ITIH4_HUMAN - dbPTM
ITIH4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITIH4_HUMAN
UniProt AC Q14624
Protein Name Inter-alpha-trypsin inhibitor heavy chain H4
Gene Name ITIH4
Organism Homo sapiens (Human).
Sequence Length 930
Subcellular Localization Secreted.
Protein Description Type II acute-phase protein (APP) involved in inflammatory responses to trauma. May also play a role in liver development or regeneration..
Protein Sequence MKPPRPVRTCSKVLVLLSLLAIHQTTTAEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRANTVQEATFQMELPKKAFITNFSMIIDGMTYPGIIKEKAEAQAQYSAAVAKGKSAGLVKATGRNMEQFQVSVSVAPNAKITFELVYEELLKRRLGVYELLLKVRPQQLVKHLQMDIHIFEPQGISFLETESTFMTNQLVDALTTWQNKTKAHIRFKPTLSQQQKSPEQQETVLDGNLIIRYDVDRAISGGSIQIENGYFVHYFAPEGLTTMPKNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEATQWRPSLVPASAENVNKARSFAAGIQALGGTNINDAMLMAVQLLDSSNQEERLPEGSVSLIILLTDGDPTVGETNPRSIQNNVREAVSGRYSLFCLGFGFDVSYAFLEKLALDNGGLARRIHEDSDSALQLQDFYQEVANPLLTAVTFEYPSNAVEEVTQNNFRLLFKGSEMVVAGKLQDRGPDVLTATVSGKLPTQNITFQTESSVAEQEAEFQSPKYIFHNFMERLWAYLTIQQLLEQTVSASDADQQALRNQALNLSLAYSFVTPLTSMVVTKPDDQEQSQVAEKPMEGESRNRNVHSGSTFFKYYLQGAKIPKPEASFSPRRGWNRQAGAAGSRMNFRPGVLSSRQLGLPGPPDVPDHAAYHPFRRLAILPASAPPATSNPDPAVSRVMNMKIEETTMTTQTPAPIQAPSAILPLPGQSVERLCVDPRHRQGPVNLLSDPEQGVEVTGQYEREKAGFSWIEVTFKNPLVWVHASPEHVVVTRNRRSSAYKWKETLFSVMPGLKMTMDKTGLLLLSDPDKVTIGLLFWDGRGEGLRLLLRDTDRFSSHVGGTLGQFYQEVLWGSPAASDDGRRTLRVQGNDHSATRERRLDYQEGPPGVEISCWSVEL
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
55PhosphorylationFAHTVVTSRVVNRAN
CCCHHHHHHHHHCCC		16.0924719451
56MethylationAHTVVTSRVVNRANT
CCHHHHHHHHHCCCC		27.3418967741
81N-linked_GlycosylationPKKAFITNFSMIIDG
CCCEEEECCCEEECC		23.3717623646
81N-linked_GlycosylationPKKAFITNFSMIIDG
CCCEEEECCCEEECC		23.3716335952
106PhosphorylationAEAQAQYSAAVAKGK
HHHHHHHHHHHHCCC		9.5524505115
114PhosphorylationAAVAKGKSAGLVKAT
HHHHCCCCCCEEEEC		35.92-
207N-linked_GlycosylationDALTTWQNKTKAHIR
HHHHHHCCCCCCEEE		45.5924884609
207N-linked_GlycosylationDALTTWQNKTKAHIR
HHHHHHCCCCCCEEE		45.5912754519
220PhosphorylationIRFKPTLSQQQKSPE
EEECCCCCCCCCCHH		28.5524505115
225PhosphorylationTLSQQQKSPEQQETV
CCCCCCCCHHHHCEE		29.3627130503
274N-linked_GlycosylationGLTTMPKNVVFVIDK
CCCCCCCEEEEEECC		29.3424884609
282PhosphorylationVVFVIDKSGSMSGRK
EEEEECCCCCCCCCH		32.14-
284PhosphorylationFVIDKSGSMSGRKIQ
EEECCCCCCCCCHHH		19.50-
286PhosphorylationIDKSGSMSGRKIQQT
ECCCCCCCCCHHHHH		36.82-
305PhosphorylationIKILDDLSPRDQFNL
HHHHHHCCHHHCCCE		25.53-
325PhosphorylationEATQWRPSLVPASAE
CCHHCCCCCCCCCCC		33.16-
489PhosphorylationFRLLFKGSEMVVAGK
EEEEECCCEEEEEEE		24.1024505115
506PhosphorylationDRGPDVLTATVSGKL
CCCCCEEEEEECCCC		21.8224505115
508O-linked_GlycosylationGPDVLTATVSGKLPT
CCCEEEEEECCCCCC		15.23OGP
508PhosphorylationGPDVLTATVSGKLPT
CCCEEEEEECCCCCC		15.2324505115
510PhosphorylationDVLTATVSGKLPTQN
CEEEEEECCCCCCCC		26.34-
517N-linked_GlycosylationSGKLPTQNITFQTES
CCCCCCCCEEEEECC		37.4318638581
517N-linked_GlycosylationSGKLPTQNITFQTES
CCCCCCCCEEEEECC		37.4317623646
577N-linked_GlycosylationALRNQALNLSLAYSF
