Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Leupaxin

Gene

LPXN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  • transcription cofactor activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell adhesion Source: ProtInc
  • negative regulation of B cell receptor signaling pathway Source: UniProtKB
  • negative regulation of cell adhesion Source: UniProtKB
  • protein complex assembly Source: ProtInc
  • regulation of cell adhesion mediated by integrin Source: Ensembl
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • signal transduction Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell adhesion, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000110031-MONOMER.
SignaLinkiO60711.

Names & Taxonomyi

Protein namesi
Recommended name:
Leupaxin
Gene namesi
Name:LPXN
Synonyms:LDLP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:14061. LPXN.

Subcellular locationi

  • Cytoplasm
  • Cell junctionfocal adhesion
  • Nucleus
  • Cytoplasmperinuclear region By similarity
  • Cell projectionpodosome
  • Cell membrane

  • 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.

GO - Cellular componenti

  • cell projection Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • podosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi9404.
OpenTargetsiENSG00000110031.
PharmGKBiPA30441.

Polymorphism and mutation databases

BioMutaiLPXN.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000758361 – 386LeupaxinAdd BLAST386

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei19PhosphoserineCombined sources1
Modified residuei22Phosphotyrosine1 Publication1
Modified residuei54PhosphoserineBy similarity1
Modified residuei62Phosphotyrosine1 Publication1
Modified residuei72Phosphotyrosine; by LYN2 Publications1
Modified residuei81PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated on tyrosine residues. Phosphorylation on Tyr-72 is important for its inhibitory function. Bombesin stimulates phosphorylation on Tyr-22, Tyr-62 and Tyr-72.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO60711.
MaxQBiO60711.
PaxDbiO60711.
PeptideAtlasiO60711.
PRIDEiO60711.

PTM databases

iPTMnetiO60711.
PhosphoSitePlusiO60711.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

BgeeiENSG00000110031.
CleanExiHS_LPXN.
ExpressionAtlasiO60711. baseline and differential.
GenevisibleiO60711. HS.

Organism-specific databases

HPAiCAB046478.
HPA043741.

Interactioni

Subunit structurei

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.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DKFZp451B226Q5HYH73EBI-744222,EBI-10173842
Hoxa1P090223EBI-744222,EBI-3957603From a different organism.
HOXC9P312745EBI-744222,EBI-1779423
LMO1P258005EBI-744222,EBI-8639312
PLEKHH2Q8IVE33EBI-744222,EBI-2815745
PLEKHN1Q494U13EBI-744222,EBI-10241513
RUNX1T1Q06455-43EBI-744222,EBI-10224192

Protein-protein interaction databases

BioGridi114801. 53 interactors.
IntActiO60711. 36 interactors.
MINTiMINT-1449182.
STRINGi9606.ENSP00000431284.

Structurei

Secondary structure

1386
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 14Combined sources13
Helixi88 – 98Combined sources11
Turni271 – 273Combined sources3
Beta strandi282 – 284Combined sources3
Beta strandi287 – 289Combined sources3
Turni291 – 293Combined sources3
Beta strandi297 – 299Combined sources3
Beta strandi309 – 313Combined sources5
Helixi318 – 325Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X3HNMR-A260-326[»]
4XEFX-ray2.50B/C/E/F1-20[»]
4XEKX-ray1.79C86-104[»]
4XEVX-ray2.01C/F86-104[»]
ProteinModelPortaliO60711.
SMRiO60711.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60711.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini150 – 208LIM zinc-binding 1PROSITE-ProRule annotationAdd BLAST59
Domaini209 – 267LIM zinc-binding 2PROSITE-ProRule annotationAdd BLAST59
Domaini268 – 326LIM zinc-binding 3PROSITE-ProRule annotationAdd BLAST59
Domaini327 – 386LIM zinc-binding 4PROSITE-ProRule annotationAdd BLAST60

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi3 – 15LD motif 1Add BLAST13
Motifi70 – 82LD motif 2Add BLAST13
Motifi92 – 103LD motif 3Add BLAST12

Domaini

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 similaritiesi

Belongs to the paxillin family.Curated
Contains 4 LIM zinc-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiKOG1703. Eukaryota.
ENOG410XRD4. LUCA.
GeneTreeiENSGT00760000118910.
HOGENOMiHOG000018764.
HOVERGENiHBG001512.
InParanoidiO60711.
OMAiELMAHLC.
OrthoDBiEOG091G05AW.
PhylomeDBiO60711.
TreeFamiTF314113.

Family and domain databases

Gene3Di2.10.110.10. 4 hits.
InterProiIPR017305. Tgfb1i1/Leupaxin.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 4 hits.
[Graphical view]
PIRSFiPIRSF037881. Leupaxin. 1 hit.
SMARTiSM00132. LIM. 4 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O60711-1) [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
MEELDALLEE LERSTLQDSD EYSNPAPLPL DQHSRKETNL DETSEILSIQ
60 70 80 90 100
DNTSPLPAQL VYTTNIQELN VYSEAQEPKE SPPPSKTSAA AQLDELMAHL
110 120 130 140 150
TEMQAKVAVR ADAGKKHLPD KQDHKASLDS MLGGLEQELQ DLGIATVPKG
160 170 180 190 200
HCASCQKPIA GKVIHALGQS WHPEHFVCTH CKEEIGSSPF FERSGLAYCP
210 220 230 240 250
NDYHQLFSPR CAYCAAPILD KVLTAMNQTW HPEHFFCSHC GEVFGAEGFH
260 270 280 290 300
EKDKKPYCRK DFLAMFSPKC GGCNRPVLEN YLSAMDTVWH PECFVCGDCF
310 320 330 340 350
TSFSTGSFFE LDGRPFCELH YHHRRGTLCH GCGQPITGRC ISAMGYKFHP
360 370 380
EHFVCAFCLT QLSKGIFREQ NDKTYCQPCF NKLFPL
Length:386
Mass (Da):43,332
Last modified:August 1, 1998 - v1
Checksum:iC8D2BE61FAB11F3A
GO
Isoform 2 (identifier: O60711-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MEEL → MSTLLISSS

