PXDN_HUMAN - dbPTM
PXDN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PXDN_HUMAN
UniProt AC Q92626
Protein Name Peroxidasin homolog
Gene Name PXDN
Organism Homo sapiens (Human).
Sequence Length 1479
Subcellular Localization Secreted, extracellular space, extracellular matrix . Enriched in the peritubular space of fibrotic kidneys.
Protein Description Displays low peroxidase activity and is likely to participate in H(2)O(2) metabolism and peroxidative reactions in the cardiovascular system. Plays a role in extracellular matrix formation..
Protein Sequence MAKRSRGPGRRCLLALVLFCAWGTLAVVAQKPGAGCPSRCLCFRTTVRCMHLLLEAVPAVAPQTSILDLRFNRIREIQPGAFRRLRNLNTLLLNNNQIKRIPSGAFEDLENLKYLYLYKNEIQSIDRQAFKGLASLEQLYLHFNQIETLDPDSFQHLPKLERLFLHNNRITHLVPGTFNHLESMKRLRLDSNTLHCDCEILWLADLLKTYAESGNAQAAAICEYPRRIQGRSVATITPEELNCERPRITSEPQDADVTSGNTVYFTCRAEGNPKPEIIWLRNNNELSMKTDSRLNLLDDGTLMIQNTQETDQGIYQCMAKNVAGEVKTQEVTLRYFGSPARPTFVIQPQNTEVLVGESVTLECSATGHPPPRISWTRGDRTPLPVDPRVNITPSGGLYIQNVVQGDSGEYACSATNNIDSVHATAFIIVQALPQFTVTPQDRVVIEGQTVDFQCEAKGNPPPVIAWTKGGSQLSVDRRHLVLSSGTLRISGVALHDQGQYECQAVNIIGSQKVVAHLTVQPRVTPVFASIPSDTTVEVGANVQLPCSSQGEPEPAITWNKDGVQVTESGKFHISPEGFLTINDVGPADAGRYECVARNTIGSASVSMVLSVNVPDVSRNGDPFVATSIVEAIATVDRAINSTRTHLFDSRPRSPNDLLALFRYPRDPYTVEQARAGEIFERTLQLIQEHVQHGLMVDLNGTSYHYNDLVSPQYLNLIANLSGCTAHRRVNNCSDMCFHQKYRTHDGTCNNLQHPMWGASLTAFERLLKSVYENGFNTPRGINPHRLYNGHALPMPRLVSTTLIGTETVTPDEQFTHMLMQWGQFLDHDLDSTVVALSQARFSDGQHCSNVCSNDPPCFSVMIPPNDSRARSGARCMFFVRSSPVCGSGMTSLLMNSVYPREQINQLTSYIDASNVYGSTEHEARSIRDLASHRGLLRQGIVQRSGKPLLPFATGPPTECMRDENESPIPCFLAGDHRANEQLGLTSMHTLWFREHNRIATELLKLNPHWDGDTIYYETRKIVGAEIQHITYQHWLPKILGEVGMRTLGEYHGYDPGINAGIFNAFATAAFRFGHTLVNPLLYRLDENFQPIAQDHLPLHKAFFSPFRIVNEGGIDPLLRGLFGVAGKMRVPSQLLNTELTERLFSMAHTVALDLAAINIQRGRDHGIPPYHDYRVYCNLSAAHTFEDLKNEIKNPEIREKLKRLYGSTLNIDLFPALVVEDLVPGSRLGPTLMCLLSTQFKRLRDGDRLWYENPGVFSPAQLTQIKQTSLARILCDNADNITRVQSDVFRVAEFPHGYGSCDEIPRVDLRVWQDCCEDCRTRGQFNAFSYHFRGRRSLEFSYQEDKPTKKTRPRKIPSVGRQGEHLSNSTSAFSTRSDASGTNDFREFVLEMQKTITDLRTQIKKLESRLSTTECVDAGGESHANNTKWKKDACTICECKDGQVTCFVEACPPATCAVPVNIPGACCPVCLQKRAEEKP
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
99UbiquitinationLLNNNQIKRIPSGAF
EECCCCCCCCCCCCC		34.21-
103PhosphorylationNQIKRIPSGAFEDLE
CCCCCCCCCCCCHHH		40.14-
118PhosphorylationNLKYLYLYKNEIQSI
HCCEEEEEHHCHHHH		9.75-
289UbiquitinationNNNELSMKTDSRLNL
CCCEECCCCCCCCCC		45.89-
292PhosphorylationELSMKTDSRLNLLDD
EECCCCCCCCCCCCC		43.85-
320UbiquitinationGIYQCMAKNVAGEVK
HHHHHHHHHCCCEEE		25.6829967540
424O-linked_GlycosylationNIDSVHATAFIIVQA
CCCCCEEEEEEEEEE		13.76OGP
483PhosphorylationDRRHLVLSSGTLRIS
CCCEEEECCCEEEEE		21.1730631047
484PhosphorylationRRHLVLSSGTLRISG
CCEEEECCCEEEEEC		31.4724719451
626PhosphorylationNGDPFVATSIVEAIA
CCCCCCHHHHHHHHH		17.4323312004
627PhosphorylationGDPFVATSIVEAIAT
CCCCCHHHHHHHHHH		18.2023312004
