PAXI_HUMAN
ID PAXI_HUMAN Reviewed; 591 AA.
AC P49023; B2RAI3; B7ZMB4; O14970; O14971; O60360; Q5HYA4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 227.
DE RecName: Full=Paxillin;
GN Name=PXN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), INTERACTION WITH VCL; SRC AND
RP CRK, AND VARIANT GLY-73.
RX PubMed=7534286; DOI=10.1074/jbc.270.10.5039;
RA Salgia R., Li J.-L., Lo S.H., Brunkhorst B., Kansas G.S., Sobhany E.S.,
RA Sun Y., Pisick E., Hallek M., Ernst T., Tantravahi R., Chen L.B.,
RA Griffin J.D.;
RT "Molecular cloning of human paxillin, a focal adhesion protein
RT phosphorylated by P210BCR/ABL.";
RL J. Biol. Chem. 270:5039-5047(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-73.
RA Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V.,
RA Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M.,
RA Lathrop M., Cox R.D., Bell G.I.;
RT "Transcription map of the 5cM region surrounding the hepatocyte nuclear
RT factor-1a/MODY3 gene on chromosome 12.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA), INTERACTION WITH VCL
RP AND PTK2, AND VARIANT GLY-73.
RC TISSUE=Placenta;
RX PubMed=9054445; DOI=10.1074/jbc.272.11.7437;
RA Mazaki Y., Hashimoto S., Sabe H.;
RT "Monocyte cells and cancer cells express novel paxillin isoforms with
RT different binding properties to focal adhesion proteins.";
RL J. Biol. Chem. 272:7437-7444(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT GLY-73.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT GLY-73.
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH ITGA4.
RX PubMed=10604475; DOI=10.1038/45264;
RA Liu S., Thomas S.M., Woodside D.G., Rose D.M., Kiosses W.B., Pfaff M.,
RA Ginsberg M.H.;
RT "Binding of paxillin to alpha4 integrins modifies integrin-dependent
RT biological responses.";
RL Nature 402:676-681(1999).
RN [9]
RP INTERACTION WITH CEACAM1.
RX PubMed=11035932; DOI=10.1006/excr.2000.5026;
RA Ebrahimnejad A., Flayeh R., Unteregger G., Wagener C., Bruemmer J.;
RT "Cell adhesion molecule CEACAM1 associates with paxillin in granulocytes
RT and epithelial and endothelial cells.";
RL Exp. Cell Res. 260:365-373(2000).
RN [10]
RP INTERACTION WITH GIT1.
RX PubMed=10938112; DOI=10.1128/mcb.20.17.6354-6363.2000;
RA Zhao Z.-S., Manser E., Loo T.-H., Lim L.;
RT "Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal
RT complex disassembly.";
RL Mol. Cell. Biol. 20:6354-6363(2000).
RN [11]
RP INTERACTION WITH ASAP2.
RX PubMed=10749932; DOI=10.1091/mbc.11.4.1315;
RA Kondo A., Hashimoto S., Yano H., Nagayama K., Mazaki Y., Sabe H.;
RT "A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an ADP-
RT ribosylation factor GTPase-activating protein activity, is involved in
RT paxillin recruitment to focal adhesions and cell migration.";
RL Mol. Biol. Cell 11:1315-1327(2000).
RN [12]
RP PHOSPHORYLATION AT TYR-31; TYR-118 AND TYR-181.
RX PubMed=11774284; DOI=10.1002/ijc.1609;
RA Iwasaki T., Nakata A., Mukai M., Shinkai K., Yano H., Sabe H., Schaefer E.,
RA Tatsuta M., Tsujimura T., Terada N., Kakishita E., Akedo H.;
RT "Involvement of phosphorylation of Tyr-31 and Tyr-118 of paxillin in MM1
RT cancer cell migration.";
RL Int. J. Cancer 97:330-335(2002).
RN [13]
RP INTERACTION WITH RNF5.
