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P49023

- PAXI_HUMAN

UniProt

P49023 - PAXI_HUMAN

Protein

Paxillin

Gene

PXN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion).

    GO - Molecular functioni

    1. beta-catenin binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. vinculin binding Source: UniProtKB
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. activation of MAPK activity Source: Ensembl
    2. branching morphogenesis of an epithelial tube Source: Ensembl
    3. cell adhesion Source: ProtInc
    4. cell junction assembly Source: Reactome
    5. cellular component movement Source: Ensembl
    6. cellular response to reactive oxygen species Source: BHF-UCL
    7. cytoskeleton organization Source: Ensembl
    8. epidermal growth factor receptor signaling pathway Source: Reactome
    9. focal adhesion assembly Source: Ensembl
    10. growth hormone receptor signaling pathway Source: BHF-UCL
    11. integrin-mediated signaling pathway Source: Ensembl
    12. lamellipodium assembly Source: Ensembl
    13. muscle contraction Source: Reactome
    14. peptidyl-tyrosine phosphorylation Source: Ensembl
    15. signal complex assembly Source: ProtInc
    16. signal transduction Source: ProtInc

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_12578. GAB1 signalosome.
    REACT_20558. Smooth Muscle Contraction.
    REACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
    REACT_20617. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
    SignaLinkiP49023.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Paxillin
    Gene namesi
    Name:PXN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9718. PXN.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cell junctionfocal adhesion 1 Publication. Cytoplasmcell cortex By similarity
    Note: Colocalizes with integrins at the cell periphery.By similarity

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. cytoplasm Source: HPA
    3. focal adhesion Source: BHF-UCL
    4. lamellipodium Source: BHF-UCL
    5. microtubule associated complex Source: ProtInc
    6. nucleus Source: HPA
    7. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 82LL → RR: Loss of interaction with PDCD10. 1 Publication

    Organism-specific databases

    PharmGKBiPA34062.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 591591PaxillinPRO_0000075853Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei31 – 311Phosphotyrosine; by PTK62 Publications
    Modified residuei83 – 831PhosphoserineBy similarity
    Modified residuei85 – 851Phosphoserine3 Publications
    Modified residuei88 – 881PhosphotyrosineBy similarity
    Modified residuei106 – 1061Phosphoserine3 Publications
    Modified residuei118 – 1181Phosphotyrosine; by PTK62 Publications
    Modified residuei119 – 1191Phosphoserine1 Publication
    Modified residuei126 – 1261Phosphoserine4 Publications
    Modified residuei130 – 1301Phosphoserine1 Publication
    Modified residuei137 – 1371Phosphoserine1 Publication
    Modified residuei181 – 1811Phosphotyrosine1 Publication
    Modified residuei244 – 2441Phosphoserine; by CDK51 Publication
    Modified residuei322 – 3221Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by MAPK1/ERK2 By similarity. Phosphorylated on tyrosine residues during integrin-mediated cell adhesion, embryonic development, fibroblast transformation and following stimulation of cells by mitogens. Phosphorylation at Ser-244 by CDK5 reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation. Phosphorylation at Tyr-31 and Tyr-118 by PTK6 promote the activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion.By similarity9 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP49023.
    PaxDbiP49023.
    PRIDEiP49023.

    PTM databases

    PhosphoSiteiP49023.

    Miscellaneous databases

    PMAP-CutDBP49023.

    Expressioni

    Gene expression databases

    ArrayExpressiP49023.
    BgeeiP49023.
    CleanExiHS_PXN.
    GenevestigatoriP49023.

    Organism-specific databases

    HPAiCAB003841.
    HPA051309.

