| Tag |
Content |
LipidDB ID |
LipidDB-10090-00030 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
4.71 |
Molecular Weight |
46549.47 |
Genbank Protein ID |
|
Genbank Nucleotide ID |
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Protein Name |
Phosphoprotein associated with glycosphingolipid-enriched microdomains 1 |
Protein Synonyms/Alias |
Csk-binding protein; Transmembrane phosphoprotein Cbp; |
Gene Name |
Pag1 |
Gene Synonyms/Alias |
Cbp; Pag; |
Created Date |
20-DEC-2005 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
39 | Canonical | ITFLVLLCSTCDREK | [1] | S-Palmitoylation |
|
Organism |
Mus musculus (Mouse) |
NCBI Taxa ID |
10090 |
Reference |
[1] Predicted from GPS-Lipid
|
Functional Description |
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. |
Sequence Annotation |
Topological domain: 1 17 Extracellular.
Transmembrane: 18 38 Helical; Signal-anchor for type IIImembrane protein.
Topological domain: 39 429 Cytoplasmic.
Region: 314 317 Interaction with CSK.
Region: 427 429 Interaction with SLC9A3R1.
Modified residue: 107 107 Phosphotyrosine; by LYN.
Modified residue: 165 165 Phosphotyrosine.
Modified residue: 183 183 Phosphotyrosine.
Modified residue: 224 224 Phosphotyrosine.
Modified residue: 226 226 Phosphoserine.
Modified residue: 314 314 Phosphotyrosine; by FYN.
Modified residue: 356 356 Phosphotyrosine.
Modified residue: 379 379 Phosphoserine.
Modified residue: 386 386 Phosphotyrosine.
Modified residue: 414 414 Phosphotyrosine.
|
Protein Length |
429 AA. |
Protein Sequence
(Canonical) |
MGPAGSVLSS GQMQMQMVLW GSLAAVAMFF LITFLVLLCS TCDREKKPRQ HSGDHENLMN 60
VPSDKDMFSH SATSLTTDAL ASSEQNGVLT NGDILSEDST LTCMQHYEEV QTSASDLLDS 120
QDSTGKAKCH QSRELPRIPP ENAVDEILTA RAADTELGPG VEGPYEVLKD SSSQENMVED 180
CLYETVKEIK EVADKGQGGK SKSTSALKEL QGAPMEGKAD FAEYASVDRN KKCRHSANAE 240
SILGTCSDLD EESPPPVPVK LLDENANLPQ EGGGQAEEQA AEGTGGHSKR FSSLSYKSRE 300
EDPTLTEEEI SAMYSSVNKP GQSAHKPGPC MKGPESACHS MKGLPQRSSS SCNDLYATVK 360
DFEKTPNSIS TLPPARRPSE EPEPDYEAIQ TLNREDEKVP LETNGHHVPK ESDYESIGDL 420
QQCRDVTRL 429
|
FASTA
(Canonical) |
>LipidDB-10090-00030|Q3U1F9
MGPAGSVLSSGQMQMQMVLWGSLAAVAMFFLITFLVLLCSTCDREKKPRQHSGDHENLMN
VPSDKDMFSHSATSLTTDALASSEQNGVLTNGDILSEDSTLTCMQHYEEVQTSASDLLDS
QDSTGKAKCHQSRELPRIPPENAVDEILTARAADTELGPGVEGPYEVLKDSSSQENMVED
CLYETVKEIKEVADKGQGGKSKSTSALKELQGAPMEGKADFAEYASVDRNKKCRHSANAE
SILGTCSDLDEESPPPVPVKLLDENANLPQEGGGQAEEQAAEGTGGHSKRFSSLSYKSRE
EDPTLTEEEISAMYSSVNKPGQSAHKPGPCMKGPESACHSMKGLPQRSSSSCNDLYATVK
DFEKTPNSISTLPPARRPSEEPEPDYEAIQTLNREDEKVPLETNGHHVPKESDYESIGDL
QQCRDVTRL
|
Gene Ontology |
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW GO:0045121; C:membrane raft; TAS:HGNC GO:0005886; C:plasma membrane; TAS:HGNC GO:0002376; P:immune system process; IEA:UniProtKB-KW GO:0035556; P:intracellular signal transduction; TAS:HGNC GO:0050868; P:negative regulation of T cell activation; IDA:HGNC GO:0050863; P:regulation of T cell activation; TAS:HGNC |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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