Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O60711

- LPXN_HUMAN

UniProt

O60711 - LPXN_HUMAN

Protein

Leupaxin

Gene

LPXN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. protein binding Source: UniProtKB
    2. transcription cofactor activity Source: UniProtKB
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: ProtInc
    2. negative regulation of B cell receptor signaling pathway Source: UniProtKB
    3. negative regulation of cell adhesion Source: UniProtKB
    4. protein complex assembly Source: ProtInc
    5. regulation of cell adhesion mediated by integrin Source: Ensembl
    6. regulation of transcription, DNA-templated Source: UniProtKB-KW
    7. signal transduction Source: ProtInc
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Cell adhesion, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiO60711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Leupaxin
    Gene namesi
    Name:LPXN
    Synonyms:LDLP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: 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

    1. cell projection Source: UniProtKB-KW
    2. cytoplasm Source: UniProtKB
    3. focal adhesion Source: UniProtKB
    4. membrane Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    7. plasma membrane Source: UniProtKB
    8. podosome Source: UniProtKB

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30441.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 386386LeupaxinPRO_0000075836Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei19 – 191Phosphoserine1 Publication
    Modified residuei22 – 221Phosphotyrosine1 Publication
    Modified residuei54 – 541PhosphoserineBy similarity
    Modified residuei62 – 621Phosphotyrosine1 Publication
    Modified residuei72 – 721Phosphotyrosine; by LYN2 Publications

    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-72.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO60711.
    PaxDbiO60711.
    PeptideAtlasiO60711.
    PRIDEiO60711.

    PTM databases

    PhosphoSiteiO60711.

    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

    ArrayExpressiO60711.
    BgeeiO60711.
    CleanExiHS_LPXN.
    GenevestigatoriO60711.

    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
    Hoxa1P090223EBI-744222,EBI-3957603From a different organism.

    Protein-protein interaction databases

    BioGridi114801. 17 interactions.
    IntActiO60711. 25 interactions.
    MINTiMINT-1449182.
    STRINGi9606.ENSP00000263845.

    Structurei

    Secondary structure

    1
    386
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni271 – 2733
    Beta strandi282 – 2843
    Beta strandi287 – 2893
    Turni291 – 2933
    Beta strandi297 – 2993
    Beta strandi309 – 3135
    Helixi318 – 3258

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X3HNMR-A260-326[»]
    ProteinModelPortaliO60711.
    SMRiO60711. Positions 152-384.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60711.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini150 – 20859LIM zinc-binding 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini209 – 26759LIM zinc-binding 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini268 – 32659LIM zinc-binding 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini327 – 38660LIM zinc-binding 4PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi3 – 1513LD motif 1Add
    BLAST
    Motifi70 – 8213LD motif 2Add
    BLAST
    Motifi92 – 10312LD motif 3Add
    BLAST

    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

    eggNOGiNOG267887.
    HOGENOMiHOG000018764.
    HOVERGENiHBG001512.
    InParanoidiO60711.
    OMAiCGEVFGA.
    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. Align

    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

    MEELDALLEE LERSTLQDSD EYSNPAPLPL DQHSRKETNL DETSEILSIQ    50
    DNTSPLPAQL VYTTNIQELN VYSEAQEPKE SPPPSKTSAA AQLDELMAHL 100
    TEMQAKVAVR ADAGKKHLPD KQDHKASLDS MLGGLEQELQ DLGIATVPKG 150
    HCASCQKPIA GKVIHALGQS WHPEHFVCTH CKEEIGSSPF FERSGLAYCP 200
    NDYHQLFSPR CAYCAAPILD KVLTAMNQTW HPEHFFCSHC GEVFGAEGFH 250
    EKDKKPYCRK DFLAMFSPKC GGCNRPVLEN YLSAMDTVWH PECFVCGDCF 300
    TSFSTGSFFE LDGRPFCELH YHHRRGTLCH GCGQPITGRC ISAMGYKFHP 350
    EHFVCAFCLT QLSKGIFREQ NDKTYCQPCF NKLFPL 386
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21E → D in CAG38768. 1 PublicationCurated
    Sequence conflicti14 – 141S → T in BAD96885. 1 PublicationCurated
    Sequence conflicti100 – 1001L → M in CAG38768. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti148 – 1481P → T.
    Corresponds to variant rs12271558 [ dbSNP | Ensembl ].
    VAR_050152

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 44MEEL → MSTLLISSS in isoform 2. 1 PublicationVSP_042655

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_001143995.1. [O60711-2]
    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.3. human. [O60711-1]
    uc010rkj.2. human. [O60711-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS53635.1. [O60711-2 ]
    CCDS7969.1. [O60711-1 ]
    RefSeqi NP_001137467.1. NM_001143995.1. [O60711-2 ]
    NP_004802.1. NM_004811.2. [O60711-1 ]
    UniGenei Hs.125474.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X3H NMR - A 260-326 [» ]
    ProteinModelPortali O60711.
    SMRi O60711. Positions 152-384.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114801. 17 interactions.
    IntActi O60711. 25 interactions.
    MINTi MINT-1449182.
    STRINGi 9606.ENSP00000263845.