RX PubMed=12861019; DOI=10.1128/mcb.23.15.5331-5345.2003;
RA Didier C., Broday L., Bhoumik A., Israeli S., Takahashi S., Nakayama K.,
RA Thomas S.M., Turner C.E., Henderson S., Sabe H., Ronai Z.;
RT "RNF5, a RING finger protein that regulates cell motility by targeting
RT paxillin ubiquitination and altered localization.";
RL Mol. Cell. Biol. 23:5331-5345(2003).
RN [14]
RP PHOSPHORYLATION AT TYR-31 AND TYR-118, AND INTERACTION WITH PTK6.
RX PubMed=15572663; DOI=10.1128/mcb.24.24.10558-10572.2004;
RA Chen H.Y., Shen C.H., Tsai Y.T., Lin F.C., Huang Y.P., Chen R.H.;
RT "Brk activates rac1 and promotes cell migration and invasion by
RT phosphorylating paxillin.";
RL Mol. Cell. Biol. 24:10558-10572(2004).
RN [15]
RP INTERACTION WITH PARVA AND ILK.
RX PubMed=15817463; DOI=10.1074/jbc.m500752200;
RA LaLonde D.P., Brown M.C., Bouverat B.P., Turner C.E.;
RT "Actopaxin interacts with TESK1 to regulate cell spreading on
RT fibronectin.";
RL J. Biol. Chem. 280:21680-21688(2005).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [18]
RP PHOSPHORYLATION AT SER-244.
RX PubMed=18042622; DOI=10.1242/jcs.018218;
RA Miyamoto Y., Yamauchi J., Chan J.R., Okada A., Tomooka Y., Hisanaga S.,
RA Tanoue A.;
RT "Cdk5 regulates differentiation of oligodendrocyte precursor cells through
RT the direct phosphorylation of paxillin.";
RL J. Cell Sci. 120:4355-4366(2007).
RN [19]
RP INTERACTION WITH NEK3.
RX PubMed=17297458; DOI=10.1038/sj.onc.1210264;
RA Miller S.L., Antico G., Raghunath P.N., Tomaszewski J.E., Clevenger C.V.;
RT "Nek3 kinase regulates prolactin-mediated cytoskeletal reorganization and
RT motility of breast cancer cells.";
RL Oncogene 26:4668-4678(2007).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-106; SER-126;
RP SER-130; SER-137 AND SER-322, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-126, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [26]
RP INTERACTION WITH PDCD10, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 7-LEU-LEU-8.
RX PubMed=20489202; DOI=10.1074/jbc.m110.128470;
RA Li X., Zhang R., Zhang H., He Y., Ji W., Min W., Boggon T.J.;
RT "Crystal structure of CCM3, a cerebral cavernous malformation protein
RT critical for vascular integrity.";
RL J. Biol. Chem. 285:24099-24107(2010).
RN [27]
RP INTERACTION WITH CD36.
RX PubMed=20037584; DOI=10.1038/ni.1836;
RA Stewart C.R., Stuart L.M., Wilkinson K., van Gils J.M., Deng J., Halle A.,
RA Rayner K.J., Boyer L., Zhong R., Frazier W.A., Lacy-Hulbert A.,
RA El Khoury J., Golenbock D.T., Moore K.J.;
RT "CD36 ligands promote sterile inflammation through assembly of a Toll-like
RT receptor 4 and 6 heterodimer.";
RL Nat. Immunol. 11:155-161(2010).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-119 AND SER-126, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [31]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 4), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 4), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; SER-272 AND SER-303, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [33]
RP PHOSPHORYLATION AT SER-250, AND SUBCELLULAR LOCATION.
RX PubMed=23128389; DOI=10.1038/onc.2012.488;
RA Quizi J.L., Baron K., Al-Zahrani K.N., O'Reilly P., Sriram R.K., Conway J.,
RA Laurin A.A., Sabourin L.A.;
RT "SLK-mediated phosphorylation of paxillin is required for focal adhesion
RT turnover and cell migration.";
RL Oncogene 32:4656-4663(2013).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-143 AND SER-533, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [35]
RP INTERACTION WITH LIMA1.
RX PubMed=24694988; DOI=10.1038/ki.2014.85;
RA Tsurumi H., Harita Y., Kurihara H., Kosako H., Hayashi K., Matsunaga A.,
RA Kajiho Y., Kanda S., Miura K., Sekine T., Oka A., Ishizuka K., Horita S.,
RA Hattori M., Hattori S., Igarashi T.;
RT "Epithelial protein lost in neoplasm modulates platelet-derived growth
RT factor-mediated adhesion and motility of mesangial cells.";
RL Kidney Int. 86:548-557(2014).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 262-274 IN COMPLEX WITH
RP PTK2/FAK1, AND INTERACTION WITH PTK2/FAK1.
RX PubMed=14527389; DOI=10.1016/j.str.2003.08.010;
RA Hoellerer M.K., Noble M.E., Labesse G., Campbell I.D., Werner J.M.,
RA Arold S.T.;
RT "Molecular recognition of paxillin LD motifs by the focal adhesion
RT targeting domain.";
RL Structure 11:1207-1217(2003).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 45-54 IN COMPLEX WITH SORBS1, AND
RP INTERACTION WITH SORBS1.
RX PubMed=17462669; DOI=10.1016/j.jmb.2007.03.050;
RA Gehmlich K., Pinotsis N., Hayess K., van der Ven P.F., Milting H.,
RA El Banayosy A., Korfer R., Wilmanns M., Ehler E., Furst D.O.;
RT "Paxillin and ponsin interact in nascent costameres of muscle cells.";
RL J. Mol. Biol. 369:665-682(2007).
RN [38]
RP STRUCTURE BY NMR OF 244-372 IN COMPLEX WITH PARVA, AND INTERACTION WITH
RP PARVA.
RX PubMed=18508764; DOI=10.1074/jbc.m801270200;
RA Wang X., Fukuda K., Byeon I.J., Velyvis A., Wu C., Gronenborn A., Qin J.;
RT "The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel
RT modular recognition for focal adhesion assembly.";
RL J. Biol. Chem. 283:21113-21119(2008).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-315 IN COMPLEX WITH PARVA, AND
RP INTERACTION WITH PARVA.
RX PubMed=18940607; DOI=10.1016/j.str.2008.08.007;
RA Lorenz S., Vakonakis I., Lowe E.D., Campbell I.D., Noble M.E.,
RA Hoellerer M.K.;
RT "Structural analysis of the interactions between paxillin LD motifs and
RT alpha-parvin.";
RL Structure 16:1521-1531(2008).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 262-274 IN COMPLEX WITH
RP PTK2B/PYK2, AND INTERACTION WITH PTK2B/PYK2.
RX PubMed=19358827; DOI=10.1016/j.bbrc.2009.04.011;
RA Lulo J., Yuzawa S., Schlessinger J.;
RT "Crystal structures of free and ligand-bound focal adhesion targeting
RT domain of Pyk2.";
RL Biochem. Biophys. Res. Commun. 383:347-352(2009).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-20 IN COMPLEX WITH PARVB, AND
RP INTERACTION WITH PARVB.
RX PubMed=22869380; DOI=10.1074/jbc.m112.367342;
RA Stiegler A.L., Draheim K.M., Li X., Chayen N.E., Calderwood D.A.,
RA Boggon T.J.;
RT "Structural basis for paxillin binding and focal adhesion targeting of
RT beta-parvin.";
RL J. Biol. Chem. 287:32566-32577(2012).
CC -!- FUNCTION: Cytoskeletal protein involved in actin-membrane attachment at
CC sites of cell adhesion to the extracellular matrix (focal adhesion).
CC -!- SUBUNIT: Interacts in vitro with VCL/vinculin as well as to the SH3
CC domain of SRC and, when tyrosine phosphorylated, to the SH2 domain of
CC CRK (PubMed:7534286). Interacts with GIT1 (PubMed:10938112). Interacts
CC with NUDT16L1/SDOS (By similarity). Interacts with PTK2/FAK1
CC (PubMed:14527389). Interacts with PTK2B/PYK2 (PubMed:19358827).
