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Protein

Phosphoprotein associated with glycosphingolipid-enriched microdomains 1

Gene

Pag1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.4 Publications

GO - Molecular functioni

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • intracellular signal transduction Source: HGNC
  • negative regulation of T cell activation Source: HGNC
  • regulation of T cell activation Source: HGNC
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Immunity

Enzyme and pathway databases

ReactomeiR-MMU-180292. GAB1 signalosome.
R-MMU-202427. Phosphorylation of CD3 and TCR zeta chains.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoprotein associated with glycosphingolipid-enriched microdomains 1
Alternative name(s):
Csk-binding protein
Transmembrane phosphoprotein Cbp
Gene namesi
Name:Pag1
Synonyms:Cbp, Pag
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:2443160. Pag1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 17ExtracellularSequence analysisAdd BLAST17
Transmembranei18 – 38Helical; Signal-anchor for type III membrane proteinSequence analysisAdd BLAST21
Topological domaini39 – 429CytoplasmicSequence analysisAdd BLAST391

GO - Cellular componenti

  • integral component of plasma membrane Source: GO_Central
  • intracellular Source: GOC
  • membrane raft Source: HGNC
  • plasma membrane Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are viable and do not show any developmental defect up to 20 months of age. They have normal T-cell development and normal T- and B-cell responses.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi314Y → F: Enhances TCR-mediated signaling. 1 Publication1
Mutagenesisi429L → A: Abolishes interaction with SLC9A3R1 and effect on synapse formation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000833391 – 429Phosphoprotein associated with glycosphingolipid-enriched microdomains 1Add BLAST429

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi39S-palmitoyl cysteineBy similarity1
Lipidationi42S-palmitoyl cysteineBy similarity1
Modified residuei107Phosphotyrosine; by LYNBy similarity1
Modified residuei165PhosphotyrosineCombined sources1
Modified residuei183PhosphotyrosineCombined sources1
Modified residuei224PhosphotyrosineCombined sources1
Modified residuei226PhosphoserineBy similarity1
Modified residuei314Phosphotyrosine; by FYN3 Publications1
Modified residuei351PhosphoserineCombined sources1
Modified residuei356PhosphotyrosineBy similarity1
Modified residuei379PhosphoserineCombined sources1
Modified residuei386PhosphotyrosineBy similarity1
Modified residuei414PhosphotyrosineBy similarity1

Post-translational modificationi

Palmitoylated.1 Publication
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.5 Publications

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDiQ3U1F9.
MaxQBiQ3U1F9.
PaxDbiQ3U1F9.
PRIDEiQ3U1F9.

PTM databases

iPTMnetiQ3U1F9.
PhosphoSitePlusiQ3U1F9.
SwissPalmiQ3U1F9.

Expressioni

Tissue specificityi

Present in T-cells (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000027508.
ExpressionAtlasiQ3U1F9. baseline and differential.
GenevisibleiQ3U1F9. MM.

Interactioni

Subunit structurei

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.4 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi220469. 3 interactors.
IntActiQ3U1F9. 1 interactor.
STRINGi10090.ENSMUSP00000104021.

Structurei

3D structure databases

ProteinModelPortaliQ3U1F9.
SMRiQ3U1F9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni314 – 317Interaction with CSK4
Regioni427 – 429Interaction with SLC9A3R11 Publication3

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFZ3. Eukaryota.
ENOG4111TW0. LUCA.
GeneTreeiENSGT00390000002061.
HOGENOMiHOG000290651.
HOVERGENiHBG055052.
InParanoidiQ3U1F9.
OMAiILGNSCD.
OrthoDBiEOG091G09DV.
PhylomeDBiQ3U1F9.
TreeFamiTF336170.

Family and domain databases

InterProiIPR032748. PAG.
[Graphical view]
PfamiPF15347. PAG. 1 hit.
[Graphical view]
ProDomiPD340439. PD340439. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

