ITIH1_MOUSE - dbPTM
ITIH1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITIH1_MOUSE
UniProt AC Q61702
Protein Name Inter-alpha-trypsin inhibitor heavy chain H1
Gene Name Itih1
Organism Mus musculus (Mouse).
Sequence Length 907
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 MEGATGLRVLLCLLPLLTLQARPALGLATGRPRGSEKRHAVDTSVNGVSIKSLKVNCKVTSRFAHYVITSQVVNNADKAREVAFDVEIPKTAFISDFAITSDGKAFIGDIKDKVTAWKQYRKAAVLGESAGLVRASGRNMEQFTIHITVGAQSKATFRLTYEEVLKRRLMQYDITIKVRPKQLVQHFEIDVDIFEPQGISKLDAQASFLSEELAAQTIKKSFSGKKGHVLFRPTVSQQQSCPTCSTSLLNGEFKVTYDVNRDKLCDLLVANNYFTHFFAPKNLTNMSKNLVFVIDISGSMEGQKVRQTKEALLKILEDMRPVDNFDLVLFGSKVQSWKGSLVPASNANLQAAQDFVRRFSLAGATNLNGGLLRGIEILNKAQGSHPELSSPASILIMLTDGEPTEGETDRSQILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMSTENNGWAQRIYEDHDATQQLQGFYNQVANPLLTDVELQYPQDAVLALTQHRHKQYYDGSEIVVAGRIANHKLNTFKADVRARGEKQEFRATCLVDEEEMKKLLRERGHVLENHVERLWAYLTIQELLAKRMKTEGEERANLSSQVLKMSLDYHFVTPLTSLTIRGLTDEDGLEPTIDKPLEDSQPLEMVGPRRTFVLSAIQPSPTAHPIDSKLPLRVTGVDTDPHFIIYVPSKEDSLCFNINEEPGVILNLVQDPDTGFTVNGQLIGNKASSPGQHESTYFGRLGISSPTSDFQLEVTPQNITLNPSSSGSMFSWRDQAVLQKDGVVVTINKKRNLVVSVDDGATFEIVLHRTWKGSAVHQDFLGFYVLDSFRMSARTKGLLGQFFSPLDFEVFDLHPGSDPTKTDATMVVKNRQLTVTRGLQKDYSKDPRHGAEVPCWFVHDNGAGLIDGVHTDYVVSDIF
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
57S-linked_GlycosylationIKSLKVNCKVTSRFA
EEEEEEEEEEEHHCC
4.14-
129PhosphorylationKAAVLGESAGLVRAS
HHHHHHCCCCEEEEC
26.3228542873
282N-linked_GlycosylationTHFFAPKNLTNMSKN
HHCCCCCCCCCCCCC
51.55-
285N-linked_GlycosylationFAPKNLTNMSKNLVF
CCCCCCCCCCCCEEE
35.58-
399PhosphorylationASILIMLTDGEPTEG
CEEEEEEECCCCCCC
25.28-
404PhosphorylationMLTDGEPTEGETDRS
EEECCCCCCCCCCHH
52.93-
537S-palmitoylationKQEFRATCLVDEEEM
CCCEEEEEECCHHHH
3.2128680068
585N-linked_GlycosylationTEGEERANLSSQVLK
CCCHHHHCCHHHHHH
46.8316944957
650O-linked_GlycosylationSAIQPSPTAHPIDSK
EEECCCCCCCCCCCC
41.77-
668OtherRVTGVDTDPHFIIYV
EEECCCCCCCEEEEC
30.16-
774PhosphorylationQKDGVVVTINKKRNL
EECCEEEEEECCCCE
13.7624719451

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITIH1_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ITIH1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITIH1_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides.";
Bernhard O.K., Kapp E.A., Simpson R.J.;
J. Proteome Res. 6:987-995(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-585, AND MASSSPECTROMETRY.
"Proteome-wide characterization of N-glycosylation events by diagonalchromatography.";
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.;
J. Proteome Res. 5:2438-2447(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-585, AND MASSSPECTROMETRY.

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