IFIT1_HUMAN - dbPTM
IFIT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IFIT1_HUMAN
UniProt AC P09914
Protein Name Interferon-induced protein with tetratricopeptide repeats 1
Gene Name IFIT1
Organism Homo sapiens (Human).
Sequence Length 478
Subcellular Localization Cytoplasm .
Protein Description Interferon-induced antiviral RNA-binding protein that specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs and inhibiting expression of viral messenger RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Exhibits antiviral activity against several viruses including human papilloma and hepatitis C viruses..
Protein Sequence MSTNGDDHQVKDSLEQLRCHFTWELSIDDDEMPDLENRVLDQIEFLDTKYSVGIHNLLAYVKHLKGQNEEALKSLKEAENLMQEEHDNQANVRSLVTWGNFAWMYYHMGRLAEAQTYLDKVENICKKLSNPFRYRMECPEIDCEEGWALLKCGGKNYERAKACFEKVLEVDPENPESSAGYAISAYRLDGFKLATKNHKPFSLLPLRQAVRLNPDNGYIKVLLALKLQDEGQEAEGEKYIEEALANMSSQTYVFRYAAKFYRRKGSVDKALELLKKALQETPTSVLLHHQIGLCYKAQMIQIKEATKGQPRGQNREKLDKMIRSAIFHFESAVEKKPTFEVAHLDLARMYIEAGNHRKAEENFQKLLCMKPVVEETMQDIHFHYGRFQEFQKKSDVNAIIHYLKAIKIEQASLTRDKSINSLKKLVLRKLRRKALDLESLSLLGFVYKLEGNMNEALEYYERALRLAADFENSVRQGP
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
2Phosphorylation------MSTNGDDHQ
------CCCCCCHHH		30.4930108239
3Phosphorylation-----MSTNGDDHQV
-----CCCCCCHHHH		41.7525394399
34UbiquitinationIDDDEMPDLENRVLD
CCCCCCCCHHHHHHH		66.3629967540
42UbiquitinationLENRVLDQIEFLDTK
HHHHHHHHHHHHCCC		32.7129967540
51PhosphorylationEFLDTKYSVGIHNLL
HHHCCCCHHCHHHHH		18.5425690035
60PhosphorylationGIHNLLAYVKHLKGQ
CHHHHHHHHHHHCCC		15.2525690035
65UbiquitinationLAYVKHLKGQNEEAL
HHHHHHHCCCCHHHH		59.1629967540
73AcetylationGQNEEALKSLKEAEN
CCCHHHHHHHHHHHH		61.8719819041
73UbiquitinationGQNEEALKSLKEAEN
CCCHHHHHHHHHHHH		61.8729967540
96UbiquitinationQANVRSLVTWGNFAW
HHCHHHHHHHHHHHH		4.4529967540
120UbiquitinationEAQTYLDKVENICKK
HHHHHHHHHHHHHHH		49.18-
127UbiquitinationKVENICKKLSNPFRY
HHHHHHHHCCCCCCC		53.3829967540
130UbiquitinationNICKKLSNPFRYRME
HHHHHCCCCCCCCCC		50.6029967540
135UbiquitinationLSNPFRYRMECPEID
CCCCCCCCCCCCCCC		15.3529967540
151UbiquitinationEEGWALLKCGGKNYE
HHHEEEEECCCCCHH		31.51-
161UbiquitinationGKNYERAKACFEKVL
CCCHHHHHHHHHHHH		52.4929967540
166UbiquitinationRAKACFEKVLEVDPE
HHHHHHHHHHCCCCC		31.6929967540
168UbiquitinationKACFEKVLEVDPENP
HHHHHHHHCCCCCCC		8.6529967540
192UbiquitinationAYRLDGFKLATKNHK
EEEECCEEEECCCCC		42.6229967540
195UbiquitinationLDGFKLATKNHKPFS
ECCEEEECCCCCCCC		42.7029967540
199UbiquitinationKLATKNHKPFSLLPL
EEECCCCCCCCCCCH		58.0929967540
218PhosphorylationRLNPDNGYIKVLLAL
HHCCCCCHHHEEEEE		12.1120068231
226UbiquitinationIKVLLALKLQDEGQE
HHEEEEEEECCCCCH		38.2029967540
238UbiquitinationGQEAEGEKYIEEALA
CCHHHHHHHHHHHHH		63.4929967540
259AcetylationYVFRYAAKFYRRKGS
HHHHHHHHHHHHCCC		34.4525953088
259MalonylationYVFRYAAKFYRRKGS
HHHHHHHHHHHHCCC		34.4526320211
269UbiquitinationRRKGSVDKALELLKK
HHCCCHHHHHHHHHH		53.3629967540
272UbiquitinationGSVDKALELLKKALQ
CCHHHHHHHHHHHHH		57.8429967540
303UbiquitinationKAQMIQIKEATKGQP
HHHEEHHHHHHCCCC		25.5629967540
305UbiquitinationQMIQIKEATKGQPRG
HEEHHHHHHCCCCCC		15.0329967540
324PhosphorylationKLDKMIRSAIFHFES
