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O60711

- LPXN_HUMAN

UniProt

O60711 - LPXN_HUMAN

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Protein

Leupaxin

Gene

LPXN

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. transcription cofactor activity Source: UniProtKB
  2. 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
Complete GO annotation...

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. plasma membrane Source: UniProtKB
  7. podosome Source: UniProtKB
Complete GO annotation...

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

BgeeiO60711.
CleanExiHS_LPXN.
ExpressionAtlasiO60711. baseline and differential.
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. 18 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.
GeneTreeiENSGT00760000118910.
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

        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)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. 18 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.
GeneTreei ENSGT00760000118910.
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

Bgeei O60711.
CleanExi HS_LPXN.
ExpressionAtlasi O60711. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 135 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