ITIH1_HUMAN - dbPTM
ITIH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITIH1_HUMAN
UniProt AC P19827
Protein Name Inter-alpha-trypsin inhibitor heavy chain H1
Gene Name ITIH1
Organism Homo sapiens (Human).
Sequence Length 911
Subcellular Localization Secreted.
Protein Description May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes.; Contains a potential peptide which could stimulate a broad spectrum of phagocytotic cells..
Protein Sequence MDGAMGPRGLLLCMYLVSLLILQAMPALGSATGRSKSSEKRQAVDTAVDGVFIRSLKVNCKVTSRFAHYVVTSQVVNTANEAREVAFDLEIPKTAFISDFAVTADGNAFIGDIKDKVTAWKQYRKAAISGENAGLVRASGRTMEQFTIHLTVNPQSKVTFQLTYEEVLKRNHMQYEIVIKVKPKQLVHHFEIDVDIFEPQGISKLDAQASFLPKELAAQTIKKSFSGKKGHVLFRPTVSQQQSCPTCSTSLLNGHFKVTYDVSRDKICDLLVANNHFAHFFAPQNLTNMNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRGFSLDEATNLNGGLLRGIEILNQVQESLPELSNHASILIMLTDGDPTEGVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEVMSMENNGRAQRIYEDHDATQQLQGFYSQVAKPLLVDVDLQYPQDAVLALTQNHHKQYYEGSEIVVAGRIADNKQSSFKADVQAHGEGQEFSITCLVDEEEMKKLLRERGHMLENHVERLWAYLTIQELLAKRMKVDREERANLSSQALQMSLDYGFVTPLTSMSIRGMADQDGLKPTIDKPSEDSPPLEMLGPRRTFVLSALQPSPTHSSSNTQRLPDRVTGVDTDPHFIIHVPQKEDTLCFNINEEPGVILSLVQDPNTGFSVNGQLIGNKARSPGQHDGTYFGRLGIANPATDFQLEVTPQNITLNPGFGGPVFSWRDQAVLRQDGVVVTINKKRNLVVSVDDGGTFEVVLHRVWKGSSVHQDFLGFYVLDSHRMSARTHGLLGQFFHPIGFEVSDIHPGSDPTKPDATMVVRNRRLTVTRGLQKDYSKDPWHGAEVSCWFIHNNGAGLIDGAYTDYIVPDIF
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
46PhosphorylationEKRQAVDTAVDGVFI
HHHHHHHHHHHEEEE		23.21-
60S-linked_GlycosylationIRSLKVNCKVTSRFA
EEEEEEEEEEECCCC		4.149425062
129PhosphorylationQYRKAAISGENAGLV
HHHHHHHCCCCCEEE		35.0127130503
159PhosphorylationVNPQSKVTFQLTYEE
ECCCCCEEEEEEHHH		14.9228674151
259PhosphorylationLNGHFKVTYDVSRDK
HCCEEEEEEECCHHH		18.0028509920
260PhosphorylationNGHFKVTYDVSRDKI
CCEEEEEEECCHHHH		19.8228509920
285N-linked_GlycosylationAHFFAPQNLTNMNKN
HHEECCCCCCCCCCC		48.0117623646
285N-linked_GlycosylationAHFFAPQNLTNMNKN
HHEECCCCCCCCCCC		48.0117623646
402PhosphorylationASILIMLTDGDPTEG
CEEEEEEECCCCCCC		22.1318669648
407PhosphorylationMLTDGDPTEGVTDRS
EEECCCCCCCCCCHH		50.5418669648
414PhosphorylationTEGVTDRSQILKNVR
CCCCCCHHHHHHHHH		25.1218669648
431PhosphorylationIRGRFPLYNLGFGHN
HCCCCCCCCCCCCCC		14.47-
504PhosphorylationQNHHKQYYEGSEIVV
HCCCHHHCCCCEEEE		16.0117924679
522PhosphorylationIADNKQSSFKADVQA
ECCCCCCCCCCEEHH		28.42-
568PhosphorylationHVERLWAYLTIQELL
HHHHHHHHHHHHHHH		7.8723909892
570PhosphorylationERLWAYLTIQELLAK
HHHHHHHHHHHHHHH		14.1323909892
588N-linked_GlycosylationVDREERANLSSQALQ
CCHHHHHCCHHHHHH		46.839425062
588N-linked_GlycosylationVDREERANLSSQALQ
CCHHHHHCCHHHHHH		46.8317623646
604O-linked_GlycosylationSLDYGFVTPLTSMSI
HHCCCCCCCCCCCCC		15.43OGP
623O-linked_GlycosylationDQDGLKPTIDKPSED
CCCCCCCCCCCCCCC		39.97OGP
651O-linked_GlycosylationVLSALQPSPTHSSSN
EEEECCCCCCCCCCC		29.48OGP
653PhosphorylationSALQPSPTHSSSNTQ
EECCCCCCCCCCCCC		38.4323663014
653O-linked_GlycosylationSALQPSPTHSSSNTQ
EECCCCCCCCCCCCC		38.439425062
653O-linked_GlycosylationSALQPSPTHSSSNTQ
EECCCCCCCCCCCCC		38.4319782370
655O-linked_GlycosylationLQPSPTHSSSNTQRL
CCCCCCCCCCCCCCC		37.63OGP
656PhosphorylationQPSPTHSSSNTQRLP
CCCCCCCCCCCCCCC		21.7223663014
657PhosphorylationPSPTHSSSNTQRLPD
CCCCCCCCCCCCCCC		47.0823663014
672Aspartate 1-(chondroitin 4-sulfate)-esterRVTGVDTDPHFIIHV
CCCCCCCCCCEEEEC		30.16-
672OtherRVTGVDTDPHFIIHV
CCCCCCCCCCEEEEC		30.16-
750N-linked_GlycosylationQLEVTPQNITLNPGF
EEEEECCCEEECCCC		30.3419782370
750N-linked_GlycosylationQLEVTPQNITLNPGF
EEEEECCCEEECCCC		30.3419782370
778PhosphorylationRQDGVVVTINKKRNL
ECCCEEEEEECCCCE		13.7624719451
788PhosphorylationKKRNLVVSVDDGGTF
CCCCEEEEECCCCEE		16.61-
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 ITIH1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITIH1_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 ITIH1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ITIH1_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 ITIH1_HUMAN

loading...

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-750, AND MASSSPECTROMETRY.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-588, AND MASSSPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-285.
"Posttranslational modifications of human inter-alpha-inhibitor:identification of glycans and disulfide bridges in heavy chains 1 and2.";
Olsen E.H.N., Rahbek-Nielsen H., Thoegersen I.B., Roepstorff P.,Enghild J.J.;
Biochemistry 37:408-416(1998).
Cited for: GLYCOSYLATION AT CYS-60; ASN-285; ASN-588 AND THR-653, DISULFIDEBONDS, AND MASS SPECTROMETRY.
"Glycosylation pattern of human inter-alpha-inhibitor heavy chains.";
Flahaut C., Capon C., Balduyck M., Ricart G., Sautiere P., Mizon J.;
Biochem. J. 333:749-756(1998).
Cited for: GLYCOSYLATION AT ASN-285 AND ASN-588, AND MASS SPECTROMETRY.
O-linked Glycosylation
ReferencePubMed
"Posttranslational modifications of human inter-alpha-inhibitor:identification of glycans and disulfide bridges in heavy chains 1 and2.";
Olsen E.H.N., Rahbek-Nielsen H., Thoegersen I.B., Roepstorff P.,Enghild J.J.;
Biochemistry 37:408-416(1998).
Cited for: GLYCOSYLATION AT CYS-60; ASN-285; ASN-588 AND THR-653, DISULFIDEBONDS, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-402 AND THR-407, ANDMASS SPECTROMETRY.
"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-504, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory