PHAG1_MOUSE - dbPTM
PHAG1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHAG1_MOUSE
UniProt AC Q3U1F9
Protein Name Phosphoprotein associated with glycosphingolipid-enriched microdomains 1
Gene Name Pag1
Organism Mus musculus (Mouse).
Sequence Length 429
Subcellular Localization Cell membrane
Single-pass type III membrane protein . Present in lipid rafts.
Protein 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..
Protein Sequence MGPAGSVLSSGQMQMQMVLWGSLAAVAMFFLITFLVLLCSTCDREKKPRQHSGDHENLMNVPSDKDMFSHSATSLTTDALASSEQNGVLTNGDILSEDSTLTCMQHYEEVQTSASDLLDSQDSTGKAKCHQSRELPRIPPENAVDEILTARAADTELGPGVEGPYEVLKDSSSQENMVEDCLYETVKEIKEVADKGQGGKSKSTSALKELQGAPMEGKADFAEYASVDRNKKCRHSANAESILGTCSDLDEESPPPVPVKLLDENANLPQEGGGQAEEQAAEGTGGHSKRFSSLSYKSREEDPTLTEEEISAMYSSVNKPGQSAHKPGPCMKGPESACHSMKGLPQRSSSSCNDLYATVKDFEKTPNSISTLPPARRPSEEPEPDYEAIQTLNREDEKVPLETNGHHVPKESDYESIGDLQQCRDVTRL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
39S-palmitoylationITFLVLLCSTCDREK
HHHHHHHHHHCCCCC		2.50-
42S-palmitoylationLVLLCSTCDREKKPR
HHHHHHHCCCCCCCC		2.39-
52PhosphorylationEKKPRQHSGDHENLM
CCCCCCCCCCCCCCC		37.2625266776
63PhosphorylationENLMNVPSDKDMFSH
CCCCCCCCCHHHHCC		53.6729899451
107PhosphorylationTLTCMQHYEEVQTSA
CCHHHHHHHHHHHCH		9.26-
165PhosphorylationGPGVEGPYEVLKDSS
CCCCCCCHHHHCCCC		29.5325177544
171PhosphorylationPYEVLKDSSSQENMV
CHHHHCCCCCCCCHH		30.2428833060
172PhosphorylationYEVLKDSSSQENMVE
HHHHCCCCCCCCHHH		46.2928833060
173PhosphorylationEVLKDSSSQENMVED
HHHCCCCCCCCHHHH		45.5328833060
183PhosphorylationNMVEDCLYETVKEIK
CHHHHHHHHHHHHHH		18.8428833060
185PhosphorylationVEDCLYETVKEIKEV
HHHHHHHHHHHHHHH		24.2628833060
201PhosphorylationDKGQGGKSKSTSALK
HCCCCCCCCCHHHHH		34.8026102028
203PhosphorylationGQGGKSKSTSALKEL
CCCCCCCCHHHHHHH		34.3823140645
224PhosphorylationGKADFAEYASVDRNK
CCCCHHHHHCCCCCC		10.7625177544
226PhosphorylationADFAEYASVDRNKKC
CCHHHHHCCCCCCCC		24.5325619855
236PhosphorylationRNKKCRHSANAESIL
CCCCCCCCCCHHHHH		12.1325619855
241PhosphorylationRHSANAESILGTCSD
CCCCCHHHHHHCCCC		22.2425619855
245PhosphorylationNAESILGTCSDLDEE
CHHHHHHCCCCCCCC		12.8525619855
247PhosphorylationESILGTCSDLDEESP
HHHHHCCCCCCCCCC		40.8326824392
253PhosphorylationCSDLDEESPPPVPVK
CCCCCCCCCCCCCEE		40.4325619855
284PhosphorylationEEQAAEGTGGHSKRF
HHHHHCCCCCCCHHH		31.3428285833
288PhosphorylationAEGTGGHSKRFSSLS
HCCCCCCCHHHCCCC		28.88-
292PhosphorylationGGHSKRFSSLSYKSR
CCCCHHHCCCCCCCC		34.1121082442
293PhosphorylationGHSKRFSSLSYKSRE
CCCHHHCCCCCCCCC		20.7226824392
295PhosphorylationSKRFSSLSYKSREED
CHHHCCCCCCCCCCC		32.2522802335
296PhosphorylationKRFSSLSYKSREEDP
HHHCCCCCCCCCCCC		20.4826745281
298PhosphorylationFSSLSYKSREEDPTL
HCCCCCCCCCCCCCC		36.3720531401
304PhosphorylationKSREEDPTLTEEEIS
CCCCCCCCCCHHHHH		59.6425367039
311PhosphorylationTLTEEEISAMYSSVN
CCCHHHHHHHHHHCC		15.4025367039
314PhosphorylationEEEISAMYSSVNKPG
HHHHHHHHHHCCCCC		9.4917210649
315PhosphorylationEEISAMYSSVNKPGQ
HHHHHHHHHCCCCCC		18.0925367039
