Pag1
entrez
64019
canonical
uniprot
Q9JM80
canonical
ensembl
ENSRNOG00000087915
resolver
ensembl
ENSRNOG00055001812
resolver
ensembl
ENSRNOG00060001924
resolver
ensembl
ENSRNOG00065013316
resolver
ensp
ENSRNOP00000099433
resolver
ensp
ENSRNOP00055002209
resolver
ensp
ENSRNOP00060001973
resolver
ensp
ENSRNOP00065016968
resolver
enst
ENSRNOT00000124833
resolver
enst
ENSRNOT00055002932
resolver
enst
ENSRNOT00060002986
resolver
enst
ENSRNOT00065021892
resolver
genesymbol
Pag1
resolver
genesymbol_syn
Cbp
resolver
genesymbol_syn
Pag
resolver
uniprot_entry
PHAG1_RAT
resolver
amino_acid_sequence
MGPAGSALSSGQMQMQMVLWGSLAAVAMFFLITFLILLCSSCDRDKKPRQHSGDHESLMNVPSDKEMFSHSATSLTTDALASSEQNGVLTNGDILSEDSTMTCMQHYEEVQTSASDLLDSQDSTGKAKCHQSRELPRIPPENAVDAMLTARAADGDSGPGVEGPYEVLKDSSSQENMVEDCLYETVKEIKEVADKSQGGKSKSTSALKELQGAHAEGKADFAEYASVDRNKKCRHSTNAESILGTSSDLDEETPPPVPVKLLDENANLPEKGEHGAEEQAPEAPSGHSKRFSSLSYKSREEDPTLTEEEISAMYSSVNKPGQSAHKPGPESTCQCPQGPPQRSSSSCNDLYATVKDFEKTPNSISMLPPARRPGEEPEPDYEAIQTLNREDDKVPLGTNGHLVPKENDYESIGDLQQGRDVTRL
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:10801129, ECO:0000269|PubMed:10918051, ECO:0000269|PubMed:11859092}.
uniprot
proteins
mass_dalton
45915
uniprot
proteins
mutagenesis
MUTAGEN 107; /note="Y->F: No effect on interaction with CSK."; /evidence="ECO:0000269|PubMed:10801129"; MUTAGEN 165; /note="Y->F: No effect on interaction with CSK."; /evidence="ECO:0000269|PubMed:10801129"; MUTAGEN 183; /note="Y->F: No effect on interaction with CSK."; /evidence="ECO:0000269|PubMed:10801129"; MUTAGEN 224; /note="Y->F: No effect on interaction with CSK."; /evidence="ECO:0000269|PubMed:10801129"; MUTAGEN 296; /note="Y->F: No effect on interaction with CSK."; /evidence="ECO:0000269|PubMed:10801129"; MUTAGEN 314; /note="Y->F: Abolishes interaction with CSK."; /evidence="ECO:0000269|PubMed:10801129, ECO:0000269|PubMed:14613929"; MUTAGEN 351; /note="Y->F: No effect on interaction with CSK."; /evidence="ECO:0000269|PubMed:10801129"; MUTAGEN 381; /note="Y->F: No effect on interaction with CSK."; /evidence="ECO:0000269|PubMed:10801129"; MUTAGEN 409; /note="Y->F: No effect on interaction with CSK."; /evidence="ECO:0000269|PubMed:10801129
uniprot
proteins
post_translational_modification
PTM: Palmitoylated. {ECO:0000250}.; 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. Phosphorylated by LYN in response to EPO. {ECO:0000269|PubMed:10801129, ECO:0000269|PubMed:10918051, ECO:0000269|PubMed:11859092, ECO:0000269|PubMed:14613929, ECO:0000269|PubMed:16920712}.
uniprot
proteins
pubmed
10801129
uniprot
proteins
pubmed
10918051
uniprot
proteins
pubmed
11859092
uniprot
proteins
pubmed
14613929
uniprot
proteins
pubmed
16920712
uniprot
proteins
pubmed
22673903
uniprot
proteins
sequence_length
424
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10801129, ECO:0000269|PubMed:11859092}; Single-pass type III membrane protein {ECO:0000269|PubMed:10801129, ECO:0000269|PubMed:11859092}. 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