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, Pancreas,
RC 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}.
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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 Genevisible; Q8VI36; MM.
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.
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
//
