INAR1_HUMAN - dbPTM
INAR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INAR1_HUMAN
UniProt AC P17181
Protein Name Interferon alpha/beta receptor 1
Gene Name IFNAR1
Organism Homo sapiens (Human).
Sequence Length 557
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein . Late endosome . Lysosome . Interferon binding triggers internalization of the receptor from the cell membrane into endosomes and then into lysosomes.
Protein Description Component of the receptor for type I interferons, including interferons alpha, IFNB1 and IFNW1. [PubMed: 2153461]
Protein Sequence MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTPVIQDYPLIYEIIFWENTSNAERKIIEKKTDVTVPNLKPLTVYCVKARAHTMDEKLNKSSVFSDAVCEKTKPGNTSKIWLIVGICIALFALPFVIYAAKVFLRCINYVFFPSLKPSSSIDEYFSEQPLKNLLLSTSEEQIEKCFIIENISTIATVEETNQTDEDHKKYSSQTSQDSGNYSNEDESESKTSEELQQDFV
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
17UbiquitinationTLVLVAVAPWVLSAA
HHHHHHHHHHHHHHH		5.19-
50N-linked_GlycosylationDNFILRWNRSDESVG
CCEEEEECCCCCCCC		27.43UniProtKB CARBOHYD
56UbiquitinationWNRSDESVGNVTFSF
ECCCCCCCCEEEEEE		6.43-
58N-linked_GlycosylationRSDESVGNVTFSFDY
CCCCCCCEEEEEEEC		27.7419349973
58N-linked_GlycosylationRSDESVGNVTFSFDY
CCCCCCCEEEEEEEC		27.7419349973
81N-linked_GlycosylationIKLSGCQNITSTKCN
EEECCCCCCCCCCCC		43.51UniProtKB CARBOHYD
85PhosphorylationGCQNITSTKCNFSSL
CCCCCCCCCCCHHHC		30.85-
86UbiquitinationCQNITSTKCNFSSLK
CCCCCCCCCCHHHCE		27.27-
88N-linked_GlycosylationNITSTKCNFSSLKLN
CCCCCCCCHHHCEEE		41.20UniProtKB CARBOHYD
91PhosphorylationSTKCNFSSLKLNVYE
CCCCCHHHCEEEEEH		25.9424719451
101UbiquitinationLNVYEEIKLRIRAEK
EEEEHHHHHHEEEEC		34.69-
110N-linked_GlycosylationRIRAEKENTSSWYEV
HEEEECCCCCCCEEE		57.2219349973
110N-linked_GlycosylationRIRAEKENTSSWYEV
HEEEECCCCCCCEEE		57.2219349973
125UbiquitinationDSFTPFRKAQIGPPE
CCCCCCCCCCCCCCC		45.05-
172N-linked_GlycosylationYSLVIWKNSSGVEER
EEEEEEECCCCHHHH		26.8121854986
185PhosphorylationERIENIYSRHKIYKL
HHHHHHHHHHCEEEC		24.9024719451
191UbiquitinationYSRHKIYKLSPETTY
HHHHCEEECCCCCCH		46.06-
209UbiquitinationVKAALLTSWKIGVYS
HHHHHHHCCCCCCCC		26.75-
254N-linked_GlycosylationKWDYTYANMTFQVQW
EEEEEEECEEEEHHH		21.44UniProtKB CARBOHYD
278UbiquitinationGNHLYKWKQIPDCEN
CCCCEEEEECCCCCC		33.91-
313N-linked_GlycosylationRVQASDGNNTSFWSE
EEECCCCCCCCCEEE		54.3019349973
313N-linked_GlycosylationRVQASDGNNTSFWSE
EEECCCCCCCCCEEE		54.3019349973
314N-linked_GlycosylationVQASDGNNTSFWSEE
EECCCCCCCCCEEEE		42.50UniProtKB CARBOHYD
314N-linked_GlycosylationVQASDGNNTSFWSEE
EECCCCCCCCCEEEE		42.5019349973
328UbiquitinationEIKFDTEIQAFLLPP
EEECCCHHHHHCCCC		3.77-
376N-linked_GlycosylationYEIIFWENTSNAERK
EEEEEEECCCHHHHH		39.13UniProtKB CARBOHYD
397UbiquitinationDVTVPNLKPLTVYCV
