PHAG1_HUMAN - dbPTM
PHAG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHAG1_HUMAN
UniProt AC Q9NWQ8
Protein Name Phosphoprotein associated with glycosphingolipid-enriched microdomains 1
Gene Name PAG1
Organism Homo sapiens (Human).
Sequence Length 432
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 MGPAGSLLGSGQMQITLWGSLAAVAIFFVITFLIFLCSSCDREKKPRQHSGDHENLMNVPSDKEMFSRSVTSLATDAPASSEQNGALTNGDILSEDSTLTCMQHYEEVQTSASDLLDSQDSTGKPKCHQSRELPRIPPESAVDTMLTARSVDGDQGLGMEGPYEVLKDSSSQENMVEDCLYETVKEIKEVAAAAHLEKGHSGKAKSTSASKELPGPQTEGKAEFAEYASVDRNKKCRQSVNVESILGNSCDPEEEAPPPVPVKLLDENENLQEKEGGEAEESATDTTSETNKRFSSLSYKSREEDPTLTEEEISAMYSSVNKPGQLVNKSGQSLTVPESTYTSIQGDPQRSPSSCNDLYATVKDFEKTPNSTLPPAGRPSEEPEPDYEAIQTLNREEEKATLGTNGHHGLVPKENDYESISDLQQGRDITRL
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
37S-palmitoylationITFLIFLCSSCDREK
HHHHHHHHHHCCCCC		1.6410790433
40S-palmitoylationLIFLCSSCDREKKPR
HHHHHHHCCCCCCCC		3.0810790433
50PhosphorylationEKKPRQHSGDHENLM
CCCCCCCCCCCHHHC		37.2626657352
61PhosphorylationENLMNVPSDKEMFSR
HHHCCCCCCHHHHHH		57.9620164059
63UbiquitinationLMNVPSDKEMFSRSV
HCCCCCCHHHHHHHH		56.25-
67PhosphorylationPSDKEMFSRSVTSLA
CCCHHHHHHHHHHHH		23.4930108239
69PhosphorylationDKEMFSRSVTSLATD
CHHHHHHHHHHHHCC		28.6626074081
71PhosphorylationEMFSRSVTSLATDAP
HHHHHHHHHHHCCCC		21.1926074081
72PhosphorylationMFSRSVTSLATDAPA
HHHHHHHHHHCCCCC		17.53-
80PhosphorylationLATDAPASSEQNGAL
HHCCCCCCHHHCCCC		33.09-
97PhosphorylationGDILSEDSTLTCMQH
CCCCCCCCCCHHHHH		22.67-
98PhosphorylationDILSEDSTLTCMQHY
CCCCCCCCCHHHHHH		38.11-
105PhosphorylationTLTCMQHYEEVQTSA
CCHHHHHHHHHHHCH		9.2625884760
110O-linked_GlycosylationQHYEEVQTSASDLLD
HHHHHHHHCHHHHHC		31.28OGP
130PhosphorylationGKPKCHQSRELPRIP
CCCCCCCCCCCCCCC		12.2128348404
150PhosphorylationDTMLTARSVDGDQGL
HHHHCCEECCCCCCC		23.3022115753
163PhosphorylationGLGMEGPYEVLKDSS
CCCCCCCCHHHCCCC		29.5328674151
169PhosphorylationPYEVLKDSSSQENMV
CCHHHCCCCCCCCHH		30.2430108239
170PhosphorylationYEVLKDSSSQENMVE
CHHHCCCCCCCCHHH		46.2930108239
171PhosphorylationEVLKDSSSQENMVED
HHHCCCCCCCCHHHH		45.5322115753
181PhosphorylationNMVEDCLYETVKEIK
CHHHHHHHHHHHHHH		18.8419605366
183PhosphorylationVEDCLYETVKEIKEV
HHHHHHHHHHHHHHH		24.2629970186
201PhosphorylationAHLEKGHSGKAKSTS
HHHHCCCCCCCCCCC		51.1323401153
218O-linked_GlycosylationKELPGPQTEGKAEFA
CCCCCCCCCCHHHHH		50.25OGP
227PhosphorylationGKAEFAEYASVDRNK
CHHHHHHHHCCCCCC		10.7625159151
229PhosphorylationAEFAEYASVDRNKKC
HHHHHHHCCCCCCCH		24.5323401153
239PhosphorylationRNKKCRQSVNVESIL
CCCCHHCCCCHHHHC		9.0529255136
