NFIC_MOUSE - dbPTM
NFIC_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NFIC_MOUSE
UniProt AC P70255
Protein Name Nuclear factor 1 C-type
Gene Name Nfic
Organism Mus musculus (Mouse).
Sequence Length 439
Subcellular Localization Nucleus.
Protein Description Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication..
Protein Sequence MYSSPLCLTQDEFHPFIEALLPHVRAFAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLGEKAEVKQKWASRLLAKLRKDIRPECREDFVLAVTGKKAPGCVLSNPDQKGKMRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLVKAAACAHPVLCVQPHHIGVAVKELDLYLAYFVRERDAEQSSSPRTGVGSDQEDSKPITLDTTDFQESFVTSGVFSVTELIQVSRTPVVTGTGPNFSLGELQGHLAYDLNPASAGMRRTLPSTSSSGSKRHKSGSMEEDVDTSPGGDYYTSPNSPTSSSRNWTEDIEGGISSPVKKTEMDKSPFNSPSPQDSPRLSSFTQHHRPVIAVHSGIARSPHPTSALHFPATPILPQTASTYFPHTAIRYPPHLNPQDPLKDLVSLACDPATQQPGPPALRPTRPLQTVPLWD
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
1Acetylation-------MYSSPLCL
-------CCCCCCCC		7.08-
2Phosphorylation------MYSSPLCLT
------CCCCCCCCC		20.1823984901
3Phosphorylation-----MYSSPLCLTQ
-----CCCCCCCCCC		24.9623984901
4Phosphorylation----MYSSPLCLTQD
----CCCCCCCCCCC		12.3826643407
9PhosphorylationYSSPLCLTQDEFHPF
CCCCCCCCCCCHHHH		32.7426643407
58UbiquitinationKDEERAVKDELLGEK
HHHHHHHHHHHHHCH		44.4922790023
192PhosphorylationRERDAEQSSSPRTGV
HHHCCCCCCCCCCCC		25.0423684622
193PhosphorylationERDAEQSSSPRTGVG
HHCCCCCCCCCCCCC		44.0225521595
194PhosphorylationRDAEQSSSPRTGVGS
HCCCCCCCCCCCCCC		24.5325521595
201PhosphorylationSPRTGVGSDQEDSKP
CCCCCCCCCCCCCCC		33.4425195567
264PhosphorylationAYDLNPASAGMRRTL
EECCCHHHCCCCCCC		26.9829514104
270PhosphorylationASAGMRRTLPSTSSS
HHCCCCCCCCCCCCC		32.4329550500
273PhosphorylationGMRRTLPSTSSSGSK
CCCCCCCCCCCCCCC		43.9927149854
274PhosphorylationMRRTLPSTSSSGSKR
CCCCCCCCCCCCCCC		30.5924899341
275PhosphorylationRRTLPSTSSSGSKRH
CCCCCCCCCCCCCCC		27.1827149854
276PhosphorylationRTLPSTSSSGSKRHK
CCCCCCCCCCCCCCC		38.5126824392
277PhosphorylationTLPSTSSSGSKRHKS
CCCCCCCCCCCCCCC		47.0222817900
279PhosphorylationPSTSSSGSKRHKSGS
CCCCCCCCCCCCCCC		28.5927149854
280AcetylationSTSSSGSKRHKSGSM
CCCCCCCCCCCCCCC		63.15133299
284PhosphorylationSGSKRHKSGSMEEDV
CCCCCCCCCCCCCCC		29.9427087446
286PhosphorylationSKRHKSGSMEEDVDT
CCCCCCCCCCCCCCC		30.0623429704
293PhosphorylationSMEEDVDTSPGGDYY
CCCCCCCCCCCCCCC		36.3523684622
294PhosphorylationMEEDVDTSPGGDYYT
CCCCCCCCCCCCCCC		19.6525521595
299PhosphorylationDTSPGGDYYTSPNSP
CCCCCCCCCCCCCCC		16.3623684622
300PhosphorylationTSPGGDYYTSPNSPT
CCCCCCCCCCCCCCC		12.8923737553
301PhosphorylationSPGGDYYTSPNSPTS
CCCCCCCCCCCCCCC		31.3223737553
302PhosphorylationPGGDYYTSPNSPTSS
CCCCCCCCCCCCCCC		13.1327087446
305PhosphorylationDYYTSPNSPTSSSRN
CCCCCCCCCCCCCCC		32.7025521595
307PhosphorylationYTSPNSPTSSSRNWT
CCCCCCCCCCCCCCC		40.8523429704
308PhosphorylationTSPNSPTSSSRNWTE
CCCCCCCCCCCCCCC		29.6924453211
309PhosphorylationSPNSPTSSSRNWTED
CCCCCCCCCCCCCCC		35.4826643407
310PhosphorylationPNSPTSSSRNWTEDI
CCCCCCCCCCCCCCC		29.4226643407
314 (in isoform 4)Phosphorylation-27.5926060331
314PhosphorylationTSSSRNWTEDIEGGI
CCCCCCCCCCCCCCC		27.5925619855
322PhosphorylationEDIEGGISSPVKKTE
CCCCCCCCCCCCCCC		31.6825521595
323PhosphorylationDIEGGISSPVKKTEM
CCCCCCCCCCCCCCC		31.6224925903
324 (in isoform 4)Phosphorylation-34.8526060331
328PhosphorylationISSPVKKTEMDKSPF
CCCCCCCCCCCCCCC		30.7227087446
328 (in isoform 4)Phosphorylation-30.7226060331
329 (in isoform 4)Phosphorylation-55.0226060331
330OxidationSPVKKTEMDKSPFNS
CCCCCCCCCCCCCCC		10.7317242355
333PhosphorylationKKTEMDKSPFNSPSP
CCCCCCCCCCCCCCC		30.3825521595
337PhosphorylationMDKSPFNSPSPQDSP
CCCCCCCCCCCCCCC		27.4324925903
339PhosphorylationKSPFNSPSPQDSPRL
CCCCCCCCCCCCCCH		34.7124925903
343PhosphorylationNSPSPQDSPRLSSFT
CCCCCCCCCCHHHHH		13.4825521595
348PhosphorylationQDSPRLSSFTQHHRP
CCCCCHHHHHHCCCC		36.5828418008
365MethylationAVHSGIARSPHPTSA
EEECCCCCCCCCCCC		49.12-
365Asymmetric dimethylarginineAVHSGIARSPHPTSA
EEECCCCCCCCCCCC		49.12-
366PhosphorylationVHSGIARSPHPTSAL
EECCCCCCCCCCCCC		20.6626824392
370PhosphorylationIARSPHPTSALHFPA
CCCCCCCCCCCCCCC		24.4926160508
371PhosphorylationARSPHPTSALHFPAT
CCCCCCCCCCCCCCC		33.0326160508
378PhosphorylationSALHFPATPILPQTA
CCCCCCCCCCCCCCC		15.8826643407
395MethylationYFPHTAIRYPPHLNP
CCCCCCCCCCCCCCC		35.13-
395Asymmetric dimethylarginineYFPHTAIRYPPHLNP
CCCCCCCCCCCCCCC		35.13-
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 NFIC_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NFIC_MOUSE !!
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 NFIC_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZFP28_MOUSEZfp28physical
20211142
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NFIC_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-337; SER-339;SER-343 AND THR-378, AND MASS SPECTROMETRY.

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