CC Interacts with ASAP2 (PubMed:10749932). Interacts with unphosphorylated
CC ITGA4 (PubMed:10604475). Interacts with RNF5 (PubMed:12861019).
CC Interacts with PDCD10 (PubMed:20489202). Interacts with NEK3, the
CC interaction is prolactin-dependent (PubMed:17297458). Interacts with
CC PTK6 (PubMed:15572663). Interacts with TGFB1I1 (By similarity).
CC Interacts with SORBS1 (PubMed:17462669). Interacts with PARVB
CC (PubMed:22869380). Interacts (via LD motif 4) with PARVA/PARVIN
CC (PubMed:15817463, PubMed:18508764, PubMed:18940607). Interacts (via LD
CC motif 4) with ILK (PubMed:15817463, PubMed:18508764, PubMed:18940607).
CC Interacts (via cytoplasmic domain) with CEACAM1; the interaction is
CC phosphotyrosyl-dependent (PubMed:11035932). Interacts with LIMA1; this
CC complex stabilizes actin dynamics (PubMed:24694988). Interacts with
CC CD36 (via C-terminus) (PubMed:20037584). {ECO:0000250|UniProtKB:Q66H76,
CC ECO:0000250|UniProtKB:Q8VI36, ECO:0000269|PubMed:10604475,
CC ECO:0000269|PubMed:10749932, ECO:0000269|PubMed:10938112,
CC ECO:0000269|PubMed:11035932, ECO:0000269|PubMed:12861019,
CC ECO:0000269|PubMed:14527389, ECO:0000269|PubMed:15572663,
CC ECO:0000269|PubMed:15817463, ECO:0000269|PubMed:17297458,
CC ECO:0000269|PubMed:17462669, ECO:0000269|PubMed:18508764,
CC ECO:0000269|PubMed:18940607, ECO:0000269|PubMed:19358827,
CC ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:20489202,
CC ECO:0000269|PubMed:22869380, ECO:0000269|PubMed:24694988,
CC ECO:0000269|PubMed:7534286}.
CC -!- SUBUNIT: [Isoform Beta]: Interacts strongly with PTK2/FAK1 and weakly
CC with VCL/vinculin. {ECO:0000269|PubMed:9054445}.
CC -!- SUBUNIT: [Isoform Gamma]: Interacts strongly with VCL/vinculin but only
CC weakly with PTK2/FAK1. {ECO:0000269|PubMed:9054445}.
CC -!- INTERACTION:
CC P49023; P41240: CSK; NbExp=4; IntAct=EBI-702209, EBI-1380630;
CC P49023; P35222: CTNNB1; NbExp=4; IntAct=EBI-702209, EBI-491549;
CC P49023; Q13480: GAB1; NbExp=2; IntAct=EBI-702209, EBI-517684;
CC P49023; Q9Y2X7: GIT1; NbExp=3; IntAct=EBI-702209, EBI-466061;
CC P49023; Q14161: GIT2; NbExp=4; IntAct=EBI-702209, EBI-1046878;
CC P49023; P13612: ITGA4; NbExp=4; IntAct=EBI-702209, EBI-703044;
CC P49023; P05556-1: ITGB1; NbExp=2; IntAct=EBI-702209, EBI-6082935;
CC P49023; Q05397: PTK2; NbExp=18; IntAct=EBI-702209, EBI-702142;
CC P49023; Q06124: PTPN11; NbExp=3; IntAct=EBI-702209, EBI-297779;
CC P49023; Q05209: PTPN12; NbExp=2; IntAct=EBI-702209, EBI-2266035;
CC P49023; Q99942: RNF5; NbExp=6; IntAct=EBI-702209, EBI-348482;
CC P49023; P06931: E6; Xeno; NbExp=3; IntAct=EBI-702209, EBI-7281937;
CC P49023; Q09463: rnf-5; Xeno; NbExp=2; IntAct=EBI-702209, EBI-963421;
CC P49023; Q62417-2: Sorbs1; Xeno; NbExp=8; IntAct=EBI-702209, EBI-7072893;
CC P49023-2; P51451: BLK; NbExp=3; IntAct=EBI-11954250, EBI-2105445;
CC P49023-2; Q9C005: DPY30; NbExp=3; IntAct=EBI-11954250, EBI-744973;
CC P49023-2; P25800: LMO1; NbExp=5; IntAct=EBI-11954250, EBI-8639312;