    PTM databases

    PhosphoSitei O60711.

    Proteomic databases

    MaxQBi O60711.
    PaxDbi O60711.
    PeptideAtlasi O60711.
    PRIDEi O60711.

    Protocols and materials databases

    DNASUi 9404.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000395074 ; ENSP00000378512 ; ENSG00000110031 . [O60711-1 ]
    ENST00000528954 ; ENSP00000431284 ; ENSG00000110031 . [O60711-2 ]
    GeneIDi 9404.
    KEGGi hsa:9404.
    UCSCi uc001nmw.3. human. [O60711-1 ]
    uc010rkj.2. human. [O60711-2 ]

    Organism-specific databases

    CTDi 9404.
    GeneCardsi GC11M058294.
    HGNCi HGNC:14061. LPXN.
    HPAi CAB046478.
    HPA043741.
    MIMi 605390. gene.
    neXtProti NX_O60711.
    PharmGKBi PA30441.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG267887.
    HOGENOMi HOG000018764.
    HOVERGENi HBG001512.
    InParanoidi O60711.
    OMAi CGEVFGA.
    PhylomeDBi O60711.
    TreeFami TF314113.

    Enzyme and pathway databases

    SignaLinki O60711.

    Miscellaneous databases

    EvolutionaryTracei O60711.
    GeneWikii LPXN.
    GenomeRNAii 9404.
    NextBioi 35232.
    PROi O60711.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60711.
    Bgeei O60711.
    CleanExi HS_LPXN.
    Genevestigatori O60711.

    Family and domain databases

    Gene3Di 2.10.110.10. 4 hits.
    InterProi IPR017305. Tgfb1i1/Leupaxin.
    IPR001781. Znf_LIM.
    [Graphical view ]
    Pfami PF00412. LIM. 4 hits.
    [Graphical view ]
    PIRSFi PIRSF037881. Leupaxin. 1 hit.
    SMARTi SM00132. LIM. 4 hits.
    [Graphical view ]
    PROSITEi PS00478. LIM_DOMAIN_1. 4 hits.
    PS50023. LIM_DOMAIN_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Leupaxin is a novel LIM domain protein that forms a complex with PYK2."
      Lipsky B.P., Beals C.R., Staunton D.E.
      J. Biol. Chem. 273:11709-11713(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PTK2B/PYK2, CHARACTERIZATION.
      Tissue: Spleen.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Small intestine and Spleen.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lung.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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).
      Tissue: B-cell.
    8. "Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses."
      Liu S., Thomas S.M., Woodside D.G., Rose D.M., Kiosses W.B., Pfaff M., Ginsberg M.H.
      Nature 402:676-681(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGA4.
    9. "Leupaxin is a critical adaptor protein in the adhesion zone of the osteoclast."
      Gupta A., Lee B.S., Khadeer M.A., Tang Z., Chellaiah M., Abu-Amer Y., Goldknopf J., Hruska K.A.
      J. Bone Miner. Res. 18:669-685(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    10. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Interaction of Pyk2 and PTP-PEST with leupaxin in prostate cancer cells."
      Sahu S.N., Nunez S., Bai G., Gupta A.
      Am. J. Physiol. 292:C2288-C2296(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTK2B/PYK2 AND PTPN12, SUBCELLULAR LOCATION.
    13. "Leupaxin negatively regulates B cell receptor signaling."
      Chew V., Lam K.P.
      J. Biol. Chem. 282:27181-27191(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-72 BY LYN, INTERACTION WITH LYN.
    14. "The LIM protein leupaxin is enriched in smooth muscle and functions as an serum response factor cofactor to induce smooth muscle cell gene transcription."
      Sundberg-Smith L.J., DiMichele L.A., Sayers R.L., Mack C.P., Taylor J.M.
      Circ. Res. 102:1502-1511(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PTK2/FAK AND SRF.
    15. "Leupaxin, a novel coactivator of the androgen receptor, is expressed in prostate cancer and plays a role in adhesion and invasion of prostate carcinoma cells."
      Kaulfuss S., Grzmil M., Hemmerlein B., Thelen P., Schweyer S., Neesen J., Bubendorf L., Glass A.G., Jarry H., Auber B., Burfeind P.
      Mol. Endocrinol. 22:1606-1621(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH AR.
    16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "Leupaxin is similar to paxillin in focal adhesion targeting and tyrosine phosphorylation but has distinct roles in cell adhesion and spreading."
      Chen P.W., Kroog G.S.
      Cell Adh. Migr. 4:527-540(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-22; TYR-62 AND TYR-72.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Solution structure of the LIM domain of human leupaxin."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JAN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 260-326.

    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: October 1, 2014
    This is version 134 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

    External Data

    Dasty 3