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Protein

Phosphoprotein associated with glycosphingolipid-enriched microdomains 1

Gene

PAG1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • SH2 domain binding Source: HGNC
  • SH3/SH2 adaptor activity Source: HGNC
  • transmembrane receptor protein tyrosine kinase adaptor activity Source: GO_Central

GO - Biological processi

Keywordsi

Biological processAdaptive immunity, Immunity

Enzyme and pathway databases

ReactomeiR-HSA-180292 GAB1 signalosome
R-HSA-202427 Phosphorylation of CD3 and TCR zeta chains
SignaLinkiQ9NWQ8

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoprotein associated with glycosphingolipid-enriched microdomains 1
Alternative name(s):
Csk-binding protein
Transmembrane adapter protein PAG
Transmembrane phosphoprotein Cbp
Gene namesi
Name:PAG1
Synonyms:CBP, PAG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiHostDB:ENSG00000076641.4
HGNCiHGNC:30043 PAG1
MIMi605767 gene
neXtProtiNX_Q9NWQ8

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 16ExtracellularSequence analysisAdd BLAST16
Transmembranei17 – 37Helical; Signal-anchor for type III membrane proteinSequence analysisAdd BLAST21
Topological domaini38 – 432CytoplasmicSequence analysisAdd BLAST395

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi105Y → F: No effect on interaction with FYN or CSK. 1 Publication1
Mutagenesisi163Y → F: No effect on interaction with FYN or CSK. 1 Publication1
Mutagenesisi181Y → F: No effect on interaction with FYN or CSK. 1 Publication1
Mutagenesisi227Y → F: No effect on interaction with FYN or CSK. 1 Publication1
Mutagenesisi299Y → F: No effect on interaction with FYN or CSK. 1 Publication1
Mutagenesisi317Y → F: No effect on interaction with FYN. Abolishes interaction with CSK. 1 Publication1
Mutagenesisi341Y → F: No effect on interaction with FYN or CSK. 1 Publication1
Mutagenesisi359Y → F: No effect on interaction with FYN or CSK. 1 Publication1
Mutagenesisi387Y → F: No effect on interaction with FYN or CSK. 1 Publication1
Mutagenesisi417Y → F: No effect on interaction with FYN or CSK. 1 Publication1

Organism-specific databases

DisGeNETi55824
OpenTargetsiENSG00000076641
PharmGKBiPA142671201

Polymorphism and mutation databases

BioMutaiPAG1
DMDMi84029384

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000833381 – 432Phosphoprotein associated with glycosphingolipid-enriched microdomains 1Add BLAST432

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi37S-palmitoyl cysteine1 Publication1
Lipidationi40S-palmitoyl cysteine1 Publication1
Modified residuei50PhosphoserineBy similarity1
Modified residuei61PhosphoserineBy similarity1
Modified residuei105Phosphotyrosine; by LYNBy similarity1
Modified residuei163PhosphotyrosineBy similarity1
Modified residuei181PhosphotyrosineBy similarity1
Modified residuei227PhosphotyrosineCombined sources1
Modified residuei229PhosphoserineCombined sources1
Modified residuei317Phosphotyrosine; by FYN and LYNCombined sources2 Publications1
Modified residuei354PhosphoserineBy similarity1
Modified residuei359PhosphotyrosineCombined sources1
Modified residuei380PhosphoserineBy similarity1
Modified residuei387PhosphotyrosineCombined sources1
Modified residuei417PhosphotyrosineCombined sources1

Post-translational modificationi

Palmitoylated.1 Publication
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.2 Publications

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDiQ9NWQ8
MaxQBiQ9NWQ8
PaxDbiQ9NWQ8
PeptideAtlasiQ9NWQ8
PRIDEiQ9NWQ8
ProteomicsDBi82961
TopDownProteomicsiQ9NWQ8

PTM databases

iPTMnetiQ9NWQ8
PhosphoSitePlusiQ9NWQ8
SwissPalmiQ9NWQ8

Expressioni

Tissue specificityi

Ubiquitously expressed. Present in germinal center B-cells, plasma cells, T-cells, monocytes and platelets (at protein level).2 Publications

Gene expression databases

BgeeiENSG00000076641
CleanExiHS_PAG1
GenevisibleiQ9NWQ8 HS

Organism-specific databases

HPAiHPA001632
HPA066527

Interactioni

Subunit structurei

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 STAT3.3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • SH2 domain binding Source: HGNC
  • SH3/SH2 adaptor activity Source: HGNC
  • transmembrane receptor protein tyrosine kinase adaptor activity Source: GO_Central

Protein-protein interaction databases

BioGridi120931, 42 interactors
IntActiQ9NWQ8, 12 interactors
MINTiQ9NWQ8
STRINGi9606.ENSP00000220597

Structurei

3D structure databases

ProteinModelPortaliQ9NWQ8
SMRiQ9NWQ8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni317 – 320Interaction with CSK1 Publication4
Regioni430 – 432Interaction with SLC9A3R11 Publication3

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFZ3 Eukaryota
ENOG4111TW0 LUCA
GeneTreeiENSGT00390000002061
HOGENOMiHOG000290651
HOVERGENiHBG055052
InParanoidiQ9NWQ8
OMAiKCHQSRE
OrthoDBiEOG091G09DV
PhylomeDBiQ9NWQ8
TreeFamiTF336170

Family and domain databases

InterProiView protein in InterPro
IPR032748 PAG
PANTHERiPTHR16322 PTHR16322, 1 hit
PfamiView protein in Pfam
PF15347 PAG, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD340439 PD340439, 1 hit

Sequencei

Sequence statusi: Complete.

Q9NWQ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPAGSLLGS GQMQITLWGS LAAVAIFFVI TFLIFLCSSC DREKKPRQHS
60 70 80 90 100
GDHENLMNVP SDKEMFSRSV TSLATDAPAS SEQNGALTNG DILSEDSTLT
110 120 130 140 150
CMQHYEEVQT SASDLLDSQD STGKPKCHQS RELPRIPPES AVDTMLTARS
160 170 180 190 200
VDGDQGLGME GPYEVLKDSS SQENMVEDCL YETVKEIKEV AAAAHLEKGH
210 220 230 240 250
SGKAKSTSAS KELPGPQTEG KAEFAEYASV DRNKKCRQSV NVESILGNSC
260 270 280 290 300
DPEEEAPPPV PVKLLDENEN LQEKEGGEAE ESATDTTSET NKRFSSLSYK
310 320 330 340 350
SREEDPTLTE EEISAMYSSV NKPGQLVNKS GQSLTVPEST YTSIQGDPQR
360 370 380 390 400
SPSSCNDLYA TVKDFEKTPN STLPPAGRPS EEPEPDYEAI QTLNREEEKA
410 420 430
TLGTNGHHGL VPKENDYESI SDLQQGRDIT RL
Length:432
Mass (Da):46,981
Last modified:December 20, 2005 - v2
Checksum:iE86272A0B7E3328C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4A → V in AAH90931 (PubMed:15489334).Curated1
Sequence conflicti36L → P in BAA91321 (PubMed:14702039).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF240634 mRNA Translation: AAF67343.1
AK000680 mRNA Translation: BAA91321.1
AK289818 mRNA Translation: BAF82507.1
CH471068 Genomic DNA Translation: EAW87086.1
BC090931 mRNA Translation: AAH90931.1
BC112159 mRNA Translation: AAI12160.1
CCDSiCCDS6227.1
RefSeqiNP_060910.3, NM_018440.3
XP_016869129.1, XM_017013640.1
XP_016869130.1, XM_017013641.1
XP_016869131.1, XM_017013642.1
XP_016869132.1, XM_017013643.1
UniGeneiHs.266175

Genome annotation databases

EnsembliENST00000220597; ENSP00000220597; ENSG00000076641
GeneIDi55824
KEGGihsa:55824
UCSCiuc003ybz.4 human

Similar proteinsi

Entry informationi

Entry nameiPHAG1_HUMAN
AccessioniPrimary (citable) accession number: Q9NWQ8
Secondary accession number(s): A8K1A3
, Q2M1Z9, Q5BKU4, Q9NYK0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: July 18, 2018
This is version 134 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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