NFIL3_HUMAN - dbPTM
NFIL3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NFIL3_HUMAN
UniProt AC Q16649
Protein Name Nuclear factor interleukin-3-regulated protein
Gene Name NFIL3
Organism Homo sapiens (Human).
Sequence Length 462
Subcellular Localization Nucleus .
Protein Description Acts as a transcriptional regulator that recognizes and binds to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many cellular and viral promoters. Represses transcription from promoters with activating transcription factor (ATF) sites. Represses promoter activity in osteoblasts (By similarity). Represses transcriptional activity of PER1 (By similarity). Represses transcriptional activity of PER2 via the B-site on the promoter (By similarity). Activates transcription from the interleukin-3 promoter in T-cells. Competes for the same consensus-binding site with PAR DNA-binding factors (DBP, HLF and TEF) (By similarity). Component of the circadian clock that acts as a negative regulator for the circadian expression of PER2 oscillation in the cell-autonomous core clock (By similarity). Protects pro-B cells from programmed cell death (By similarity)..
Protein Sequence MQLRKMQTVKKEQASLDASSNVDKMMVLNSALTEVSEDSTTGEELLLSEGSVGKNKSSACRRKREFIPDEKKDAMYWEKRRKNNEAAKRSREKRRLNDLVLENKLIALGEENATLKAELLSLKLKFGLISSTAYAQEIQKLSNSTAVYFQDYQTSKSNVSSFVDEHEPSMVSSSCISVIKHSPQSSLSDVSEVSSVEHTQESSVQGSCRSPENKFQIIKQEPMELESYTREPRDDRGSYTASIYQNYMGNSFSGYSHSPPLLQVNRSSSNSPRTSETDDGVVGKSSDGEDEQQVPKGPIHSPVELKHVHATVVKVPEVNSSALPHKLRIKAKAMQIKVEAFDNEFEATQKLSSPIDMTSKRHFELEKHSAPSMVHSSLTPFSVQVTNIQDWSLKSEHWHQKELSGKTQNSFKTGVVEMKDSGYKVSDPENLYLKQGIANLSAEVVSLKRLIATQPISASDSG
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
11AcetylationRKMQTVKKEQASLDA
CCCHHHCHHHHCCCC		51.2026051181
19PhosphorylationEQASLDASSNVDKMM
HHHCCCCCCCHHHHH		23.3225627689
20PhosphorylationQASLDASSNVDKMMV
HHCCCCCCCHHHHHH		42.4625627689
24SumoylationDASSNVDKMMVLNSA
CCCCCHHHHHHHHHH		25.3128112733
30PhosphorylationDKMMVLNSALTEVSE
HHHHHHHHHHEECCC		22.09-
72SumoylationEFIPDEKKDAMYWEK
CCCCHHHHHHHHHHH		48.98-
72SumoylationEFIPDEKKDAMYWEK
CCCCHHHHHHHHHHH		48.98-
82AcetylationMYWEKRRKNNEAAKR
HHHHHHHHCCHHHHH		69.067910691
82SumoylationMYWEKRRKNNEAAKR
HHHHHHHHCCHHHHH		69.06-
104UbiquitinationNDLVLENKLIALGEE
HHHHHHHHHHHHCCC		31.71-
116UbiquitinationGEENATLKAELLSLK
CCCCHHHHHHHHHHH		35.15-
121PhosphorylationTLKAELLSLKLKFGL
HHHHHHHHHHHHHCC		35.7624719451
152PhosphorylationTAVYFQDYQTSKSNV
CEEEEECHHCCCCCH		11.6929759185
154PhosphorylationVYFQDYQTSKSNVSS
EEEECHHCCCCCHHH		31.7129759185
155PhosphorylationYFQDYQTSKSNVSSF
EEECHHCCCCCHHHH		20.6829759185
182PhosphorylationCISVIKHSPQSSLSD
HHHHHCCCCCCCCCC		21.4520873877
185PhosphorylationVIKHSPQSSLSDVSE
HHCCCCCCCCCCCCC		36.3120873877
186PhosphorylationIKHSPQSSLSDVSEV
HCCCCCCCCCCCCCC		27.0120873877
199PhosphorylationEVSSVEHTQESSVQG
CCCCCEECCCCCCCC		22.1128348404