    Interactioni

    Subunit structurei

    Binds in vitro to vinculin as well as to the SH3 domain of SRC and, when tyrosine phosphorylated, to the SH2 domain of V-CRK. Isoform beta binds to PTK2/FAK1 but weakly to vinculin. Isoform gamma binds to vinculin but only weakly to PTK2/FAK1. Interacts with GIT1, NUDT16L1/SDOS and TGFB1I1. Component of cytoplasmic complexes, which also contain GIT1, ARHGEF6 and PAK1 By similarity. Interacts with PTK2/FAK1 and PTK2B/PYK2. Binds ASAP2. Interacts with unphosphorylated ITGA4. Interacts with RNF5 and PDCD10. Interacts with NEK3 and this interaction is prolactin-dependent. Interacts with PTK6. Interacts with SORBS1, PARVA and PARVB.By similarity13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CSKP412402EBI-702209,EBI-1380630
    CTNNB1P352224EBI-702209,EBI-491549
    GAB1Q134802EBI-702209,EBI-517684
    GIT2Q141612EBI-702209,EBI-1046878
    ITGA4P136123EBI-702209,EBI-703044
    ITGB1P05556-12EBI-702209,EBI-6082935
    PIK3R1P279862EBI-702209,EBI-79464
    PTK2Q0539715EBI-702209,EBI-702142
    PTPN11Q061243EBI-702209,EBI-297779
    rnf-5Q094632EBI-702209,EBI-963421From a different organism.
    RNF5Q999426EBI-702209,EBI-348482
    Sorbs1Q62417-28EBI-702209,EBI-7072893From a different organism.
    SrcP054802EBI-702209,EBI-298680From a different organism.

    Protein-protein interaction databases

    BioGridi111787. 70 interactions.
    DIPiDIP-33851N.
    IntActiP49023. 50 interactions.
    MINTiMINT-92615.
    STRINGi9606.ENSP00000228307.

    Structurei

    Secondary structure

    1
    591
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 119
    Helixi144 – 15411
    Helixi263 – 27311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KKYmodel-A142-157[»]
    1KL0model-B142-157[»]
    1OW6X-ray2.35D/F262-274[»]
    1OW7X-ray2.60D/E/F262-274[»]
    1OW8X-ray2.85D/F141-153[»]
    2K2RNMR-B3-12[»]
    2O9VX-ray1.63B45-54[»]
    2VZDX-ray2.10C/D1-20[»]
    2VZGX-ray1.80A141-160[»]
    2VZIX-ray2.20A262-315[»]
    3GM1X-ray2.95C/D/E/F262-274[»]
    3PY7X-ray2.29A1-10[»]
    3RQEX-ray2.80E2-15[»]
    3RQFX-ray2.70E141-153[»]
    3RQGX-ray2.50E262-274[»]
    3U3CX-ray3.70B/C139-160[»]
    3U3FX-ray3.10E/F/G/H/I/J261-277[»]
    4EDNX-ray2.90K/L/M/N/O/P/Q1-20[»]
    ProteinModelPortaliP49023.
    SMRiP49023. Positions 357-590.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49023.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini356 – 41560LIM zinc-binding 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini416 – 47358LIM zinc-binding 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini474 – 53360LIM zinc-binding 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini534 – 59158LIM zinc-binding 4PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi3 – 1513LD motif 1Add
    BLAST
    Motifi144 – 15613LD motif 2Add
    BLAST
    Motifi216 – 22813LD motif 3Add
    BLAST
    Motifi265 – 27612LD motif 4Add
    BLAST
    Motifi333 – 34513LD motif 5Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi46 – 538Pro-rich

    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.
    HOVERGENiHBG001512.
    KOiK05760.
    OMAiLSDFKFM.
    OrthoDBiEOG70ZZQN.
    PhylomeDBiP49023.
    TreeFamiTF314113.