CC P49023-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-11954250, EBI-11742507;
CC P49023-2; Q9GZM8: NDEL1; NbExp=5; IntAct=EBI-11954250, EBI-928842;
CC P49023-2; Q9NVD7-1: PARVA; NbExp=3; IntAct=EBI-11954250, EBI-15735104;
CC P49023-2; Q8IVE3-3: PLEKHH2; NbExp=3; IntAct=EBI-11954250, EBI-11954248;
CC P49023-2; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-11954250, EBI-12014286;
CC P49023-2; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-11954250, EBI-11955057;
CC P49023-2; Q9P202: WHRN; NbExp=3; IntAct=EBI-11954250, EBI-310886;
CC P49023-2; P07947: YES1; NbExp=3; IntAct=EBI-11954250, EBI-515331;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20489202}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:20489202, ECO:0000269|PubMed:23128389}. Cytoplasm,
CC cell cortex {ECO:0000250|UniProtKB:Q8VI36}. Note=Colocalizes with
CC integrins at the cell periphery. Colocalize with PXN to membrane
CC ruffles and the leading edge of migrating cells (PubMed:23128389).
CC {ECO:0000250, ECO:0000269|PubMed:23128389}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Beta;
CC IsoId=P49023-1; Sequence=Displayed;
CC Name=Alpha;
CC IsoId=P49023-2; Sequence=VSP_003114;
CC Name=Gamma;
CC IsoId=P49023-3; Sequence=VSP_003115;
CC Name=4;
CC IsoId=P49023-4; Sequence=VSP_040483, VSP_003114;
CC -!- PTM: Phosphorylated by MAPK1/ERK2 (By similarity). Phosphorylated on
CC tyrosine residues during integrin-mediated cell adhesion, embryonic
CC development, fibroblast transformation and following stimulation of
CC cells by mitogens. Phosphorylation at Ser-244 by CDK5 reduces its
CC interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during
CC oligodendrocytes (OLs) differentiation. Phosphorylation at Tyr-31 and
CC Tyr-118 by PTK6 promote the activation of RAC1 via CRK/CrKII, thereby
CC promoting migration and invasion. Phosphorylation at Ser-250 by SLK is
CC required for PXN redistribution and cell motility (PubMed:23128389).
CC {ECO:0000250, ECO:0000269|PubMed:11774284, ECO:0000269|PubMed:15572663,
CC ECO:0000269|PubMed:18042622, ECO:0000269|PubMed:23128389}.
CC -!- SIMILARITY: Belongs to the paxillin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PXNID41953ch12q24.html";
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DR EMBL; U14588; AAC50104.1; -; mRNA.
DR EMBL; U87946; AAD00648.1; -; Genomic_DNA.
DR EMBL; U87941; AAD00648.1; JOINED; Genomic_DNA.
DR EMBL; U87942; AAD00648.1; JOINED; Genomic_DNA.
DR EMBL; U87943; AAD00648.1; JOINED; Genomic_DNA.
DR EMBL; U87944; AAD00648.1; JOINED; Genomic_DNA.
DR EMBL; U87945; AAD00648.1; JOINED; Genomic_DNA.
DR EMBL; D86862; BAA18997.1; -; mRNA.
DR EMBL; D86863; BAA18998.1; -; mRNA.
DR EMBL; AK314204; BAG36880.1; -; mRNA.
DR EMBL; BX648777; CAI46024.1; -; mRNA.
DR EMBL; AC004263; AAC05175.1; -; Genomic_DNA.
DR EMBL; BC136787; AAI36788.1; -; mRNA.
DR EMBL; BC136794; AAI36795.1; -; mRNA.
DR EMBL; BC144410; AAI44411.1; -; mRNA.