202PhosphorylationSVEHTQESSVQGSCR
CCEECCCCCCCCCCC		26.4529116813
203PhosphorylationVEHTQESSVQGSCRS
CEECCCCCCCCCCCC		20.0829116813
207PhosphorylationQESSVQGSCRSPENK
CCCCCCCCCCCCCCC		6.8330576142
210PhosphorylationSVQGSCRSPENKFQI
CCCCCCCCCCCCEEE		40.6730576142
214SumoylationSCRSPENKFQIIKQE
CCCCCCCCEEEEECC		36.6628112733
219SumoylationENKFQIIKQEPMELE
CCCEEEEECCCCCHH		50.68-
219SumoylationENKFQIIKQEPMELE
CCCEEEEECCCCCHH		50.6825114211
242PhosphorylationDRGSYTASIYQNYMG
CCCCCEEEEEHHHCC		17.6527080861
247PhosphorylationTASIYQNYMGNSFSG
EEEEEHHHCCCCCCC		7.2927080861
251PhosphorylationYQNYMGNSFSGYSHS
EHHHCCCCCCCCCCC		18.3027080861
253PhosphorylationNYMGNSFSGYSHSPP
HHCCCCCCCCCCCCC		36.3227080861
255PhosphorylationMGNSFSGYSHSPPLL
CCCCCCCCCCCCCEE		11.3027080861
256PhosphorylationGNSFSGYSHSPPLLQ
CCCCCCCCCCCCEEE		22.4827080861
258PhosphorylationSFSGYSHSPPLLQVN
CCCCCCCCCCEEECC		23.4419276368
267PhosphorylationPLLQVNRSSSNSPRT
CEEECCCCCCCCCCC		32.6830576142
268PhosphorylationLLQVNRSSSNSPRTS
EEECCCCCCCCCCCC		30.2427732954
269PhosphorylationLQVNRSSSNSPRTSE
EECCCCCCCCCCCCC		42.4430576142
271PhosphorylationVNRSSSNSPRTSETD
CCCCCCCCCCCCCCC		20.0827732954
274PhosphorylationSSSNSPRTSETDDGV
CCCCCCCCCCCCCCC		34.0130576142
275PhosphorylationSSNSPRTSETDDGVV
CCCCCCCCCCCCCCC		39.5223927012
277PhosphorylationNSPRTSETDDGVVGK
CCCCCCCCCCCCCCC		38.8728450419
285PhosphorylationDDGVVGKSSDGEDEQ
CCCCCCCCCCCCCCC		27.9423401153
286PhosphorylationDGVVGKSSDGEDEQQ
CCCCCCCCCCCCCCC		53.7925159151
301PhosphorylationVPKGPIHSPVELKHV
CCCCCCCCCCCCCEE		31.2129255136
306SumoylationIHSPVELKHVHATVV
CCCCCCCCEEEEEEE		30.03-
306SumoylationIHSPVELKHVHATVV
CCCCCCCCEEEEEEE		30.0328112733
311PhosphorylationELKHVHATVVKVPEV
CCCEEEEEEEECCCC		15.7923312004
314SumoylationHVHATVVKVPEVNSS
EEEEEEEECCCCCCC		47.9728112733
326SumoylationNSSALPHKLRIKAKA
CCCCCCCHHHHCEEE		37.2128112733
332SumoylationHKLRIKAKAMQIKVE
CHHHHCEEEEEEEEE		39.1128112733
337SumoylationKAKAMQIKVEAFDNE
CEEEEEEEEEECCCC		19.68-
337SumoylationKAKAMQIKVEAFDNE
CEEEEEEEEEECCCC		19.6828112733
350SumoylationNEFEATQKLSSPIDM
CCHHHHHHCCCCCCC		46.0828112733
350UbiquitinationNEFEATQKLSSPIDM
CCHHHHHHCCCCCCC		46.08-
352PhosphorylationFEATQKLSSPIDMTS
HHHHHHCCCCCCCCC		40.8930266825
353PhosphorylationEATQKLSSPIDMTSK
HHHHHCCCCCCCCCH		35.9929255136
358PhosphorylationLSSPIDMTSKRHFEL
CCCCCCCCCHHHHEE		27.6130266825
359PhosphorylationSSPIDMTSKRHFELE
CCCCCCCCHHHHEEC		22.5119691289
360UbiquitinationSPIDMTSKRHFELEK
CCCCCCCHHHHEECC		40.50-
360SumoylationSPIDMTSKRHFELEK
CCCCCCCHHHHEECC		40.5028112733
369PhosphorylationHFELEKHSAPSMVHS
HHEECCCCCCCCCCC		53.6029978859
372PhosphorylationLEKHSAPSMVHSSLT
ECCCCCCCCCCCCCC		32.9029978859
376PhosphorylationSAPSMVHSSLTPFSV
CCCCCCCCCCCCCEE		18.6829978859
377PhosphorylationAPSMVHSSLTPFSVQ
CCCCCCCCCCCCEEE		22.7629978859
379PhosphorylationSMVHSSLTPFSVQVT