    Family and domain databases

    Gene3Di2.10.110.10. 4 hits.
    InterProiIPR001904. Paxillin.
    IPR001781. Znf_LIM.
    [Graphical view]
    PfamiPF00412. LIM. 4 hits.
    [Graphical view]
    PRINTSiPR00832. PAXILLIN.
    SMARTiSM00132. LIM. 4 hits.
    [Graphical view]
    PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
    PS50023. LIM_DOMAIN_2. 4 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform Beta (identifier: P49023-1) [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

    MDDLDALLAD LESTTSHISK RPVFLSEETP YSYPTGNHTY QEIAVPPPVP    50
    PPPSSEALNG TILDPLDQWQ PSSSRFIHQQ PQSSSPVYGS SAKTSSVSNP 100
    QDSVGSPCSR VGEEEHVYSF PNKQKSAEPS PTVMSTSLGS NLSELDRLLL 150
    ELNAVQHNPP GFPADEANSS PPLPGALSPL YGVPETNSPL GGKAGPLTKE 200
    KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG EMSSPQRVTS 250
    TQQQTRISAS SATRELDELM ASLSDFKIQG LEQRADGERC WAAGWPRDGG 300
    RSSPGGQDEG GFMAQGKTGS SSPPGGPPKP GSQLDSMLGS LQSDLNKLGV 350
    ATVAKGVCGA CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD 400
    GQPYCEKDYH NLFSPRCYYC NGPILDKVVT ALDRTWHPEH FFCAQCGAFF 450
    GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA RAILENYISA LNTLWHPECF 500
    VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK PITGRCITAM 550
    AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQNCFLKLF C 591
    Length:591
    Mass (Da):64,505
    Last modified:January 11, 2011 - v3
    Checksum:iABF6C0BE5939623F
    GO
    Isoform Alpha (identifier: P49023-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         278-311: Missing.

    Show »
    Length:557
    Mass (Da):60,967
    Checksum:i94A6C321E4735076
    GO
    Isoform Gamma (identifier: P49023-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         278-311: IQGLEQRADGERCWAAGWPRDGGRSSPGGQDEGG → GSWPLEEVVL...SPDQPPPCPQ

    Show »
    Length:605
    Mass (Da):66,212
    Checksum:i0121D1C68C6F7398
    GO
    Isoform 4 (identifier: P49023-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-133: Missing.
         278-311: Missing.

    Show »
    Length:424
    Mass (Da):46,604
    Checksum:i74D536A48B653D6D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti280 – 2801G → D in BAA18997. (PubMed:9054445)Curated
    Sequence conflicti327 – 3271P → L in CAI46024. (PubMed:17974005)Curated
    Sequence conflicti413 – 4131F → S in CAI46024. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti73 – 731S → G.5 Publications
    Corresponds to variant rs4767884 [ dbSNP | Ensembl ].
    VAR_065099

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 133133Missing in isoform 4. 1 PublicationVSP_040483Add
    BLAST
    Alternative sequencei278 – 31134Missing in isoform Alpha and isoform 4. 4 PublicationsVSP_003114Add
    BLAST
    Alternative sequencei278 – 31134IQGLE…QDEGG → GSWPLEEVVLLVSISSSVQE GEKYPHPCAARHRTPSLRSP DQPPPCPQ in isoform Gamma. 1 PublicationVSP_003115Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14588 mRNA. Translation: AAC50104.1.
    U87946
    , U87941, U87942, U87943, U87944, U87945 Genomic DNA. Translation: AAD00648.1.
    D86862 mRNA. Translation: BAA18997.1.
    D86863 mRNA. Translation: BAA18998.1.
    AK314204 mRNA. Translation: BAG36880.1.
    BX648777 mRNA. Translation: CAI46024.1.
    AC004263 Genomic DNA. Translation: AAC05175.1.
    BC136787 mRNA. Translation: AAI36788.1.
    BC136794 mRNA. Translation: AAI36795.1.
    BC144410 mRNA. Translation: AAI44411.1.
    CCDSiCCDS44996.1. [P49023-2]
    CCDS44997.1. [P49023-1]
    CCDS44998.1. [P49023-4]
    CCDS58281.1. [P49023-3]
    PIRiA55933.
    RefSeqiNP_001074324.1. NM_001080855.2. [P49023-1]
    NP_001230685.1. NM_001243756.1. [P49023-3]
    NP_002850.2. NM_002859.3. [P49023-2]
    NP_079433.3. NM_025157.4. [P49023-4]
    UniGeneiHs.446336.

