ID PAXI_MOUSE Reviewed; 591 AA. AC Q8VI36; Q3TB62; Q3TZQ6; Q8VI37; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 177. DE RecName: Full=Paxillin; GN Name=Pxn; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA). RC STRAIN=BALB/cJ; TISSUE=Testis; RX PubMed=11825902; DOI=10.1074/jbc.m111639200; RA Chay K.O., Park S.S., Mushinski J.F.; RT "Linkage of caspase-mediated degradation of paxillin to apoptosis in Ba/F3 RT murine pro-B lymphocytes."; RL J. Biol. Chem. 277:14521-14529(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND BETA). RC STRAIN=C57BL/6J, and NOD; TISSUE=Placenta, and Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP INTERACTION WITH PTK2B/PYK2, AND SUBCELLULAR LOCATION. RX PubMed=8940124; DOI=10.1074/jbc.271.49.31222; RA Salgia R., Avraham S., Pisick E., Li J.L., Raja S., Greenfield E.A., RA Sattler M., Avraham H., Griffin J.D.; RT "The related adhesion focal tyrosine kinase forms a complex with paxillin RT in hematopoietic cells."; RL J. Biol. Chem. 271:31222-31226(1996). RN [4] RP PHOSPHORYLATION BY MAPK1/ERK2. RX PubMed=10753946; DOI=10.1074/jbc.275.15.11333; RA Ku H., Meier K.E.; RT "Phosphorylation of paxillin via the ERK mitogen-activated protein kinase RT cascade in EL4 thymoma cells."; RL J. Biol. Chem. 275:11333-11340(2000). RN [5] RP INTERACTION WITH PARVA. RX PubMed=11134073; DOI=10.1083/jcb.151.7.1435; RA Nikolopoulos S.N., Turner C.E.; RT "Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and RT actin and regulates cell adhesion."; RL J. Cell Biol. 151:1435-1448(2000). RN [6] RP INTERACTION WITH NUDT16L1. RX PubMed=11805099; DOI=10.1074/jbc.m110291200; RA Denhez F., Wilcox-Adelman S.A., Baciu P.C., Saoncella S., Lee S., RA French B., Neveu W., Goetinck P.F.; RT "Syndesmos, a syndecan-4 cytoplasmic domain interactor, binds to the focal RT adhesion adaptor proteins paxillin and Hic-5."; RL J. Biol. Chem. 277:12270-12274(2002). RN [7] RP INTERACTION WITH PTK2/FAK1. RX PubMed=11799401; DOI=10.1038/nsb755; RA Hayashi I., Vuori K., Liddington R.C.; RT "The focal adhesion targeting (FAT) region of focal adhesion kinase is a RT four-helix bundle that binds paxillin."; RL Nat. Struct. Biol. 9:101-106(2002). RN [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; TYR-88 AND TYR-118, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; TYR-118; SER-126; RP SER-130; THR-132; SER-137; SER-140; SER-143; SER-272; SER-322 AND SER-340, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [12] RP PHOSPHORYLATION AT TYR-118. RX PubMed=21430700; DOI=10.1038/jid.2011.69; RA Kopecki Z., O'Neill G.M., Arkell R.M., Cowin A.J.; RT "Regulation of focal adhesions by flightless i involves inhibition of RT paxillin phosphorylation via a Rac1-dependent pathway."; RL J. Invest. Dermatol. 131:1450-1459(2011). 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:0000250|UniProtKB:P49023}. 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 (By similarity). Interacts with GIT1 (By similarity). Interacts CC with NUDT16L1/SDOS (PubMed:11805099). Interacts with PTK2/FAK1 CC (PubMed:11799401). Interacts with PTK2B/PYK2 (PubMed:8940124). CC Interacts with ASAP2 (By similarity). Interacts with unphosphorylated CC ITGA4 (By similarity). Interacts with RNF5 (By similarity). Interacts CC with PDCD10 (By similarity). Interacts with NEK3, the interaction is CC prolactin-dependent (By similarity). Interacts with PTK6 (By CC similarity). Interacts with TGFB1I1 (By similarity). Interacts with CC SORBS1 (By similarity). Interacts with PARVB (By similarity). Interacts CC (via LD motif 4) with PARVA/PARVIN (PubMed:11134073). Interacts (via LD CC motif 4) with ILK (By similarity). Interacts (via cytoplasmic domain) CC with CEACAM1; the interaction is phosphotyrosyl-dependent (By CC similarity). Interacts with LIMA1; this complex stabilizes actin CC dynamics (By similarity). Interacts with CD36 (via C-terminus) (By CC similarity). Interacts with TRIM15 (By similarity). CC {ECO:0000250|UniProtKB:P49023, ECO:0000250|UniProtKB:Q66H76, CC ECO:0000269|PubMed:11134073, ECO:0000269|PubMed:11799401, CC ECO:0000269|PubMed:11805099, ECO:0000269|PubMed:8940124}. CC -!