Note: No experimental confirmation available.
Show »
Length:391
Mass (Da):43,750
Checksum:iA8F1FFD11D4DB7BD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2E → D in CAG38768 (Ref. 3) Curated1
Sequence conflicti14S → T in BAD96885 (Ref. 4) Curated1
Sequence conflicti100L → M in CAG38768 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_050152148P → T.Corresponds to variant rs12271558dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0426551 – 4MEEL → MSTLLISSS in isoform 2. 1 Publication4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062075 mRNA. Translation: AAC16014.1.
AK300955 mRNA. Translation: BAG62583.1.
AK313306 mRNA. Translation: BAG36111.1.
CR536531 mRNA. Translation: CAG38768.1.
AK223165 mRNA. Translation: BAD96885.1.
AP001350 Genomic DNA. No translation available.
AP003557 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW73808.1.
BC019035 mRNA. Translation: AAH19035.1.
CCDSiCCDS53635.1. [O60711-2]
CCDS7969.1. [O60711-1]
RefSeqiNP_001137467.1. NM_001143995.2. [O60711-2]
NP_001294880.1. NM_001307951.1.
NP_004802.1. NM_004811.2. [O60711-1]
UniGeneiHs.125474.

Genome annotation databases

EnsembliENST00000395074; ENSP00000378512; ENSG00000110031. [O60711-1]
ENST00000528954; ENSP00000431284; ENSG00000110031. [O60711-2]
GeneIDi9404.
KEGGihsa:9404.
UCSCiuc001nmw.4. human. [O60711-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062075 mRNA. Translation: AAC16014.1.
AK300955 mRNA. Translation: BAG62583.1.
AK313306 mRNA. Translation: BAG36111.1.
CR536531 mRNA. Translation: CAG38768.1.
AK223165 mRNA. Translation: BAD96885.1.
AP001350 Genomic DNA. No translation available.
AP003557 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW73808.1.
BC019035 mRNA. Translation: AAH19035.1.
CCDSiCCDS53635.1. [O60711-2]
CCDS7969.1. [O60711-1]
RefSeqiNP_001137467.1. NM_001143995.2. [O60711-2]
NP_001294880.1. NM_001307951.1.
NP_004802.1. NM_004811.2. [O60711-1]
UniGeneiHs.125474.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X3HNMR-A260-326[»]
4XEFX-ray2.50B/C/E/F1-20[»]
4XEKX-ray1.79C86-104[»]
4XEVX-ray2.01C/F86-104[»]
ProteinModelPortaliO60711.
SMRiO60711.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114801. 53 interactors.
IntActiO60711. 36 interactors.
MINTiMINT-1449182.
STRINGi9606.ENSP00000431284.

PTM databases

iPTMnetiO60711.
PhosphoSitePlusiO60711.

Polymorphism and mutation databases

BioMutaiLPXN.

Proteomic databases

EPDiO60711.
MaxQBiO60711.
PaxDbiO60711.
PeptideAtlasiO60711.
PRIDEiO60711.

Protocols and materials databases

DNASUi9404.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000395074; ENSP00000378512; ENSG00000110031. [O60711-1]
ENST00000528954; ENSP00000431284; ENSG00000110031. [O60711-2]
GeneIDi9404.
KEGGihsa:9404.
UCSCiuc001nmw.4. human. [O60711-1]

Organism-specific databases

CTDi9404.
DisGeNETi9404.
GeneCardsiLPXN.
HGNCiHGNC:14061. LPXN.
HPAiCAB046478.
HPA043741.
MIMi605390. gene.
neXtProtiNX_O60711.
OpenTargetsiENSG00000110031.
PharmGKBiPA30441.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1703. Eukaryota.
ENOG410XRD4. LUCA.
GeneTreeiENSGT00760000118910.
HOGENOMiHOG000018764.
HOVERGENiHBG001512.
InParanoidiO60711.
OMAiELMAHLC.
OrthoDBiEOG091G05AW.
PhylomeDBiO60711.
TreeFamiTF314113.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000110031-MONOMER.
SignaLinkiO60711.

Miscellaneous databases

ChiTaRSiLPXN. human.
EvolutionaryTraceiO60711.
GeneWikiiLPXN.
GenomeRNAii9404.
PROiO60711.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000110031.
CleanExiHS_LPXN.
ExpressionAtlasiO60711. baseline and differential.
GenevisibleiO60711. HS.

Family and domain databases

Gene3Di2.10.110.10. 4 hits.
InterProiIPR017305. Tgfb1i1/Leupaxin.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 4 hits.
[Graphical view]
PIRSFiPIRSF037881. Leupaxin. 1 hit.
SMARTiSM00132. LIM. 4 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLPXN_HUMAN
AccessioniPrimary (citable) accession number: O60711
Secondary accession number(s): B2R8B4
, B4DV71, Q53FW6, Q6FI07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 30, 2016
This is version 153 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.