UniProt ID | ITIH3_HUMAN | |
---|---|---|
UniProt AC | Q06033 | |
Protein Name | Inter-alpha-trypsin inhibitor heavy chain H3 | |
Gene Name | ITIH3 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 890 | |
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 | MAFAWWPCLILALLSSLAASGFPRSPFRLLGKRSLPEGVANGIEVYSTKINSKVTSRFAHNVVTMRAVNRADTAKEVSFDVELPKTAFITNFTLTIDGVTYPGNVKEKEVAKKQYEKAVSQGKTAGLVKASGRKLEKFTVSVNVAAGSKVTFELTYEELLKRHKGKYEMYLKVQPKQLVKHFEIEVDIFEPQGISMLDAEASFITNDLLGSALTKSFSGKKGHVSFKPSLDQQRSCPTCTDSLLNGDFTITYDVNRESPGNVQIVNGYFVHFFAPQGLPVVPKNVAFVIDISGSMAGRKLEQTKEALLRILEDMQEEDYLNFILFSGDVSTWKEHLVQATPENLQEARTFVKSMEDKGMTNINDGLLRGISMLNKAREEHRIPERSTSIVIMLTDGDANVGESRPEKIQENVRNAIGGKFPLYNLGFGNNLNYNFLENMALENHGFARRIYEDSDADLQLQGFYEEVANPLLTGVEMEYPENAILDLTQNTYQHFYDGSEIVVAGRLVDEDMNSFKADVKGHGATNDLTFTEEVDMKEMEKALQERDYIFGNYIERLWAYLTIEQLLEKRKNAHGEEKENLTARALDLSLKYHFVTPLTSMVVTKPEDNEDERAIADKPGEDAEATPVSPAMSYLTSYQPPQNPYYYVDGDPHFIIQIPEKDDALCFNIDEAPGTVLRLIQDAVTGLTVNGQITGDKRGSPDSKTRKTYFGKLGIANAQMDFQVEVTTEKITLWNRAVPSTFSWLDTVTVTQDGLSMMINRKNMVVSFGDGVTFVVVLHQVWKKHPVHRDFLGFYVVDSHRMSAQTHGLLGQFFQPFDFKVSDIRPGSDPTKPDATLVVKNHQLIVTRGSQKDYRKDASIGTKVVCWFVHNNGEGLIDGVHTDYIVPNLF | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
52 | Phosphorylation | VYSTKINSKVTSRFA EEEEECCCHHHHHHC | 31.79 | 26270265 | |
91 | N-linked_Glycosylation | PKTAFITNFTLTIDG CCEEEECEEEEEECC | 24.08 | 16335952 | |
124 | Phosphorylation | KAVSQGKTAGLVKAS HHHHCCCCEEEEECC | 32.55 | - | |
167 | Phosphorylation | LKRHKGKYEMYLKVQ HHHCCCEEEEEEEEC | 18.01 | - | |
170 | Phosphorylation | HKGKYEMYLKVQPKQ CCCEEEEEEEECHHH | 7.45 | - | |
195 | Phosphorylation | IFEPQGISMLDAEAS EECCCCCCCHHHHHH | 21.81 | 20068231 | |
205 | Phosphorylation | DAEASFITNDLLGSA HHHHHHHHHHHHHHH | 22.22 | 20068231 | |
211 | Phosphorylation | ITNDLLGSALTKSFS HHHHHHHHHHCHHCC | 21.78 | 20068231 | |
214 | Phosphorylation | DLLGSALTKSFSGKK HHHHHHHCHHCCCCC | 25.10 | 20068231 | |
292 | Phosphorylation | VAFVIDISGSMAGRK EEEEEECCCCCCCCC | 22.52 | - | |
294 | Phosphorylation | FVIDISGSMAGRKLE EEEECCCCCCCCCHH | 9.92 | - | |
340 | O-linked_Glycosylation | KEHLVQATPENLQEA HHHHHHCCHHHHHHH | 17.65 | OGP | |
340 | Phosphorylation | KEHLVQATPENLQEA HHHHHHCCHHHHHHH | 17.65 | 24505115 | |
353 | Phosphorylation | EARTFVKSMEDKGMT HHHHHHHHHHHCCCC | 23.31 | 29083192 | |
360 | Phosphorylation | SMEDKGMTNINDGLL HHHHCCCCCCCHHHH | 41.43 | 20860994 | |
386 | Phosphorylation | EHRIPERSTSIVIML HCCCCCCCCEEEEEE | 25.50 | - | |
387 | Phosphorylation | HRIPERSTSIVIMLT CCCCCCCCEEEEEEE | 28.79 | - | |
388 | Phosphorylation | RIPERSTSIVIMLTD CCCCCCCEEEEEEEC | 18.99 | - | |
571 | Acetylation | EQLLEKRKNAHGEEK HHHHHHHHHCCCCHH | 70.34 | 20167786 | |
580 | N-linked_Glycosylation | AHGEEKENLTARALD CCCCHHHHHHHHHHH | 54.48 | 17623646 | |
580 | N-linked_Glycosylation | AHGEEKENLTARALD CCCCHHHHHHHHHHH | 54.48 | 16335952 | |
589 | Phosphorylation | TARALDLSLKYHFVT HHHHHHHHHEEEEEC | 23.60 | 20860994 | |
592 | Phosphorylation | ALDLSLKYHFVTPLT HHHHHHEEEEECCCC | 13.04 | - | |
651 | Other | PYYYVDGDPHFIIQI CCEEECCCCCEEEEC | 29.10 | - | |
651 | Aspartate 1-(chondroitin 4-sulfate)-ester | PYYYVDGDPHFIIQI CCEEECCCCCEEEEC | 29.10 | - | |
700 | Phosphorylation | ITGDKRGSPDSKTRK ECCCCCCCCCCCCCC | 29.57 | - | |
703 | Phosphorylation | DKRGSPDSKTRKTYF CCCCCCCCCCCCEEE | 39.03 | - | |
705 | Phosphorylation | RGSPDSKTRKTYFGK CCCCCCCCCCEEEHH | 41.15 | 20068231 | |
708 | Phosphorylation | PDSKTRKTYFGKLGI CCCCCCCEEEHHHCC | 22.31 | 20068231 | |
709 | Phosphorylation | DSKTRKTYFGKLGIA CCCCCCEEEHHHCCC | 17.23 | 20068231 | |
727 | Phosphorylation | MDFQVEVTTEKITLW EEEEEEEECCEEEEC | 18.74 | 20068231 | |
728 | Phosphorylation | DFQVEVTTEKITLWN EEEEEEECCEEEECC | 40.22 | 20068231 | |
822 | Phosphorylation | QPFDFKVSDIRPGSD CCCCEEHHHCCCCCC | 28.10 | 30576142 | |
828 | Phosphorylation | VSDIRPGSDPTKPDA HHHCCCCCCCCCCCC | 43.00 | 30576142 | |
831 | Phosphorylation | IRPGSDPTKPDATLV CCCCCCCCCCCCEEE | 61.27 | 30576142 | |
831 | O-linked_Glycosylation | IRPGSDPTKPDATLV CCCCCCCCCCCCEEE | 61.27 | OGP | |
832 | Methylation | RPGSDPTKPDATLVV CCCCCCCCCCCEEEE | 46.41 | - | |
840 | Methylation | PDATLVVKNHQLIVT CCCEEEEECCEEEEE | 41.03 | - | |
847 | O-linked_Glycosylation | KNHQLIVTRGSQKDY ECCEEEEECCCCHHH | 23.48 | OGP | |
862 | Phosphorylation | RKDASIGTKVVCWFV HHCCCCCCEEEEEEE | 20.99 | 30257219 |
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 ITIH3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ITIH3_HUMAN !! |
* 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 ITIH3_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ITIH3_HUMAN !! |
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. |
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N-linked Glycosylation | |
Reference | PubMed |
"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-91 AND ASN-580, AND MASSSPECTROMETRY. |