O60711 · LPXN_HUMAN
- ProteinLeupaxin
- GeneLPXN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids386 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cell projection | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | focal adhesion | |
Cellular Component | membrane | |
Cellular Component | nuclear speck | |
Cellular Component | nucleus | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | podosome | |
Molecular Function | metal ion binding | |
Molecular Function | transcription coregulator activity | |
Biological Process | cell adhesion | |
Biological Process | endothelial cell migration | |
Biological Process | negative regulation of B cell receptor signaling pathway | |
Biological Process | negative regulation of cell adhesion | |
Biological Process | protein-containing complex assembly | |
Biological Process | regulation of cell adhesion mediated by integrin | |
Biological Process | signal transduction | |
Biological Process | substrate adhesion-dependent cell spreading | |
Biological Process | transforming growth factor beta receptor signaling pathway |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLeupaxin
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO60711
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_050152 | 148 | in dbSNP:rs12271558 | |||
Sequence: P → T |
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.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000075836 | 1-386 | UniProt | Leupaxin | |||
Sequence: MEELDALLEELERSTLQDSDEYSNPAPLPLDQHSRKETNLDETSEILSIQDNTSPLPAQLVYTTNIQELNVYSEAQEPKESPPPSKTSAAAQLDELMAHLTEMQAKVAVRADAGKKHLPDKQDHKASLDSMLGGLEQELQDLGIATVPKGHCASCQKPIAGKVIHALGQSWHPEHFVCTHCKEEIGSSPFFERSGLAYCPNDYHQLFSPRCAYCAAPILDKVLTAMNQTWHPEHFFCSHCGEVFGAEGFHEKDKKPYCRKDFLAMFSPKCGGCNRPVLENYLSAMDTVWHPECFVCGDCFTSFSTGSFFELDGRPFCELHYHHRRGTLCHGCGQPITGRCISAMGYKFHPEHFVCAFCLTQLSKGIFREQNDKTYCQPCFNKLFPL | |||||||
Modified residue | 19 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 19 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 22 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 22 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 34 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 54 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 62 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 72 | UniProt | Phosphotyrosine; by LYN | ||||
Sequence: Y | |||||||
Modified residue | 81 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 146 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 187 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 188 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 203 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 208 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 267 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 375 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
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
- PTM
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
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
Structure
Family & Domains
Features
Showing features for motif, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 3-15 | LD motif 1 | ||||
Sequence: ELDALLEELERST | ||||||
Region | 13-41 | Disordered | ||||
Sequence: RSTLQDSDEYSNPAPLPLDQHSRKETNLD | ||||||
Motif | 70-82 | LD motif 2 | ||||
Sequence: NVYSEAQEPKESP | ||||||
Motif | 92-103 | LD motif 3 | ||||
Sequence: QLDELMAHLTEM | ||||||
Domain | 150-208 | LIM zinc-binding 1 | ||||
Sequence: GHCASCQKPIAGKVIHALGQSWHPEHFVCTHCKEEIGSSPFFERSGLAYCPNDYHQLFS | ||||||
Domain | 209-267 | LIM zinc-binding 2 | ||||
Sequence: PRCAYCAAPILDKVLTAMNQTWHPEHFFCSHCGEVFGAEGFHEKDKKPYCRKDFLAMFS | ||||||
Domain | 268-326 | LIM zinc-binding 3 | ||||
Sequence: PKCGGCNRPVLENYLSAMDTVWHPECFVCGDCFTSFSTGSFFELDGRPFCELHYHHRRG | ||||||
Domain | 327-386 | LIM zinc-binding 4 | ||||
Sequence: TLCHGCGQPITGRCISAMGYKFHPEHFVCAFCLTQLSKGIFREQNDKTYCQPCFNKLFPL |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- Name1
- Length386
- Mass (Da)43,332
- Last updated1998-08-01 v1
- ChecksumC8D2BE61FAB11F3A
O60711-2
- Name2
- Differences from canonical
- 1-4: MEEL → MSTLLISSS
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_042655 | 1-4 | in isoform 2 | |||
Sequence: MEEL → MSTLLISSS | ||||||
Sequence conflict | 2 | in Ref. 3; CAG38768 | ||||
Sequence: E → D | ||||||
Sequence conflict | 14 | in Ref. 4; BAD96885 | ||||
Sequence: S → T | ||||||
Sequence conflict | 100 | in Ref. 3; CAG38768 | ||||
Sequence: L → M |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |