IID00537
Uniprot P08575
Protein Receptor-type tyrosine-protein phosphatase C
Gene PTPRC
Organism Homo sapiens
Sequence
LLPS
Network
xml
rdf
Structure
atLeast majority ProS Experiment
:order disorder conflict PDB cluster ProS Pfam Domain SEG
1306
order/disorder by at least rule
disorder by at least rule
order/disorder by majority rule
Region 5fn7 A 225-390 order
Region 5fn7 A 391-394 disorder
Region 5fn7 B 225-389 order
Region 5fn7 B 390-394 disorder
Region 5fmv A 225-225 disorder
Region 5fmv A 226-573 order
Region 5fmv B 225-227 disorder
Region 5fmv B 228-573 order
Region 5fn6 A 225-226 disorder
Region 5fn6 A 227-261 order
Region 5fn6 A 262-264 disorder
Region 5fn6 A 265-481 order
Seq 624-1233 Hetero dimer : IID90016 Complex
Region 1ygu B 624-624 disorder
Region 1ygu B 625-990 order
Region 1ygu B 991-1014 disorder
Region 1ygu B 1015-1230 order
Region 1ygu B 1231-1233 disorder
Region 1ygu A 624-988 order
Region 1ygu A 989-1014 disorder
Region 1ygu A 1015-1152 order
Region 1ygu A 1153-1162 disorder
Region 1ygu A 1163-1230 order
Region 1ygu A 1231-1233 disorder
Seq 624-1233 Hetero dimer : IID00544 Complex
Region 1ygr B 624-624 disorder
Region 1ygr B 625-990 order
Region 1ygr B 991-1014 disorder
Region 1ygr B 1015-1149 order
Region 1ygr B 1150-1160 disorder
Region 1ygr B 1161-1233 order
Region 1ygr A 624-988 order
Region 1ygr A 989-1014 disorder
Region 1ygr A 1015-1152 order
Region 1ygr A 1153-1159 disorder
Region 1ygr A 1160-1230 order
Region 1ygr A 1231-1233 disorder
Prediction
Disorder 31-227,609-618,995-1010,1251-1306
Order 1-26,228-608,619-990,1011-1250
ProS 52-57,64-79,135-195,215-220,1251-1264
Disorder 1-225,261-263,604-621,821-821,844-844,989-1014,1128-1128,1150-1163,1232-1306
Order 226-260,264-603,622-820,822-843,845-988,1015-1127,1129-1149,1164-1231
PF00102 968-1227 1.1e-106
SEG 164-182
,214-227
,992-1015
Function
Function in SwissProt
Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity.
Biological Process
See also
Diagram with PDB data
LCK SH3-SH2 DOMAIN FRAGMENT OF HUMAN P56-LCK TYROSINE KINASE COMPLEXED WITH
THE 10 RESIDUE SYNTHETIC PHOSPHOTYROSYL PEPTIDE TEGQPYQPQPA
FYN Fyn SH2 domain in complex with the
natural inhibitory phosphotyrosine
peptide