INGR1_HUMAN - dbPTM
INGR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INGR1_HUMAN
UniProt AC P15260
Protein Name Interferon gamma receptor 1 {ECO:0000312|HGNC:HGNC:5439}
Gene Name IFNGR1 {ECO:0000312|HGNC:HGNC:5439}
Organism Homo sapiens (Human).
Sequence Length 489
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Associates with IFNGR2 to form a receptor for the cytokine interferon gamma (IFNG). [PubMed: 7615558]
Protein Sequence MALLFLLPLVMQGVSRAEMGTADLGPSSVPTPTNVTIESYNMNPIVYWEYQIMPQVPVFTVEVKNYGVKNSEWIDACINISHHYCNISDHVGDPSNSLWVRVKARVGQKESAYAKSEEFAVCRDGKIGPPKLDIRKEEKQIMIDIFHPSVFVNGDEQEVDYDPETTCYIRVYNVYVRMNGSEIQYKILTQKEDDCDEIQCQLAIPVSSLNSQYCVSAEGVLHVWGVTTEKSKEVCITIFNSSIKGSLWIPVVAALLLFLVLSLVFICFYIKKINPLKEKSIILPKSLISVVRSATLETKPESKYVSLITSYQPFSLEKEVVCEEPLSPATVPGMHTEDNPGKVEHTEELSSITEVVTTEENIPDVVPGSHLTPIERESSSPLSSNQSEPGSIALNSYHSRNCSESDHSRNGFDTDSSCLESHSSLSDSEFPPNNKGEIKTEGQELITVIKAPTSFGYDKPHVLVDLLVDDSGKESLIGYRPTEDSKEFS
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
34N-linked_GlycosylationSSVPTPTNVTIESYN
CCCCCCCEEEEEEEE		30.09UniProtKB CARBOHYD
79N-linked_GlycosylationEWIDACINISHHYCN
HHHHHHHHHHCCCCC		29.60UniProtKB CARBOHYD
86N-linked_GlycosylationNISHHYCNISDHVGD
HHHCCCCCCHHHCCC		29.63UniProtKB CARBOHYD
105UbiquitinationLWVRVKARVGQKESA
EEEEEEEECCCCCCH		27.64-
115UbiquitinationQKESAYAKSEEFAVC
CCCCHHCCCCCEEEE		45.80-
179N-linked_GlycosylationYNVYVRMNGSEIQYK
EEEEEEECCEEEEEE		40.03UniProtKB CARBOHYD
181PhosphorylationVYVRMNGSEIQYKIL
EEEEECCEEEEEEEE		26.9028787133
240N-linked_GlycosylationEVCITIFNSSIKGSL
EEEEEECCCCCCCCC		30.88UniProtKB CARBOHYD
262PhosphorylationLLLFLVLSLVFICFY
HHHHHHHHHHHHHHH		18.27-
279UbiquitinationKINPLKEKSIILPKS
HHCCCCCCEEECCHH		45.4221906983
280PhosphorylationINPLKEKSIILPKSL
HCCCCCCEEECCHHH		18.8928111955
285UbiquitinationEKSIILPKSLISVVR
CCEEECCHHHHHHHH		55.2221906983
286PhosphorylationKSIILPKSLISVVRS
CEEECCHHHHHHHHH		29.0626434776
289PhosphorylationILPKSLISVVRSATL
ECCHHHHHHHHHHCC		21.6126434776
293PhosphorylationSLISVVRSATLETKP
HHHHHHHHHCCCCCC		17.6228102081
295PhosphorylationISVVRSATLETKPES
HHHHHHHCCCCCCCC		26.7727273156
298PhosphorylationVRSATLETKPESKYV
HHHHCCCCCCCCCEE		55.8223403867
299UbiquitinationRSATLETKPESKYVS
HHHCCCCCCCCCEEE		37.1021906983
302PhosphorylationTLETKPESKYVSLIT
CCCCCCCCCEEEEEE		37.5023403867
304PhosphorylationETKPESKYVSLITSY
CCCCCCCEEEEEEEC		12.4421945579
306PhosphorylationKPESKYVSLITSYQP
CCCCCEEEEEEECCC		15.8021945579
309PhosphorylationSKYVSLITSYQPFSL
CCEEEEEEECCCCCC		27.0321945579
310PhosphorylationKYVSLITSYQPFSLE
CEEEEEEECCCCCCC		18.1221945579
311PhosphorylationYVSLITSYQPFSLEK
EEEEEEECCCCCCCC		16.1421945579
315PhosphorylationITSYQPFSLEKEVVC
EEECCCCCCCCEEEE		42.1521945579
327PhosphorylationVVCEEPLSPATVPGM
EEECCCCCCCCCCCC		24.1726657352
330PhosphorylationEEPLSPATVPGMHTE
CCCCCCCCCCCCCCC		30.5325850435
336PhosphorylationATVPGMHTEDNPGKV
CCCCCCCCCCCCCCC		35.8227732954
346PhosphorylationNPGKVEHTEELSSIT