HHHHHHHHHHHHHHH		18.1328857561
327UbiquitinationKMIRSAIFHFESAVE
HHHHHHHHHHHHHHH		5.5929967540
331PhosphorylationSAIFHFESAVEKKPT
HHHHHHHHHHHCCCC		36.3528857561
336MalonylationFESAVEKKPTFEVAH
HHHHHHCCCCEEEEE		35.4726320211
336UbiquitinationFESAVEKKPTFEVAH
HHHHHHCCCCEEEEE		35.4729967540
358UbiquitinationIEAGNHRKAEENFQK
HHCCCHHHHHHHHHH		53.2329967540
361UbiquitinationGNHRKAEENFQKLLC
CCHHHHHHHHHHHHC		69.1129967540
362UbiquitinationNHRKAEENFQKLLCM
CHHHHHHHHHHHHCC		35.8329967540
376UbiquitinationMKPVVEETMQDIHFH
CHHHHHHHHHHHHHH		13.4629967540
386UbiquitinationDIHFHYGRFQEFQKK
HHHHHHCCHHHHHHH		23.9429967540
392UbiquitinationGRFQEFQKKSDVNAI
CCHHHHHHHHCHHHH		60.6129967540
393UbiquitinationRFQEFQKKSDVNAII
CHHHHHHHHCHHHHH		40.9029967540
402PhosphorylationDVNAIIHYLKAIKIE
CHHHHHHHHHHHHHH		10.25-
407UbiquitinationIHYLKAIKIEQASLT
HHHHHHHHHHHHHCC		45.0829967540
412PhosphorylationAIKIEQASLTRDKSI
HHHHHHHHCCCCCCH		29.9320068231
414PhosphorylationKIEQASLTRDKSINS
HHHHHHCCCCCCHHH		34.0326074081
417UbiquitinationQASLTRDKSINSLKK
HHHCCCCCCHHHHHH		50.3629967540
418PhosphorylationASLTRDKSINSLKKL
HHCCCCCCHHHHHHH		31.1526074081
421PhosphorylationTRDKSINSLKKLVLR
CCCCCHHHHHHHHHH		39.6426074081
423UbiquitinationDKSINSLKKLVLRKL
CCCHHHHHHHHHHHH		43.8329967540
473PhosphorylationLAADFENSVRQGP--
HHHHHHHHHHCCC--		16.1030108239
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 IFIT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IFIT1_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 IFIT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IFIT3_HUMANIFIT3physical
16189514
ISG15_HUMANISG15physical
16009940
RLA1_HUMANRPLP1physical
21642987
RUXF_HUMANSNRPFphysical
21642987
HS90A_HUMANHSP90AA1physical
21642987
SMD3_HUMANSNRPD3physical
21642987
IFT1B_HUMANIFIT1Bphysical
21642987
SMD1_HUMANSNRPD1physical
21642987
RU2B_HUMANSNRPB2physical
21642987
RSMB_HUMANSNRPBphysical
21642987
RU17_HUMANSNRNP70physical
21642987
MCCB_HUMANMCCC2physical
21642987
PCCB_HUMANPCCBphysical
21642987
ACACA_HUMANACACAphysical
21642987
PCCA_HUMANPCCAphysical
21642987
PYC_HUMANPCphysical
21642987
MCCA_HUMANMCCC1physical
21642987
PABP4_HUMANPABPC4physical
21642987
SMD2_HUMANSNRPD2physical
21642987
SNRPA_HUMANSNRPAphysical
21642987
DCD_HUMANDCDphysical
21642987
RUXE_HUMANSNRPEphysical
21642987
RU1C_HUMANSNRPCphysical
21642987
HS90B_HUMANHSP90AB1physical
21642987
GRPE1_HUMANGRPEL1physical
21642987
HNRPC_HUMANHNRNPCphysical
21642987
TOE1_HUMANTOE1physical
21642987
ILF2_HUMANILF2physical
21642987
NUCL_HUMANNCLphysical
21642987
IF2B1_HUMANIGF2BP1physical
21642987
PABP1_HUMANPABPC1physical
21642987
IFIT2_HUMANIFIT2physical
21642987
IFIT3_HUMANIFIT3physical
21642987
RU2A_HUMANSNRPA1physical
21642987
MOV10_HUMANMOV10physical
21642987
YBOX1_HUMANYBX1physical
21642987
S10A7_HUMANS100A7physical
21642987
IFIT5_HUMANIFIT5physical
21642987
IFIT3_HUMANIFIT3physical
25416956
IFIT3_HUMANIFIT3physical
21516116
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IFIT1_HUMAN

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Related Literatures of Post-Translational Modification

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