244PhosphorylationRQSVNVESILGNSCD
HCCCCHHHHCCCCCC		20.8729255136
249PhosphorylationVESILGNSCDPEEEA
HHHHCCCCCCCCCCC		20.3526074081
282PhosphorylationEGGEAEESATDTTSE
CCCCCCHHCCCCCCH		28.1528192239
284PhosphorylationGEAEESATDTTSETN
CCCCHHCCCCCCHHH		43.0630108239
286PhosphorylationAEESATDTTSETNKR
CCHHCCCCCCHHHHH		28.0623401153
287PhosphorylationEESATDTTSETNKRF
CHHCCCCCCHHHHHH		27.6329255136
288PhosphorylationESATDTTSETNKRFS
HHCCCCCCHHHHHHH		44.5123401153
290PhosphorylationATDTTSETNKRFSSL
CCCCCCHHHHHHHHC		45.8929255136
295PhosphorylationSETNKRFSSLSYKSR
CHHHHHHHHCCCCCC		34.1120164059
296PhosphorylationETNKRFSSLSYKSRE
HHHHHHHHCCCCCCC		20.7223401153
298PhosphorylationNKRFSSLSYKSREED
HHHHHHCCCCCCCCC		32.2528355574
299PhosphorylationKRFSSLSYKSREEDP
HHHHHCCCCCCCCCC		20.4826074081
301PhosphorylationFSSLSYKSREEDPTL
HHHCCCCCCCCCCCC		36.3722115753
307PhosphorylationKSREEDPTLTEEEIS
CCCCCCCCCCHHHHH		59.6428450419
309PhosphorylationREEDPTLTEEEISAM
CCCCCCCCHHHHHHH		43.7728450419
314PhosphorylationTLTEEEISAMYSSVN
CCCHHHHHHHHHHCC		15.4028152594
317PhosphorylationEEEISAMYSSVNKPG
HHHHHHHHHHCCCCC		9.4927155012
318PhosphorylationEEISAMYSSVNKPGQ
HHHHHHHHHCCCCCC		18.0927155012
319PhosphorylationEISAMYSSVNKPGQL
HHHHHHHHCCCCCCE		16.5427273156
330PhosphorylationPGQLVNKSGQSLTVP
CCCEECCCCCCCCCC		36.5426356563
333PhosphorylationLVNKSGQSLTVPEST
EECCCCCCCCCCHHH		29.5426356563
335PhosphorylationNKSGQSLTVPESTYT
CCCCCCCCCCHHHCC		38.9826356563
339PhosphorylationQSLTVPESTYTSIQG
CCCCCCHHHCCCCCC		22.2028796482
340PhosphorylationSLTVPESTYTSIQGD
CCCCCHHHCCCCCCC		29.2025884760
340O-linked_GlycosylationSLTVPESTYTSIQGD
CCCCCHHHCCCCCCC		29.20OGP
341PhosphorylationLTVPESTYTSIQGDP
CCCCHHHCCCCCCCC		14.0427273156
342PhosphorylationTVPESTYTSIQGDPQ
CCCHHHCCCCCCCCC		21.3128796482
343PhosphorylationVPESTYTSIQGDPQR
CCHHHCCCCCCCCCC		11.5128796482
351PhosphorylationIQGDPQRSPSSCNDL
CCCCCCCCCCCCCHH		24.7228450419
353PhosphorylationGDPQRSPSSCNDLYA
CCCCCCCCCCCHHEE		49.0919605366
354PhosphorylationDPQRSPSSCNDLYAT
CCCCCCCCCCHHEEH		21.9619605366
359PhosphorylationPSSCNDLYATVKDFE
CCCCCHHEEHHHHHH		11.7727273156
361PhosphorylationSCNDLYATVKDFEKT
CCCHHEEHHHHHHHC		17.9628796482
368PhosphorylationTVKDFEKTPNSTLPP
HHHHHHHCCCCCCCC		22.0926074081
371PhosphorylationDFEKTPNSTLPPAGR
HHHHCCCCCCCCCCC		32.3126074081
372PhosphorylationFEKTPNSTLPPAGRP
HHHCCCCCCCCCCCC		50.3426074081
380PhosphorylationLPPAGRPSEEPEPDY
CCCCCCCCCCCCCCH		53.9126074081
387PhosphorylationSEEPEPDYEAIQTLN
CCCCCCCHHHHHHCC		20.2722115753
392PhosphorylationPDYEAIQTLNREEEK