    Genome annotation databases

    EnsembliENST00000228307; ENSP00000228307; ENSG00000089159. [P49023-1]
    ENST00000267257; ENSP00000267257; ENSG00000089159. [P49023-3]
    ENST00000424649; ENSP00000391283; ENSG00000089159. [P49023-2]
    ENST00000458477; ENSP00000395536; ENSG00000089159. [P49023-4]
    GeneIDi5829.
    KEGGihsa:5829.
    UCSCiuc001txt.3. human. [P49023-1]
    uc001txv.3. human. [P49023-3]
    uc001txx.3. human. [P49023-4]
    uc001txy.3. human. [P49023-2]

    Polymorphism databases

    DMDMi317373486.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14588 mRNA. Translation: AAC50104.1 .
    U87946
    , U87941 , U87942 , U87943 , U87944 , U87945 Genomic DNA. Translation: AAD00648.1 .
    D86862 mRNA. Translation: BAA18997.1 .
    D86863 mRNA. Translation: BAA18998.1 .
    AK314204 mRNA. Translation: BAG36880.1 .
    BX648777 mRNA. Translation: CAI46024.1 .
    AC004263 Genomic DNA. Translation: AAC05175.1 .
    BC136787 mRNA. Translation: AAI36788.1 .
    BC136794 mRNA. Translation: AAI36795.1 .
    BC144410 mRNA. Translation: AAI44411.1 .
    CCDSi CCDS44996.1. [P49023-2 ]
    CCDS44997.1. [P49023-1 ]
    CCDS44998.1. [P49023-4 ]
    CCDS58281.1. [P49023-3 ]
    PIRi A55933.
    RefSeqi NP_001074324.1. NM_001080855.2. [P49023-1 ]
    NP_001230685.1. NM_001243756.1. [P49023-3 ]
    NP_002850.2. NM_002859.3. [P49023-2 ]
    NP_079433.3. NM_025157.4. [P49023-4 ]
    UniGenei Hs.446336.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KKY model - A 142-157 [» ]
    1KL0 model - B 142-157 [» ]
    1OW6 X-ray 2.35 D/F 262-274 [» ]
    1OW7 X-ray 2.60 D/E/F 262-274 [» ]
    1OW8 X-ray 2.85 D/F 141-153 [» ]
    2K2R NMR - B 3-12 [» ]
    2O9V X-ray 1.63 B 45-54 [» ]
    2VZD X-ray 2.10 C/D 1-20 [» ]
    2VZG X-ray 1.80 A 141-160 [» ]
    2VZI X-ray 2.20 A 262-315 [» ]
    3GM1 X-ray 2.95 C/D/E/F 262-274 [» ]
    3PY7 X-ray 2.29 A 1-10 [» ]
    3RQE X-ray 2.80 E 2-15 [» ]
    3RQF X-ray 2.70 E 141-153 [» ]
    3RQG X-ray 2.50 E 262-274 [» ]
    3U3C X-ray 3.70 B/C 139-160 [» ]
    3U3F X-ray 3.10 E/F/G/H/I/J 261-277 [» ]
    4EDN X-ray 2.90 K/L/M/N/O/P/Q 1-20 [» ]
    ProteinModelPortali P49023.
    SMRi P49023. Positions 357-590.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111787. 70 interactions.
    DIPi DIP-33851N.
    IntActi P49023. 50 interactions.
    MINTi MINT-92615.
    STRINGi 9606.ENSP00000228307.

    Chemistry

    ChEMBLi CHEMBL5715.

    PTM databases

    PhosphoSitei P49023.

    Polymorphism databases

    DMDMi 317373486.

