IFIT3_HUMAN - dbPTM
IFIT3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IFIT3_HUMAN
UniProt AC O14879
Protein Name Interferon-induced protein with tetratricopeptide repeats 3
Gene Name IFIT3
Organism Homo sapiens (Human).
Sequence Length 490
Subcellular Localization Cytoplasm. Mitochondrion.
Protein Description IFN-induced antiviral protein which acts as an inhibitor of cellular as well as viral processes, cell migration, proliferation, signaling, and viral replication. Enhances MAVS-mediated host antiviral responses by serving as an adapter bridging TBK1 to MAVS which leads to the activation of TBK1 and phosphorylation of IRF3 and phosphorylated IRF3 translocates into nucleus to promote antiviral gene transcription. Exihibits an antiproliferative activity via the up-regulation of cell cycle negative regulators CDKN1A/p21 and CDKN1B/p27. Normally, CDKN1B/p27 turnover is regulated by COPS5, which binds CDKN1B/p27 in the nucleus and exports it to the cytoplasm for ubiquitin-dependent degradation. IFIT3 sequesters COPS5 in the cytoplasm, thereby increasing nuclear CDKN1B/p27 protein levels. Upregulates CDKN1A/p21 by downregulating MYC, a repressor of CDKN1A/p21. Can negatively regulate the apoptotic effects of IFIT2..
Protein Sequence MSEVTKNSLEKILPQLKCHFTWNLFKEDSVSRDLEDRVCNQIEFLNTEFKATMYNLLAYIKHLDGNNEAALECLRQAEELIQQEHADQAEIRSLVTWGNYAWVYYHLGRLSDAQIYVDKVKQTCKKFSNPYSIEYSELDCEEGWTQLKCGRNERAKVCFEKALEEKPNNPEFSSGLAIAMYHLDNHPEKQFSTDVLKQAIELSPDNQYVKVLLGLKLQKMNKEAEGEQFVEEALEKSPCQTDVLRSAAKFYRRKGDLDKAIELFQRVLESTPNNGYLYHQIGCCYKAKVRQMQNTGESEASGNKEMIEALKQYAMDYSNKALEKGLNPLNAYSDLAEFLETECYQTPFNKEVPDAEKQQSHQRYCNLQKYNGKSEDTAVQHGLEGLSISKKSTDKEEIKDQPQNVSENLLPQNAPNYWYLQGLIHKQNGDLLQAAKCYEKELGRLLRDAPSGIGSIFLSASELEDGSEEMGQGAVSSSPRELLSNSEQLN
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
5Phosphorylation---MSEVTKNSLEKI
---CCCCCHHHHHHH		22.0630108239
6Ubiquitination--MSEVTKNSLEKIL
--CCCCCHHHHHHHH		50.11-
8PhosphorylationMSEVTKNSLEKILPQ
CCCCCHHHHHHHHHH		39.1925849741
11UbiquitinationVTKNSLEKILPQLKC
CCHHHHHHHHHHCHH		55.63-
54PhosphorylationTEFKATMYNLLAYIK
HHHHHHHHHHHHHHH		9.78-
59PhosphorylationTMYNLLAYIKHLDGN
HHHHHHHHHHHHCCC		15.52-
93PhosphorylationADQAEIRSLVTWGNY
CCHHHHHHHHHHCHH		32.6225262027
96PhosphorylationAEIRSLVTWGNYAWV
HHHHHHHHHCHHHHH		32.7125262027
126UbiquitinationKVKQTCKKFSNPYSI
HHHHHHHHHCCCEEE		57.05-
135PhosphorylationSNPYSIEYSELDCEE
CCCEEEEEEEECCCC		13.0322817900
148UbiquitinationEEGWTQLKCGRNERA
CCCEEEEECCCCHHH		25.48-
156UbiquitinationCGRNERAKVCFEKAL
CCCCHHHHHHHHHHH		45.84-
