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Phosphoprotein associated with glycosphingolipid-enriched microdomains 1 (Csk-binding protein) (Transmembrane adapter protein PAG) (Transmembrane phosphoprotein Cbp)

 PHAG1_HUMAN             Reviewed;         432 AA.
Q9NWQ8; A8K1A3; Q2M1Z9; Q5BKU4; Q9NYK0;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 2.
22-NOV-2017, entry version 128.
RecName: Full=Phosphoprotein associated with glycosphingolipid-enriched microdomains 1;
AltName: Full=Csk-binding protein;
AltName: Full=Transmembrane adapter protein PAG;
AltName: Full=Transmembrane phosphoprotein Cbp;
Name=PAG1; Synonyms=CBP, PAG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 264-274,
IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-317,
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-37 AND
CYS-40, MUTAGENESIS OF TYR-105; TYR-163; TYR-181; TYR-227; TYR-299;
TYR-317; TYR-341; TYR-359; TYR-387 AND TYR-417, INTERACTION WITH FYN
AND CSK, AND FUNCTION.
PubMed=10790433; DOI=10.1084/jem.191.9.1591;
Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V.,
Angelisova P., Scherer J., Shevchenko A., Shevchenko A., Hilgert I.,
Cerny J., Drbal K., Kuramitsu Y., Horejsi V., Schraven B.;
"Phosphoprotein associated with glycosphingolipid-enriched
microdomains (PAG), a novel ubiquitously expressed transmembrane
adaptor protein, binds the protein tyrosine kinase csk and is involved
in regulation of T cell activation.";
J. Exp. Med. 191:1591-1604(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Ileal mucosa;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH SLC9A3R1.
PubMed=11684085; DOI=10.1016/S0014-5793(01)02955-6;
Brdickova N., Brdicka T., Andera L., Spicka J., Angelisova P.,
Milgram S.L., Horejsi V.;
"Interaction between two adapter proteins, PAG and EBP50: a possible
link between membrane rafts and actin cytoskeleton.";
FEBS Lett. 507:133-136(2001).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[7]
TISSUE SPECIFICITY.
PubMed=16160011; DOI=10.1182/blood-2005-06-2273;
Tedoldi S., Paterson J.C., Hansmann M.-L., Natkunam Y., Rudiger T.,
Angelisova P., Du M.Q., Roberton H., Roncador G., Sanchez L.,
Pozzobon M., Masir N., Barry R., Pileri S., Mason D.Y., Marafioti T.,
Horejsi V.;
"Transmembrane adaptor molecules: a new category of lymphoid-cell
markers.";
Blood 107:213-221(2006).
[8]
PHOSPHORYLATION AT TYR-317, INTERACTION WITH LYN AND STAT3, AND
SUBCELLULAR LOCATION.
PubMed=18070987; DOI=10.1182/blood-2007-05-090985;
Tauzin S., Ding H., Khatib K., Ahmad I., Burdevet D.,
van Echten-Deckert G., Lindquist J.A., Schraven B., Din N.U.,
Borisch B., Hoessli D.C.;
"Oncogenic association of the Cbp/PAG adaptor protein with the Lyn
tyrosine kinase in human B-NHL rafts.";
Blood 111:2310-2320(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-227; SER-229; TYR-317;
TYR-359; TYR-387 AND TYR-417, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
-!- 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}.
-!- SUBUNIT: Interacts with FYN. When phosphorylated, interacts with
CSK. Interacts with SLC9A3R1/EBP50. In resting T-cells, part of a
PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation.
Interacts with LYN on plasma membrane lipid rafts. Identified in a
complex with LYN and STAT3. {ECO:0000269|PubMed:10790433,
ECO:0000269|PubMed:11684085, ECO:0000269|PubMed:18070987}.
-!- INTERACTION:
P41240:CSK; NbExp=3; IntAct=EBI-2828115, EBI-1380630;
P06241:FYN; NbExp=5; IntAct=EBI-2828115, EBI-515315;
P07948:LYN; NbExp=16; IntAct=EBI-2828115, EBI-79452;
P63244:RACK1; NbExp=2; IntAct=EBI-2828115, EBI-296739;
-!- 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.