Q3U1F9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPAGSVLSS GQMQMQMVLW GSLAAVAMFF LITFLVLLCS TCDREKKPRQ
60 70 80 90 100
HSGDHENLMN VPSDKDMFSH SATSLTTDAL ASSEQNGVLT NGDILSEDST
110 120 130 140 150
LTCMQHYEEV QTSASDLLDS QDSTGKAKCH QSRELPRIPP ENAVDEILTA
160 170 180 190 200
RAADTELGPG VEGPYEVLKD SSSQENMVED CLYETVKEIK EVADKGQGGK
210 220 230 240 250
SKSTSALKEL QGAPMEGKAD FAEYASVDRN KKCRHSANAE SILGTCSDLD
260 270 280 290 300
EESPPPVPVK LLDENANLPQ EGGGQAEEQA AEGTGGHSKR FSSLSYKSRE
310 320 330 340 350
EDPTLTEEEI SAMYSSVNKP GQSAHKPGPC MKGPESACHS MKGLPQRSSS
360 370 380 390 400
SCNDLYATVK DFEKTPNSIS TLPPARRPSE EPEPDYEAIQ TLNREDEKVP
410 420
LETNGHHVPK ESDYESIGDL QQCRDVTRL
Length:429
Mass (Da):46,549
Last modified:December 20, 2005 - v2
Checksum:iF5A95257B4C4DADC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti58L → P in AAG44565 (PubMed:10790433).Curated1
Sequence conflicti287H → R in AAG44565 (PubMed:10790433).Curated1
Sequence conflicti360K → R in BAE33539 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250192 mRNA. Translation: AAG44565.1.
AK156000 mRNA. Translation: BAE33539.1.
AK040230 mRNA. Translation: BAC30545.1.
AK089329 mRNA. Translation: BAC40842.1.
AK172106 mRNA. Translation: BAE42829.1.
CCDSiCCDS17235.1.
RefSeqiNP_001181960.1. NM_001195031.1.
NP_444412.2. NM_053182.5.
XP_006530170.1. XM_006530107.1.
XP_011246453.1. XM_011248151.2.
UniGeneiMm.23897.
Mm.486503.

Genome annotation databases

EnsembliENSMUST00000108384; ENSMUSP00000104021; ENSMUSG00000027508.
ENSMUST00000161949; ENSMUSP00000124529; ENSMUSG00000027508.
GeneIDi94212.
KEGGimmu:94212.
UCSCiuc008opc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250192 mRNA. Translation: AAG44565.1.
AK156000 mRNA. Translation: BAE33539.1.
AK040230 mRNA. Translation: BAC30545.1.
AK089329 mRNA. Translation: BAC40842.1.
AK172106 mRNA. Translation: BAE42829.1.
CCDSiCCDS17235.1.
RefSeqiNP_001181960.1. NM_001195031.1.
NP_444412.2. NM_053182.5.
XP_006530170.1. XM_006530107.1.
XP_011246453.1. XM_011248151.2.
UniGeneiMm.23897.
Mm.486503.

3D structure databases

ProteinModelPortaliQ3U1F9.
SMRiQ3U1F9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi220469. 3 interactors.
IntActiQ3U1F9. 1 interactor.
STRINGi10090.ENSMUSP00000104021.

PTM databases

iPTMnetiQ3U1F9.
PhosphoSitePlusiQ3U1F9.
SwissPalmiQ3U1F9.

Proteomic databases

EPDiQ3U1F9.
MaxQBiQ3U1F9.
PaxDbiQ3U1F9.
PRIDEiQ3U1F9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108384; ENSMUSP00000104021; ENSMUSG00000027508.
ENSMUST00000161949; ENSMUSP00000124529; ENSMUSG00000027508.
GeneIDi94212.
KEGGimmu:94212.
UCSCiuc008opc.2. mouse.

Organism-specific databases

CTDi55824.
MGIiMGI:2443160. Pag1.

Phylogenomic databases

eggNOGiENOG410IFZ3. Eukaryota.
ENOG4111TW0. LUCA.
GeneTreeiENSGT00390000002061.
HOGENOMiHOG000290651.
HOVERGENiHBG055052.
InParanoidiQ3U1F9.
OMAiILGNSCD.
OrthoDBiEOG091G09DV.
PhylomeDBiQ3U1F9.
TreeFamiTF336170.

Enzyme and pathway databases

ReactomeiR-MMU-180292. GAB1 signalosome.
R-MMU-202427. Phosphorylation of CD3 and TCR zeta chains.

Miscellaneous databases

ChiTaRSiPag1. mouse.
PROiQ3U1F9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027508.
ExpressionAtlasiQ3U1F9. baseline and differential.
GenevisibleiQ3U1F9. MM.

Family and domain databases

InterProiIPR032748. PAG.
[Graphical view]
PfamiPF15347. PAG. 1 hit.
[Graphical view]
ProDomiPD340439. PD340439. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Entry informationi

Entry nameiPHAG1_MOUSE
AccessioniPrimary (citable) accession number: Q3U1F9
Secondary accession number(s): Q8BFS1, Q9EQF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: November 2, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.