PZP_HUMAN - dbPTM
PZP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PZP_HUMAN
UniProt AC P20742
Protein Name Pregnancy zone protein
Gene Name PZP
Organism Homo sapiens (Human).
Sequence Length 1482
Subcellular Localization Secreted.
Protein Description Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase..
Protein Sequence MRKDRLLHLCLVLLLILLSASDSNSTEPQYMVLVPSLLHTEAPKKGCVLLSHLNETVTVSASLESGRENRSLFTDLVAEKDLFHCVSFTLPRISASSEVAFLSIQIKGPTQDFRKRNTVLVLNTQSLVFVQTDKPMYKPGQTVRFRVVSVDENFRPRNELIPLIYLENPRRNRIAQWQSLKLEAGINQLSFPLSSEPIQGSYRVVVQTESGGRIQHPFTVEEFVLPKFEVKVQVPKIISIMDEKVNITVCGEYTYGKPVPGLATVSLCRKLSRVLNCDKQEVCEEFSQQLNSNGCITQQVHTKMLQITNTGFEMKLRVEARIREEGTDLEVTANRISEITNIVSKLKFVKVDSHFRQGIPFFAQVLLVDGKGVPIPNKLFFISVNDANYYSNATTNEQGLAQFSINTTSISVNKLFVRVFTVHPNLCFHYSWVAEDHQGAQHTANRVFSLSGSYIHLEPVAGTLPCGHTETITAHYTLNRQAMGELSELSFHYLIMAKGVIVRSGTHTLPVESGDMKGSFALSFPVESDVAPIARMFIFAILPDGEVVGDSEKFEIENCLANKVDLSFSPAQSPPASHAHLQVAAAPQSLCALRAVDQSVLLMKPEAELSVSSVYNLLTVKDLTNFPDNVDQQEEEQGHCPRPFFIHNGAIYVPLSSNEADIYSFLKGMGLKVFTNSKIRKPKSCSVIPSVSAGAVGQGYYGAGLGVVERPYVPQLGTYNVIPLNNEQSSGPVPETVRSYFPETWIWELVAVNSSGVAEVGVTVPDTITEWKAGAFCLSEDAGLGISSTASLRAFQPFFVELTMPYSVIRGEVFTLKATVLNYLPKCIRVSVQLKASPAFLASQNTKGEESYCICGNERQTLSWTVTPKTLGNVNFSVSAEAMQSLELCGNEVVEVPEIKRKDTVIKTLLVEAEGIEQEKTFSSMTCASGANVSEQLSLKLPSNVVKESARASFSVLGDILGSAMQNIQNLLQMPYGCGEQNMVLFAPNIYVLNYLNETQQLTQEIKAKAVGYLITGYQRQLNYKHQDGSYSTFGERYGRNQGNTWLTAFVLKTFAQARSYIFIDEAHITQSLTWLSQMQKDNGCFRSSGSLLNNAIKGGVEDEATLSAYVTIALLEIPLPVTNPIVRNALFCLESAWNVAKEGTHGSHVYTKALLAYAFSLLGKQNQNREILNSLDKEAVKEDNLVHWERPQRPKAPVGHLYQTQAPSAEVEMTSYVLLAYLTAQPAPTSGDLTSATNIVKWIMKQQNAQGGFSSTQDTVVALHALSRYGAATFTRTEKTAQVTVQDSQTFSTNFQVDNNNLLLLQQISLPELPGEYVITVTGERCVYLQTSMKYNILPEKEDSPFALKVQTVPQTCDGHKAHTSFQISLTISYTGNRPASNMVIVDVKMVSGFIPLKPTVKMLERSSSVSRTEVSNNHVLIYVEQVTNQTLSFSFMVLQDIPVGDLKPAIVKVYDYYETDESVVAEYIAPCSTDTEHGNV
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
24N-linked_GlycosylationLLSASDSNSTEPQYM
HHHCCCCCCCCCCEE		58.92UniProtKB CARBOHYD
54N-linked_GlycosylationCVLLSHLNETVTVSA
EEEEECCCCEEEEEE		37.15UniProtKB CARBOHYD
69N-linked_GlycosylationSLESGRENRSLFTDL
ECCCCCCCHHHHHHH		37.16UniProtKB CARBOHYD
89PhosphorylationLFHCVSFTLPRISAS
HHHHHHCCCCCCCCC		28.4824719451
96PhosphorylationTLPRISASSEVAFLS
CCCCCCCCCCEEEEE		21.9028464451
110PhosphorylationSIQIKGPTQDFRKRN
EEEEECCCCCHHHCC		49.8128464451
239PhosphorylationVQVPKIISIMDEKVN
EECCCEEEECCCCCC		18.48-
246N-linked_GlycosylationSIMDEKVNITVCGEY
EECCCCCCEEEEEEC		34.97UniProtKB CARBOHYD
248PhosphorylationMDEKVNITVCGEYTY
CCCCCCEEEEEECCC		12.44-
308PhosphorylationHTKMLQITNTGFEMK
EEEEEEEECCCCEEE		17.4824719451
310PhosphorylationKMLQITNTGFEMKLR
EEEEEECCCCEEEEE		34.3024719451
327PhosphorylationARIREEGTDLEVTAN
EEECCCCCCCEEEHH		40.4623403867
392N-linked_GlycosylationNDANYYSNATTNEQG
CCCCCCCCCCCCCCC		25.78UniProtKB CARBOHYD
406N-linked_GlycosylationGLAQFSINTTSISVN
CEEEEEEECCEEEEC		35.7916335952
487PhosphorylationRQAMGELSELSFHYL
HHHHHHHHHHHHHHH		31.9923403867
490PhosphorylationMGELSELSFHYLIMA
HHHHHHHHHHHHHHC		13.1123403867
493PhosphorylationLSELSFHYLIMAKGV
HHHHHHHHHHHCCCE		8.9123403867
504PhosphorylationAKGVIVRSGTHTLPV
CCCEEEECCCEEEEC		36.8323403867
519PhosphorylationESGDMKGSFALSFPV
