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 27-MAR-2024, entry version 236. 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 FUNCTION, INTERACTION WITH TRIM15, AND SUBCELLULAR LOCATION. RX PubMed=25015296; DOI=10.1242/jcs.143537; RA Uchil P.D., Pawliczek T., Reynolds T.D., Ding S., Hinz A., Munro J.B., RA Huang F., Floyd R.W., Yang H., Hamilton W.L., Bewersdorf J., Xiong Y., RA Calderwood D.A., Mothes W.; RT "TRIM15 is a focal adhesion protein that regulates focal adhesion RT disassembly."; RL J. Cell Sci. 127:3928-3942(2014). RN [35] 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 [36] 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 [37] 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 [38] 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 [39] 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 [40] 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 [41] 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 [42] 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 Recruits other proteins such as TRIM15 to focal adhesion. CC {ECO:0000269|PubMed:25015296}. 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). Interacts with TRIM15 CC (PubMed:25015296). {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:25015296, 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=5; IntAct=EBI-702209, EBI-703044; 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, CC ECO:0000269|PubMed:25015296}. Cytoplasm, cell cortex CC {ECO:0000250|UniProtKB:Q8VI36}. Note=Colocalizes with integrins at the CC cell periphery. Colocalize with PXN to membrane ruffles and the leading CC edge of migrating cells (PubMed:23128389). {ECO:0000250, CC 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="https://atlasgeneticsoncology.org/gene/41953/PXN"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. 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 PDB; 7QB0; NMR; -; A=414-533. 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 PDBsum; 7QB0; -. DR AlphaFoldDB; P49023; -. DR SMR; P49023; -. DR BioGRID; 111787; 316. DR CORUM; P49023; -. DR DIP; DIP-33851N; -. DR ELM; P49023; -. DR IntAct; P49023; 131. DR MINT; P49023; -. DR STRING; 9606.ENSP00000267257; -. DR ChEMBL; CHEMBL5715; -. DR GlyCosmos; P49023; 2 sites, 1 glycan. DR GlyGen; P49023; 5 sites, 1 O-linked glycan (5 sites). DR iPTMnet; P49023; -. DR MetOSite; P49023; -. DR PhosphoSitePlus; P49023; -. DR SwissPalm; P49023; -. DR BioMuta; PXN; -. DR DMDM; 317373486; -. DR EPD; P49023; -. DR jPOST; P49023; -. DR MassIVE; P49023; -. DR MaxQB; P49023; -. DR PaxDb; 9606-ENSP00000267257; -. DR PeptideAtlas; P49023; -. DR ProteomicsDB; 55957; -. [P49023-1] DR ProteomicsDB; 55958; -. [P49023-2] DR ProteomicsDB; 55959; -. [P49023-3] DR ProteomicsDB; 55960; -. [P49023-4] DR Pumba; P49023; -. DR TopDownProteomics; P49023-2; -. [P49023-2] DR TopDownProteomics; P49023-3; -. [P49023-3] DR ABCD; P49023; 2 sequenced antibodies. DR Antibodypedia; 3546; 1923 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 AGR; HGNC:9718; -. 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; 370973at2759; -. 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; 174 hits in 1158 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 181 other cell types or tissues. DR ExpressionAtlas; P49023; baseline and differential. 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:HPA. 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:0017166; F:vinculin binding; IPI:UniProtKB. DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc. DR GO; GO:0016477; P:cell migration; IMP:BHF-UCL. 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 CDD; cd09336; LIM1_Paxillin_like; 1. DR CDD; cd09407; LIM2_Paxillin; 1. DR CDD; cd09338; LIM3_Paxillin_like; 1. DR CDD; cd09411; LIM4_Paxillin; 1. DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4. DR InterPro; IPR047072; Paxillin_Lim_dom2. DR InterPro; IPR001904; Paxillin_Lim_dom4. DR InterPro; IPR047075; Paxillin_TGFB1I1_LIM_dom1. DR InterPro; IPR001781; Znf_LIM. DR PANTHER; PTHR24216:SF11; PAXILLIN; 1. DR PANTHER; PTHR24216; PAXILLIN-RELATED; 1. DR Pfam; PF00412; LIM; 4. DR Pfam; PF03535; Paxillin; 1. DR PRINTS; PR00832; PAXILLIN. DR SMART; SM00132; LIM; 4. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 5. DR PROSITE; PS00478; LIM_DOMAIN_1; 4. DR PROSITE; PS50023; LIM_DOMAIN_2; 4. DR Genevisible; P49023; HS. 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 418..421 FT /evidence="ECO:0007829|PDB:7QB0" FT STRAND 429..431 FT /evidence="ECO:0007829|PDB:7QB0" FT STRAND 434..436 FT /evidence="ECO:0007829|PDB:7QB0" FT STRAND 438..440 FT /evidence="ECO:0007829|PDB:7QB0" FT STRAND 444..446 FT /evidence="ECO:0007829|PDB:7QB0" FT STRAND 456..458 FT /evidence="ECO:0007829|PDB:7QB0" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:7QB0" FT HELIX 465..472 FT /evidence="ECO:0007829|PDB:7QB0" FT STRAND 477..479 FT /evidence="ECO:0007829|PDB:7QB0" FT STRAND 488..490 FT /evidence="ECO:0007829|PDB:7QB0" FT STRAND 493..495 FT /evidence="ECO:0007829|PDB:7QB0" FT STRAND 497..499 FT /evidence="ECO:0007829|PDB:7QB0" FT TURN 503..505 FT /evidence="ECO:0007829|PDB:7QB0" FT STRAND 515..517 FT /evidence="ECO:0007829|PDB:7QB0" FT STRAND 520..522 FT /evidence="ECO:0007829|PDB:7QB0" FT HELIX 524..532 FT /evidence="ECO:0007829|PDB:7QB0" 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 //