STAT3_RAT
ID STAT3_RAT Reviewed; 770 AA.
AC P52631;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Signal transducer and activator of transcription 3;
GN Name=Stat3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8530402; DOI=10.1074/jbc.270.50.29998;
RA Ripperger J.A., Fritz S., Richter K., Hocke G.M., Lottspeich F., Fey G.H.;
RT "Transcription factors Stat3 and Stat5b are present in rat liver nuclei
RT late in an acute phase response and bind interleukin-6 response elements.";
RL J. Biol. Chem. 270:29998-30006(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP INTERACTION WITH CAV2.
RX PubMed=19427337; DOI=10.1016/j.bbamcr.2009.04.015;
RA Kwon H., Jeong K., Hwang E.M., Park J.-Y., Hong S.-G., Choi W.-S., Pak Y.;
RT "Caveolin-2 regulation of STAT3 transcriptional activation in response to
RT insulin.";
RL Biochim. Biophys. Acta 1793:1325-1333(2009).
CC -!- FUNCTION: Signal transducer and transcription activator that mediates
CC cellular responses to interleukins, KITLG/SCF, LEP and other growth
CC factors. Once activated, recruits coactivators, such as NCOA1 or MED1,
CC to the promoter region of the target gene. May mediate cellular
CC responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Upon activation
CC of IL6ST/gp130 signaling by interleukin-6 (IL6), binds to the IL6-
CC responsive elements identified in the promoters of various acute-phase
CC protein genes. Activated by IL31 through IL31RA (By similarity). Acts
CC as a regulator of inflammatory response by regulating differentiation
CC of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells
CC (Treg): deacetylation and oxidation of lysine residues by LOXL3, leads
CC to disrupt STAT3 dimerization and inhibit its transcription activity
CC (By similarity). Involved in cell cycle regulation by inducing the
CC expression of key genes for the progression from G1 to S phase, such as
CC CCND1 (By similarity). Mediates the effects of LEP on melanocortin
CC production, body energy homeostasis and lactation. May play an
CC apoptotic role by transctivating BIRC5 expression under LEP activation
CC (By similarity). Cytoplasmic STAT3 represses macroautophagy by
CC inhibiting EIF2AK2/PKR activity (By similarity). Plays a crucial role
CC in basal beta cell functions, such as regulation of insulin secretion.
CC Plays an important role in host defense in methicillin-resistant
CC S.aureus lung infection by regulating the expression of the
CC antimicrobial lectin REG3G (By similarity).
CC {ECO:0000250|UniProtKB:P40763, ECO:0000250|UniProtKB:P42227}.
CC -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
CC member (at least STAT1). Interacts with IL31RA, NCOA1, PELP1, SIPAR,
CC SOCS7, STATIP1 and TMF1. Interacts with IL23R in presence of IL23.
CC Interacts (via SH2 domain) with NLK. Interacts with ARL2BP; the
CC interaction is enhanced by LIF and JAK1 expression (By similarity).
CC Interacts with KPNA4 and KPNA5; KPNA4 may be the primary mediator of
CC nuclear import (By similarity). Interacts with CAV2; the interaction is
CC increased on insulin-induced tyrosine phosphorylation of CAV2 and leads
CC to STAT3 activation (PubMed:19427337). Interacts with ARL2BP;
CC interaction is enhanced with ARL2. Interacts with NEK6 (By similarity).
CC Binds to CDK9 when activated and nuclear. Interacts with BMX. Interacts
CC with ZIPK/DAPK3. Interacts with PIAS3; the interaction occurs on
CC stimulation by IL6, CNTF or OSM and inhibits the DNA binding activity
CC of STAT3. In prostate cancer cells, interacts with PRKCE and promotes
CC DNA binding activity of STAT3 (By similarity). Interacts with STMN3,
CC antagonizing its microtubule-destabilizing activity (By similarity).
CC Interacts with the 'Lys-129' acetylated form of BIRC5/survivin.