CCCCCCCCCEEEEEE		44.62-
414UbiquitinationRAHTMDEKLNKSSVF
CCCCCCHHHCCCCCC		53.77-
416N-linked_GlycosylationHTMDEKLNKSSVFSD
CCCCHHHCCCCCCCH		53.91UniProtKB CARBOHYD
417UbiquitinationTMDEKLNKSSVFSDA
CCCHHHCCCCCCCHH		55.32-
433N-linked_GlycosylationCEKTKPGNTSKIWLI
HCCCCCCCCHHHHHH		50.10UniProtKB CARBOHYD
463S-palmitoylationAAKVFLRCINYVFFP
HHHHHHHHHHHHCCC		2.2919561067
466PhosphorylationVFLRCINYVFFPSLK
HHHHHHHHHCCCCCC		4.449677371
475PhosphorylationFFPSLKPSSSIDEYF
CCCCCCCCCCHHHHH		34.8226657352
481PhosphorylationPSSSIDEYFSEQPLK
CCCCHHHHHCCCHHH		14.5222817900
493PhosphorylationPLKNLLLSTSEEQIE
HHHHHCCCCCHHHHH		29.8323401153
494PhosphorylationLKNLLLSTSEEQIEK
HHHHCCCCCHHHHHH		39.8830266825
495PhosphorylationKNLLLSTSEEQIEKC
HHHCCCCCHHHHHHH		35.4429255136
501UbiquitinationTSEEQIEKCFIIENI
CCHHHHHHHEEEECC		35.75PubMed
525UbiquitinationNQTDEDHKKYSSQTS
CCCCCCHHHHCCCCC		66.77PubMed
526UbiquitinationQTDEDHKKYSSQTSQ
CCCCCHHHHCCCCCC		47.1215337770
528PhosphorylationDEDHKKYSSQTSQDS
CCCHHHHCCCCCCCC		25.5027642862
532PhosphorylationKKYSSQTSQDSGNYS
HHHCCCCCCCCCCCC		25.0921695243
535PhosphorylationSSQTSQDSGNYSNED
CCCCCCCCCCCCCCC		22.6921695243
538PhosphorylationTSQDSGNYSNEDESE
CCCCCCCCCCCCCCC		19.1925884760
539PhosphorylationSQDSGNYSNEDESES
CCCCCCCCCCCCCCC		37.4328450419
544PhosphorylationNYSNEDESESKTSEE
CCCCCCCCCCCCCHH		60.5428450419
546PhosphorylationSNEDESESKTSEELQ
CCCCCCCCCCCHHHH		50.9828450419
548PhosphorylationEDESESKTSEELQQD
CCCCCCCCCHHHHHH		51.1229514088
549PhosphorylationDESESKTSEELQQDF
CCCCCCCCHHHHHHC		32.5829514088
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
466YPhosphorylationKinaseTYK2P29597
Uniprot
481YPhosphorylationKinaseTYK2P29597
Uniprot
532SPhosphorylationKinaseMAPK14Q16539
GPS
535SPhosphorylationKinaseCSNK1A1P48729
GPS
535SPhosphorylationKinasePRKD2Q9BZL6
PSP
-KUbiquitinationE3 ubiquitin ligaseFBXW11Q9UKB1
PMID:14532120
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:16551269
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
463CPalmitoylation

19561067
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 INAR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANM1_HUMANPRMT1physical
9029147
TYK2_HUMANTYK2physical
9733772
STAT2_HUMANSTAT2physical
9121453
STAT2_HUMANSTAT2physical
7559568
P85A_HUMANPIK3R1physical
10542297
STAT2_HUMANSTAT2physical
8605876
STAT3_HUMANSTAT3physical
8626489
TYK2_HUMANTYK2physical
18474601
AP2M1_HUMANAP2M1physical
18474601
FBW1B_HUMANFBXW11physical
15337770
TYK2_HUMANTYK2physical
15337770
FBW1B_HUMANFBXW11physical
14532120
TYK2_HUMANTYK2physical
15356134
STAT2_HUMANSTAT2physical
15356134
FBW1A_HUMANBTRCphysical
18056411
FBW1B_HUMANFBXW11physical
18056411
AP2M1_HUMANAP2M1physical
18056411
KPCD2_HUMANPRKD2physical
21173164
FBW1A_HUMANBTRCphysical
21173164
SOCS1_HUMANSOCS1physical
21757742
STAT6_HUMANSTAT6physical
10490982
INAR2_HUMANIFNAR2physical
26008745
UBP7_HUMANUSP7physical
28656291
GLYM_HUMANSHMT2physical
24075985
INAR2_HUMANIFNAR2physical
24075985
CH60_HUMANHSPD1physical
24075985
GLYC_HUMANSHMT1physical
24075985
KPYM_HUMANPKMphysical
24075985
UBA1_HUMANUBA1physical
24075985
1433B_HUMANYWHABphysical
24075985
HNRPK_HUMANHNRNPKphysical
24075985
HNRPU_HUMANHNRNPUphysical
24075985
1433E_HUMANYWHAEphysical
24075985
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
D00745 Interferon alfa-2a (genetical recombination) (JAN); Interferon alfa-2a (USAN/INN); Roferon A (TN)
D00746 Interferon beta-1b (genetical recombination) (JAN); Interferon beta-1b (USAN/INN); Betaseron (TN); E
D02744 Interferon alfacon-1 (genetical recombination) (JAN); Interferon alfacon-1 (USAN/INN); Advaferon (TN
D02745 Interferon alfa-2b (genetical recombination) (JAN); Interferon alfa-2b (USAN); Intron A (TN)
D02747 Peginterferon alfa-2a (genetical recombination) (JAN); Peginterferon alfa-2a (USAN/INN); Pegasys (TN
D02748 Peginterferon alfa-2b (generical recombination) (JAN); Peginterferon alfa-2b (INN); Pegintron (TN);
D03304 Interferon beta (JAN); Feron (TN)
D03305 Interferon alfa (BALL-1) (JAN); Interferon alfa (NAMAWA) (JAN); Interferon alfa (INN); OIF (TN)
D04552 Interferon alfa-n1 (USAN); alfa-Interferon; Well-feron (TN)
D04554 Interferon beta-1a (genetical recombination) (JAN); Interferon beta-1a (USAN); Avonex (TN); Rebif (T
D08844 Albinterferon alfa-2b (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of INAR1_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structural linkage between ligand discrimination and receptoractivation by type I interferons.";
Thomas C., Moraga I., Levin D., Krutzik P.O., Podoplelova Y.,Trejo A., Lee C., Yarden G., Vleck S.E., Glenn J.S., Nolan G.P.,Piehler J., Schreiber G., Garcia K.C.;
Cell 146:621-632(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 28-436 IN COMPLEX WITH IFNAR2AND IFNW1, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-172.
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-58; ASN-110 AND ASN-313,AND MASS SPECTROMETRY.
Palmitoylation
ReferencePubMed
"Palmitoylation of interferon-alpha (IFN-alpha) receptor subunitIFNAR1 is required for the activation of Stat1 and Stat2 by IFN-alpha.";
Claudinon J., Gonnord P., Beslard E., Marchetti M., Mitchell K.,Boularan C., Johannes L., Eid P., Lamaze C.;
J. Biol. Chem. 284:24328-24340(2009).
Cited for: PALMITOYLATION AT CYS-463.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-494, AND MASSSPECTROMETRY.

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