PAG1
entrez
55824
canonical
uniprot
Q9NWQ8
canonical
ensembl
ENSG00000076641
resolver
ensp
ENSP00000220597
resolver
ensp
ENSP00000554289
resolver
ensp
ENSP00000554290
resolver
ensp
ENSP00000554291
resolver
ensp
ENSP00000554292
resolver
ensp
ENSP00000554293
resolver
ensp
ENSP00000554294
resolver
ensp
ENSP00000554295
resolver
ensp
ENSP00000554296
resolver
ensp
ENSP00000554297
resolver
ensp
ENSP00000554298
resolver
ensp
ENSP00000554299
resolver
ensp
ENSP00000554303
resolver
ensp
ENSP00000554304
resolver
ensp
ENSP00000554305
resolver
ensp
ENSP00000554306
resolver
ensp
ENSP00000554307
resolver
ensp
ENSP00000640390
resolver
ensp
ENSP00000640392
resolver
ensp
ENSP00000640393
resolver
enst
ENST00000220597
resolver
enst
ENST00000884230
resolver
enst
ENST00000884231
resolver
enst
ENST00000884232
resolver
enst
ENST00000884233
resolver
enst
ENST00000884234
resolver
enst
ENST00000884235
resolver
enst
ENST00000884236
resolver
enst
ENST00000884237
resolver
enst
ENST00000884238
resolver
enst
ENST00000884239
resolver
enst
ENST00000884240
resolver
enst
ENST00000884244
resolver
enst
ENST00000884245
resolver
enst
ENST00000884246
resolver
enst
ENST00000884247
resolver
enst
ENST00000884248
resolver
enst
ENST00000970331
resolver
enst
ENST00000970334
resolver
genesymbol
PAG1
resolver
genesymbol_syn
CBP
resolver
genesymbol_syn
PAG
resolver
hgnc
HGNC:30043
resolver
uniprot
A8K1A3
resolver
uniprot
Q2M1Z9
resolver
uniprot
Q5BKU4
resolver
uniprot
Q9NYK0
resolver
uniprot_entry
PHAG1_HUMAN
resolver
uniprot_sec
A8K1A3
resolver
uniprot_sec
Q2M1Z9
resolver
uniprot_sec
Q5BKU4
resolver
uniprot_sec
Q9NYK0
resolver
amino_acid_sequence
MGPAGSLLGSGQMQITLWGSLAAVAIFFVITFLIFLCSSCDREKKPRQHSGDHENLMNVPSDKEMFSRSVTSLATDAPASSEQNGALTNGDILSEDSTLTCMQHYEEVQTSASDLLDSQDSTGKPKCHQSRELPRIPPESAVDTMLTARSVDGDQGLGMEGPYEVLKDSSSQENMVEDCLYETVKEIKEVAAAAHLEKGHSGKAKSTSASKELPGPQTEGKAEFAEYASVDRNKKCRQSVNVESILGNSCDPEEEAPPPVPVKLLDENENLQEKEGGEAEESATDTTSETNKRFSSLSYKSREEDPTLTEEEISAMYSSVNKPGQLVNKSGQSLTVPESTYTSIQGDPQRSPSSCNDLYATVKDFEKTPNSTLPPAGRPSEEPEPDYEAIQTLNREEEKATLGTNGHHGLVPKENDYESISDLQQGRDITRL
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:10790433}.
uniprot
proteins
mass_dalton
46981
uniprot
proteins
mutagenesis
MUTAGEN 105; /note="Y->F: No effect on interaction with FYN or CSK."; /evidence="ECO:0000269|PubMed:10790433"; MUTAGEN 163; /note="Y->F: No effect on interaction with FYN or CSK."; /evidence="ECO:0000269|PubMed:10790433"; MUTAGEN 181; /note="Y->F: No effect on interaction with FYN or CSK."; /evidence="ECO:0000269|PubMed:10790433"; MUTAGEN 227; /note="Y->F: No effect on interaction with FYN or CSK."; /evidence="ECO:0000269|PubMed:10790433"; MUTAGEN 299; /note="Y->F: No effect on interaction with FYN or CSK."; /evidence="ECO:0000269|PubMed:10790433"; MUTAGEN 317; /note="Y->F: No effect on interaction with FYN. Abolishes interaction with CSK."; /evidence="ECO:0000269|PubMed:10790433"; MUTAGEN 341; /note="Y->F: No effect on interaction with FYN or CSK."; /evidence="ECO:0000269|PubMed:10790433"; MUTAGEN 359; /note="Y->F: No effect on interaction with FYN or CSK."; /evidence="ECO:0000269|PubMed:10790433"; MUTAGEN 387; /note="Y->F: No effect on interaction with FYN or CSK."; /evidence="ECO:0000269|PubMed:10790433"; MUTAGEN 417; /note="Y->F: No effect on interaction with FYN or CSK."; /evidence="ECO:0000269|PubMed:10790433
uniprot
proteins
post_translational_modification
PTM: Palmitoylated. {ECO:0000269|PubMed:10790433}.; PTM: Phosphorylated by FYN on Tyr-317 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. {ECO:0000269|PubMed:10790433, ECO:0000269|PubMed:18070987}.
uniprot
proteins
pubmed
10790433
uniprot
proteins
pubmed
11684085
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15144186
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16160011
uniprot
proteins
pubmed
18070987
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19690332
uniprot
proteins
sequence_length
432
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10790433, ECO:0000269|PubMed:18070987}; Single-pass type III membrane protein {ECO:0000269|PubMed:10790433, ECO:0000269|PubMed:18070987}. Note=Present in lipid rafts.
uniprot
proteins
transmembrane_region
TRANSMEM 17..37; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255
uniprot
proteins