Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008083 | molecular_function | growth factor activity |
B | 0008083 | molecular_function | growth factor activity |
Functional Information from PROSITE/UniProt
site_id | PS00247 |
Number of Residues | 24 |
Details | HBGF_FGF HBGF/FGF family signature. GrLlAsksvtd.ECfFfErlesnnY |
Chain | Residue | Details |
A | GLY80-TYR103 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 32 |
Details | Region: {"description":"Heparin-binding","evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | Motif: {"description":"Cell attachment site; atypical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | Site: {"description":"Important for interaction with integrin","evidences":[{"source":"PubMed","id":"28302677","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphotyrosine; by TEC","evidences":[{"source":"PubMed","id":"20230531","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI7 |
Number of Residues | 176 |
Details | Domain: {"description":"Ig-like C2-type 2"} |
site_id | SWS_FT_FI8 |
Number of Residues | 102 |
Details | Domain: {"description":"Ig-like C2-type 3"} |
site_id | SWS_FT_FI9 |
Number of Residues | 34 |
Details | Region: {"description":"Heparin-binding"} |
site_id | SWS_FT_FI10 |
Number of Residues | 10 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]} |