##gff-version 3 P05230 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03968 P05230 UniProtKB Propeptide 2 15 . . . ID=PRO_0000008907 P05230 UniProtKB Chain 16 155 . . . ID=PRO_0000008908;Note=Fibroblast growth factor 1 P05230 UniProtKB Region 127 143 . . . Note=Heparin-binding P05230 UniProtKB Motif 24 27 . . . Note=Nuclear localization signal P05230 UniProtKB Binding site 33 33 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11069186,ECO:0000269|PubMed:9655399;Dbxref=PMID:11069186,PMID:9655399 P05230 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03968 P05230 UniProtKB Alternative sequence 57 60 . . . ID=VSP_036536;Note=In isoform 2. IQLQ->TDTK;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7504343;Dbxref=PMID:7504343 P05230 UniProtKB Alternative sequence 61 155 . . . ID=VSP_036537;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7504343;Dbxref=PMID:7504343 P05230 UniProtKB Natural variant 21 21 . . . ID=VAR_021357;Note=G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.8;Dbxref=dbSNP:rs17223632 P05230 UniProtKB Mutagenesis 24 27 . . . Note=Loss of nuclear import leading to loss of phosphorylation by PKC/PRKCD. KKPK->AAPA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22321063;Dbxref=PMID:22321063 P05230 UniProtKB Mutagenesis 33 33 . . . Note=No effect on integrin-binding. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18441324;Dbxref=PMID:18441324 P05230 UniProtKB Mutagenesis 50 50 . . . Note=Dominant-negative mutant. Defective in integrin-binding and in ternary complex formation with integrin and FGFR1. No effect on heparin- and FGFR1-binding. Defective in inducing FGF1 signaling%2C cell proliferation and cell migration. Defective in inducing angiogenesis%2C and suppression of angiogenesis in different in vitro and in vivo angiogenesis models. R->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18441324,ECO:0000269|PubMed:20422052,ECO:0000269|PubMed:23469107;Dbxref=PMID:18441324,PMID:20422052,PMID:23469107 P05230 UniProtKB Mutagenesis 102 102 . . . Note=No effect on integrin-binding. No effect on integrin- and heparin-binding%2C loss of FGFR1-binding%2C defective in inducing FGF1 signaling%2C cell proliferation and cell migration%3B when associated with A-109 and A-110. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18441324;Dbxref=PMID:18441324 P05230 UniProtKB Mutagenesis 109 109 . . . Note=No effect on integrin- and heparin-binding%2C loss of FGFR1-binding%2C defective in inducing FGF1 signaling%2C cell proliferation and cell migration%3B when associated with A-102 and A-110. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18441324;Dbxref=PMID:18441324 P05230 UniProtKB Mutagenesis 110 110 . . . Note=No effect on integrin-binding. No effect on integrin- and heparin-binding%2C loss of FGFR1-binding%2C defective in inducing FGF1 signaling%2C cell proliferation and cell migration%3B when associated with A-102 and A-109. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18441324;Dbxref=PMID:18441324 P05230 UniProtKB Mutagenesis 114 114 . . . Note=Decrease in LRRC59-binding. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11964394;Dbxref=PMID:11964394 P05230 UniProtKB Mutagenesis 127 127 . . . Note=Reduced integrin-binding%3B when associated with E-128. Defective in integrin-%2C heparin- and FGFR1-binding%2C and defective in inducing FGF1 signaling%2C cell proliferation and cell migration%3B when associated with E-128%3B E-133 and E-134. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18441324;Dbxref=PMID:18441324 P05230 UniProtKB Mutagenesis 128 128 . . . Note=Reduced integrin-binding%3B when associated with E-127. Defective in integrin-%2C heparin- and FGFR1-binding%2C and defective in inducing FGF1 signaling%2C cell proliferation and cell migration%3B when associated with E-127%3B E-133 and E-134. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18441324;Dbxref=PMID:18441324 P05230 UniProtKB Mutagenesis 131 131 . . . Note=Decrease in LRRC59-binding. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11964394;Dbxref=PMID:11964394 P05230 UniProtKB Mutagenesis 131 131 . . . Note=Decrease in LRRC59-binding. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11964394;Dbxref=PMID:11964394 P05230 UniProtKB Mutagenesis 133 133 . . . Note=Loss of LRRC59-binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11964394;Dbxref=PMID:11964394 P05230 UniProtKB Mutagenesis 133 133 . . . Note=Loss of CSNK2A-%2C CSNK2B- and LRRC59-binding. Reduced integrin-binding%3B when associated with E-134. Defective in integrin-%2C heparin- and FGFR1-binding%2C and defective in inducing FGF1 signaling%2C cell proliferation and cell migration%3B when associated with E-128%3B E-133 and E-134. K->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11964394,ECO:0000269|PubMed:18441324;Dbxref=PMID:11964394,PMID:18441324 P05230 UniProtKB Mutagenesis 133 133 . . . Note=No effect on LRRC59-binding. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11964394;Dbxref=PMID:11964394 P05230 UniProtKB Mutagenesis 134 134 . . . Note=Reduced integrin-binding%3B when associated with E-133. Defective in integrin-%2C heparin- and FGFR1-binding%2C and defective in inducing FGF1 signaling%2C cell proliferation and cell migration%3B when associated with E-127%3B E-128 and E-133. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18441324;Dbxref=PMID:18441324 P05230 UniProtKB Turn 11 13 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OJM P05230 UniProtKB Beta strand 23 25 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Beta strand 27 31 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Turn 32 35 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Beta strand 36 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Turn 42 44 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DZC P05230 UniProtKB Beta strand 46 49 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Helix 55 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3B9U P05230 UniProtKB Beta strand 59 65 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Beta strand 68 73 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Turn 74 76 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Beta strand 79 82 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Beta strand 84 86 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OJ2 P05230 UniProtKB Beta strand 88 93 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Beta strand 100 105 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Turn 106 108 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Beta strand 109 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Helix 118 120 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Beta strand 123 126 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O3Q P05230 UniProtKB Beta strand 130 132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4QC4 P05230 UniProtKB Helix 135 137 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8 P05230 UniProtKB Turn 138 141 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2K43 P05230 UniProtKB Helix 143 145 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3B9U P05230 UniProtKB Beta strand 147 151 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1RG8