DR CCDS; CCDS44996.1; -. [P49023-2]
DR CCDS; CCDS44997.1; -. [P49023-1]
DR CCDS; CCDS44998.1; -. [P49023-4]
DR CCDS; CCDS58281.1; -. [P49023-3]
DR PIR; A55933; A55933.
DR RefSeq; NP_001074324.1; NM_001080855.2. [P49023-1]
DR RefSeq; NP_001230685.1; NM_001243756.1. [P49023-3]
DR RefSeq; NP_002850.2; NM_002859.3. [P49023-2]
DR RefSeq; NP_079433.3; NM_025157.4. [P49023-4]
DR RefSeq; XP_016875232.1; XM_017019743.1. [P49023-4]
DR PDB; 1OW6; X-ray; 2.35 A; D/F=262-274.
DR PDB; 1OW7; X-ray; 2.60 A; D/E/F=262-274.
DR PDB; 1OW8; X-ray; 2.85 A; D/F=141-153.
DR PDB; 2K2R; NMR; -; B=3-12.
DR PDB; 2O9V; X-ray; 1.63 A; B=45-54.
DR PDB; 2VZD; X-ray; 2.10 A; C/D=1-20.
DR PDB; 2VZG; X-ray; 1.80 A; A=141-160.
DR PDB; 2VZI; X-ray; 2.20 A; A=262-277.
DR PDB; 3GM1; X-ray; 2.95 A; C/D/E/F=262-274.
DR PDB; 3PY7; X-ray; 2.29 A; A=1-10.
DR PDB; 3RQE; X-ray; 2.80 A; E=2-15.
DR PDB; 3RQF; X-ray; 2.70 A; E=141-153.
DR PDB; 3RQG; X-ray; 2.50 A; E=262-274.
DR PDB; 3U3F; X-ray; 3.10 A; E/F/G/H/I/J=261-277.
DR PDB; 4EDN; X-ray; 2.90 A; K/L/M/N/O/P/Q=1-20.
DR PDB; 4R32; X-ray; 3.70 A; B/C=139-160.
DR PDB; 4XGZ; X-ray; 2.50 A; a/c/e/g/h/j/m/o/q/s/u/w=141-159.
DR PDB; 4XH2; X-ray; 2.00 A; a/c/e/g/h/j=261-275.
DR PDB; 5UWH; X-ray; 2.26 A; D=264-277.
DR PDB; 6IUI; X-ray; 2.60 A; C/D=261-280.
DR PDB; 6PW8; X-ray; 1.95 A; B=141-153.
DR PDB; 6U4M; NMR; -; A=527-591.
DR PDB; 6U4N; NMR; -; B=527-591.
DR PDBsum; 1OW6; -.
DR PDBsum; 1OW7; -.
DR PDBsum; 1OW8; -.
DR PDBsum; 2K2R; -.
DR PDBsum; 2O9V; -.
DR PDBsum; 2VZD; -.
DR PDBsum; 2VZG; -.
DR PDBsum; 2VZI; -.
DR PDBsum; 3GM1; -.
DR PDBsum; 3PY7; -.
DR PDBsum; 3RQE; -.
DR PDBsum; 3RQF; -.
DR PDBsum; 3RQG; -.
DR PDBsum; 3U3F; -.
DR PDBsum; 4EDN; -.
DR PDBsum; 4R32; -.
DR PDBsum; 4XGZ; -.
DR PDBsum; 4XH2; -.
DR PDBsum; 5UWH; -.
DR PDBsum; 6IUI; -.
DR PDBsum; 6PW8; -.
DR PDBsum; 6U4M; -.
DR PDBsum; 6U4N; -.
DR AlphaFoldDB; P49023; -.
DR SMR; P49023; -.
DR BioGRID; 111787; 281.
DR CORUM; P49023; -.
DR DIP; DIP-33851N; -.
DR ELM; P49023; -.
DR IntAct; P49023; 128.
DR MINT; P49023; -.
DR STRING; 9606.ENSP00000267257; -.
DR ChEMBL; CHEMBL5715; -.
