IFIT2_HUMAN - dbPTM
IFIT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IFIT2_HUMAN
UniProt AC P09913
Protein Name Interferon-induced protein with tetratricopeptide repeats 2
Gene Name IFIT2
Organism Homo sapiens (Human).
Sequence Length 472
Subcellular Localization Cytoplasm . Endoplasmic reticulum .
Protein Description IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. 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). Binds AU-rich viral RNAs, with or without 5' triphosphorylation, RNA-binding is required for antiviral activity. Can promote apoptosis..
Protein Sequence MSENNKNSLESSLRQLKCHFTWNLMEGENSLDDFEDKVFYRTEFQNREFKATMCNLLAYLKHLKGQNEAALECLRKAEELIQQEHADQAEIRSLVTWGNYAWVYYHMGRLSDVQIYVDKVKHVCEKFSSPYRIESPELDCEEGWTRLKCGGNQNERAKVCFEKALEKKPKNPEFTSGLAIASYRLDNWPPSQNAIDPLRQAIRLNPDNQYLKVLLALKLHKMREEGEEEGEGEKLVEEALEKAPGVTDVLRSAAKFYRRKDEPDKAIELLKKALEYIPNNAYLHCQIGCCYRAKVFQVMNLRENGMYGKRKLLELIGHAVAHLKKADEANDNLFRVCSILASLHALADQYEDAEYYFQKEFSKELTPVAKQLLHLRYGNFQLYQMKCEDKAIHHFIEGVKINQKSREKEKMKDKLQKIAKMRLSKNGADSEALHVLAFLQELNEKMQQADEDSERGLESGSLIPSASSWNGE
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
2Acetylation------MSENNKNSL
------CCCCCHHHH		49.3722814378
2Phosphorylation------MSENNKNSL
------CCCCCHHHH		49.3728857561
6Ubiquitination--MSENNKNSLESSL
--CCCCCHHHHHHHH		60.54-
8PhosphorylationMSENNKNSLESSLRQ
CCCCCHHHHHHHHHH		34.81-
30PhosphorylationNLMEGENSLDDFEDK
HCCCCCCCCCHHCCC		28.9528258704
64UbiquitinationLAYLKHLKGQNEAAL
HHHHHHHCCCCHHHH		59.16-
93PhosphorylationADQAEIRSLVTWGNY
CCHHHHHHHHHHCHH		32.6225954137
96PhosphorylationAEIRSLVTWGNYAWV
HHHHHHHHHCHHHHH		32.7125954137
100PhosphorylationSLVTWGNYAWVYYHM
HHHHHCHHHHHEEEC		9.6325262027
104PhosphorylationWGNYAWVYYHMGRLS
HCHHHHHEEECCCCC		4.1325262027
105PhosphorylationGNYAWVYYHMGRLSD
CHHHHHEEECCCCCC		3.9225954137
111PhosphorylationYYHMGRLSDVQIYVD
EEECCCCCCEEEHHH		34.0825954137
126UbiquitinationKVKHVCEKFSSPYRI
HHHHHHHHCCCCCEE		45.48-
148UbiquitinationEEGWTRLKCGGNQNE
CCCCEEEECCCCCCH		27.78-
158UbiquitinationGNQNERAKVCFEKAL
CCCCHHHHHHHHHHH		45.84-
163UbiquitinationRAKVCFEKALEKKPK
HHHHHHHHHHHHCCC		37.71-
163AcetylationRAKVCFEKALEKKPK
HHHHHHHHHHHHCCC		37.7126051181
191PhosphorylationRLDNWPPSQNAIDPL
ECCCCCCCCCCCHHH		31.80-
212UbiquitinationNPDNQYLKVLLALKL
CCCCHHHHHHHHHHH		26.38-
218UbiquitinationLKVLLALKLHKMREE
HHHHHHHHHHHHHHH		42.83-
221UbiquitinationLLALKLHKMREEGEE
HHHHHHHHHHHHCCC		50.52-
234UbiquitinationEEEGEGEKLVEEALE
CCCCCHHHHHHHHHH		69.55-
242UbiquitinationLVEEALEKAPGVTDV
HHHHHHHHCCCHHHH		61.81-
255UbiquitinationDVLRSAAKFYRRKDE
HHHHHHHHHHHCCCC		42.52-
265UbiquitinationRRKDEPDKAIELLKK
HCCCCHHHHHHHHHH		63.08-
272UbiquitinationKAIELLKKALEYIPN
HHHHHHHHHHHHCCC		59.16-
294UbiquitinationIGCCYRAKVFQVMNL
CCCCHHCEEEEEEEH		34.29-
294MalonylationIGCCYRAKVFQVMNL
CCCCHHCEEEEEEEH		34.2926320211
309MethylationRENGMYGKRKLLELI
HHHCCCCHHHHHHHH		28.95-
325UbiquitinationHAVAHLKKADEANDN
HHHHHHHHHHHCCCH		68.39-
363UbiquitinationYFQKEFSKELTPVAK
HHHHHHCHHCHHHHH		63.16-
366PhosphorylationKEFSKELTPVAKQLL
HHHCHHCHHHHHHHH		19.4627794612
366O-linked_GlycosylationKEFSKELTPVAKQLL
HHHCHHCHHHHHHHH		19.4630379171
370UbiquitinationKELTPVAKQLLHLRY
HHCHHHHHHHHHHHH		41.53-
383PhosphorylationRYGNFQLYQMKCEDK
HHCCEEEEEEEECHH		8.8622461510
390UbiquitinationYQMKCEDKAIHHFIE
EEEEECHHHHHHHHH		27.26-
400UbiquitinationHHFIEGVKINQKSRE
HHHHHHCCCCHHHHH		46.96-
417AcetylationKMKDKLQKIAKMRLS
HHHHHHHHHHHHHHH		55.887960879
420AcetylationDKLQKIAKMRLSKNG
HHHHHHHHHHHHCCC		28.207960889
424PhosphorylationKIAKMRLSKNGADSE
HHHHHHHHCCCCCHH		17.4522817900
425UbiquitinationIAKMRLSKNGADSEA
HHHHHHHCCCCCHHH		65.08-
445UbiquitinationFLQELNEKMQQADED
HHHHHHHHHHHCCHH		40.72-
461PhosphorylationERGLESGSLIPSASS
HHHHHCCCCCCCCCC		32.1927251275
467PhosphorylationGSLIPSASSWNGE--
CCCCCCCCCCCCC--		39.9828348404
468PhosphorylationSLIPSASSWNGE---
CCCCCCCCCCCC---		25.0325159151
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 IFIT2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IFIT2_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 IFIT2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IFIT3_HUMANIFIT3physical
16189514
RL31_HUMANRPL31physical
21642987
RLA1_HUMANRPLP1physical
21642987
RCN2_HUMANRCN2physical
21642987
YBOX1_HUMANYBX1physical
21642987
SMD1_HUMANSNRPD1physical
21642987
TBB5_HUMANTUBBphysical
21642987
IFIT1_HUMANIFIT1physical
21642987
IFIT3_HUMANIFIT3physical
21642987
SMD2_HUMANSNRPD2physical
21642987
RUXE_HUMANSNRPEphysical
21642987
ODB2_HUMANDBTphysical
21642987
DNJA2_HUMANDNAJA2physical
21642987
RUXF_HUMANSNRPFphysical
21642987
MATR3_HUMANMATR3physical
21642987
HNRPD_HUMANHNRNPDphysical
21642987
SMD3_HUMANSNRPD3physical
21642987
ILF2_HUMANILF2physical
21642987
ROA2_HUMANHNRNPA2B1physical
21642987
SNRPA_HUMANSNRPAphysical
21642987
RU2B_HUMANSNRPB2physical
21642987
RSMB_HUMANSNRPBphysical
21642987
RU2A_HUMANSNRPA1physical
21642987
RU17_HUMANSNRNP70physical
21642987
PABP1_HUMANPABPC1physical
21642987
PABP4_HUMANPABPC4physical
21642987
ILF3_HUMANILF3physical
21642987
ROA1_HUMANHNRNPA1physical
21642987
HNRPL_HUMANHNRNPLphysical
21642987
HNRDL_HUMANHNRNPDLphysical
21642987
ROAA_HUMANHNRNPABphysical
21642987
RU1C_HUMANSNRPCphysical
21642987
YBOX3_HUMANYBX3physical
21642987
TOE1_HUMANTOE1physical
21642987
NUTM1_HUMANNUTM1physical
25416956
PHAR4_HUMANPHACTR4physical
28514442
IFIT1_HUMANIFIT1physical
28514442
HOME3_HUMANHOMER3physical
28514442
IFIT3_HUMANIFIT3physical
28514442
BATF3_HUMANBATF3physical
28514442
DPOG2_HUMANPOLG2physical
28514442
RB11B_HUMANRAB11Bphysical
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 IFIT2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND MASSSPECTROMETRY.

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