HHHHHHHCHHHHHHH		30.5116335952
620 (in isoform 3)Phosphorylation-30.10-
620PhosphorylationSRNRNVHSGSTFFKY
CCCCCCCCCCCHHHH		30.1028857561
620 (in isoform 2)Phosphorylation-30.10-
620 (in isoform 4)Phosphorylation-30.10-
622PhosphorylationNRNVHSGSTFFKYYL
CCCCCCCCCHHHHHH		25.6724505115
623PhosphorylationRNVHSGSTFFKYYLQ
CCCCCCCCHHHHHHC		36.2928857561
626 (in isoform 2)Phosphorylation-28.8828787133
626 (in isoform 3)Phosphorylation-28.8828787133
626 (in isoform 4)Phosphorylation-28.8828787133
626AcetylationHSGSTFFKYYLQGAK
CCCCCHHHHHHCCCC		28.887697065
633AcetylationKYYLQGAKIPKPEAS
HHHHCCCCCCCCCCC		67.387697073
640O-linked_GlycosylationKIPKPEASFSPRRGW
CCCCCCCCCCCCCCC		25.29OGP
656PhosphorylationRQAGAAGSRMNFRPG
CCCCCCCCCCCCCCC		24.5127251275
666PhosphorylationNFRPGVLSSRQLGLP
CCCCCCCCCCCCCCC		22.5227130503
667PhosphorylationFRPGVLSSRQLGLPG
CCCCCCCCCCCCCCC		21.6427130503
696O-linked_GlycosylationRLAILPASAPPATSN
CEEEEECCCCCCCCC		39.09-
701O-linked_GlycosylationPASAPPATSNPDPAV
ECCCCCCCCCCCHHH		34.51-
702O-linked_GlycosylationASAPPATSNPDPAVS
CCCCCCCCCCCHHHH		48.77-
709O-linked_GlycosylationSNPDPAVSRVMNMKI
CCCCHHHHHHHCCEE		22.66OGP
719O-linked_GlycosylationMNMKIEETTMTTQTP
HCCEEEEEEEECCCC		14.74UniProtKB CARBOHYD
719PhosphorylationMNMKIEETTMTTQTP
HCCEEEEEEEECCCC		14.7426657352
720O-linked_GlycosylationNMKIEETTMTTQTPA
CCEEEEEEEECCCCC		18.7922171320
720PhosphorylationNMKIEETTMTTQTPA
CCEEEEEEEECCCCC		18.7926657352
722O-linked_GlycosylationKIEETTMTTQTPAPI
EEEEEEEECCCCCCC		17.41UniProtKB CARBOHYD
723PhosphorylationIEETTMTTQTPAPIQ
EEEEEEECCCCCCCC		21.4426657352
723O-linked_GlycosylationIEETTMTTQTPAPIQ
EEEEEEECCCCCCCC		21.44OGP
725O-linked_GlycosylationETTMTTQTPAPIQAP
EEEEECCCCCCCCCC		21.23OGP
725PhosphorylationETTMTTQTPAPIQAP
EEEEECCCCCCCCCC		21.2326657352
733O-linked_GlycosylationPAPIQAPSAILPLPG
CCCCCCCCEEECCCC		30.84OGP
828PhosphorylationVMPGLKMTMDKTGLL
HCCCCCEEECCCCEE		22.1927461979
831MethylationGLKMTMDKTGLLLLS
CCCEEECCCCEEEEC		33.4023644510
832PhosphorylationLKMTMDKTGLLLLSD
CCEEECCCCEEEECC		28.8827461979
842MethylationLLLSDPDKVTIGLLF
EEECCCCCEEEEEEE		46.8223644510
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 ITIH4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
719TGlycosylation

7541790
725TGlycosylation

7541790
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 ITIH4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P63_HUMANTP63physical
21988832
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 ITIH4_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-81; ASN-207 AND ASN-517,AND MASS SPECTROMETRY.
"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-81; ASN-207; ASN-517 ANDASN-577, AND MASS SPECTROMETRY.
"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-517, 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-207.
O-linked Glycosylation
ReferencePubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT THR-720, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.

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