DR GlyGen; P49023; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P49023; -.
DR MetOSite; P49023; -.
DR PhosphoSitePlus; P49023; -.
DR BioMuta; PXN; -.
DR DMDM; 317373486; -.
DR EPD; P49023; -.
DR jPOST; P49023; -.
DR MassIVE; P49023; -.
DR MaxQB; P49023; -.
DR PaxDb; P49023; -.
DR PeptideAtlas; P49023; -.
DR PRIDE; P49023; -.
DR ProteomicsDB; 55957; -. [P49023-1]
DR ProteomicsDB; 55958; -. [P49023-2]
DR ProteomicsDB; 55959; -. [P49023-3]
DR ProteomicsDB; 55960; -. [P49023-4]
DR TopDownProteomics; P49023-2; -. [P49023-2]
DR TopDownProteomics; P49023-3; -. [P49023-3]
DR ABCD; P49023; 2 sequenced antibodies.
DR Antibodypedia; 3546; 1669 antibodies from 47 providers.
DR DNASU; 5829; -.
DR Ensembl; ENST00000228307.11; ENSP00000228307.7; ENSG00000089159.17. [P49023-1]
DR Ensembl; ENST00000267257.11; ENSP00000267257.7; ENSG00000089159.17. [P49023-3]
DR Ensembl; ENST00000424649.6; ENSP00000391283.2; ENSG00000089159.17. [P49023-2]
DR Ensembl; ENST00000458477.6; ENSP00000395536.2; ENSG00000089159.17. [P49023-4]
DR GeneID; 5829; -.
DR KEGG; hsa:5829; -.
DR UCSC; uc001txt.4; human. [P49023-1]
DR CTD; 5829; -.
DR DisGeNET; 5829; -.
DR GeneCards; PXN; -.
DR HGNC; HGNC:9718; PXN.
DR HPA; ENSG00000089159; Low tissue specificity.
DR MIM; 602505; gene.
DR neXtProt; NX_P49023; -.
DR OpenTargets; ENSG00000089159; -.
DR PharmGKB; PA34062; -.
DR VEuPathDB; HostDB:ENSG00000089159; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000158897; -.
DR HOGENOM; CLU_001357_1_2_1; -.
DR InParanoid; P49023; -.
DR OrthoDB; 1593918at2759; -.
DR PhylomeDB; P49023; -.
DR TreeFam; TF314113; -.
DR PathwayCommons; P49023; -.
DR Reactome; R-HSA-180292; GAB1 signalosome.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR Reactome; R-HSA-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR Reactome; R-HSA-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR SignaLink; P49023; -.
DR SIGNOR; P49023; -.
DR BioGRID-ORCS; 5829; 170 hits in 1080 CRISPR screens.
DR ChiTaRS; PXN; human.
DR EvolutionaryTrace; P49023; -.
DR GeneWiki; Paxillin; -.
DR GenomeRNAi; 5829; -.
DR Pharos; P49023; Tbio.
DR PRO; PR:P49023; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P49023; protein.
DR Bgee; ENSG00000089159; Expressed in granulocyte and 179 other tissues.
DR ExpressionAtlas; P49023; baseline and differential.
DR Genevisible; P49023; HS.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IMP:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:BHF-UCL.
DR GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038191; F:neuropilin binding; IPI:BHF-UCL.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0017166; F:vinculin binding; IPI:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEP:BHF-UCL.
DR GO; GO:0043542; P:endothelial cell migration; IMP:BHF-UCL.
DR GO; GO:0060396; P:growth hormone receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:BHF-UCL.
DR GO; GO:0007172; P:signal complex assembly; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR InterPro; IPR001904; Paxillin.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24216:SF11; PTHR24216:SF11; 4.
DR Pfam; PF00412; LIM; 4.
DR SMART; SM00132; LIM; 4.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell adhesion;
KW Cell junction; Cytoplasm; Cytoskeleton; LIM domain; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc.
