ID PGFRB_RAT Reviewed; 1097 AA. AC Q05030; Q8R406; Q925F7; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2003, sequence version 2. DT 27-MAR-2024, entry version 199. DE RecName: Full=Platelet-derived growth factor receptor beta; DE Short=PDGF-R-beta; DE Short=PDGFR-beta; DE EC=2.7.10.1; DE AltName: Full=Beta platelet-derived growth factor receptor; DE AltName: Full=Beta-type platelet-derived growth factor receptor; DE AltName: Full=CD140 antigen-like family member B; DE AltName: Full=Platelet-derived growth factor receptor 1; DE Short=PDGFR-1; DE AltName: CD_antigen=CD140b; DE Flags: Precursor; GN Name=Pdgfrb; Synonyms=Pdgfr, Pdgfr1; 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 STRAIN=Sprague-Dawley; RA Wang Y., Culty M.; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-533. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RX PubMed=8318539; DOI=10.1016/0167-4781(93)90127-y; RA Herren B., Weyer K.A., Rouge M., Loetscher P., Pech M.; RT "Conservation in sequence and affinity of human and rodent PDGF ligands and RT receptors."; RL Biochim. Biophys. Acta 1173:294-302(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 528-1090. RC STRAIN=Wistar; RX PubMed=11346654; DOI=10.1074/jbc.m102995200; RA Okuyama H., Shimahara Y., Kawada N., Seki S., Kristensen D.B., RA Yoshizato K., Uyama N., Yamaoka Y.; RT "Regulation of cell growth by redox-mediated extracellular proteolysis of RT platelet-derived growth factor receptor beta."; RL J. Biol. Chem. 276:28274-28280(2001). CC -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor CC for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA CC and PDGFB, and plays an essential role in the regulation of embryonic CC development, cell proliferation, survival, differentiation, chemotaxis CC and migration. Plays an essential role in blood vessel development by CC promoting proliferation, migration and recruitment of pericytes and CC smooth muscle cells to endothelial cells. Plays a role in the migration CC of vascular smooth muscle cells and the formation of neointima at CC vascular injury sites. Required for normal development of the CC cardiovascular system. Required for normal recruitment of pericytes CC (mesangial cells) in the kidney glomerulus, and for normal formation of CC a branched network of capillaries in kidney glomeruli. Promotes CC rearrangement of the actin cytoskeleton and the formation of membrane CC ruffles. Binding of its cognate ligands - homodimeric PDGFB, CC heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to CC the activation of several signaling cascades; the response depends on CC the nature of the bound ligand and is modulated by the formation of CC heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, CC PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the CC production of the cellular signaling molecules diacylglycerol and CC inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the CC activation of protein kinase C. Phosphorylation of PIK3R1, the CC regulatory subunit of phosphatidylinositol 3-kinase, leads to the CC activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or CC of the C-terminus of PTPN11, creates a binding site for GRB2, resulting CC in the activation of HRAS, RAF1 and down-stream MAP kinases, including CC MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation CC of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and CC STAM. Receptor signaling is down-regulated by protein phosphatases that CC dephosphorylate the receptor and its down-stream effectors, and by CC rapid internalization of the activated receptor (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; CC -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence CC of bound ligand. Binding of PDGFB and/or PDGFD leads to dimerization CC and activation by autophosphorylation on tyrosine residues (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with homodimeric PDGFB and PDGFD, and with CC heterodimers formed by PDGFA and PDGFB. May also interact with CC homodimeric PDGFC. Monomer in the absence of bound ligand. Interaction CC with homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or CC homodimeric PDGFD, leads to receptor dimerization, where both PDGFRA CC homodimers and heterodimers with PDGFRB are observed. Interacts with CC SH2B2/APS. Interacts directly (tyrosine phosphorylated) with SHB. CC Interacts (tyrosine phosphorylated) with PIK3R1 and RASA1. Interacts CC (tyrosine phosphorylated) with CBL. Interacts (tyrosine phosphorylated) CC with SRC and SRC family kinases. Interacts (tyrosine phosphorylated) CC with PIK3C2B, maybe indirectly. Interacts (tyrosine phosphorylated) CC with SHC1, GRB7, GRB10 and NCK1. Interaction with GRB2 is mediated by CC SHC1. Interacts (via C-terminus) with NHERF1 (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I CC membrane protein {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. CC Lysosome lumen {ECO:0000250}. Note=After ligand binding, the CC autophosphorylated receptor is ubiquitinated and internalized, leading CC to its degradation. {ECO:0000250}. CC -!