CCCCCCCEEEEECCC		11.2229457462
664PhosphorylationSNEADIYSFLKGMGL
CCHHHHHHHHHHCCC		25.1624719451
675PhosphorylationGMGLKVFTNSKIRKP
HCCCEEEECCCCCCC		41.38-
677PhosphorylationGLKVFTNSKIRKPKS
CCEEEECCCCCCCCC		26.80-
700PhosphorylationAGAVGQGYYGAGLGV
CCCCCCCCCCCCCCE		7.2822817900
701PhosphorylationGAVGQGYYGAGLGVV
CCCCCCCCCCCCCEE		13.8122817900
753N-linked_GlycosylationIWELVAVNSSGVAEV
EEEEEEECCCCEEEE		22.26UniProtKB CARBOHYD
815PhosphorylationVIRGEVFTLKATVLN
EECCCEEEEHHHHHH		32.31-
823PhosphorylationLKATVLNYLPKCIRV
EHHHHHHHHHCCEEE		21.8825884760
826AcetylationTVLNYLPKCIRVSVQ
HHHHHHHCCEEEEEE		39.43-
867PhosphorylationQTLSWTVTPKTLGNV
EEEEEEECCCCCCCE		16.2224719451
875N-linked_GlycosylationPKTLGNVNFSVSAEA
CCCCCCEEEEECHHH		27.72UniProtKB CARBOHYD
908PhosphorylationRKDTVIKTLLVEAEG
CCCCCEEEEEEEECC		17.7526270265
921PhosphorylationEGIEQEKTFSSMTCA
CCCCCCCCCCCCCCC		28.1826270265
923PhosphorylationIEQEKTFSSMTCASG
CCCCCCCCCCCCCCC		25.1626270265
924PhosphorylationEQEKTFSSMTCASGA
CCCCCCCCCCCCCCC		17.5826270265
926PhosphorylationEKTFSSMTCASGANV
CCCCCCCCCCCCCCH		13.5826270265
929PhosphorylationFSSMTCASGANVSEQ
CCCCCCCCCCCHHHH		40.3526270265
932N-linked_GlycosylationMTCASGANVSEQLSL
CCCCCCCCHHHHHCC		41.1816335952
934PhosphorylationCASGANVSEQLSLKL
CCCCCCHHHHHCCCC		21.3126270265
938PhosphorylationANVSEQLSLKLPSNV
CCHHHHHCCCCCCHH		24.1326270265
943PhosphorylationQLSLKLPSNVVKESA
HHCCCCCCHHHHHHH		53.33-
949PhosphorylationPSNVVKESARASFSV
CCHHHHHHHHHHHHH		19.8220068231
997N-linked_GlycosylationIYVLNYLNETQQLTQ
EEEECCCCHHHHHHH		39.6516335952
1045PhosphorylationYGRNQGNTWLTAFVL
CCCCCCCCHHHHHHH		28.7724719451
1088PhosphorylationKDNGCFRSSGSLLNN
HHCCCCCCCCHHHHH		20.8528270605
1089PhosphorylationDNGCFRSSGSLLNNA
HCCCCCCCCHHHHHH		28.3028270605
1091PhosphorylationGCFRSSGSLLNNAIK
CCCCCCCHHHHHHHC		31.4728270605
1106PhosphorylationGGVEDEATLSAYVTI
CCCCCHHHHHHHEEE		21.1424719451
1123PhosphorylationLEIPLPVTNPIVRNA
CCCCCCCCCHHHHHH		33.0824719451
1345PhosphorylationILPEKEDSPFALKVQ
CCCCCCCCCCEEEEE		24.0228634298
1365PhosphorylationCDGHKAHTSFQISLT
CCCCCCCCEEEEEEE		35.7830576142
1374PhosphorylationFQISLTISYTGNRPA
EEEEEEEEECCCCCC		16.0630576142
1382PhosphorylationYTGNRPASNMVIVDV
ECCCCCCCCEEEEEE		28.3022210691
1393PhosphorylationIVDVKMVSGFIPLKP
EEEEEEECCCCCCCC		25.20-
1399GlycationVSGFIPLKPTVKMLE
ECCCCCCCCHHHHHH		33.03-
1401PhosphorylationGFIPLKPTVKMLERS
CCCCCCCHHHHHHCC		31.04-
1403GlycationIPLKPTVKMLERSSS
CCCCCHHHHHHCCCC		40.00-
1412PhosphorylationLERSSSVSRTEVSNN
HHCCCCCCCEECCCC		35.12-
1430N-linked_GlycosylationIYVEQVTNQTLSFSF
EEEEEECCCEEEEEE		33.7016335952
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 PZP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PZP_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 PZP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TGFB1_HUMANTGFB1physical
7513640
TGFB2_HUMANTGFB2physical
7513640
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 PZP_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-997, AND MASSSPECTROMETRY.
"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-406; ASN-932; ASN-997 ANDASN-1430, AND MASS SPECTROMETRY.

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