IFNA2_HUMAN - dbPTM
IFNA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IFNA2_HUMAN
UniProt AC P01563
Protein Name Interferon alpha-2
Gene Name IFNA2
Organism Homo sapiens (Human).
Sequence Length 188
Subcellular Localization Secreted.
Protein Description Produced by macrophages, IFN-alpha have antiviral activities..
Protein Sequence MALTFALLVALLVLSCKSSCSVGCDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
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
19PhosphorylationLVLSCKSSCSVGCDL
HHHHCCCCCCCCCCC
8.91-
24GlutathionylationKSSCSVGCDLPQTHS
CCCCCCCCCCCCCCC
4.5622833525
121GlutathionylationQLNDLEACVIQGVGV
HHHCHHHHHHCCCCC
1.7022833525
129O-linked_GlycosylationVIQGVGVTETPLMKE
HHCCCCCCCCCCCCC
28.36UniProtKB CARBOHYD
175PhosphorylationAEIMRSFSLSTNLQE
HHHHHHCCCCHHHHH
23.74-

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 IFNA2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IFNA2_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 IFNA2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IFNA5_HUMANIFNA5physical
26186194
IFIT3_HUMANIFIT3physical
26186194
ZER1_HUMANZER1physical
26186194
ISG15_HUMANISG15physical
26186194
ISG15_HUMANISG15physical
28514442
IFNA5_HUMANIFNA5physical
28514442
IFIT3_HUMANIFIT3physical
28514442
UBR3_HUMANUBR3physical
28514442

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 IFNA2_HUMAN

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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"Natural human interferon-alpha 2 is O-glycosylated.";
Adolf G.R., Kalsner I., Ahorn H., Maurer-Fogy I., Cantell K.;
Biochem. J. 276:511-518(1991).
Cited for: GLYCOSYLATION AT THR-129, AND VARIANTS ALPHA-2B AND ALPHA-2C.

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