CC Interacts with FER. Interacts (via SH2 domain) with EIF2AK2/PKR (via
CC the kinase catalytic domain) (By similarity). Interacts with FGFR4 (By
CC similarity). Interacts with INPP5F; the interaction is independent of
CC STAT3 Tyr-705 phosphorylation status (By similarity). Interacts with
CC OCAD1 (By similarity). Interacts (unphosphorylated or phosphorylated at
CC Ser-727) with PHB1 (By similarity). Interacts and may form heterodimers
CC with NHLH1 (By similarity). {ECO:0000250|UniProtKB:P40763,
CC ECO:0000250|UniProtKB:P42227, ECO:0000269|PubMed:19427337}.
CC -!- INTERACTION:
CC P52631; O13097: efnb1; Xeno; NbExp=4; IntAct=EBI-10764775, EBI-15667006;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40763}. Nucleus
CC {ECO:0000250|UniProtKB:P40763}. Note=Shuttles between the nucleus and
CC the cytoplasm. Translocated into the nucleus upon tyrosine
CC phosphorylation and dimerization, in response to signaling by activated
CC FGFR1, FGFR2, FGFR3 or FGFR4. Constitutive nuclear presence is
CC independent of tyrosine phosphorylation. Predominantly present in the
CC cytoplasm without stimuli. Upon leukemia inhibitory factor (LIF)
CC stimulation, accumulates in the nucleus. The complex composed of BART
CC and ARL2 plays an important role in the nuclear translocation and
CC retention of STAT3 (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in lung, heart, oviduct, ovary, uterus and
CC kidney (at protein level). Detected in ovary, oviduct, and at lower
CC levels in uterus and lung.
CC -!- PTM: Activated through tyrosine phosphorylation by BMX. Tyrosine
CC phosphorylated in response to IL6, IL11, CNTF, LIF, KITLG/SCF, CSF1,
CC EGF, PDGF, IFN-alpha and OSM. Activated KIT promotes phosphorylation on
CC tyrosine residues and subsequent translocation to the nucleus. Tyrosine
CC phosphorylated in response to constitutively activated FGFR1, FGFR2,
CC FGFR3 and FGFR4. Phosphorylated on serine upon DNA damage, probably by
CC ATM or ATR. Serine phosphorylation is important for the formation of
CC stable DNA-binding STAT3 homodimers and maximal transcriptional
CC activity. ARL2BP may participate in keeping the phosphorylated state of
CC STAT3 within the nucleus. Tyrosine phosphorylated upon stimulation with
CC EGF. Upon LPS challenge, phosphorylated within the nucleus by IRAK1.
CC Phosphorylated on Ser-727 by RPS6KA5 (By similarity). Phosphorylation
CC at Tyr-705 by FER, isoform M2 of PKM (PKM2) or PTK6 leads to an
CC increase of its transcriptional activity. Dephosphorylation on tyrosine
CC residues by PTPN2 negatively regulates IL6/interleukin-6 signaling (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Acetylated on lysine residues by CREBBP. Deacetylation by LOXL3
CC leads to disrupt STAT3 dimerization and inhibit STAT3 transcription
CC activity. Oxidation of lysine residues to allysine on STAT3
CC preferentially takes place on lysine residues that are acetylated.
CC {ECO:0000250|UniProtKB:P40763}.
CC -!- PTM: Some lysine residues are oxidized to allysine by LOXL3, leading to
CC disrupt STAT3 dimerization and inhibit STAT3 transcription activity.
CC Oxidation of lysine residues to allysine on STAT3 preferentially takes
CC place on lysine residues that are acetylated.
CC {ECO:0000250|UniProtKB:P40763}.
CC -!- MISCELLANEOUS: Involved in the gp130-mediated signaling pathway.
CC -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC {ECO:0000305}.
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DR EMBL; X91810; CAA62920.1; -; mRNA.
DR EMBL; BC087025; AAH87025.1; -; mRNA.
DR RefSeq; NP_036879.1; NM_012747.2.
DR AlphaFoldDB; P52631; -.
DR SMR; P52631; -.
DR BioGRID; 247196; 3.
DR CORUM; P52631; -.
DR DIP; DIP-44909N; -.
DR IntAct; P52631; 18.
DR MINT; P52631; -.
DR STRING; 10116.ENSRNOP00000026760; -.
DR ChEMBL; CHEMBL1764933; -.