316PhosphorylationEISAMYSSVNKPGQS
HHHHHHHHCCCCCCC		16.5425367039
323PhosphorylationSVNKPGQSAHKPGPC
HCCCCCCCCCCCCCC		37.9525367039
340PhosphorylationGPESACHSMKGLPQR
CHHHHHHHCCCCCCC		23.2925266776
348PhosphorylationMKGLPQRSSSSCNDL
CCCCCCCCCCCHHHH		29.3525619855
349PhosphorylationKGLPQRSSSSCNDLY
CCCCCCCCCCHHHHH		28.5825619855
350PhosphorylationGLPQRSSSSCNDLYA
CCCCCCCCCHHHHHH		39.9125521595
351PhosphorylationLPQRSSSSCNDLYAT
CCCCCCCCHHHHHHH		20.9125521595
356PhosphorylationSSSCNDLYATVKDFE
CCCHHHHHHHHHHHH		11.7720438120
358PhosphorylationSCNDLYATVKDFEKT
CHHHHHHHHHHHHHC		17.9625619855
370PhosphorylationEKTPNSISTLPPARR
HHCCCCCCCCCCCCC		24.5829899451
379PhosphorylationLPPARRPSEEPEPDY
CCCCCCCCCCCCCCH		53.4325521595
386PhosphorylationSEEPEPDYEAIQTLN
CCCCCCCHHHHHHCC		20.2728833060
391PhosphorylationPDYEAIQTLNREDEK
CCHHHHHHCCCCCCC		21.6428833060
412PhosphorylationGHHVPKESDYESIGD
CCCCCCCCCCCCCCC		52.1725266776
414PhosphorylationHVPKESDYESIGDLQ
CCCCCCCCCCCCCHH		22.3630352176
416PhosphorylationPKESDYESIGDLQQC
CCCCCCCCCCCHHHH		26.1622817900
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
107YPhosphorylationKinaseLYNP25911
Uniprot
314YPhosphorylationKinaseFYNP39688
Uniprot
314YPhosphorylationKinaseSRCQ9WUD9
PSP
386YPhosphorylationKinaseLYNP25911
PSP
414YPhosphorylationKinaseLYNP25911
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHAG1_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PHAG1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSK_MOUSECskphysical
16920712
SOCS1_MOUSESocs1physical
16920712
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHAG1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-165; TYR-183; TYR-224AND SER-379, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND MASSSPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-224, AND MASSSPECTROMETRY.
"Shp2 regulates SRC family kinase activity and Ras/Erk activation bycontrolling Csk recruitment.";
Zhang S.Q., Yang W., Kontaridis M.I., Bivona T.G., Wen G., Araki T.,Luo J., Thompson J.A., Schraven B.L., Philips M.R., Neel B.G.;
Mol. Cell 13:341-355(2004).
Cited for: PHOSPHORYLATION AT TYR-314, AND INTERACTION WITH CSK.
"Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp,a lipid raft-associated transmembrane adaptor.";
Davidson D., Bakinowski M., Thomas M.L., Horejsi V., Veillette A.;
Mol. Cell. Biol. 23:2017-2028(2003).
Cited for: PHOSPHORYLATION AT TYR-314, MUTAGENESIS OF TYR-314, INTERACTION WITHCSK, SUBCELLULAR LOCATION, AND FUNCTION.
"Fyn is essential for tyrosine phosphorylation of Csk-bindingprotein/phosphoprotein associated with glycolipid-enrichedmicrodomains in lipid rafts in resting T cells.";
Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T.,Minaki Y., Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.;
J. Immunol. 169:2813-2817(2002).
Cited for: PHOSPHORYLATION AT TYR-314, INTERACTION WITH CSK, AND FUNCTION.

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