ILEU_HUMAN - dbPTM
ILEU_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ILEU_HUMAN
UniProt AC P30740
Protein Name Leukocyte elastase inhibitor
Gene Name SERPINB1
Organism Homo sapiens (Human).
Sequence Length 379
Subcellular Localization Cytoplasm. Cytoplasmic granule .
Protein Description Regulates the activity of the neutrophil proteases elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and kallikrein-3. Also functions as a potent intracellular inhibitor of granzyme H..
Protein Sequence MEQLSSANTRFALDLFLALSENNPAGNIFISPFSISSAMAMVFLGTRGNTAAQLSKTFHFNTVEEVHSRFQSLNADINKRGASYILKLANRLYGEKTYNFLPEFLVSTQKTYGADLASVDFQHASEDARKTINQWVKGQTEGKIPELLASGMVDNMTKLVLVNAIYFKGNWKDKFMKEATTNAPFRLNKKDRKTVKMMYQKKKFAYGYIEDLKCRVLELPYQGEELSMVILLPDDIEDESTGLKKIEEQLTLEKLHEWTKPENLDFIEVNVSLPRFKLEESYTLNSDLARLGVQDLFNSSKADLSGMSGARDIFISKIVHKSFVEVNEEGTEAAAATAGIATFCMLMPEENFTADHPFLFFIRHNSSGSILFLGRFSSP
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
1Sulfoxidation-------MEQLSSAN
-------CHHHHCHH		7.1728465586
1Acetylation-------MEQLSSAN
-------CHHHHCHH		7.1722814378
26UbiquitinationLSENNPAGNIFISPF
HHCCCCCCCEEECCC		29.08-
45UbiquitinationAMAMVFLGTRGNTAA
HHHHHHHCCCCCHHH		11.25-
62PhosphorylationSKTFHFNTVEEVHSR
HHHCCCCCHHHHHHH		28.4923312004
72PhosphorylationEVHSRFQSLNADINK
HHHHHHHHHCCCHHH		22.3720873877
792-HydroxyisobutyrylationSLNADINKRGASYIL
HHCCCHHHHHHHHHH		53.17-
79UbiquitinationSLNADINKRGASYIL
HHCCCHHHHHHHHHH		53.17-
79AcetylationSLNADINKRGASYIL
HHCCCHHHHHHHHHH		53.1726051181
83PhosphorylationDINKRGASYILKLAN
CHHHHHHHHHHHHHH		18.6122210691
84PhosphorylationINKRGASYILKLANR
HHHHHHHHHHHHHHH		15.1123312004
87AcetylationRGASYILKLANRLYG
HHHHHHHHHHHHHHC		35.6726051181
97PhosphorylationNRLYGEKTYNFLPEF
HHHHCCCCCCCCCHH		21.28-
110UbiquitinationEFLVSTQKTYGADLA
HHHHCCCCCCCCCHH		43.75-
130UbiquitinationHASEDARKTINQWVK
CCCHHHHHHHHHHHH		56.32-
131PhosphorylationASEDARKTINQWVKG
CCHHHHHHHHHHHHC		21.43-
137AcetylationKTINQWVKGQTEGKI
HHHHHHHHCCCCCCH		42.2019608861
137UbiquitinationKTINQWVKGQTEGKI
HHHHHHHHCCCCCCH		42.2019608861
143UbiquitinationVKGQTEGKIPELLAS
HHCCCCCCHHHHHHH		49.18-
150UbiquitinationKIPELLASGMVDNMT
CHHHHHHHCCCCHHH		27.65-
150PhosphorylationKIPELLASGMVDNMT
CHHHHHHHCCCCHHH		27.6520068231
166PhosphorylationLVLVNAIYFKGNWKD
HHEEEEEEECCCCHH		9.2327259358
177AcetylationNWKDKFMKEATTNAP
CCHHHHHHHHHCCCC		47.5319608861
177UbiquitinationNWKDKFMKEATTNAP
CCHHHHHHHHHCCCC		47.5321890473
177UbiquitinationNWKDKFMKEATTNAP
CCHHHHHHHHHCCCC		47.5321890473
177UbiquitinationNWKDKFMKEATTNAP
CCHHHHHHHHHCCCC		47.5321890473
196UbiquitinationKKDRKTVKMMYQKKK
HHCHHHHHHHHCHHC		24.1521890473
196UbiquitinationKKDRKTVKMMYQKKK
HHCHHHHHHHHCHHC		24.1521890473
196UbiquitinationKKDRKTVKMMYQKKK
HHCHHHHHHHHCHHC		24.1521890473
196AcetylationKKDRKTVKMMYQKKK
HHCHHHHHHHHCHHC		24.1527178108
203UbiquitinationKMMYQKKKFAYGYIE
HHHHCHHCHHHHHHC		42.11-
2032-HydroxyisobutyrylationKMMYQKKKFAYGYIE
HHHHCHHCHHHHHHC		42.11-
208PhosphorylationKKKFAYGYIEDLKCR
HHCHHHHHHCCCEEE		6.61-
2132-HydroxyisobutyrylationYGYIEDLKCRVLELP
HHHHCCCEEEEEECC		32.11-
245UbiquitinationDESTGLKKIEEQLTL
CCCCCHHHHHHHHCH		61.46-
272PhosphorylationDFIEVNVSLPRFKLE
CEEEEECCCCCEECE		27.7024719451
277AcetylationNVSLPRFKLEESYTL
ECCCCCEECEECEEC		57.1626051181
282PhosphorylationRFKLEESYTLNSDLA
CEECEECEECCHHHH		20.6617924679
286PhosphorylationEESYTLNSDLARLGV
EECEECCHHHHHHCH		36.7917924679
299PhosphorylationGVQDLFNSSKADLSG
CHHHHHHCCCHHHCC		26.3628450419
300PhosphorylationVQDLFNSSKADLSGM
HHHHHHCCCHHHCCC		32.7325159151
301UbiquitinationQDLFNSSKADLSGMS
HHHHHCCCHHHCCCC		45.8221890473
307SulfoxidationSKADLSGMSGARDIF
CCHHHCCCCCCHHHH		2.7630846556
317UbiquitinationARDIFISKIVHKSFV
CHHHHHHHHHHHHHE		43.88-
3172-HydroxyisobutyrylationARDIFISKIVHKSFV
CHHHHHHHHHHHHHE		43.88-
317AcetylationARDIFISKIVHKSFV
CHHHHHHHHHHHHHE		43.8827452117
366PhosphorylationLFFIRHNSSGSILFL
EEEEEECCCCCEEEE		29.9223312004
367PhosphorylationFFIRHNSSGSILFLG
EEEEECCCCCEEEEE		41.7128348404
369PhosphorylationIRHNSSGSILFLGRF
EEECCCCCEEEEEEE		20.3328348404
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 ILEU_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ILEU_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 ILEU_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ITPA_HUMANITPAphysical
26344197
TES_HUMANTESphysical
26344197
TPPC4_HUMANTRAPPC4physical
26344197
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 ILEU_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 1-10, AND ACETYLATION AT MET-1.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137 AND LYS-177, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-282 AND SER-286, ANDMASS SPECTROMETRY.

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