMG PPSIPPSFRP EDELEHLTKK MLYDMENPPA DDYFGRCARC 

       430        440        450        460        470        480 
GENVVGEGTG CTAMDQVFHV DCFTCIVCDV KLRGQPFYAV EKKAYCEPCY INTLEQCSVC 

       490        500        510        520        530        540 
SKPIMERILR ATGKAYHPHC FTCVMCHRSL DGIPFTVDAC GLIHCIEDFH KKFAPRCSVC 

       550        560        570        580        590        600 
KEPIMPAPGQ EETVRIVALD RDFHVHCYRC EDCGGLLSEG DNQGCYPLDG HILCKTCNSA 

       610 
RIRVLTAKAS TDL 

« Hide

Isoform 2 [UniParc].

Checksum: 2D25715A6A8CD79A
Show »

FASTA15216,071
Isoform 3 [UniParc].

Checksum: 0DEB9F3A114646C1
Show »

FASTA15115,943
Isoform 4 [UniParc].

Checksum: 1C6BFA1A10350549
Show »

FASTA48852,536
Isoform 5 [UniParc].

Checksum: 666D0E86F1E394DD
Show »

FASTA37839,835

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS28083.1. [Q8BFW7-1]
CCDS49807.1. [Q8BFW7-4]
RefSeqNP_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]
UniGeneMm.209385.
Mm.450045.

3D structure databases

ProteinModelPortalQ8BFW7.
SMRQ8BFW7. Positions 383-581.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229132. 2 interactions.
IntActQ8BFW7. 5 interactions.
MINTMINT-4111189.

PTM databases

PhosphoSiteQ8BFW7.

Proteomic databases

MaxQBQ8BFW7.
PaxDbQ8BFW7.
PRIDEQ8BFW7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000038053; ENSMUSP00000036304; ENSMUSG00000033306. [Q8BFW7-1]
ENSMUST00000078988; ENSMUSP00000078005; ENSMUSG00000033306. [Q8BFW7-1]
ENSMUST00000115314; ENSMUSP00000110969; ENSMUSG00000033306. [Q8BFW7-4]
GeneID210126.
KEGGmmu:210126.
UCSCuc007yub.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

CTD4026.
MGIMGI:2441849. Lpp.

Phylogenomic databases

eggNOGNOG279196.
GeneTreeENSGT00750000117529.
HOVERGENHBG093602.
InParanoidQ8BFW7.
KOK16676.
OMAQPKGGHT.
OrthoDBEOG7992Q6.
PhylomeDBQ8BFW7.
TreeFamTF320310.

Gene expression databases

BgeeQ8BFW7.
GenevestigatorQ8BFW7.

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. mouse.
NextBio372874.
PROQ8BFW7.
SOURCESearch...

Entry information

Entry nameLPP_MOUSE
AccessionPrimary (citable) accession number: Q8BFW7
Secondary accession number(s): Q5U407 expand/collapse secondary AC list , Q8BHI1, Q8BKI0, Q8BKN2, Q8BLF4, Q8BLG3, Q8C101
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot