ITIH2_HUMAN - dbPTM
ITIH2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITIH2_HUMAN
UniProt AC P19823
Protein Name Inter-alpha-trypsin inhibitor heavy chain H2
Gene Name ITIH2
Organism Homo sapiens (Human).
Sequence Length 946
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..
Protein Sequence MKRLTCFFICFFLSEVSGFEIPINGLSEFVDYEDLVELAPGKFQLVAENRRYQRSLPGESEEMMEEVDQVTLYSYKVQSTITSRMATTMIQSKVVNNSPQPQNVVFDVQIPKGAFISNFSMTVDGKTFRSSIKEKTVGRALYAQARAKGKTAGLVRSSALDMENFRTEVNVLPGAKVQFELHYQEVKWRKLGSYEHRIYLQPGRLAKHLEVDVWVIEPQGLRFLHVPDTFEGHFDGVPVISKGQQKAHVSFKPTVAQQRICPNCRETAVDGELVVLYDVKREEKAGELEVFNGYFVHFFAPDNLDPIPKNILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAEDHFSVIDFNQNIRTWRNDLISATKTQVADAKRYIEKIQPSGGTNINEALLRAIFILNEANNLGLLDPNSVSLIILVSDGDPTVGELKLSKIQKNVKENIQDNISLFSLGMGFDVDYDFLKRLSNENHGIAQRIYGNQDTSSQLKKFYNQVSTPLLRNVQFNYPHTSVTDVTQNNFHNYFGGSEIVVAGKFDPAKLDQIESVITATSANTQLVLETLAQMDDLQDFLSKDKHADPDFTRKLWAYLTINQLLAERSLAPTAAAKRRITRSILQMSLDHHIVTPLTSLVIENEAGDERMLADAPPQDPSCCSGALYYGSKVVPDSTPSWANPSPTPVISMLAQGSQVLESTPPPHVMRVENDPHFIIYLPKSQKNICFNIDSEPGKILNLVSDPESGIVVNGQLVGAKKPNNGKLSTYFGKLGFYFQSEDIKIEISTETITLSHGSSTFSLSWSDTAQVTNQRVQISVKKEKVVTITLDKEMSFSVLLHRVWKKHPVNVDFLGIYIPPTNKFSPKAHGLIGQFMQEPKIHIFNERPGKDPEKPEASMEVKGQKLIITRGLQKDYRTDLVFGTDVTCWFVHNSGKGFIDGHYKDYFVPQLYSFLKRP
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
55PhosphorylationENRRYQRSLPGESEE
ECHHCCCCCCCCCHH		24.3227130503
60PhosphorylationQRSLPGESEEMMEEV
CCCCCCCCHHHHHHH		44.7821082442
79PhosphorylationLYSYKVQSTITSRMA
EEEEEHHHHHHHHHC		25.4326437602
82PhosphorylationYKVQSTITSRMATTM
EEHHHHHHHHHCHHH		15.4626437602
96N-linked_GlycosylationMIQSKVVNNSPQPQN
HHEEEECCCCCCCCC		46.3716335952
117PhosphorylationIPKGAFISNFSMTVD
ECCCCEECEEEEEEC		25.9328060719
118N-linked_GlycosylationPKGAFISNFSMTVDG
CCCCEECEEEEEECC		28.3517623646
118N-linked_GlycosylationPKGAFISNFSMTVDG
CCCCEECEEEEEECC		28.3518638581
120PhosphorylationGAFISNFSMTVDGKT
CCEECEEEEEECCEE		20.1428060719
122PhosphorylationFISNFSMTVDGKTFR
EECEEEEEECCEEHH		17.7828060719
127PhosphorylationSMTVDGKTFRSSIKE
EEEECCEEHHHHHCH		29.7922210691
130PhosphorylationVDGKTFRSSIKEKTV
ECCEEHHHHHCHHHH		32.0229449344
131PhosphorylationDGKTFRSSIKEKTVG
CCEEHHHHHCHHHHH		33.1629449344
190UbiquitinationYQEVKWRKLGSYEHR
EEEEEEEECCCCCCE		56.9624816145
267PhosphorylationICPNCRETAVDGELV
CCCCCCCCCCCCEEE		16.78-
277PhosphorylationDGELVVLYDVKREEK
CCEEEEEEEEECHHH		13.6922817900
2824-carboxyglutamateVLYDVKREEKAGELE
EEEEEECHHHCCEEE		59.12-
282Gamma-carboxyglutamic_acidVLYDVKREEKAGELE
EEEEEECHHHCCEEE		59.122450046
282Gamma-carboxyglutamic_acidVLYDVKREEKAGELE
EEEEEECHHHCCEEE		59.122450046
283Gamma-carboxyglutamic_acidLYDVKREEKAGELEV
EEEEECHHHCCEEEE		52.842450046
283Gamma-carboxyglutamic_acidLYDVKREEKAGELEV
EEEEECHHHCCEEEE		52.842450046
2834-carboxyglutamateLYDVKREEKAGELEV
EEEEECHHHCCEEEE		52.84-
318PhosphorylationILFVIDVSGSMWGVK
EEEEEECCCCCCCCC		22.7730278072
320PhosphorylationFVIDVSGSMWGVKMK
EEEECCCCCCCCCHH		12.1230278072
364PhosphorylationTWRNDLISATKTQVA
HHHHHHHHHCHHHHH		36.8624114839
383O-linked_GlycosylationYIEKIQPSGGTNINE
HHHHHCCCCCCCHHH		33.22OGP
445N-linked_GlycosylationVKENIQDNISLFSLG
HHHHHHHCHHHHHHC		14.9016335952
466PhosphorylationYDFLKRLSNENHGIA
HHHHHHHCCCCCCCC		46.2428270605
597PhosphorylationNQLLAERSLAPTAAA
HHHHHHCCCCCCHHH		22.01-
601PhosphorylationAERSLAPTAAAKRRI
HHCCCCCCHHHHHHH		24.26-
601O-linked_GlycosylationAERSLAPTAAAKRRI
HHCCCCCCHHHHHHH		24.2668724103
652O-linked_GlycosylationPQDPSCCSGALYYGS
CCCCCCCCCCEEECC		31.28OGP
652PhosphorylationPQDPSCCSGALYYGS
CCCCCCCCCCEEECC		31.2824505115
666O-linked_GlycosylationSKVVPDSTPSWANPS
CEECCCCCCCCCCCC		28.819425062
666O-linked_GlycosylationSKVVPDSTPSWANPS
CEECCCCCCCCCCCC		28.819677337
668O-linked_GlycosylationVVPDSTPSWANPSPT
ECCCCCCCCCCCCCC		38.62OGP
671N-linked_GlycosylationDSTPSWANPSPTPVI
CCCCCCCCCCCCCHH		31.189425062
673O-linked_GlycosylationTPSWANPSPTPVISM
CCCCCCCCCCCHHHH		41.019425062
673O-linked_GlycosylationTPSWANPSPTPVISM
CCCCCCCCCCCHHHH		41.019677337
675O-linked_GlycosylationSWANPSPTPVISMLA
CCCCCCCCCHHHHHH		34.239425062
675O-linked_GlycosylationSWANPSPTPVISMLA
CCCCCCCCCHHHHHH		34.239677337
679O-linked_GlycosylationPSPTPVISMLAQGSQ
CCCCCHHHHHHCCCC		14.15OGP
685O-linked_GlycosylationISMLAQGSQVLESTP
HHHHHCCCCHHCCCC		12.68OGP
690O-linked_GlycosylationQGSQVLESTPPPHVM
CCCCHHCCCCCCCEE		41.89OGP
691O-linked_GlycosylationGSQVLESTPPPHVMR
CCCHHCCCCCCCEEE		30.367682553
691O-linked_GlycosylationGSQVLESTPPPHVMR
CCCHHCCCCCCCEEE		30.369425062
702OtherHVMRVENDPHFIIYL
CEEEECCCCCEEEEE		25.25-
702Aspartate 1-(chondroitin 4-sulfate)-esterHVMRVENDPHFIIYL
CEEEECCCCCEEEEE		25.25-
783PhosphorylationSTETITLSHGSSTFS
EEEEEEEECCCEEEE		19.70-
807PhosphorylationTNQRVQISVKKEKVV
ECCEEEEEECCCEEE		15.7024961811
815PhosphorylationVKKEKVVTITLDKEM
ECCCEEEEEEECCCC		15.9520860994
817PhosphorylationKEKVVTITLDKEMSF
CCEEEEEEECCCCCH		21.3820860994
825PhosphorylationLDKEMSFSVLLHRVW
ECCCCCHHHHHHHHH		12.4420860994
853PhosphorylationIPPTNKFSPKAHGLI
ECCCCCCCCCHHCHH		27.4024719451
886PhosphorylationDPEKPEASMEVKGQK
CCCCCCCCCEECCEE		17.5126074081
897PhosphorylationKGQKLIITRGLQKDY
CCEEEEEECCCCCCC		16.2226074081
904PhosphorylationTRGLQKDYRTDLVFG
ECCCCCCCCCCEEEE		23.5826074081
906PhosphorylationGLQKDYRTDLVFGTD
CCCCCCCCCEEEECC		27.7026074081
912PhosphorylationRTDLVFGTDVTCWFV
CCCEEEECCEEEEEE		18.8126074081
941PhosphorylationYFVPQLYSFLKRP--
CCHHHHHHHHCCC--		32.4724719451
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
60SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
466SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
886SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITIH2_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 ITIH2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPIT2_HUMANSPINT2physical
8601712
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 ITIH2_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-118, 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-96; ASN-118 AND ASN-445,AND MASS SPECTROMETRY.
"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-118.
"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 ASN-118; THR-666; SER-673; THR-675 AND THR-691, ANDDISULFIDE BONDS.
"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-118; THR-666; SER-673; THR-675 AND THR-691, ANDMASS 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 ASN-118; THR-666; SER-673; THR-675 AND THR-691, ANDDISULFIDE BONDS.
"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-118; THR-666; SER-673; THR-675 AND THR-691, ANDMASS SPECTROMETRY.
"Presence of the protein-glycosaminoglycan-protein covalent cross-linkin the inter-alpha-inhibitor-related proteinase inhibitor heavy chain2/bikunin.";
Enghild J.J., Salvesen G., Thoegersen I.B., Valnickova Z., Pizzo S.V.,Hefta S.A.;
J. Biol. Chem. 268:8711-8716(1993).
Cited for: PROTEIN SEQUENCE OF 55-64 AND 681-702, CROSS-LINK STRUCTURE, ANDGLYCOSYLATION AT THR-691.
Phosphorylation
ReferencePubMed
"An initial characterization of the serum phosphoproteome.";
Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A.,Liotta L.A., Petricoin E.F. III;
J. Proteome Res. 8:5523-5531(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, TISSUE SPECIFICITY,AND MASS SPECTROMETRY.

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