Pag1
entrez
94212
canonical
uniprot
Q3U1F9
canonical
ensembl
ENSMUSG00000027508
resolver
ensp
ENSMUSP00000104021
resolver
ensp
ENSMUSP00000124529
resolver
ensp
ENSMUSP00000200341
resolver
enst
ENSMUST00000108384
resolver
enst
ENSMUST00000161949
resolver
genesymbol
Pag1
resolver
genesymbol_syn
Cbp
resolver
genesymbol_syn
Pag
resolver
uniprot
A6H659
resolver
uniprot
Q8BFS1
resolver
uniprot
Q9EQF3
resolver
uniprot_entry
A6H659_MOUSE
resolver
uniprot_entry
PHAG1_MOUSE
resolver
uniprot_sec
Q8BFS1
resolver
uniprot_sec
Q9EQF3
resolver
amino_acid_sequence
MGPAGSVLSSGQMQMQMVLWGSLAAVAMFFLITFLVLLCSTCDREKKPRQHSGDHENLMNVPSDKDMFSHSATSLTTDALASSEQNGVLTNGDILSEDSTLTCMQHYEEVQTSASDLLDSQDSTGKAKCHQSRELPRIPPENAVDEILTARAADTELGPGVEGPYEVLKDSSSQENMVEDCLYETVKEIKEVADKGQGGKSKSTSALKELQGAPMEGKADFAEYASVDRNKKCRHSANAESILGTCSDLDEESPPPVPVKLLDENANLPQEGGGQAEEQAAEGTGGHSKRFSSLSYKSREEDPTLTEEEISAMYSSVNKPGQSAHKPGPCMKGPESACHSMKGLPQRSSSSCNDLYATVKDFEKTPNSISTLPPARRPSEEPEPDYEAIQTLNREDEKVPLETNGHHVPKESDYESIGDLQQCRDVTRL
uniprot
proteins
function
FUNCTION: Negatively regulates TCR (T-cell antigen receptor)-mediated signaling in T-cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Promotes CSK activation and recruitment to lipid rafts, which results in LCK inhibition. Inhibits immunological synapse formation by preventing dynamic arrangement of lipid raft proteins. May be involved in cell adhesion signaling. {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:12612075, ECO:0000269|PubMed:14645715, ECO:0000269|PubMed:16166631}.
uniprot
proteins
mass_dalton
46549
uniprot
proteins
mutagenesis
MUTAGEN 314; /note="Y->F: Enhances TCR-mediated signaling."; /evidence="ECO:0000269|PubMed:12612075"; MUTAGEN 429; /note="L->A: Abolishes interaction with NHERF1 and effect on synapse formation."; /evidence="ECO:0000269|PubMed:11777944
uniprot
proteins
post_translational_modification
PTM: Palmitoylated. {ECO:0000269|PubMed:12626544}.; PTM: Phosphorylated by FYN on Tyr-314 in resting T-cells; which promotes interaction with CSK. Dephosphorylated by PTPRC/CD45 upon TCR activation; which leads to CSK dissociation. May also be dephosphorylated by PTPN11. Hyperphosphorylated in mast cells upon FCER1 activation. {ECO:0000269|PubMed:11777944, ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:12612075, ECO:0000269|PubMed:14645715, ECO:0000269|PubMed:14967142}.
uniprot
proteins
pubmed
10790433
uniprot
proteins
pubmed
11777944
uniprot
proteins
pubmed
12218089
uniprot
proteins
pubmed
12612075
uniprot
proteins
pubmed
12626544
uniprot
proteins
pubmed
14645715
uniprot
proteins
pubmed
14967142
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16166631
uniprot
proteins
pubmed
17947660
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
429
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11777944, ECO:0000269|PubMed:12612075, ECO:0000269|PubMed:14645715, ECO:0000269|PubMed:16166631}; Single-pass type III membrane protein {ECO:0000269|PubMed:11777944, ECO:0000269|PubMed:12612075, ECO:0000269|PubMed:14645715, ECO:0000269|PubMed:16166631}. Note=Present in lipid rafts.
uniprot
proteins
transmembrane_region
TRANSMEM 18..38; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255
uniprot
proteins