8DFP
Ectodomain of full-length KIT(DupA502,Y503)-SCF dimers
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004713 | molecular_function | protein tyrosine kinase activity |
A | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
A | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
A | 0019955 | molecular_function | cytokine binding |
A | 0038093 | biological_process | Fc receptor signaling pathway |
A | 0038109 | biological_process | Kit signaling pathway |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004713 | molecular_function | protein tyrosine kinase activity |
B | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
B | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
B | 0019955 | molecular_function | cytokine binding |
B | 0038093 | biological_process | Fc receptor signaling pathway |
B | 0038109 | biological_process | Kit signaling pathway |
C | 0005173 | molecular_function | stem cell factor receptor binding |
C | 0007155 | biological_process | cell adhesion |
C | 0016020 | cellular_component | membrane |
D | 0005173 | molecular_function | stem cell factor receptor binding |
D | 0007155 | biological_process | cell adhesion |
D | 0016020 | cellular_component | membrane |
Functional Information from PROSITE/UniProt
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNILL |
Chain | Residue | Details |
A | CYS786-LEU798 |
site_id | PS00240 |
Number of Residues | 14 |
Details | RECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GnHmNIVNLLGACT |
Chain | Residue | Details |
A | GLY646-THR659 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | SITE: Not glycosylated |
Chain | Residue | Details |
C | ASN72 | |
D | ASN72 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:1381905 |
Chain | Residue | Details |
C | ASN65 | |
C | ASN93 | |
D | ASN65 | |
D | ASN93 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1381905 |
Chain | Residue | Details |
C | ASN120 | |
D | ASN120 |
site_id | SWS_FT_FI4 |
Number of Residues | 14 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP570 | |
B | PRO625 | |
B | TYR673 | |
B | LEU798 | |
B | THR799 | |
B | ALA812 | |
A | PHE598 | |
A | PRO625 | |
A | TYR673 | |
A | LEU798 | |
A | THR799 | |
A | ALA812 | |
B | ASP570 | |
B | PHE598 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Important for interaction with phosphotyrosine-binding proteins |
Chain | Residue | Details |
A | ALA938 | |
B | ALA938 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:20147452 |
Chain | Residue | Details |
A | PRO549 | |
A | TRP555 | |
A | THR732 | |
B | PRO549 | |
B | TRP555 | |
B | THR732 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:21030588, ECO:0000269|PubMed:9038210 |
Chain | Residue | Details |
A | ASP570 | |
B | ASP570 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:9038210 |
Chain | Residue | Details |
A | THR572 | |
B | THR572 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10377264, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:20147452 |
Chain | Residue | Details |
A | LEU705 | |
B | LEU705 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:20147452, ECO:0000269|PubMed:9038210 |
Chain | Residue | Details |
A | LYS723 | |
B | LYS723 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; by PKC/PRKCA => ECO:0000269|PubMed:7539802 |
Chain | Residue | Details |
A | GLY743 | |
A | ARG748 | |
B | GLY743 | |
B | ARG748 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:7539802 |
Chain | Residue | Details |
A | VAL823 | |
B | VAL823 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20147452 |
Chain | Residue | Details |
A | GLY825 | |
B | GLY825 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:12878163 |
Chain | Residue | Details |
A | ALA893 | |
B | ALA893 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:20147452 |
Chain | Residue | Details |
A | LYS902 | |
B | LYS902 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10377264, ECO:0000269|PubMed:19265199 |
Chain | Residue | Details |
A | ALA938 | |
B | ALA938 |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:7539802, ECO:0007744|PubMed:19369195 |
Chain | Residue | Details |
A | THR961 | |
B | THR961 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17662946 |
Chain | Residue | Details |
A | ASN130 | |
B | ASN130 |
site_id | SWS_FT_FI19 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN145 | |
A | ASN463 | |
A | ASN486 | |
B | ASN145 | |
B | ASN463 | |
B | ASN486 |
site_id | SWS_FT_FI20 |
Number of Residues | 12 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17662946 |
Chain | Residue | Details |
A | ASN283 | |
B | ASN320 | |
B | ASN352 | |
B | ASN367 | |
A | ASN293 | |
A | ASN300 | |
A | ASN320 | |
A | ASN352 | |
A | ASN367 | |
B | ASN283 | |
B | ASN293 | |
B | ASN300 |