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Protein

Phosphoprotein associated with glycosphingolipid-enriched microdomains 1

Gene

Pag1

Organism
Rattus norvegicus (Rat)
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.3 Publications

GO - Molecular functioni

  • SH2 domain binding Source: GO_Central
  • transmembrane receptor protein tyrosine kinase adaptor activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Immunity

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620394. 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 – 424CytoplasmicSequence analysisAdd BLAST386

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi107Y → F: No effect on interaction with CSK. 1 Publication1
Mutagenesisi165Y → F: No effect on interaction with CSK. 1 Publication1
Mutagenesisi183Y → F: No effect on interaction with CSK. 1 Publication1
Mutagenesisi224Y → F: No effect on interaction with CSK. 1 Publication1
Mutagenesisi296Y → F: No effect on interaction with CSK. 1 Publication1
Mutagenesisi314Y → F: Abolishes interaction with CSK. 2 Publications1
Mutagenesisi351Y → F: No effect on interaction with CSK. 1 Publication1
Mutagenesisi381Y → F: No effect on interaction with CSK. 1 Publication1
Mutagenesisi409Y → F: No effect on interaction with CSK. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000833401 – 424Phosphoprotein associated with glycosphingolipid-enriched microdomains 1Add BLAST424

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi39S-palmitoyl cysteineBy similarity1
Lipidationi42S-palmitoyl cysteineBy similarity1
Modified residuei107Phosphotyrosine; by LYN1 Publication1
Modified residuei165Phosphotyrosine1 Publication1
Modified residuei183Phosphotyrosine1 Publication1
Modified residuei224Phosphotyrosine1 Publication1
Modified residuei226PhosphoserineBy similarity1
Modified residuei314Phosphotyrosine; by FYN and LYN3 Publications1
Modified residuei346PhosphoserineBy similarity1
Modified residuei351PhosphotyrosineBy similarity1
Modified residuei381Phosphotyrosine1 Publication1
Modified residuei409Phosphotyrosine1 Publication1

Post-translational modificationi

Palmitoylated.By similarity
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.5 Publications

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiQ9JM80.
PRIDEiQ9JM80.

PTM databases

iPTMnetiQ9JM80.
PhosphoSitePlusiQ9JM80.

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in developing brain, lung, thymus, spleen and testis. Present in mast cells.2 Publications

Interactioni

Subunit structurei

Interacts with SLC9A3R1/EBP50. In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation (By similarity). When phosphorylated, interacts with CSK. Identified in a complex with LYN and STAT3 (By similarity). Interacts with LYN.By similarity4 Publications

GO - Molecular functioni

  • SH2 domain binding Source: GO_Central
  • transmembrane receptor protein tyrosine kinase adaptor activity Source: RGD

Protein-protein interaction databases

BioGridi248938. 1 interactor.
STRINGi10116.ENSRNOP00000065200.

Structurei

Secondary structure

1424
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni299 – 301Combined sources3
Helixi307 – 312Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RSYNMR-B288-321[»]
SMRiQ9JM80.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni314 – 317Interaction with CSK4
Regioni422 – 424Interaction with SLC9A3R1By similarity3

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4111TW0. LUCA.
HOVERGENiHBG055052.
InParanoidiQ9JM80.
PhylomeDBiQ9JM80.

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.

Q9JM80-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPAGSALSS GQMQMQMVLW GSLAAVAMFF LITFLILLCS SCDRDKKPRQ
60 70 80 90 100
HSGDHESLMN VPSDKEMFSH SATSLTTDAL ASSEQNGVLT NGDILSEDST
110 120 130 140 150
MTCMQHYEEV QTSASDLLDS QDSTGKAKCH QSRELPRIPP ENAVDAMLTA
160 170 180 190 200
RAADGDSGPG VEGPYEVLKD SSSQENMVED CLYETVKEIK EVADKSQGGK
210 220 230 240 250
SKSTSALKEL QGAHAEGKAD FAEYASVDRN KKCRHSTNAE SILGTSSDLD
260 270 280 290 300
EETPPPVPVK LLDENANLPE KGEHGAEEQA PEAPSGHSKR FSSLSYKSRE
310 320 330 340 350
EDPTLTEEEI SAMYSSVNKP GQSAHKPGPE STCQCPQGPP QRSSSSCNDL
360 370 380 390 400
YATVKDFEKT PNSISMLPPA RRPGEEPEPD YEAIQTLNRE DDKVPLGTNG
410 420
HLVPKENDYE SIGDLQQGRD VTRL
Length:424
Mass (Da):45,915
Last modified:October 1, 2000 - v1
Checksum:i49ED52D44B3FB154
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038038 mRNA. Translation: BAA95413.1.
RefSeqiNP_071589.1. NM_022253.1.
UniGeneiRn.127786.

Genome annotation databases

GeneIDi64019.
KEGGirno:64019.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038038 mRNA. Translation: BAA95413.1.
RefSeqiNP_071589.1. NM_022253.1.
UniGeneiRn.127786.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RSYNMR-B288-321[»]
SMRiQ9JM80.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248938. 1 interactor.
STRINGi10116.ENSRNOP00000065200.

PTM databases

iPTMnetiQ9JM80.
PhosphoSitePlusiQ9JM80.

Proteomic databases

PaxDbiQ9JM80.
PRIDEiQ9JM80.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64019.
KEGGirno:64019.

Organism-specific databases

CTDi55824.
RGDi620394. Pag1.

Phylogenomic databases

eggNOGiENOG4111TW0. LUCA.
HOVERGENiHBG055052.
InParanoidiQ9JM80.
PhylomeDBiQ9JM80.

Miscellaneous databases

PROiQ9JM80.

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_RAT
AccessioniPrimary (citable) accession number: Q9JM80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

In contrast to the human ortholog, does not seem to interact with FYN.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.