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Present in germinal
center B-cells, plasma cells, T-cells, monocytes and platelets (at
protein level). {ECO:0000269|PubMed:10790433,
ECO:0000269|PubMed:16160011}.
-!- 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}.
-----------------------------------------------------------------------
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EMBL; AF240634; AAF67343.1; -; mRNA.
EMBL; AK000680; BAA91321.1; -; mRNA.
EMBL; AK289818; BAF82507.1; -; mRNA.
EMBL; CH471068; EAW87086.1; -; Genomic_DNA.
EMBL; BC090931; AAH90931.1; -; mRNA.
EMBL; BC112159; AAI12160.1; -; mRNA.
CCDS; CCDS6227.1; -.
RefSeq; NP_060910.3; NM_018440.3.
RefSeq; XP_016869129.1; XM_017013640.1.
RefSeq; XP_016869130.1; XM_017013641.1.
RefSeq; XP_016869131.1; XM_017013642.1.
RefSeq; XP_016869132.1; XM_017013643.1.
UniGene; Hs.266175; -.
ProteinModelPortal; Q9NWQ8; -.
SMR; Q9NWQ8; -.
BioGrid; 120931; 42.
IntAct; Q9NWQ8; 11.
MINT; MINT-220429; -.
STRING; 9606.ENSP00000220597; -.
iPTMnet; Q9NWQ8; -.
PhosphoSitePlus; Q9NWQ8; -.
SwissPalm; Q9NWQ8; -.
BioMuta; PAG1; -.
DMDM; 84029384; -.
EPD; Q9NWQ8; -.
MaxQB; Q9NWQ8; -.
PaxDb; Q9NWQ8; -.
PeptideAtlas; Q9NWQ8; -.
PRIDE; Q9NWQ8; -.
TopDownProteomics; Q9NWQ8; -.
DNASU; 55824; -.
Ensembl; ENST00000220597; ENSP00000220597; ENSG00000076641.
GeneID; 55824; -.
KEGG; hsa:55824; -.
UCSC; uc003ybz.4; human.
CTD; 55824; -.
DisGeNET; 55824; -.
EuPathDB; HostDB:ENSG00000076641.4; -.
GeneCards; PAG1; -.
HGNC; HGNC:30043; PAG1.
HPA; HPA001632; -.
HPA; HPA066527; -.
MIM; 605767; gene.
neXtProt; NX_Q9NWQ8; -.
OpenTargets; ENSG00000076641; -.
PharmGKB; PA142671201; -.
eggNOG; ENOG410IFZ3; Eukaryota.
eggNOG; ENOG4111TW0; LUCA.
GeneTree; ENSGT00390000002061; -.
HOGENOM; HOG000290651; -.
HOVERGEN; HBG055052; -.
InParanoid; Q9NWQ8; -.
OMA; KCHQSRE; -.
OrthoDB; EOG091G09DV; -.
PhylomeDB; Q9NWQ8; -.
TreeFam; TF336170; -.
Reactome; R-HSA-180292; GAB1 signalosome.
Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
SignaLink; Q9NWQ8; -.
ChiTaRS; PAG1; human.
GeneWiki; PAG1; -.
GenomeRNAi; 55824; -.
PRO; PR:Q9NWQ8; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000076641; -.
CleanEx; HS_PAG1; -.
Genevisible; Q9NWQ8; HS.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0045121; C:membrane raft; IDA:HGNC.
GO; GO:0005886; C:plasma membrane; IDA:HGNC.
GO; GO:0042169; F:SH2 domain binding; IDA:HGNC.
GO; GO:0005070; F:SH3/SH2 adaptor activity; NAS:HGNC.
GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IBA:GO_Central.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0035556; P:intracellular signal transduction; IDA:HGNC.
GO; GO:0050868; P:negative regulation of T cell activation; IBA:GO_Central.
GO; GO:0050863; P:regulation of T cell activation; IDA:ProtInc.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
InterPro; IPR032748; PAG.
PANTHER; PTHR16322; PTHR16322; 1.
Pfam; PF15347; PAG; 1.
ProDom; PD340439; PD340439; 1.
1: Evidence at protein level;
Adaptive immunity; Cell membrane; Complete proteome;
Direct protein sequencing; Immunity; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 432 Phosphoprotein associated with
glycosphingolipid-enriched microdomains
1.