CCCCCEEHHHHHCCE		20.0426471730
350PhosphorylationVEHTEELSSITEVVT
CEEHHHHHCCEEEEE		23.9928348404
351PhosphorylationEHTEELSSITEVVTT
EEHHHHHCCEEEEEC		46.2728348404
353PhosphorylationTEELSSITEVVTTEE
HHHHHCCEEEEECCC		25.3626471730
369PhosphorylationIPDVVPGSHLTPIER
CCCCCCCCCCCCCCC		14.84-
372PhosphorylationVVPGSHLTPIERESS
CCCCCCCCCCCCCCC		19.4524275569
378PhosphorylationLTPIERESSSPLSSN
CCCCCCCCCCCCCCC		42.1921945579
379PhosphorylationTPIERESSSPLSSNQ
CCCCCCCCCCCCCCC		31.0821945579
380PhosphorylationPIERESSSPLSSNQS
CCCCCCCCCCCCCCC		38.8621945579
383PhosphorylationRESSSPLSSNQSEPG
CCCCCCCCCCCCCCC		30.5421945579
384PhosphorylationESSSPLSSNQSEPGS
CCCCCCCCCCCCCCC		46.7221945579
387PhosphorylationSPLSSNQSEPGSIAL
CCCCCCCCCCCCEEE		50.4321945579
391PhosphorylationSNQSEPGSIALNSYH
CCCCCCCCEEEEEEC		18.5321945579
396PhosphorylationPGSIALNSYHSRNCS
CCCEEEEEECCCCCC		25.6825849741
397PhosphorylationGSIALNSYHSRNCSE
CCEEEEEECCCCCCC		11.6221945579
399PhosphorylationIALNSYHSRNCSESD
EEEEEECCCCCCCCC		19.5621945579
403PhosphorylationSYHSRNCSESDHSRN
EECCCCCCCCCCCCC		43.6224275569
405PhosphorylationHSRNCSESDHSRNGF
CCCCCCCCCCCCCCC		25.0823898821
408PhosphorylationNCSESDHSRNGFDTD
CCCCCCCCCCCCCCC		32.2223898821
450UbiquitinationQELITVIKAPTSFGY
EEEEEEEECCCCCCC		43.93-
454PhosphorylationTVIKAPTSFGYDKPH
EEEECCCCCCCCCCE		18.6726356563
457PhosphorylationKAPTSFGYDKPHVLV
ECCCCCCCCCCEEEE		20.8425159151
459UbiquitinationPTSFGYDKPHVLVDL
CCCCCCCCCEEEEEE		28.65-
479PhosphorylationGKESLIGYRPTEDSK
CCCCCCCEECCCCCC		13.3629978859
482PhosphorylationSLIGYRPTEDSKEFS
CCCCEECCCCCCCCC		43.3529978859
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
457YPhosphorylationKinaseJAK1P23458
PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseK3P90495
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseK5P90489
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INGR1_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 INGR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JAK2_HUMANJAK2physical
7673114
JAK1_HUMANJAK1physical
12133952
STAT1_HUMANSTAT1physical
10848598
JAK1_HUMANJAK1physical
21689637
JAK2_HUMANJAK2physical
21689637
STAT1_HUMANSTAT1physical
21689637
MD2L2_HUMANMAD2L2physical
28514442
BMR1A_HUMANBMPR1Aphysical
28514442
NFIP1_HUMANNDFIP1physical
28514442
CD320_HUMANCD320physical
28514442
RHOU_HUMANRHOUphysical
28514442
SRC_HUMANSRCphysical
28514442
FGFR1_HUMANFGFR1physical
28514442
JAK1_HUMANJAK1physical
28514442
NOTC3_HUMANNOTCH3physical
28514442
LRP10_HUMANLRP10physical
28514442
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
209950Immunodeficiency 27A (IMD27A)
615978Immunodeficiency 27B (IMD27B)
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
There are no disease associations of PTM sites.
Regulatory Network of INGR1_HUMAN

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Related Literatures of Post-Translational Modification

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