PIGR_HUMAN - dbPTM
PIGR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIGR_HUMAN
UniProt AC P01833
Protein Name Polymeric immunoglobulin receptor
Gene Name PIGR
Organism Homo sapiens (Human).
Sequence Length 764
Subcellular Localization Cell membrane
Single-pass type I membrane protein.
Secretory component: Secreted.
Protein Description This receptor binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment..
Protein Sequence MLLFVLTCLLAVFPAISTKSPIFGPEEVNSVEGNSVSITCYYPPTSVNRHTRKYWCRQGARGGCITLISSEGYVSSKYAGRANLTNFPENGTFVVNIAQLSQDDSGRYKCGLGINSRGLSFDVSLEVSQGPGLLNDTKVYTVDLGRTVTINCPFKTENAQKRKSLYKQIGLYPVLVIDSSGYVNPNYTGRIRLDIQGTGQLLFSVVINQLRLSDAGQYLCQAGDDSNSNKKNADLQVLKPEPELVYEDLRGSVTFHCALGPEVANVAKFLCRQSSGENCDVVVNTLGKRAPAFEGRILLNPQDKDGSFSVVITGLRKEDAGRYLCGAHSDGQLQEGSPIQAWQLFVNEESTIPRSPTVVKGVAGGSVAVLCPYNRKESKSIKYWCLWEGAQNGRCPLLVDSEGWVKAQYEGRLSLLEEPGNGTFTVILNQLTSRDAGFYWCLTNGDTLWRTTVEIKIIEGEPNLKVPGNVTAVLGETLKVPCHFPCKFSSYEKYWCKWNNTGCQALPSQDEGPSKAFVNCDENSRLVSLTLNLVTRADEGWYWCGVKQGHFYGETAAVYVAVEERKAAGSRDVSLAKADAAPDEKVLDSGFREIENKAIQDPRLFAEEKAVADTRDQADGSRASVDSGSSEEQGGSSRALVSTLVPLGLVLAVGAVAVGVARARHRKNVDRVSIRSYRTDISMSDFENSREFGANDNMGASSITQETSLGGKEEFVATTESTTETKEPKKAKRSSKEEAEMAYKDFLLQSSTVAAEAQDGPQEA
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
64S-nitrosylationRQGARGGCITLISSE
CCCCCCCEEEEECCC		2.0925040305
66PhosphorylationGARGGCITLISSEGY
CCCCCEEEEECCCCC		23.3228102081
69PhosphorylationGGCITLISSEGYVSS
CCEEEEECCCCCCCC		26.0028102081
70PhosphorylationGCITLISSEGYVSSK
CEEEEECCCCCCCCC		28.2228102081
73PhosphorylationTLISSEGYVSSKYAG
EEECCCCCCCCCCCC		7.9728102081
75PhosphorylationISSEGYVSSKYAGRA
ECCCCCCCCCCCCCC		16.7828102081
76PhosphorylationSSEGYVSSKYAGRAN
CCCCCCCCCCCCCCC		21.4628102081
83N-linked_GlycosylationSKYAGRANLTNFPEN
CCCCCCCCCCCCCCC		46.1415084671
83N-linked_GlycosylationSKYAGRANLTNFPEN
CCCCCCCCCCCCCCC		46.1415084671
90N-linked_GlycosylationNLTNFPENGTFVVNI
CCCCCCCCCEEEEEE		55.8515084671
90N-linked_GlycosylationNLTNFPENGTFVVNI
CCCCCCCCCEEEEEE		55.8515084671
116PhosphorylationKCGLGINSRGLSFDV
CCCCEECCCCCEEEE		26.2922210691
124PhosphorylationRGLSFDVSLEVSQGP
CCCEEEEEEEECCCC		22.2122210691
128PhosphorylationFDVSLEVSQGPGLLN
EEEEEEECCCCCCCC		21.75-
135N-linked_GlycosylationSQGPGLLNDTKVYTV
CCCCCCCCCCEEEEE		61.0118780401
135N-linked_GlycosylationSQGPGLLNDTKVYTV
CCCCCCCCCCEEEEE		61.0110556562
137PhosphorylationGPGLLNDTKVYTVDL
CCCCCCCCEEEEEEC		22.72-
147PhosphorylationYTVDLGRTVTINCPF
EEEECCCEEEEECCC		21.8722210691
149PhosphorylationVDLGRTVTINCPFKT
EECCCEEEEECCCCC		13.08-
186N-linked_GlycosylationSSGYVNPNYTGRIRL
CCCCCCCCCCCEEEE		41.6218780401
186N-linked_GlycosylationSSGYVNPNYTGRIRL
CCCCCCCCCCCEEEE		41.6218780401
