O60711 · LPXN_HUMAN

  • Protein
    Leupaxin
  • Gene
    LPXN
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF). Contributes to the regulation of cell adhesion, spreading and cell migration and acts as a negative regulator in integrin-mediated cell adhesion events. Suppresses the integrin-induced tyrosine phosphorylation of paxillin (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell projection
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentfocal adhesion
Cellular Componentmembrane
Cellular Componentnuclear speck
Cellular Componentnucleus
Cellular Componentperinuclear region of cytoplasm
Cellular Componentplasma membrane
Cellular Componentpodosome
Molecular Functionmetal ion binding
Molecular Functiontranscription coregulator activity
Biological Processcell adhesion
Biological Processendothelial cell migration
Biological Processnegative regulation of B cell receptor signaling pathway
Biological Processnegative regulation of cell adhesion
Biological Processprotein-containing complex assembly
Biological Processregulation of cell adhesion mediated by integrin
Biological Processsignal transduction
Biological Processsubstrate adhesion-dependent cell spreading
Biological Processtransforming growth factor beta receptor signaling pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Leupaxin

Gene names

    • Name
      LPXN
    • Synonyms
      LDLP

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    O60711
  • Secondary accessions
    • B2R8B4
    • B4DV71
    • Q53FW6
    • Q6FI07

Proteomes

Organism-specific databases

Subcellular Location

Note: Shuttles between the cytoplasm and nucleus. Recruited to the cell membrane following B-cell antigen receptor (BCR) cross-linking in B-cells. Enhanced focal adhesion kinase activity (PTK2/FAK) attenuates its nuclear accumulation and limits its ability to enhance serum response factor (SRF)-dependent gene transcription. Targeting to focal adhesions is essential for its tyrosine phosphorylation in response to bombesin.

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_050152148in dbSNP:rs12271558

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 465 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for modified residue, chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Modified residue1UniProtN-acetylmethionine
ChainPRO_00000758361-386UniProtLeupaxin
Modified residue19UniProtPhosphoserine
Modified residue (large scale data)19PRIDEPhosphoserine
Modified residue22UniProtPhosphotyrosine
Modified residue (large scale data)22PRIDEPhosphotyrosine
Modified residue (large scale data)23PRIDEPhosphoserine
Modified residue (large scale data)34PRIDEPhosphoserine
Modified residue54UniProtPhosphoserine
Modified residue62UniProtPhosphotyrosine
Modified residue72UniProtPhosphotyrosine; by LYN
Modified residue81UniProtPhosphoserine
Modified residue (large scale data)146PRIDEPhosphothreonine
Modified residue (large scale data)187PRIDEPhosphoserine
Modified residue (large scale data)188PRIDEPhosphoserine
Modified residue (large scale data)203PRIDEPhosphotyrosine
Modified residue (large scale data)208PRIDEPhosphoserine
Modified residue (large scale data)267PRIDEPhosphoserine
Modified residue (large scale data)375PRIDEPhosphotyrosine

Post-translational modification

Phosphorylated on tyrosine residues. Phosphorylation on Tyr-72 is important for its inhibitory function. Bombesin stimulates phosphorylation on Tyr-22, Tyr-62 and Tyr-72.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Macrophages, monocytes and osteoclasts (at protein level). Strongly expressed in cells and tissues of hematopoietic origin. Highest expression in lymphoid tissues such as spleen, lymph node, thymus and appendix and in the vascular smooth muscle. Lower levels in bone marrow and fetal liver. Also expressed in peripheral blood lymphocytes and a number of hematopoietic cell lines. Very low levels found in epithelial cell lines. Expressed in prostate cancer (PCa) cells and its expression intensity is directly linked to PCa progression.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with PTPN22 (By similarity).
Interacts with unphosphorylated ITGA4. Interacts with PTK2B/PYK2, PTPN12, AR and SRF. Interacts (via LD motif 3) with LYN and the interaction is induced upon B-cell antigen receptor (BCR) activation. Interacts (via LD motif 3) with PTK2/FAK

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for motif, region, domain.

TypeIDPosition(s)Description
Motif3-15LD motif 1
Region13-41Disordered
Motif70-82LD motif 2
Motif92-103LD motif 3
Domain150-208LIM zinc-binding 1
Domain209-267LIM zinc-binding 2
Domain268-326LIM zinc-binding 3
Domain327-386LIM zinc-binding 4

Domain

The LIM domain 3 is critical for focal adhesion targeting and the suppression of paxillin (PXN) tyrosine phosphorylation. The LIM domain 3 alone or both LIM domains 3 and 4 can mediate interaction with AR.

Sequence similarities

Belongs to the paxillin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

O60711-1

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.

  • Length
    386
  • Mass (Da)
    43,332
  • Last updated
    1998-08-01 v1
  • Checksum
    C8D2BE61FAB11F3A
MEELDALLEELERSTLQDSDEYSNPAPLPLDQHSRKETNLDETSEILSIQDNTSPLPAQLVYTTNIQELNVYSEAQEPKESPPPSKTSAAAQLDELMAHLTEMQAKVAVRADAGKKHLPDKQDHKASLDSMLGGLEQELQDLGIATVPKGHCASCQKPIAGKVIHALGQSWHPEHFVCTHCKEEIGSSPFFERSGLAYCPNDYHQLFSPRCAYCAAPILDKVLTAMNQTWHPEHFFCSHCGEVFGAEGFHEKDKKPYCRKDFLAMFSPKCGGCNRPVLENYLSAMDTVWHPECFVCGDCFTSFSTGSFFELDGRPFCELHYHHRRGTLCHGCGQPITGRCISAMGYKFHPEHFVCAFCLTQLSKGIFREQNDKTYCQPCFNKLFPL

O60711-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-4: MEEL → MSTLLISSS

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
B7Z5P7B7Z5P7_HUMANLPXN366
E9PNX9E9PNX9_HUMANLPXN106

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0426551-4in isoform 2
Sequence conflict2in Ref. 3; CAG38768
Sequence conflict14in Ref. 4; BAD96885
Sequence conflict100in Ref. 3; CAG38768

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF062075
EMBL· GenBank· DDBJ
AAC16014.1
EMBL· GenBank· DDBJ
mRNA
AK300955
EMBL· GenBank· DDBJ
BAG62583.1
EMBL· GenBank· DDBJ
mRNA
AK313306
EMBL· GenBank· DDBJ
BAG36111.1
EMBL· GenBank· DDBJ
mRNA
CR536531
EMBL· GenBank· DDBJ
CAG38768.1
EMBL· GenBank· DDBJ
mRNA
AK223165
EMBL· GenBank· DDBJ
BAD96885.1
EMBL· GenBank· DDBJ
mRNA
AP001350
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AP003557
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471076
EMBL· GenBank· DDBJ
EAW73808.1
EMBL· GenBank· DDBJ
Genomic DNA
BC019035
EMBL· GenBank· DDBJ
AAH19035.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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