/FTId=PRO_0000083338.
TOPO_DOM 1 16 Extracellular. {ECO:0000255}.
TRANSMEM 17 37 Helical; Signal-anchor for type III
membrane protein. {ECO:0000255}.
TOPO_DOM 38 432 Cytoplasmic. {ECO:0000255}.
REGION 317 320 Interaction with CSK.
{ECO:0000269|PubMed:10790433}.
REGION 430 432 Interaction with SLC9A3R1.
{ECO:0000269|PubMed:11684085}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JM80}.
MOD_RES 61 61 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JM80}.
MOD_RES 105 105 Phosphotyrosine; by LYN.
{ECO:0000250|UniProtKB:Q9JM80}.
MOD_RES 163 163 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q3U1F9}.
MOD_RES 181 181 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q3U1F9}.
MOD_RES 227 227 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 317 317 Phosphotyrosine; by FYN and LYN.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:10790433,
ECO:0000269|PubMed:18070987}.
MOD_RES 354 354 Phosphoserine.
{ECO:0000250|UniProtKB:Q3U1F9}.
MOD_RES 359 359 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 380 380 Phosphoserine.
{ECO:0000250|UniProtKB:Q3U1F9}.
MOD_RES 387 387 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 417 417 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
LIPID 37 37 S-palmitoyl cysteine.
{ECO:0000305|PubMed:10790433}.
LIPID 40 40 S-palmitoyl cysteine.
{ECO:0000305|PubMed:10790433}.
MUTAGEN 105 105 Y->F: No effect on interaction with FYN
or CSK. {ECO:0000269|PubMed:10790433}.
MUTAGEN 163 163 Y->F: No effect on interaction with FYN
or CSK. {ECO:0000269|PubMed:10790433}.
MUTAGEN 181 181 Y->F: No effect on interaction with FYN
or CSK. {ECO:0000269|PubMed:10790433}.
MUTAGEN 227 227 Y->F: No effect on interaction with FYN
or CSK. {ECO:0000269|PubMed:10790433}.
MUTAGEN 299 299 Y->F: No effect on interaction with FYN
or CSK. {ECO:0000269|PubMed:10790433}.
MUTAGEN 317 317 Y->F: No effect on interaction with FYN.
Abolishes interaction with CSK.
{ECO:0000269|PubMed:10790433}.
MUTAGEN 341 341 Y->F: No effect on interaction with FYN
or CSK. {ECO:0000269|PubMed:10790433}.
MUTAGEN 359 359 Y->F: No effect on interaction with FYN
or CSK. {ECO:0000269|PubMed:10790433}.
MUTAGEN 387 387 Y->F: No effect on interaction with FYN
or CSK. {ECO:0000269|PubMed:10790433}.
MUTAGEN 417 417 Y->F: No effect on interaction with FYN
or CSK. {ECO:0000269|PubMed:10790433}.
CONFLICT 4 4 A -> V (in Ref. 4; AAH90931).
{ECO:0000305}.
CONFLICT 36 36 L -> P (in Ref. 2; BAA91321).
{ECO:0000305}.
SEQUENCE 432 AA; 46981 MW; E86272A0B7E3328C CRC64;
MGPAGSLLGS GQMQITLWGS LAAVAIFFVI TFLIFLCSSC DREKKPRQHS GDHENLMNVP
SDKEMFSRSV TSLATDAPAS SEQNGALTNG DILSEDSTLT CMQHYEEVQT SASDLLDSQD
STGKPKCHQS RELPRIPPES AVDTMLTARS VDGDQGLGME GPYEVLKDSS SQENMVEDCL
YETVKEIKEV AAAAHLEKGH SGKAKSTSAS KELPGPQTEG KAEFAEYASV DRNKKCRQSV
NVESILGNSC DPEEEAPPPV PVKLLDENEN LQEKEGGEAE ESATDTTSET NKRFSSLSYK
SREEDPTLTE EEISAMYSSV NKPGQLVNKS GQSLTVPEST YTSIQGDPQR SPSSCNDLYA
TVKDFEKTPN STLPPAGRPS EEPEPDYEAI QTLNREEEKA TLGTNGHHGL VPKENDYESI
SDLQQGRDIT RL


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