INGR2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: INGR2_HUMAN
• UniProt AC: P38484
• Protein Name: Interferon gamma receptor 2 {ECO:0000312|HGNC:HGNC:5440}
• Gene Name: IFNGR2 {ECO:0000312|HGNC:HGNC:5440}
• Organism: Homo sapiens (Human).
• Sequence Length: 337
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein . Cytoplasmic vesicle membrane ; Single-pass type I membrane protein . Golgi apparatus membrane ; Single-pass type I membrane protein . Endoplasmic reticulum membrane ; Single-pass type I membrane protei
• Protein Description: Associates with IFNGR1 to form a receptor for the cytokine interferon gamma (IFNG). [PubMed: 8124716]
• Protein Sequence: MRPTLLWSLLLLLGVFAAAAAAPPDPLSQLPAPQHPKIRLYNAEQVLSWEPVALSNSTRPVVYQVQFKYTDSKWFTADIMSIGVNCTQITATECDFTAASPSAGFPMDFNVTLRLRAELGALHSAWVTMPWFQHYRNVTVGPPENIEVTPGEGSLIIRFSSPFDIADTSTAFFCYYVHYWEKGGIQQVKGPFRSNSISLDNLKPSRVYCLQVQAQLLWNKSNIFRVGHLSNISCYETMADASTELQQVILISVGTFSLLSVLAGACFFLVLKYRGLIKYWFHTPPSIPLQIEEYLKDPTQPILEALDKDSSPKDDVWDSVSIISFPEKEQEDVLQTL

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
56	N-linked_Glycosylation	WEPVALSNSTRPVVY EEEEEECCCCCCEEE	48.53	27599734
85	N-linked_Glycosylation	DIMSIGVNCTQITAT EEEEECCCCEEEEEE	20.22	27599734
110	N-linked_Glycosylation	AGFPMDFNVTLRLRA CCCCCCCEEEEHHHH	22.92	27599734
137	N-linked_Glycosylation	PWFQHYRNVTVGPPE CHHHCCCCCCCCCCC	27.01	27599734
198	Phosphorylation	PFRSNSISLDNLKPS CCCCCCCCCCCCCCC	29.50	17924679
219	N-linked_Glycosylation	VQAQLLWNKSNIFRV HHHHHHCCCCCCEEE	37.54	27599734
231	N-linked_Glycosylation	FRVGHLSNISCYETM EEEECHHCCCCHHCC	36.23	27599734
308	Ubiquitination	PILEALDKDSSPKDD HHHHHHCCCCCCCCC	61.43	-
319	Phosphorylation	PKDDVWDSVSIISFP CCCCCCCCEEEEECC	11.31	29514088
321	Phosphorylation	DDVWDSVSIISFPEK CCCCCCEEEEECCHH	20.39	29514088
324	Phosphorylation	WDSVSIISFPEKEQE CCCEEEEECCHHHHH	32.83	29507054
328	Ubiquitination	SIISFPEKEQEDVLQ EEEECCHHHHHHHHH	66.01	-
336	Phosphorylation	EQEDVLQTL------ HHHHHHHHC------	30.21	29514088

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of INGR2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of INGR2_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
56	N-linked Glycosylation	64 (8)	Q ⇒ R	rs9808753	Multiple sclerosis	24076602

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
JAK2_HUMAN	JAK2	physical	7673114
RL37A_HUMAN	RPL37A	physical	21988832

Drug and Disease Associations

• Kegg Disease
• H00089: IFN-gamma/IL-12 axis, including the following five diseases: IL-12 p40 subunit deficiency; IL-12 rec
• H00342: Tuberculosis
• OMIM Disease
• 614889: Immunodeficiency 28 (IMD28)
• Kegg Drug
• D00747: Interferon gamma-1b (USAN/INN); Actimmune (TN)
• D03357: Interferon gamma-1a (genetical recombination) (JAN); Interferon gamma-1a; Biogamma (TN)
• D08805: Interferon gamma-n1 (JAN); Ogamma (TN)
• DrugBank
• DB00033: Interferon gamma-1b

Related Literatures of Post-Translational Modification

Phosphorylation

"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND MASSSPECTROMETRY.
PubMed: 17924679