IL22_HUMAN - dbPTM
IL22_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IL22_HUMAN
UniProt AC Q9GZX6
Protein Name Interleukin-22
Gene Name IL22
Organism Homo sapiens (Human).
Sequence Length 179
Subcellular Localization Secreted.
Protein Description Cytokine that contributes to the inflammatory response in vivo..
Protein Sequence MAALQKSVSSFLMGTLATSCLLLLALLVQGGAAAPISSHCRLDKSNFQQPYITNRTFMLAKEASLADNNTDVRLIGEKLFHGVSMSERCYLMKQVLNFTLEEVLFPQSDRFQPYMQEVVPFLARLSNRLSTCHIEGDDLHIQRNVQKLKDTVKKLGESGEIKAIGELDLLFMSLRNACI
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
54N-linked_GlycosylationFQQPYITNRTFMLAK
CCCCCCCCCCEEHHH
31.2815983417
68N-linked_GlycosylationKEASLADNNTDVRLI
HHHHHCCCCCCEEEH
47.93UniProtKB CARBOHYD
97N-linked_GlycosylationYLMKQVLNFTLEEVL
HHHHHHHCCCHHHHH
29.0615983417
126PhosphorylationVPFLARLSNRLSTCH
HHHHHHHHHHHCCCE
17.8522617229
130PhosphorylationARLSNRLSTCHIEGD
HHHHHHHCCCEECCC
26.2522617229

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 IL22_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IL22_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 IL22_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
I22R2_HUMANIL22RA2physical
11390453
I10R2_HUMANIL10RBphysical
10875937
I22R1_HUMANIL22RA1physical
10875937

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 IL22_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structure of insect-cell-derived IL-22.";
Xu T., Logsdon N.J., Walter M.R.;
Acta Crystallogr. D 61:942-950(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 38-179, AND GLYCOSYLATION ATASN-54 AND ASN-97.

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