- PTM: N-glycosylated. {ECO:0000250}. CC -!- PTM: Ubiquitinated. After autophosphorylation, the receptor is CC polyubiquitinated, leading to its degradation (By similarity). CC {ECO:0000250}. CC -!- PTM: Autophosphorylated on tyrosine residues upon ligand binding. CC Autophosphorylation occurs in trans, i.e. one subunit of the dimeric CC receptor phosphorylates tyrosine residues on the other subunit. CC Phosphorylation at Tyr-578, and to a lesser degree, Tyr-580 is CC important for interaction with SRC. Phosphorylation at Tyr-715 is CC important for interaction with GRB2. Phosphorylation at Tyr-739 and CC Tyr-750 is important for interaction with PIK3R1. Phosphorylation at CC Tyr-750 is important for interaction with NCK1. Phosphorylation at Tyr- CC 770 and Tyr-856 is important for interaction with RASA1/GAP. CC Phosphorylation at Tyr-856 is important for efficient phosphorylation CC of PLCG1 and PTPN11, resulting in increased phosphorylation of AKT1, CC MAPK1/ERK2 and/or MAPK3/ERK1, PDCD6IP/ALIX and STAM, and in increased CC cell proliferation. Phosphorylation at Tyr-1008 is important for CC interaction with PTPN11. Phosphorylation at Tyr-1008 and Tyr-1020 is CC important for interaction with PLCG1. Dephosphorylated by PTPRJ at Tyr- CC 750, Tyr-856, Tyr-1008 and Tyr-1020. Dephosphorylated by PTPN2 at Tyr- CC 578 and Tyr-1020 (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU00159}. 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; AY090783; AAM09098.1; -; mRNA. DR EMBL; Z14119; CAA78489.1; -; mRNA. DR EMBL; AF359356; AAK43716.1; -; mRNA. DR PIR; S33766; S33766. DR RefSeq; NP_113713.1; NM_031525.1. DR RefSeq; XP_006254851.1; XM_006254789.3. DR AlphaFoldDB; Q05030; -. DR SMR; Q05030; -. DR BioGRID; 246767; 2. DR IntAct; Q05030; 2. DR MINT; Q05030; -. DR STRING; 10116.ENSRNOP00000060534; -. DR BindingDB; Q05030; -. DR ChEMBL; CHEMBL4125; -. DR GlyCosmos; Q05030; 11 sites, No reported glycans. DR GlyGen; Q05030; 11 sites. DR iPTMnet; Q05030; -. DR PhosphoSitePlus; Q05030; -. DR jPOST; Q05030; -. DR PaxDb; 10116-ENSRNOP00000060534; -. DR ABCD; Q05030; 1 sequenced antibody. DR GeneID; 24629; -. DR KEGG; rno:24629; -. DR UCSC; RGD:3285; rat. DR AGR; RGD:3285; -. DR CTD; 5159; -. DR RGD; 3285; Pdgfrb. DR VEuPathDB; HostDB:ENSRNOG00000018461; -. DR eggNOG; KOG0200; Eukaryota. DR HOGENOM; CLU_000288_49_0_1; -. DR InParanoid; Q05030; -. DR OrthoDB; 1614410at2759; -. DR PhylomeDB; Q05030; -. DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling. DR Reactome; R-RNO-186763; Downstream signal transduction. DR Reactome; R-RNO-186797; Signaling by PDGF. DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade. DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR PRO; PR:Q05030; -. DR Proteomes; UP000002494; Chromosome 18. DR Bgee; ENSRNOG00000018461; Expressed in ovary and 18 other cell types or tissues. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0009986; C:cell surface; IDA:RGD. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0001726; C:ruffle; ISO:RGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0019899; F:enzyme binding; ISO:RGD. DR GO; GO:0016301; F:kinase activity; ISO:RGD. DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:RGD. DR GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; ISS:UniProtKB. DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:RGD. DR GO; GO:0005017; F:platelet-derived growth factor receptor activity; IDA:RGD. DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISO:RGD. DR GO; GO:0004672; F:protein kinase activity; ISO:RGD. DR GO; GO:0019901; F:protein kinase binding; ISO:RGD. DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD. DR GO; GO:0038085; F:vascular endothelial growth factor binding; ISO:RGD. DR GO; GO:0030325; P:adrenal gland development; ISO:RGD. DR GO; GO:0035909; P:aorta morphogenesis; ISO:RGD. DR GO; GO:0001568; P:blood vessel development; ISO:RGD. DR GO; GO:0055003; P:cardiac myofibril assembly; ISS:UniProtKB. DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB. DR GO; GO:0060981; P:cell migration involved in coronary angiogenesis; ISS:UniProtKB. DR GO; GO:0035441; P:cell migration involved in vasculogenesis; ISS:UniProtKB. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:RGD. DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISO:RGD. DR GO; GO:0048568; P:embryonic organ development; ISO:RGD. DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IMP:RGD. DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD. DR GO; GO:0048839; P:inner ear development; IEP:RGD. DR GO; GO:0035556; P:intracellular signal transduction; IMP:RGD. DR GO; GO:0001822; P:kidney development; ISO:RGD. DR GO; GO:0060437; P:lung growth; IMP:RGD. DR GO; GO:0008584; P:male gonad development; IEP:RGD. DR GO; GO:0072278; P:metanephric comma-shaped body morphogenesis; IEP:UniProtKB. DR GO; GO:0072277; P:metanephric glomerular capillary formation; ISS:UniProtKB. DR GO; GO:0072262; P:metanephric glomerular mesangial cell proliferation involved in metanephros development; ISS:UniProtKB. DR GO; GO:0072223; P:metanephric glomerular mesangium development; ISO:RGD. DR GO; GO:0072275; P:metanephric glomerulus morphogenesis; IEP:UniProtKB. DR GO; GO:0035789; P:metanephric mesenchymal cell migration; IDA:UniProtKB. DR GO; GO:0072075; P:metanephric mesenchyme development; IEP:UniProtKB. DR GO; GO:0072284; P:metanephric S-shaped body morphogenesis; IEP:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD. DR GO; GO:0006807; P:nitrogen compound metabolic process; ISO:RGD. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB. DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB. DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISO:RGD. DR GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; ISO:RGD. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD. DR GO; GO:0090280; P:positive regulation of calcium ion import; ISS:UniProtKB. DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; ISS:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD. DR GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; ISO:RGD. DR GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB. DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IMP:RGD. DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:RGD. DR GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; IMP:RGD. DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB. DR GO; GO:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; ISS:UniProtKB. DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISS:UniProtKB. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB. DR GO; GO:0010863; P:positive regulation of phospholipase C activity; ISS:UniProtKB. DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISS:UniProtKB. DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:RGD. DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISS:UniProtKB. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB. DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD. DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:RGD. DR GO; GO:0106096; P:response to ceramide; ISO:RGD. DR GO; GO:0032355; P:response to estradiol; IEP:RGD. DR GO; GO:0043627; P:response to estrogen; IEP:RGD. DR GO; GO:0034405; P:response to fluid shear stress; IEP:RGD. DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD. DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD. DR GO; GO:0033993; P:response to lipid; IEP:RGD. DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD. DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD. DR GO; GO:0009636; P:response to toxic substance; IEP:RGD. DR GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:UniProtKB. DR GO; GO:0097178; P:ruffle assembly; ISO:RGD. DR GO; GO:0007165; P:signal transduction; ISO:RGD. DR GO; GO:0048705; P:skeletal system morphogenesis; ISO:RGD. DR GO; GO:0071670; P:smooth muscle cell chemotaxis; ISO:RGD. DR GO; GO:0048745; P:smooth muscle tissue development; ISO:RGD. DR GO; GO:0001894; P:tissue homeostasis; ISO:RGD. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central. DR CDD; cd00096; Ig; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 5. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR013151; Immunoglobulin. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR027288; PGFRB. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR InterPro; IPR001824; Tyr_kinase_rcpt_3_CS. DR PANTHER; PTHR24416:SF53; PLATELET-DERIVED GROWTH FACTOR RECEPTOR BETA; 1. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR Pfam; PF07679; I-set; 1. DR Pfam; PF00047; ig; 1. DR Pfam; PF13927; Ig_3; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR PIRSF; PIRSF500948; Beta-PDGF_receptor; 1. DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1. DR PRINTS; PR01832; VEGFRECEPTOR. DR SMART; SM00409; IG; 3. DR SMART; SM00408; IGc2; 3. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF48726; Immunoglobulin; 4. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50835; IG_LIKE; 3. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1. DR Genevisible; Q05030; RN. PE 2: Evidence at transcript level; KW ATP-binding; Cell membrane; Chemotaxis; Cytoplasmic vesicle; KW Developmental protein; Disulfide bond; Glycoprotein; Immunoglobulin domain; KW Kinase; Lysosome; Membrane; Nucleotide-binding; Phosphoprotein; Receptor; KW Reference proteome; Repeat; Signal; Transferase; Transmembrane; KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation. FT SIGNAL 1..31 FT /evidence="ECO:0000255" FT CHAIN 32..1097 FT /note="Platelet-derived growth factor receptor beta" FT /id="PRO_0000016759" FT TOPO_DOM 32..531 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 532..552 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 553..1097 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 32..119 FT /note="Ig-like C2-type 1" FT DOMAIN 128..209 FT /note="Ig-like C2-type 2" FT DOMAIN 213..308 FT /note="Ig-like C2-type 3" FT DOMAIN 415..523 FT /note="Ig-like C2-type 4" FT DOMAIN 599..961 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1016..1097 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1040..1063 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 825 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 605..613 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 633 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 561 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P09619" FT MOD_RES 578 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P09619" FT MOD_RES 580 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P09619" FT MOD_RES 685 FT /note="Phosphotyrosine; by ABL1 and ABL2" FT /evidence="ECO:0000250|UniProtKB:P05622" FT MOD_RES 715 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P09619" FT MOD_RES 739 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P09619" FT MOD_RES 750 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P09619" FT MOD_RES 762 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P09619" FT MOD_RES 770 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P09619" FT MOD_RES 774 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P09619" FT MOD_RES 777 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P09619" FT MOD_RES 856 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P09619" FT MOD_RES 933 FT /note="Phosphotyrosine; by ABL1 and ABL2" FT /evidence="ECO:0000250|UniProtKB:P05622" FT MOD_RES 969 FT /note="Phosphotyrosine; by ABL1 and ABL2" FT /evidence="ECO:0000250|UniProtKB:P05622" FT MOD_RES 1008 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P09619" FT MOD_RES 1020 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P09619" FT CARBOHYD 44 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 88 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 102 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 214 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 291 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 306 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 353 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 370 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 444 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 467 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 478 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 53..99 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 148..189 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 234..290 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 435..507 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" SQ SEQUENCE 1097 AA; 122828 MW; 5E6540FA0C5CF22B CRC64; MGLPEVMPAS VLRGQLLLFV LLLLGPQISQ GLVITPPGPE FVLNISSTFV LTCSSSAPVM WEQMSQVPWQ EAAMNQDGTF SSVLTLTNVT GGDTGEYFCV YNNSLGPELS ERKRIYIFVP DPTMGFLPMD SEDLFIFVTD VTETTIPCRV TDPQLEVTLH EKKVDIPLHV PYDHQRGFIG TFEDKTYICK TTIGDREVDS DTYYVYSLQV SSINVSVNAV QTVVRQGESI TIRCIVMGND VVNFQWTYPR MKSGRLVEPV TDYLFGVPSR IGSILHIPTA ELSDSGTYTC NVSVSVNDHG DEKAINVTVI ENGYVRLLET LEDVQIAELH RSRTLQVVFE AYPTPSVLWF KDNRTLGDSS AGELVLSTRN VSETRYVSEL TLVRVKVSEA GYYTMRAFHA DDQVQLSFKL QVNVPVRVLE LSESHPANGE QILRCRGRGM PQPNVTWSTC RDLKRCPRKL SPTPLGNSSK EESQLETNVT FWEEDQEYEV VSTLRLRHVD QPLSVRCMLQ NSMGRDSQEV TVVPHSLPFK VVVISAILAL VVLTVISLII LIMLWQRKPR YEIRWKVIES VSSDGHEYIY VDPVQLPYDS TWELPRDQLV LGRTLGSGAF GQVVEATAHG LSHSQATMKV AVKMLKSTAR SSEKQALMSE LKIMSHLGPH LNVVNLLGAC TKGGPIYIIT EYCRYGDLVD YLHRNKHTFL QRHSNKHCPP STELYSNALP VGLSLPSHLN LTGESDGGYM DMSKDESVDY VPMLDMKGHI KYADIESSSY MAPYDNYVPS APERTYRATL INDSPVLSYT DLVGFSYQVA NGMEFLASKN CVHRDLAARN VLICEGKLVK ICDFGLARDI MRDSNYISKG STFLPLKWMA PESIFNSLYT TLSDVWSFGI LLWEIFTLGG TPYPELPMND QFYNAIKRGY RMAQPAHASD EIYEIMQKCW EEKFETRPPF SQLVLLLERL LGEGYKKKYQ QVDEEFLRSD HPAILRSQAR LPGLHSLRSP LDTSSVLYTA VQPNETDNDY IIPLPDPKPD AADEGLLEGS PSLASSTLNE VNTSSTISCD SPLELQEEPQ AEPEAQLEQP QDSGCPGPLA EAEDSFL //