    Proteomic databases

    MaxQBi P49023.
    PaxDbi P49023.
    PRIDEi P49023.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000228307 ; ENSP00000228307 ; ENSG00000089159 . [P49023-1 ]
    ENST00000267257 ; ENSP00000267257 ; ENSG00000089159 . [P49023-3 ]
    ENST00000424649 ; ENSP00000391283 ; ENSG00000089159 . [P49023-2 ]
    ENST00000458477 ; ENSP00000395536 ; ENSG00000089159 . [P49023-4 ]
    GeneIDi 5829.
    KEGGi hsa:5829.
    UCSCi uc001txt.3. human. [P49023-1 ]
    uc001txv.3. human. [P49023-3 ]
    uc001txx.3. human. [P49023-4 ]
    uc001txy.3. human. [P49023-2 ]

    Organism-specific databases

    CTDi 5829.
    GeneCardsi GC12M120648.
    HGNCi HGNC:9718. PXN.
    HPAi CAB003841.
    HPA051309.
    MIMi 602505. gene.
    neXtProti NX_P49023.
    PharmGKBi PA34062.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG267887.
    HOVERGENi HBG001512.
    KOi K05760.
    OMAi LSDFKFM.
    OrthoDBi EOG70ZZQN.
    PhylomeDBi P49023.
    TreeFami TF314113.

    Enzyme and pathway databases

    Reactomei REACT_12578. GAB1 signalosome.
    REACT_20558. Smooth Muscle Contraction.
    REACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
    REACT_20617. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
    SignaLinki P49023.

    Miscellaneous databases

    ChiTaRSi PXN. human.
    EvolutionaryTracei P49023.
    GeneWikii Paxillin.
    GenomeRNAii 5829.
    NextBioi 22710.
    PMAP-CutDB P49023.
    PROi P49023.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49023.
    Bgeei P49023.
    CleanExi HS_PXN.
    Genevestigatori P49023.