FT CHAIN 1..591
FT /note="Paxillin"
FT /id="PRO_0000075853"
FT DOMAIN 356..415
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 416..473
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 474..533
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 534..591
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 17..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..315
FT /note="Required for binding to PARVA and ILK"
FT /evidence="ECO:0000250|UniProtKB:P49024"
FT REGION 291..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..15
FT /note="LD motif 1"
FT MOTIF 144..156
FT /note="LD motif 2"
FT MOTIF 216..228
FT /note="LD motif 3"
FT MOTIF 265..276
FT /note="LD motif 4"
FT MOTIF 333..345
FT /note="LD motif 5"
FT COMPBIAS 65..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 31
FT /note="Phosphotyrosine; by PTK6"
FT /evidence="ECO:0000269|PubMed:11774284,
FT ECO:0000269|PubMed:15572663"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI36"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 88
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI36"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648"
FT MOD_RES 118
FT /note="Phosphotyrosine; by PTK6"
FT /evidence="ECO:0000269|PubMed:11774284,
FT ECO:0000269|PubMed:15572663"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 132
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI36"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI36"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 181
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11774284"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H76"
FT MOD_RES 244
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000269|PubMed:18042622"
FT MOD_RES 250
FT /note="Phosphoserine; by SLK"
FT /evidence="ECO:0000269|PubMed:23128389"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H76"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H76"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H76"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI36"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..133
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_040483"
FT VAR_SEQ 278..311
FT /note="Missing (in isoform Alpha and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:7534286"
FT /id="VSP_003114"
FT VAR_SEQ 278..311
FT /note="IQGLEQRADGERCWAAGWPRDGGRSSPGGQDEGG -> GSWPLEEVVLLVSI
FT SSSVQEGEKYPHPCAARHRTPSLRSPDQPPPCPQ (in isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:9054445"
FT /id="VSP_003115"
FT VARIANT 73
FT /note="S -> G (in dbSNP:rs4767884)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7534286,
FT ECO:0000269|PubMed:9054445, ECO:0000269|Ref.2"
FT /id="VAR_065099"
FT MUTAGEN 7..8
FT /note="LL->RR: Loss of interaction with PDCD10."
FT /evidence="ECO:0000269|PubMed:20489202"
FT CONFLICT 280
FT /note="G -> D (in Ref. 3; BAA18997)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="P -> L (in Ref. 5; CAI46024)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="F -> S (in Ref. 5; CAI46024)"
FT /evidence="ECO:0000305"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:2VZD"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:2VZG"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:4XH2"
FT TURN 536..538
FT /evidence="ECO:0007829|PDB:6U4M"
FT STRAND 547..551
FT /evidence="ECO:0007829|PDB:6U4M"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:6U4M"
FT TURN 562..564
FT /evidence="ECO:0007829|PDB:6U4M"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:6U4M"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:6U4M"
FT STRAND 579..582
FT /evidence="ECO:0007829|PDB:6U4M"
FT HELIX 583..589
FT /evidence="ECO:0007829|PDB:6U4M"
FT INIT_MET P49023-4:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES P49023-4:2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 591 AA; 64505 MW; ABF6C0BE5939623F CRC64;
MDDLDALLAD LESTTSHISK RPVFLSEETP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG
TILDPLDQWQ PSSSRFIHQQ PQSSSPVYGS SAKTSSVSNP QDSVGSPCSR VGEEEHVYSF
PNKQKSAEPS PTVMSTSLGS NLSELDRLLL ELNAVQHNPP GFPADEANSS PPLPGALSPL
YGVPETNSPL GGKAGPLTKE KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG
EMSSPQRVTS TQQQTRISAS SATRELDELM ASLSDFKIQG LEQRADGERC WAAGWPRDGG
RSSPGGQDEG GFMAQGKTGS SSPPGGPPKP GSQLDSMLGS LQSDLNKLGV ATVAKGVCGA
CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD GQPYCEKDYH NLFSPRCYYC
NGPILDKVVT ALDRTWHPEH FFCAQCGAFF GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA
RAILENYISA LNTLWHPECF VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK
PITGRCITAM AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQNCFLKLF C