161UbiquitinationRAKVCFEKALEEKPN
HHHHHHHHHHHHCCC		37.71-
166UbiquitinationFEKALEEKPNNPEFS
HHHHHHHCCCCCCCC		43.61-
189UbiquitinationHLDNHPEKQFSTDVL
HCCCCCCHHCCHHHH		62.18-
192PhosphorylationNHPEKQFSTDVLKQA
CCCCHHCCHHHHHHH		22.6220068231
193PhosphorylationHPEKQFSTDVLKQAI
CCCHHCCHHHHHHHH		31.2621815630
197UbiquitinationQFSTDVLKQAIELSP
HCCHHHHHHHHHCCC		37.22-
203PhosphorylationLKQAIELSPDNQYVK
HHHHHHCCCCCHHHH		19.8828355574
208PhosphorylationELSPDNQYVKVLLGL
HCCCCCHHHHHHHHH		14.4324927040
216UbiquitinationVKVLLGLKLQKMNKE
HHHHHHHHHHHCCHH		47.26-
236AcetylationFVEEALEKSPCQTDV
HHHHHHHHCCCCHHH		61.6219822875
236UbiquitinationFVEEALEKSPCQTDV
HHHHHHHHCCCCHHH		61.62-
237PhosphorylationVEEALEKSPCQTDVL
HHHHHHHCCCCHHHH		22.8725159151
241PhosphorylationLEKSPCQTDVLRSAA
HHHCCCCHHHHHHHH		34.4930108239
249UbiquitinationDVLRSAAKFYRRKGD
HHHHHHHHHHHHCCC		42.52-
249AcetylationDVLRSAAKFYRRKGD
HHHHHHHHHHHHCCC		42.5226051181
271PhosphorylationFQRVLESTPNNGYLY
HHHHHHHCCCCCCEE		22.2129496963
295PhosphorylationKVRQMQNTGESEASG
CHHHHHHCCCCCCCC		25.9923532336
295O-linked_GlycosylationKVRQMQNTGESEASG
CHHHHHHCCCCCCCC		25.9930379171
298O-linked_GlycosylationQMQNTGESEASGNKE
HHHHCCCCCCCCCHH		39.5530379171
311UbiquitinationKEMIEALKQYAMDYS
HHHHHHHHHHHHHHH		48.59-
313PhosphorylationMIEALKQYAMDYSNK
HHHHHHHHHHHHHHH		11.4222817900
317PhosphorylationLKQYAMDYSNKALEK
HHHHHHHHHHHHHHC		10.8929116813
318PhosphorylationKQYAMDYSNKALEKG
HHHHHHHHHHHHHCC		27.8229116813
320UbiquitinationYAMDYSNKALEKGLN
HHHHHHHHHHHCCCC		48.70-
324UbiquitinationYSNKALEKGLNPLNA
HHHHHHHCCCCHHHH		70.33-
350UbiquitinationCYQTPFNKEVPDAEK
CCCCCCCCCCCCHHH		61.54-
369UbiquitinationQRYCNLQKYNGKSED
HHHHCHHHHCCCCHH		43.80-
369AcetylationQRYCNLQKYNGKSED
HHHHCHHHHCCCCHH		43.8026051181
373AcetylationNLQKYNGKSEDTAVQ
CHHHHCCCCHHHHHH		47.2126051181
373UbiquitinationNLQKYNGKSEDTAVQ
CHHHHCCCCHHHHHH		47.21-
374PhosphorylationLQKYNGKSEDTAVQH
HHHHCCCCHHHHHHH		41.9420164059
377PhosphorylationYNGKSEDTAVQHGLE
HCCCCHHHHHHHHHH		25.3623090842
387PhosphorylationQHGLEGLSISKKSTD
HHHHHCCCCCCCCCC		35.3628857561
389PhosphorylationGLEGLSISKKSTDKE
HHHCCCCCCCCCCHH		30.5628857561
390UbiquitinationLEGLSISKKSTDKEE
HHCCCCCCCCCCHHH		49.42-
417PhosphorylationLPQNAPNYWYLQGLI
CCCCCCCHHHHHHHH		8.3827642862
436UbiquitinationGDLLQAAKCYEKELG
CHHHHHHHHHHHHHH		40.12-
459PhosphorylationGIGSIFLSASELEDG
CCCEEEEEHHHCCCC		20.9928176443
461PhosphorylationGSIFLSASELEDGSE
CEEEEEHHHCCCCCH		39.0628176443
467PhosphorylationASELEDGSEEMGQGA
HHHCCCCCHHCCCCC		42.5828176443
476PhosphorylationEMGQGAVSSSPRELL