CCHHHHHHCCHHHHH		21.6429978859
401PhosphorylationNREEEKATLGTNGHH
CHHHHHHCCCCCCCC		36.4726356563
404PhosphorylationEEKATLGTNGHHGLV
HHHHCCCCCCCCCCC		40.9326356563
417PhosphorylationLVPKENDYESISDLQ
CCCCCCCCCCHHHHH		24.1325159151
419PhosphorylationPKENDYESISDLQQG
CCCCCCCCHHHHHCC		22.5927155012
421PhosphorylationENDYESISDLQQGRD
CCCCCCHHHHHCCCC		41.3628152594
430PhosphorylationLQQGRDITRL-----
HHCCCCCCCC-----		30.1522115753
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
105YPhosphorylationKinaseLYNP07948
Uniprot
317YPhosphorylationKinaseFYNP06241
Uniprot
317YPhosphorylationKinaseLYNP07948
Uniprot
317YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHAG1_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSK_HUMANCSKphysical
10790433
FYN_HUMANFYNphysical
10790433
NHRF1_HUMANSLC9A3R1physical
11684085
PHAG1_HUMANPAG1physical
12665526
CSK_HUMANCSKphysical
12665526
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHAG1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-163; TYR-227; TYR-317;TYR-359; TYR-387 AND TYR-417, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-227 AND TYR-341, ANDMASS SPECTROMETRY.
"Oncogenic association of the Cbp/PAG adaptor protein with the Lyntyrosine kinase in human B-NHL rafts.";
Tauzin S., Ding H., Khatib K., Ahmad I., Burdevet D.,van Echten-Deckert G., Lindquist J.A., Schraven B., Din N.U.,Borisch B., Hoessli D.C.;
Blood 111:2310-2320(2008).
Cited for: PHOSPHORYLATION AT TYR-317, INTERACTION WITH LYN AND STAT3, ANDSUBCELLULAR LOCATION.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-417, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-317; TYR-341; TYR-359AND TYR-417, AND MASS SPECTROMETRY.
"Phosphoprotein associated with glycosphingolipid-enrichedmicrodomains (PAG), a novel ubiquitously expressed transmembraneadaptor protein, binds the protein tyrosine kinase csk and is involvedin regulation of T cell activation.";
Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V.,Angelisova P., Scherer J., Shevchenko A., Shevchenko A., Hilgert I.,Cerny J., Drbal K., Kuramitsu Y., Horejsi V., Schraven B.;
J. Exp. Med. 191:1591-1604(2000).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 264-274,IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-317,TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-37 ANDCYS-40, MUTAGENESIS OF TYR-105; TYR-163; TYR-181; TYR-227; TYR-299;TYR-317; TYR-341; TYR-359; TYR-387 AND TYR-417, INTERACTION WITH FYNAND CSK, AND FUNCTION.

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