634PhosphorylationSIVEAIATVDRAINS
HHHHHHHHHHHHHHH		19.4723312004
640N-linked_GlycosylationATVDRAINSTRTHLF
HHHHHHHHHCCCCCC		36.02UniProtKB CARBOHYD
641PhosphorylationTVDRAINSTRTHLFD
HHHHHHHHCCCCCCC		17.1023312004
642PhosphorylationVDRAINSTRTHLFDS
HHHHHHHCCCCCCCC		34.7923312004
699N-linked_GlycosylationHGLMVDLNGTSYHYN
CCCEEECCCCCCCCC		47.43UniProtKB CARBOHYD
719N-linked_GlycosylationQYLNLIANLSGCTAH
HHHHHHHHHHCCCHH		27.96UniProtKB CARBOHYD
731N-linked_GlycosylationTAHRRVNNCSDMCFH
CHHHCCCCCCHHHCC		24.66UniProtKB CARBOHYD
740UbiquitinationSDMCFHQKYRTHDGT
CHHHCCCCCCCCCCC		28.29-
768UbiquitinationTAFERLLKSVYENGF
HHHHHHHHHHHHCCC		42.33-
865N-linked_GlycosylationFSVMIPPNDSRARSG
EEEEECCCCHHHCCC		55.31UniProtKB CARBOHYD
887PhosphorylationRSSPVCGSGMTSLLM
ECCCCCCCCHHHHHH		21.92-
890PhosphorylationPVCGSGMTSLLMNSV
CCCCCCHHHHHHHCC		21.54-
896PhosphorylationMTSLLMNSVYPREQI
HHHHHHHCCCCHHHH		14.73-
898PhosphorylationSLLMNSVYPREQINQ
HHHHHCCCCHHHHHH		9.08-
957PhosphorylationPFATGPPTECMRDEN
CCCCCCCCCCCCCCC		44.97-
1004UbiquitinationRIATELLKLNPHWDG
CHHHHHHHHCCCCCC		59.86-
1100UbiquitinationQDHLPLHKAFFSPFR
CCCCCCCHHHCCCEE		55.35-
1104PhosphorylationPLHKAFFSPFRIVNE
CCCHHHCCCEEEECC		19.3725867546
1176PhosphorylationPYHDYRVYCNLSAAH
CCCCEEEEEECCCCC		2.6818318008
1178N-linked_GlycosylationHDYRVYCNLSAAHTF
CCEEEEEECCCCCCH		21.2419159218
1180PhosphorylationYRVYCNLSAAHTFED
EEEEEECCCCCCHHH		14.9318318008
1241UbiquitinationCLLSTQFKRLRDGDR
HHHHHHHHHCCCCCC		40.48-
1248MethylationKRLRDGDRLWYENPG
HHCCCCCCCCCCCCC		32.42115489715
1266UbiquitinationPAQLTQIKQTSLARI
HHHHHHHCHHHHHHH		37.39-
1280N-linked_GlycosylationILCDNADNITRVQSD
HHCCCCCCEEEECCC		34.81UniProtKB CARBOHYD
1337PhosphorylationYHFRGRRSLEFSYQE
EEECCCCEEEEECCC		30.7819691289
1358PhosphorylationTRPRKIPSVGRQGEH
CCCCCCCCCCCCCCC		40.4519691289
1368N-linked_GlycosylationRQGEHLSNSTSAFST
CCCCCCCCCCCCCCC		56.52UniProtKB CARBOHYD
1375PhosphorylationNSTSAFSTRSDASGT
CCCCCCCCCCCCCCC		27.95-
1395PhosphorylationFVLEMQKTITDLRTQ
HHHHHHHHHHHHHHH		16.5326437602
1397PhosphorylationLEMQKTITDLRTQIK
HHHHHHHHHHHHHHH		33.9229083192
1425N-linked_GlycosylationAGGESHANNTKWKKD
CCCCCCCCCCCCCCC		51.81UniProtKB CARBOHYD
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 PXDN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PXDN_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 PXDN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPTN1_HUMANSPTAN1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
269400Corneal opacification with other ocular anomalies (COPOA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PXDN_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-1178, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1176 AND SER-1180, ANDMASS SPECTROMETRY.

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