DR iPTMnet; P52631; -.
DR PhosphoSitePlus; P52631; -.
DR jPOST; P52631; -.
DR PaxDb; P52631; -.
DR PRIDE; P52631; -.
DR Ensembl; ENSRNOT00000026760; ENSRNOP00000026760; ENSRNOG00000019742.
DR GeneID; 25125; -.
DR KEGG; rno:25125; -.
DR CTD; 6774; -.
DR RGD; 3772; Stat3.
DR eggNOG; KOG3667; Eukaryota.
DR GeneTree; ENSGT01050000244905; -.
DR HOGENOM; CLU_014189_3_0_1; -.
DR InParanoid; P52631; -.
DR OMA; RCLWEEN; -.
DR OrthoDB; 327469at2759; -.
DR PhylomeDB; P52631; -.
DR TreeFam; TF318648; -.
DR Reactome; R-RNO-1059683; Interleukin-6 signaling.
DR Reactome; R-RNO-1266695; Interleukin-7 signaling.
DR Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR Reactome; R-RNO-186763; Downstream signal transduction.
DR Reactome; R-RNO-201556; Signaling by ALK.
DR Reactome; R-RNO-6783783; Interleukin-10 signaling.
DR Reactome; R-RNO-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-RNO-8849474; PTK6 Activates STAT3.
DR Reactome; R-RNO-8854691; Interleukin-20 family signaling.
DR Reactome; R-RNO-8875791; MET activates STAT3.
DR Reactome; R-RNO-8983432; Interleukin-15 signaling.
DR Reactome; R-RNO-8984722; Interleukin-35 Signalling.
DR Reactome; R-RNO-8985947; Interleukin-9 signaling.
DR Reactome; R-RNO-9008059; Interleukin-37 signaling.
DR Reactome; R-RNO-9020933; Interleukin-23 signaling.
DR Reactome; R-RNO-9020956; Interleukin-27 signaling.
DR Reactome; R-RNO-9020958; Interleukin-21 signaling.
DR Reactome; R-RNO-9701898; STAT3 nuclear events downstream of ALK signaling.
DR PRO; PR:P52631; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000019742; Expressed in heart and 20 other tissues.
DR Genevisible; P52631; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0031730; F:CCR5 chemokine receptor binding; IPI:RGD.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IPI:RGD.
DR GO; GO:0004879; F:nuclear receptor activity; ISO:RGD.
DR GO; GO:0070878; F:primary miRNA binding; ISO:RGD.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0035591; F:signaling adaptor activity; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0006953; P:acute-phase response; IEP:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0048708; P:astrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:MGI.
DR GO; GO:0032870; P:cellular response to hormone stimulus; ISO:RGD.
DR GO; GO:0097398; P:cellular response to interleukin-17; ISO:RGD.
DR GO; GO:0044320; P:cellular response to leptin stimulus; ISS:UniProtKB.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0042755; P:eating behavior; ISS:UniProtKB.
DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR GO; GO:0001754; P:eye photoreceptor cell differentiation; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0060396; P:growth hormone receptor signaling pathway; ISO:RGD.
DR GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0030522; P:intracellular receptor signaling pathway; ISO:RGD.
DR GO; GO:0033210; P:leptin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045820; P:negative regulation of glycolytic process; ISO:RGD.
DR GO; GO:0010730; P:negative regulation of hydrogen peroxide biosynthetic process; IMP:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
DR GO; GO:2001223; P:negative regulation of neuron migration; ISO:RGD.
DR GO; GO:2000635; P:negative regulation of primary miRNA processing; ISO:RGD.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; ISO:RGD.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; ISO:RGD.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1902728; P:positive regulation of growth factor dependent skeletal muscle satellite cell proliferation; IMP:RGD.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:RGD.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISO:RGD.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IGI:ARUK-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:RGD.
DR GO; GO:1904685; P:positive regulation of metalloendopeptidase activity; ISO:RGD.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IGI:ARUK-UCL.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:RGD.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IDA:SynGO.
DR GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0060019; P:radial glial cell differentiation; ISS:UniProtKB.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0060259; P:regulation of feeding behavior; ISS:UniProtKB.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IMP:RGD.
DR GO; GO:0040014; P:regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0034097; P:response to cytokine; IDA:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0044321; P:response to leptin; ISS:UniProtKB.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0019953; P:sexual reproduction; ISS:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; ISO:RGD.
DR GO; GO:0072540; P:T-helper 17 cell lineage commitment; ISS:UniProtKB.
DR GO; GO:0072538; P:T-helper 17 type immune response; ISO:RGD.
DR GO; GO:0001659; P:temperature homeostasis; ISS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR CDD; cd10374; SH2_STAT3; 1.
DR Gene3D; 1.10.532.10; -; 1.
DR Gene3D; 2.60.40.630; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR001217; STAT.
DR InterPro; IPR035855; STAT3_SH2.
DR InterPro; IPR036535; STAT_N_sf.
DR InterPro; IPR013800; STAT_TF_alpha.
DR InterPro; IPR015988; STAT_TF_coiled-coil.
DR InterPro; IPR013801; STAT_TF_DNA-bd.
DR InterPro; IPR012345; STAT_TF_DNA-bd_N.
DR InterPro; IPR013799; STAT_TF_prot_interaction.
DR PANTHER; PTHR11801; PTHR11801; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF01017; STAT_alpha; 1.
DR Pfam; PF02864; STAT_bind; 1.
DR Pfam; PF02865; STAT_int; 1.
DR SMART; SM00964; STAT_int; 1.
DR SUPFAM; SSF47655; SSF47655; 1.
DR SUPFAM; SSF48092; SSF48092; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; SH2 domain; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT CHAIN 2..770
FT /note="Signal transducer and activator of transcription 3"
FT /id="PRO_0000182419"
FT DOMAIN 580..670
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT MOTIF 150..162
FT /note="Essential for nuclear import"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 601
FT /note="Allysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 601
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 615
FT /note="Allysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 615
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 631
FT /note="Allysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 631
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 685
FT /note="Allysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 685
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 705
FT /note="Phosphotyrosine; by FER and PTK6"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 707
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 714
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 727
FT /note="Phosphoserine; by DYRK2, NLK, NEK6, IRAK1, RPS6KA5,
FT ZIPK/DAPK3 and PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:P40763"
SQ SEQUENCE 770 AA; 88040 MW; D74A0C76954754ED CRC64;
MAQWNQLQQL DTRYLEQLHQ LYSDSFPMEL RQFLAPWIES QDWAYAASKE SHATLVFHNL
LGEIDQQYSR FLQESNVLYQ HNLRRIKQFL QSRYLEKPME IARIVARCLW EESRLLQTAA
TAAQQGGQAN HPTAAVVTEK QQMLEQHLQD VRKRVQDLEQ KMKVVENLQD DFDFNYKTLK
SQGDMQDLNG NNQSVTRQKM QQLEQMLTAL DQMRRSIVSE LAGLLSAMEY VQKTLTDEEL
ADWKRRQQIA CIGGPPNICL DRLENWITSL AESQLQTRQQ IKKLEELQQK VSYKGDPIVQ
HRPMLEERIV DLFRNLMKSA FVVERQPCMP MHPDRPLVIK TGVQFTTKVR LLVKFPELNY
QLKIKVCIDK DSGDVAALRG SRKFNILGTN TKVMNMEESN NGSLSAEFKH LTLREQRCGN
GGRANCDASL IVTEELHLIT FETEVYHQGL KIDLETHSLP VVVISNICQM PNAWASILWY
NMLTNNPKNV NFFTKPPIGT WDQVAEVLSW QFSSTTKRGL SIEQLTTLAE KLLGPGVNYS
GCQITWAKFC KENMAGKGFS FWVWLDNIID LVKKYILALW NEGYIMGFIS KERERAILST
KPPGTFLLRF SESSKEGGVT FTWVEKDISG KTQIQSVEPY TKQQLNNMSF AEIIMGYKIM
DATNILVSPL VYLYPDIPKE EAFGKYCRPE SQEHPEADPG SAAPYLKTKF ICVTPTTCSN
TIDLPMSPRT LDSLMQFGNN GEGAEPSAGG QFESLTFDMD LTSECATSPM