HCCCCCCCCCHHHHH		25.2730108239
477PhosphorylationMGQGAVSSSPRELLS
CCCCCCCCCHHHHHH		37.4530108239
478PhosphorylationGQGAVSSSPRELLSN
CCCCCCCCHHHHHHC		22.0728176443
484PhosphorylationSSPRELLSNSEQLN-
CCHHHHHHCCHHCC-		51.4330108239
486PhosphorylationPRELLSNSEQLN---
HHHHHHCCHHCC---		24.2830108239
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 IFIT3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IFIT3_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 IFIT3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DEUP1_HUMANCCDC67physical
16189514
IFIT3_HUMANIFIT3physical
16189514
APOE_HUMANAPOEphysical
21163940
IFIT5_HUMANIFIT5physical
21163940
LONM_HUMANLONP1physical
21163940
RD23A_HUMANRAD23Aphysical
21163940
IFIT3_HUMANIFIT3physical
21163940
A4_HUMANAPPphysical
21163940
CDC37_HUMANCDC37physical
21163940
SMD2_HUMANSNRPD2physical
21642987
IFIT1_HUMANIFIT1physical
21642987
RUXF_HUMANSNRPFphysical
21642987
RBMX_HUMANRBMXphysical
21642987
LA_HUMANSSBphysical
21642987
HNRPD_HUMANHNRNPDphysical
21642987
SMD3_HUMANSNRPD3physical
21642987
YBOX1_HUMANYBX1physical
21642987
RUXE_HUMANSNRPEphysical
21642987
HNRPL_HUMANHNRNPLphysical
21642987
NUCL_HUMANNCLphysical
21642987
ROA2_HUMANHNRNPA2B1physical
21642987
SNRPA_HUMANSNRPAphysical
21642987
RU2B_HUMANSNRPB2physical
21642987
RSMB_HUMANSNRPBphysical
21642987
RU2A_HUMANSNRPA1physical
21642987
RU17_HUMANSNRNP70physical
21642987
IFIT2_HUMANIFIT2physical
21642987
PABP1_HUMANPABPC1physical
21642987
PABP4_HUMANPABPC4physical
21642987
ILF3_HUMANILF3physical
21642987
ROA1_HUMANHNRNPA1physical
21642987
SMD1_HUMANSNRPD1physical
21642987
IFT1B_HUMANIFIT1Bphysical
21642987
HNRPU_HUMANHNRNPUphysical
21642987
HNRDL_HUMANHNRNPDLphysical
21642987
ROAA_HUMANHNRNPABphysical
21642987
RU1C_HUMANSNRPCphysical
21642987
YBOX3_HUMANYBX3physical
21642987
SF3B3_HUMANSF3B3physical
21642987
DESP_HUMANDSPphysical
21642987
ROA3_HUMANHNRNPA3physical
21642987
MOV10_HUMANMOV10physical
21642987
THIO_HUMANTXNphysical
21642987
IFIT5_HUMANIFIT5physical
21642987
TPM3_HUMANTPM3physical
25416956
T183A_HUMANTMEM183Aphysical
25416956
HAUS1_HUMANHAUS1physical
25416956
DEUP1_HUMANCCDC67physical
25416956
AMPQ_HUMANAQPEPphysical
25416956
TBK1_HUMANTBK1physical
21813773
MAVS_HUMANMAVSphysical
21813773
TPM3_HUMANTPM3physical
21516116
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 IFIT3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-237, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY.

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