220S-nitrosylationSDAGQYLCQAGDDSN
CCHHHHHHHCCCCCC		1.9125040305
274PhosphorylationAKFLCRQSSGENCDV
HHHHHHHCCCCCCCE		22.4326657352
275PhosphorylationKFLCRQSSGENCDVV
HHHHHHCCCCCCCEE		41.6126657352
285PhosphorylationNCDVVVNTLGKRAPA
CCCEEEECCCCCCCC		25.8520068231
313PhosphorylationGSFSVVITGLRKEDA
CCEEEEEECCCHHHC		20.6724719451
323PhosphorylationRKEDAGRYLCGAHSD
CHHHCCCEECEECCC		12.86-
350PhosphorylationQLFVNEESTIPRSPT
EEECCCCCCCCCCCC		26.00-
351PhosphorylationLFVNEESTIPRSPTV
EECCCCCCCCCCCCE		37.98-
355PhosphorylationEESTIPRSPTVVKGV
CCCCCCCCCCEEECC		21.4025278378
357PhosphorylationSTIPRSPTVVKGVAG
CCCCCCCCEEECCCC		38.9025278378
366PhosphorylationVKGVAGGSVAVLCPY
EECCCCCCEEEEECC		13.1425278378
373PhosphorylationSVAVLCPYNRKESKS
CEEEEECCCCCCCCC		26.9720068231
385S-nitrosylationSKSIKYWCLWEGAQN
CCCCEEEEEECCHHC		2.6225040305
395S-nitrosylationEGAQNGRCPLLVDSE
CCHHCCCCCEEECCC		2.7025040305
421N-linked_GlycosylationSLLEEPGNGTFTVIL
EEEEECCCCEEEEEE		57.9815084671
421N-linked_GlycosylationSLLEEPGNGTFTVIL
EEEEECCCCEEEEEE		57.9815084671
469N-linked_GlycosylationPNLKVPGNVTAVLGE
CCCCCCCCEEEEECC		23.1515084671
469N-linked_GlycosylationPNLKVPGNVTAVLGE
CCCCCCCCEEEEECC		23.1515084671
489PhosphorylationCHFPCKFSSYEKYWC
CCCCCCCCCCCEEEE		19.9427251275
490PhosphorylationHFPCKFSSYEKYWCK
CCCCCCCCCCEEEEE		40.2127251275
499N-linked_GlycosylationEKYWCKWNNTGCQAL
CEEEEEECCCCCCCC		22.9818780401
499N-linked_GlycosylationEKYWCKWNNTGCQAL
CEEEEEECCCCCCCC		22.9818780401
544S-nitrosylationADEGWYWCGVKQGHF
CCCCEEEEEEECCEE		2.3525040305
555PhosphorylationQGHFYGETAAVYVAV
CCEEECCEEEEEEEH		18.6324719451
570PhosphorylationEERKAAGSRDVSLAK
HHHHHCCCCCCCHHH		22.1524719451
574PhosphorylationAAGSRDVSLAKADAA
HCCCCCCCHHHCCCC		27.2221299198
589PhosphorylationPDEKVLDSGFREIEN
CCHHHHCCCHHHHHH		35.3521299198
624PhosphorylationQADGSRASVDSGSSE
CCCCCCEECCCCCCC		25.9121406692
627PhosphorylationGSRASVDSGSSEEQG
CCCEECCCCCCCCCC		38.1221406692
629PhosphorylationRASVDSGSSEEQGGS
CEECCCCCCCCCCCC		38.2329759185
630PhosphorylationASVDSGSSEEQGGSS
EECCCCCCCCCCCCC		48.9921406692
636PhosphorylationSSEEQGGSSRALVST
CCCCCCCCCHHHHHH		24.3921406692
637PhosphorylationSEEQGGSSRALVSTL
CCCCCCCCHHHHHHH		25.5021406692
673PhosphorylationRKNVDRVSIRSYRTD
CCCCCCEEEEEECCC		17.1230183078
676PhosphorylationVDRVSIRSYRTDISM
CCCEEEEEECCCCCH		19.8024670416
677PhosphorylationDRVSIRSYRTDISMS
CCEEEEEECCCCCHH		14.0028102081
679PhosphorylationVSIRSYRTDISMSDF
EEEEEECCCCCHHHC		29.4726657352
682PhosphorylationRSYRTDISMSDFENS
EEECCCCCHHHCCCC		18.2926657352
684PhosphorylationYRTDISMSDFENSRE
ECCCCCHHHCCCCCC		32.1528857561
689PhosphorylationSMSDFENSREFGAND
CHHHCCCCCCCCCCC		26.4529759185
701PhosphorylationANDNMGASSITQETS