- INTERACTION: CC Q8VI36; P11627: L1cam; NbExp=2; IntAct=EBI-983394, EBI-397964; CC Q8VI36; P34152: Ptk2; NbExp=5; IntAct=EBI-983394, EBI-77070; CC Q8VI36; Q64727: Vcl; NbExp=3; IntAct=EBI-983394, EBI-432047; CC Q8VI36; P18031: PTPN1; Xeno; NbExp=2; IntAct=EBI-983394, EBI-968788; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P49023}. Cell junction, focal adhesion CC {ECO:0000250|UniProtKB:P49023}. Cytoplasm, cell cortex CC {ECO:0000269|PubMed:8940124}. Note=Colocalizes with integrins at the CC cell periphery. Colocalizes with PXN to membrane ruffles and the CC leading edge of migrating cells (By similarity). CC {ECO:0000250|UniProtKB:P49023}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Beta; CC IsoId=Q8VI36-1; Sequence=Displayed; CC Name=Alpha; CC IsoId=Q8VI36-2; Sequence=VSP_016357; CC -!- PTM: Phosphorylated by MAPK1/ERK2. Phosphorylated on tyrosine residues CC during integrin-mediated cell adhesion, embryonic development, CC fibroblast transformation and following stimulation of cells by CC mitogens. Phosphorylation at Ser-244 by CDK5 reduces its interaction CC with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during CC oligodendrocytes (OLs) differentiation (By similarity). Phosphorylation CC at Tyr-31 and Tyr-118 by PTK6 promote the activation of RAC1 via CC CRK/CrKII, thereby promoting migration and invasion (By similarity). CC Phosphorylation at Ser-250 by SLK is required for PXN redistribution CC and cell motility (By similarity). {ECO:0000250|UniProtKB:P49023}. CC -!- SIMILARITY: Belongs to the paxillin family. {ECO:0000305}. 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; AF293883; AAL71910.1; -; mRNA. DR EMBL; AF293882; AAL71909.1; -; mRNA. DR EMBL; AK149933; BAE29176.1; -; mRNA. DR EMBL; AK157688; BAE34151.1; -; mRNA. DR EMBL; AK167299; BAE39404.1; -; mRNA. DR EMBL; AK171436; BAE42452.1; -; mRNA. DR CCDS; CCDS19593.1; -. [Q8VI36-2] DR CCDS; CCDS39229.1; -. [Q8VI36-1] DR RefSeq; NP_035353.1; NM_011223.3. [Q8VI36-2] DR RefSeq; NP_598676.2; NM_133915.3. DR PDB; 5W93; X-ray; 2.00 A; D/E/F=1-20. DR PDB; 6JMU; X-ray; 2.00 A; C/D=260-282. DR PDBsum; 5W93; -. DR PDBsum; 6JMU; -. DR AlphaFoldDB; Q8VI36; -. DR SMR; Q8VI36; -. DR BioGRID; 202525; 23. DR CORUM; Q8VI36; -. DR IntAct; Q8VI36; 17. DR MINT; Q8VI36; -. DR STRING; 10090.ENSMUSP00000083709; -. DR GlyGen; Q8VI36; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q8VI36; -. DR PhosphoSitePlus; Q8VI36; -. DR SwissPalm; Q8VI36; -. DR EPD; Q8VI36; -. DR jPOST; Q8VI36; -. DR MaxQB; Q8VI36; -. DR PaxDb; 10090-ENSMUSP00000083709; -. DR PeptideAtlas; Q8VI36; -. DR ProteomicsDB; 287789; -. [Q8VI36-1] DR ProteomicsDB; 287790; -. [Q8VI36-2] DR Pumba; Q8VI36; -. DR Antibodypedia; 3546; 1923 antibodies from 47 providers. DR DNASU; 19303; -. DR Ensembl; ENSMUST00000067268.15; ENSMUSP00000069624.9; ENSMUSG00000029528.20. [Q8VI36-2] DR GeneID; 19303; -. DR KEGG; mmu:19303; -. DR UCSC; uc008zeb.2; mouse. [Q8VI36-2] DR AGR; MGI:108295; -. DR CTD; 5829; -. DR MGI; MGI:108295; Pxn. DR VEuPathDB; HostDB:ENSMUSG00000029528; -. DR eggNOG; KOG1703; Eukaryota. DR GeneTree; ENSGT00940000158897; -. DR InParanoid; Q8VI36; -. DR OrthoDB; 370973at2759; -. DR PhylomeDB; Q8VI36; -. DR Reactome; R-MMU-180292; GAB1 signalosome. DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-MMU-445355; Smooth Muscle Contraction. DR Reactome; R-MMU-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions. DR Reactome; R-MMU-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components. DR Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases. DR BioGRID-ORCS; 19303; 4 hits in 78 CRISPR screens. DR ChiTaRS; Pxn; mouse. DR PRO; PR:Q8VI36; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; Q8VI36; Protein. DR Bgee; ENSMUSG00000029528; Expressed in granulocyte and 255 other cell types or tissues. DR ExpressionAtlas; Q8VI36; baseline and differential. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0031252; C:cell leading edge; IDA:MGI. DR GO; GO:0005911; C:cell-cell junction; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005925; C:focal adhesion; IDA:BHF-UCL. DR GO; GO:0030027; C:lamellipodium; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0001725; C:stress fiber; ISO:MGI. DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI. DR GO; GO:0051435; F:BH4 domain binding; IPI:MGI. DR GO; GO:0005178; F:integrin binding; ISO:MGI. DR GO; GO:0005078; F:MAP-kinase scaffold activity; IDA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0038191; F:neuropilin binding; IPI:BHF-UCL. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0030159; F:signaling receptor complex adaptor activity; TAS:MGI. DR GO; GO:0017166; F:vinculin binding; ISO:MGI. DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IDA:MGI. DR GO; GO:0016477; P:cell migration; IMP:MGI. DR GO; GO:0007010; P:cytoskeleton organization; IMP:MGI. DR GO; GO:0043542; P:endothelial cell migration; ISO:MGI. DR GO; GO:0048041; P:focal adhesion assembly; IDA:MGI. DR GO; GO:0060396; P:growth hormone receptor signaling pathway; ISO:MGI. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:MGI. DR GO; GO:0030032; P:lamellipodium assembly; IDA:MGI. DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL. DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI. DR GO; GO:0008360; P:regulation of cell shape; IMP:MGI. DR GO; GO:1901652; P:response to peptide; ISO:MGI. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:MGI. 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; Q8VI36; MM. 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_0000075854" 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..139 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 156..261 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 289..338 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..139 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..261 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 296..338 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P49023" FT MOD_RES 31 FT /note="Phosphotyrosine; by PTK6" FT /evidence="ECO:0000250|UniProtKB:P49023" FT MOD_RES 83 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:21183079" FT MOD_RES 88 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:19131326" FT MOD_RES 106 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P49023" FT MOD_RES 118 FT /note="Phosphotyrosine; by PTK6" FT /evidence="ECO:0000269|PubMed:21430700, FT ECO:0007744|PubMed:18034455, ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:21183079" FT MOD_RES 119 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P49023" FT MOD_RES 126 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 130 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 132 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 137 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 140 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 143 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 181 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P49023" 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:0000250|UniProtKB:P49023" FT MOD_RES 250 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P49023" 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:21183079" FT MOD_RES 303 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P49023" FT MOD_RES 322 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 332 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q66H76" FT MOD_RES 340 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 533 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P49023" FT VAR_SEQ 278..311 FT /note="Missing (in isoform Alpha)" FT /evidence="ECO:0000303|PubMed:11825902, FT ECO:0000303|PubMed:16141072" FT /id="VSP_016357" FT CONFLICT 71 FT /note="P -> R (in Ref. 2; BAE42452)" FT /evidence="ECO:0000305" FT CONFLICT 212 FT /note="D -> N (in Ref. 2; BAE34151)" FT /evidence="ECO:0000305" FT CONFLICT 294 FT /note="G -> S (in Ref. 2; BAE34151)" FT /evidence="ECO:0000305" FT HELIX 4..9 FT /evidence="ECO:0007829|PDB:5W93" FT HELIX 260..276 FT /evidence="ECO:0007829|PDB:6JMU" SQ SEQUENCE 591 AA; 64476 MW; B41A1892E6F60544 CRC64; MDDLDALLAD LESTTSHISK RPVFLSEEPP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG TVLDPLDQWQ PSGSRYAHQQ PPSPLPVYSS SAKNSSASNT QDGVGSLCSR AGEEEHVYSF PNKQKSAEPS PTVMSSSLGS NLSELDRLLL ELNAVQHSPP GFPADEAESS PPLPGALSPL YGIPENNTPL GGKAGPLVKE KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG EMSSPQRVTS SQQQTRISAS SATRELDELM ASLSDFKMQG LEQRVDGERP WAAGWPPSSR QSSPEGQDEG GFMAQGKTGS SSPPGGLSKP GSQLDSMLGS LQSDLNKLGV ATVAKGVCGA CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD GQPYCEKDYH SLFSPRCYYC NGPILDKVVT ALDRTWHPEH FFCAQCGAFF GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA RAILENYISA LNTLWHPECF VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK PITGRCITAM AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQSCFVKLF C //