    Family and domain databases

    Gene3Di 2.10.110.10. 4 hits.
    InterProi IPR001904. Paxillin.
    IPR001781. Znf_LIM.
    [Graphical view ]
    Pfami PF00412. LIM. 4 hits.
    [Graphical view ]
    PRINTSi PR00832. PAXILLIN.
    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. "Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL."
      Salgia R., Li J.-L., Lo S.H., Brunkhorst B., Kansas G.S., Sobhany E.S., Sun Y., Pisick E., Hallek M., Ernst T., Tantravahi R., Chen L.B., Griffin J.D.
      J. Biol. Chem. 270:5039-5047(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), VARIANT GLY-73.
    2. "Transcription map of the 5cM region surrounding the hepatocyte nuclear factor-1a/MODY3 gene on chromosome 12."
      Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V., Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M., Lathrop M., Cox R.D., Bell G.I.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-73.
    3. "Monocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteins."
      Mazaki Y., Hashimoto S., Sabe H.
      J. Biol. Chem. 272:7437-7444(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA), VARIANT GLY-73.
      Tissue: Placenta.
    4. "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] (ISOFORM ALPHA), VARIANT GLY-73.
      Tissue: Placenta.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Fetal kidney.
    6. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      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 ALPHA), VARIANT GLY-73.
      Tissue: Brain and Testis.
    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. "Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly."
      Zhao Z.-S., Manser E., Loo T.-H., Lim L.
      Mol. Cell. Biol. 20:6354-6363(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GIT1.
    10. "A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an ADP-ribosylation factor GTPase-activating protein activity, is involved in paxillin recruitment to focal adhesions and cell migration."
      Kondo A., Hashimoto S., Yano H., Nagayama K., Mazaki Y., Sabe H.
      Mol. Biol. Cell 11:1315-1327(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ASAP2.
    11. "Involvement of phosphorylation of Tyr-31 and Tyr-118 of paxillin in MM1 cancer cell migration."
      Iwasaki T., Nakata A., Mukai M., Shinkai K., Yano H., Sabe H., Schaefer E., Tatsuta M., Tsujimura T., Terada N., Kakishita E., Akedo H.
      Int. J. Cancer 97:330-335(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-31; TYR-118 AND TYR-181.
    12. "RNF5, a RING finger protein that regulates cell motility by targeting paxillin ubiquitination and altered localization."
      Didier C., Broday L., Bhoumik A., Israeli S., Takahashi S., Nakayama K., Thomas S.M., Turner C.E., Henderson S., Sabe H., Ronai Z.
      Mol. Cell. Biol. 23:5331-5345(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF5.
    13. "Brk activates rac1 and promotes cell migration and invasion by phosphorylating paxillin."
      Chen H.Y., Shen C.H., Tsai Y.T., Lin F.C., Huang Y.P., Chen R.H.
      Mol. Cell. Biol. 24:10558-10572(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-31 AND TYR-118, INTERACTION WITH PTK6.
    14. "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].
    15. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Cdk5 regulates differentiation of oligodendrocyte precursor cells through the direct phosphorylation of paxillin."
      Miyamoto Y., Yamauchi J., Chan J.R., Okada A., Tomooka Y., Hisanaga S., Tanoue A.
      J. Cell Sci. 120:4355-4366(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-244.
    17. "Nek3 kinase regulates prolactin-mediated cytoskeletal reorganization and motility of breast cancer cells."
      Miller S.L., Antico G., Raghunath P.N., Tomaszewski J.E., Clevenger C.V.
      Oncogene 26:4668-4678(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEK3.
    18. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-106; SER-126; SER-130; SER-137 AND SER-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    24. "Crystal structure of CCM3, a cerebral cavernous malformation protein critical for vascular integrity."
      Li X., Zhang R., Zhang H., He Y., Ji W., Min W., Boggon T.J.
      J. Biol. Chem. 285:24099-24107(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDCD10, SUBCELLULAR LOCATION, MUTAGENESIS OF 7-LEU-LEU-8.
    25. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-119 AND SER-126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain."
      Hoellerer M.K., Noble M.E., Labesse G., Campbell I.D., Werner J.M., Arold S.T.
      Structure 11:1207-1217(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 262-274 IN COMPLEX WITH PTK2/FAK1, INTERACTION WITH PTK2/FAK1.
    30. Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 45-54 IN COMPLEX WITH SORBS1, INTERACTION WITH SORBS1.
    31. "The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly."
      Wang X., Fukuda K., Byeon I.J., Velyvis A., Wu C., Gronenborn A., Qin J.
      J. Biol. Chem. 283:21113-21119(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 244-372 IN COMPLEX WITH PARVA, INTERACTION WITH PARVA.
    32. "Structural analysis of the interactions between paxillin LD motifs and alpha-parvin."
      Lorenz S., Vakonakis I., Lowe E.D., Campbell I.D., Noble M.E., Hoellerer M.K.
      Structure 16:1521-1531(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-315 IN COMPLEX WITH PARVA, INTERACTION WITH PARVA.
    33. "Crystal structures of free and ligand-bound focal adhesion targeting domain of Pyk2."
      Lulo J., Yuzawa S., Schlessinger J.
      Biochem. Biophys. Res. Commun. 383:347-352(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 262-274 IN COMPLEX WITH PTK2B/PYK2, INTERACTION WITH PTK2B/PYK2.
    34. "Structural basis for paxillin binding and focal adhesion targeting of beta-parvin."
      Stiegler A.L., Draheim K.M., Li X., Chayen N.E., Calderwood D.A., Boggon T.J.
      J. Biol. Chem. 287:32566-32577(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-20 IN COMPLEX WITH PARVB, INTERACTION WITH PARVB.

    Entry informationi

    Entry nameiPAXI_HUMAN
    AccessioniPrimary (citable) accession number: P49023
    Secondary accession number(s): B2RAI3
    , B7ZMB4, O14970, O14971, O60360, Q5HYA4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 161 of the entry and version 3 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 12
      Human chromosome 12: 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