CCCCCCCCCCEEEEE		25.0029978859
382PhosphorylationHSSLTPFSVQVTNIQ
CCCCCCCEEEEECCC		16.9129978859
386PhosphorylationTPFSVQVTNIQDWSL
CCCEEEEECCCCCCC		14.9829978859
392PhosphorylationVTNIQDWSLKSEHWH
EECCCCCCCCCCCEE		33.9229978859
394SumoylationNIQDWSLKSEHWHQK
CCCCCCCCCCCEEHH		48.56-
394SumoylationNIQDWSLKSEHWHQK
CCCCCCCCCCCEEHH		48.5628112733
395PhosphorylationIQDWSLKSEHWHQKE
CCCCCCCCCCEEHHH		39.7329978859
401UbiquitinationKSEHWHQKELSGKTQ
CCCCEEHHHHCCCCC		47.97-
401SumoylationKSEHWHQKELSGKTQ
CCCCEEHHHHCCCCC		47.9728112733
406SumoylationHQKELSGKTQNSFKT
EHHHHCCCCCCCEEC		43.4928112733
406SumoylationHQKELSGKTQNSFKT
EHHHHCCCCCCCEEC		43.49-
406UbiquitinationHQKELSGKTQNSFKT
EHHHHCCCCCCCEEC		43.49-
412SumoylationGKTQNSFKTGVVEMK
CCCCCCEECCEEEEC		44.1628112733
412UbiquitinationGKTQNSFKTGVVEMK
CCCCCCEECCEEEEC		44.16-
412SumoylationGKTQNSFKTGVVEMK
CCCCCCEECCEEEEC		44.16-
413PhosphorylationKTQNSFKTGVVEMKD
CCCCCEECCEEEECC		32.9522468782
419UbiquitinationKTGVVEMKDSGYKVS
ECCEEEECCCCCCCC		34.9221906983
419SumoylationKTGVVEMKDSGYKVS
ECCEEEECCCCCCCC		34.9228112733
419SumoylationKTGVVEMKDSGYKVS
ECCEEEECCCCCCCC		34.92-
424SumoylationEMKDSGYKVSDPENL
EECCCCCCCCCHHHC		38.50-
424UbiquitinationEMKDSGYKVSDPENL
EECCCCCCCCCHHHC		38.5021906983
424SumoylationEMKDSGYKVSDPENL
EECCCCCCCCCHHHC		38.5028112733
434SumoylationDPENLYLKQGIANLS
CHHHCHHHHHHHHCC		32.6828112733
434UbiquitinationDPENLYLKQGIANLS
CHHHCHHHHHHHHCC		32.68-
441PhosphorylationKQGIANLSAEVVSLK
HHHHHHCCHHEEEHH		23.3828060719
446PhosphorylationNLSAEVVSLKRLIAT
HCCHHEEEHHHHHHC		33.0928060719
448SumoylationSAEVVSLKRLIATQP
CHHEEEHHHHHHCCC		37.3428112733
448UbiquitinationSAEVVSLKRLIATQP
CHHEEEHHHHHHCCC		37.34-
459PhosphorylationATQPISASDSG----
HCCCCCCCCCC----		26.0628450419
461PhosphorylationQPISASDSG------
CCCCCCCCC------		43.8625159151
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 NFIL3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NFIL3_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 NFIL3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NC2B_HUMANDR1physical
8836190
MAFF_HUMANMAFFphysical
23661758
BATF_HUMANBATFphysical
23661758
NFIL3_HUMANNFIL3physical
23661758
TRAF2_HUMANTRAF2physical
25416956
AMOL2_HUMANAMOTL2physical
25416956
AMOL2_HUMANAMOTL2physical
21516116
RFWD2_HUMANRFWD2physical
28514442
STK40_HUMANSTK40physical
28514442
CREB1_HUMANCREB1physical
28514442
ATF1_HUMANATF1physical
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 NFIL3_HUMAN

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Related Literatures of Post-Translational Modification
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-353, AND MASSSPECTROMETRY.
"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-301, AND MASSSPECTROMETRY.
"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-301, AND MASSSPECTROMETRY.

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