CCCCCCCCCCEEECC		19.2826657352
702PhosphorylationNDNMGASSITQETSL
CCCCCCCCCEEECCC		29.1726657352
704PhosphorylationNMGASSITQETSLGG
CCCCCCCEEECCCCC		23.4626657352
707PhosphorylationASSITQETSLGGKEE
CCCCEEECCCCCEEE		21.3128348404
708PhosphorylationSSITQETSLGGKEEF
CCCEEECCCCCEEEE		25.0228348404
718PhosphorylationGKEEFVATTESTTET
CEEEEEEECCCCCCC		26.2923312004
719PhosphorylationKEEFVATTESTTETK
EEEEEEECCCCCCCC		20.4323312004
721PhosphorylationEFVATTESTTETKEP
EEEEECCCCCCCCCC		38.2423312004
722PhosphorylationFVATTESTTETKEPK
EEEECCCCCCCCCCC		23.5523312004
723PhosphorylationVATTESTTETKEPKK
EEECCCCCCCCCCCC		51.4323312004
725PhosphorylationTTESTTETKEPKKAK
ECCCCCCCCCCCCCC		38.3223312004
734PhosphorylationEPKKAKRSSKEEAEM
CCCCCCCCCHHHHHH		45.0930108239
735PhosphorylationPKKAKRSSKEEAEMA
CCCCCCCCHHHHHHH		48.3927794612
743PhosphorylationKEEAEMAYKDFLLQS
HHHHHHHHHHHHHHH		15.1328857561
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

Oops, there are no upstream regulatory protein records of PIGR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIGR_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 PIGR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PIGR_HUMAN !!
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 PIGR_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-421 AND ASN-469, AND MASSSPECTROMETRY.
"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry.";
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
Proteomics 8:3833-3847(2008).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-135;ASN-186; ASN-421; ASN-469 AND ASN-499, AND MASS SPECTROMETRY.
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry.";
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.;
J. Proteome Res. 5:1493-1503(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-186;ASN-421; ASN-469 AND ASN-499, AND MASS SPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-90; ASN-421 AND ASN-469,AND MASS SPECTROMETRY.
"A proteomic analysis of human bile.";
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
Mol. Cell. Proteomics 3:715-728(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-421 ANDASN-469, AND MASS SPECTROMETRY.
"The primary structure of human free secretory component and thearrangement of disulfide bonds.";
Eiffert H., Quentin E., Decker J., Hillemeir S., Hufschmidt M.,Klingmueller D., Weber M.H., Hilschmann N.;
Hoppe-Seyler's Z. Physiol. Chem. 365:1489-1495(1984).
Cited for: PROTEIN SEQUENCE OF 19-577, VARIANT SER-365, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-83; ASN-90; ASN-135; ASN-186; ASN-421; ASN-469AND ASN-499.

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