PHAG1_RAT - dbPTM
PHAG1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHAG1_RAT
UniProt AC Q9JM80
Protein Name Phosphoprotein associated with glycosphingolipid-enriched microdomains 1
Gene Name Pag1
Organism Rattus norvegicus (Rat).
Sequence Length 424
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 MGPAGSALSSGQMQMQMVLWGSLAAVAMFFLITFLILLCSSCDRDKKPRQHSGDHESLMNVPSDKEMFSHSATSLTTDALASSEQNGVLTNGDILSEDSTMTCMQHYEEVQTSASDLLDSQDSTGKAKCHQSRELPRIPPENAVDAMLTARAADGDSGPGVEGPYEVLKDSSSQENMVEDCLYETVKEIKEVADKSQGGKSKSTSALKELQGAHAEGKADFAEYASVDRNKKCRHSTNAESILGTSSDLDEETPPPVPVKLLDENANLPEKGEHGAEEQAPEAPSGHSKRFSSLSYKSREEDPTLTEEEISAMYSSVNKPGQSAHKPGPESTCQCPQGPPQRSSSSCNDLYATVKDFEKTPNSISMLPPARRPGEEPEPDYEAIQTLNREDDKVPLGTNGHLVPKENDYESIGDLQQGRDVTRL
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-palmitoylationITFLILLCSSCDRDK
HHHHHHHHHHCCCCC		2.23-
42S-palmitoylationLILLCSSCDRDKKPR
HHHHHHHCCCCCCCC		2.60-
52PhosphorylationDKKPRQHSGDHESLM
CCCCCCCCCCHHHHH		37.2627097102
57PhosphorylationQHSGDHESLMNVPSD
CCCCCHHHHHCCCCC		29.5127097102
63PhosphorylationESLMNVPSDKEMFSH
HHHHCCCCCHHHHHC		57.9622673903
107PhosphorylationTMTCMQHYEEVQTSA
CCHHHHHHHHHHHCH		9.2616920712
157PhosphorylationARAADGDSGPGVEGP
HHHCCCCCCCCCCCC		53.0327097102
165PhosphorylationGPGVEGPYEVLKDSS
CCCCCCCHHHHCCCC		29.5327097102
171PhosphorylationPYEVLKDSSSQENMV
CHHHHCCCCCCCCHH		30.2427097102
172PhosphorylationYEVLKDSSSQENMVE
HHHHCCCCCCCCHHH		46.2927097102
173PhosphorylationEVLKDSSSQENMVED
HHHCCCCCCCCHHHH		45.5327097102
183PhosphorylationNMVEDCLYETVKEIK
CHHHHHHHHHHHHHH		18.8427097102
185PhosphorylationVEDCLYETVKEIKEV
HHHHHHHHHHHHHHH		24.2627097102
201PhosphorylationDKSQGGKSKSTSALK
HHHCCCCCHHHHHHH		34.8025575281
203PhosphorylationSQGGKSKSTSALKEL
HCCCCCHHHHHHHHH		34.3825575281
204PhosphorylationQGGKSKSTSALKELQ
CCCCCHHHHHHHHHH		23.0425575281
205PhosphorylationGGKSKSTSALKELQG
CCCCHHHHHHHHHHH		38.4025575281
224PhosphorylationGKADFAEYASVDRNK
CCCCHHHHHCCCCCC		10.7627097102
226PhosphorylationADFAEYASVDRNKKC
CCHHHHHCCCCCCCC		24.5329779826
236PhosphorylationRNKKCRHSTNAESIL
CCCCCCCCCCHHHHH		12.1927097102
237PhosphorylationNKKCRHSTNAESILG
CCCCCCCCCHHHHHC		32.1127097102
241PhosphorylationRHSTNAESILGTSSD
CCCCCHHHHHCCCCC		22.2427097102
245PhosphorylationNAESILGTSSDLDEE
CHHHHHCCCCCCCCC		22.9327097102
246PhosphorylationAESILGTSSDLDEET
HHHHHCCCCCCCCCC		21.7627097102
247PhosphorylationESILGTSSDLDEETP
HHHHCCCCCCCCCCC		41.8727097102
253PhosphorylationSSDLDEETPPPVPVK
CCCCCCCCCCCCCCE		38.7627097102
292PhosphorylationSGHSKRFSSLSYKSR
CCCCCCCCCCCCCCC		34.1127097102
293PhosphorylationGHSKRFSSLSYKSRE
CCCCCCCCCCCCCCC		20.7227097102
295PhosphorylationSKRFSSLSYKSREED
CCCCCCCCCCCCCCC		32.2527097102
296PhosphorylationKRFSSLSYKSREEDP
CCCCCCCCCCCCCCC		20.4827097102
298PhosphorylationFSSLSYKSREEDPTL
CCCCCCCCCCCCCCC		36.3727097102
304PhosphorylationKSREEDPTLTEEEIS
CCCCCCCCCCHHHHH		59.6430181290
306PhosphorylationREEDPTLTEEEISAM
CCCCCCCCHHHHHHH		43.7730181290
311PhosphorylationTLTEEEISAMYSSVN
CCCHHHHHHHHHHCC		15.4030181290
314PhosphorylationEEEISAMYSSVNKPG
HHHHHHHHHHCCCCC		9.4910918051
315PhosphorylationEEISAMYSSVNKPGQ
HHHHHHHHHCCCCCC		18.0930181290
316PhosphorylationEISAMYSSVNKPGQS
HHHHHHHHCCCCCCC		16.5430181290
323PhosphorylationSVNKPGQSAHKPGPE
HCCCCCCCCCCCCCC		37.95-
343PhosphorylationPQGPPQRSSSSCNDL
CCCCCCCCCCCCHHH		29.3527097102
344PhosphorylationQGPPQRSSSSCNDLY
CCCCCCCCCCCHHHH		28.5827097102
345PhosphorylationGPPQRSSSSCNDLYA
CCCCCCCCCCHHHHH		39.9127097102
346PhosphorylationPPQRSSSSCNDLYAT
CCCCCCCCCHHHHHH		20.9121738781
351PhosphorylationSSSCNDLYATVKDFE
CCCCHHHHHHHHHHH		11.7727097102
381PhosphorylationGEEPEPDYEAIQTLN
CCCCCCCHHHHHHCC		20.2727097102
386PhosphorylationPDYEAIQTLNREDDK
CCHHHHHHCCCCCCC		21.6427097102
409PhosphorylationLVPKENDYESIGDLQ
CCCCCCCCCCCCCHH		24.1327097102
411PhosphorylationPKENDYESIGDLQQG
CCCCCCCCCCCHHCC		26.1627097102
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
107YPhosphorylationKinaseLYNQ07014
Uniprot
314YPhosphorylationKinaseFYNQ62844
Uniprot
314YPhosphorylationKinaseLYNP25911
PSP
314YPhosphorylationKinaseLYNQ07014
Uniprot
314YPhosphorylationKinaseSRCQ9WUD9
PSP
381YPhosphorylationKinaseLYNP25911
PSP
409YPhosphorylationKinaseLYNP25911
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHAG1_RAT !!
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_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSK_RATCskphysical
10801129
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHAG1_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Csk-binding protein mediates sequential enzymatic down-regulation anddegradation of Lyn in erythropoietin-stimulated cells.";
Ingley E., Schneider J.R., Payne C.J., McCarthy D.J., Harder K.W.,Hibbs M.L., Klinken S.P.;
J. Biol. Chem. 281:31920-31929(2006).
Cited for: INTERACTION WITH LYN AND CSK, AND PHOSPHORYLATION AT TYR-107 ANDTYR-314.
"Transmembrane phosphoprotein Cbp positively regulates the activity ofthe carboxyl-terminal Src kinase, Csk.";
Takeuchi S., Takayama Y., Ogawa A., Tamura K., Okada M.;
J. Biol. Chem. 275:29183-29186(2000).
Cited for: PHOSPHORYLATION AT TYR-165; TYR-183; TYR-224; TYR-314; TYR-381 ANDTYR-409, AND FUNCTION.
"Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases.";
Kawabuchi M., Satomi Y., Takao T., Shimonishi Y., Nada S., Nagai K.,Tarakhovsky A., Okada M.;
Nature 404:999-1003(2000).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY,INTERACTION WITH CSK, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,MUTAGENESIS OF TYR-107; TYR-165; TYR-183; TYR-224; TYR-296; TYR-314;TYR-351; TYR-381 AND TYR-409, PHOSPHORYLATION AT TYR-314, ANDFUNCTION.

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