NFIC_HUMAN - dbPTM
NFIC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NFIC_HUMAN
UniProt AC P08651
Protein Name Nuclear factor 1 C-type
Gene Name NFIC
Organism Homo sapiens (Human).
Sequence Length 508
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 MYSSPLCLTQDEFHPFIEALLPHVRAFAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLGEKPEVKQKWASRLLAKLRKDIRPECREDFVLSITGKKAPGCVLSNPDQKGKMRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLVKAAQCGHPVLCVQPHHIGVAVKELDLYLAYFVRERDAEQSGSPRTGMGSDQEDSKPITLDTTDFQESFVTSGVFSVTELIQVSRTPVVTGTGPNFSLGELQGHLAYDLNPASTGLRRTLPSTSSSGSKRHKSGSMEEDVDTSPGGDYYTSPSSPTSSSRNWTEDMEGGISSPVKKTEMDKSPFNSPSPQDSPRLSSFTQHHRPVIAVHSGIARSPHPSSALHFPTTSILPQTASTYFPHTAIRYPPHLNPQDPLKDLVSLACDPASQQPGPLNGSGQLKMPSHCLSAQMLAPPPPGLPRLALPPATKPATTSEGGATSPTSPSYSPPDTSPANRSFVGLGPRDPAGIYQAQSWYLG
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		7.0820068231
2Phosphorylation------MYSSPLCLT
------CCCCCCCCC		20.1828450419
3Phosphorylation-----MYSSPLCLTQ
-----CCCCCCCCCC		24.9628450419
4Phosphorylation----MYSSPLCLTQD
----CCCCCCCCCCC		12.3825159151
9PhosphorylationYSSPLCLTQDEFHPF
CCCCCCCCCCHHHHH		32.7428450419
41PhosphorylationLQARKRKYFKKHEKR
HHHHHHHHHHHHHHH		25.3522817900
50PhosphorylationKKHEKRMSKDEERAV
HHHHHHCCHHHHHHH		40.7720068231
58AcetylationKDEERAVKDELLGEK
HHHHHHHHHHHCCCC		44.4926051181
58UbiquitinationKDEERAVKDELLGEK
HHHHHHHHHHHCCCC		44.49-
65AcetylationKDELLGEKPEVKQKW
HHHHCCCCHHHHHHH		44.6826051181
65UbiquitinationKDELLGEKPEVKQKW
HHHHCCCCHHHHHHH		44.68-
99UbiquitinationFVLSITGKKAPGCVL
CEEEEECCCCCCCCC		36.79-
112UbiquitinationVLSNPDQKGKMRRID
CCCCCCCCCCCCHHH		68.80-
146PhosphorylationKGIPLESTDGERLVK
CCCCCCCCCHHHHHH		38.35-
192PhosphorylationRERDAEQSGSPRTGM
HHHCHHHCCCCCCCC		32.5130266825
194PhosphorylationRDAEQSGSPRTGMGS
HCHHHCCCCCCCCCC		19.2230266825
194 (in isoform 5)Phosphorylation-19.2224719451
197PhosphorylationEQSGSPRTGMGSDQE
HHCCCCCCCCCCCCC		34.6024275569
201PhosphorylationSPRTGMGSDQEDSKP
CCCCCCCCCCCCCCC		27.5128102081
206PhosphorylationMGSDQEDSKPITLDT
CCCCCCCCCCEEEEC		39.3128102081
237PhosphorylationELIQVSRTPVVTGTG
HEEEEECCCEEECCC		16.9620068231
241PhosphorylationVSRTPVVTGTGPNFS
EECCCEEECCCCCCC		29.2920068231
243PhosphorylationRTPVVTGTGPNFSLG
CCCEEECCCCCCCHH		39.8523663014
248PhosphorylationTGTGPNFSLGELQGH
ECCCCCCCHHHHCCE		41.9523663014
258PhosphorylationELQGHLAYDLNPAST
HHCCEEEECCCHHCC		27.5923663014
264PhosphorylationAYDLNPASTGLRRTL
EECCCHHCCCHHHCC		25.0225159151
264 (in isoform 5)Phosphorylation-25.0224719451
265PhosphorylationYDLNPASTGLRRTLP
ECCCHHCCCHHHCCC		42.2028348404
270PhosphorylationASTGLRRTLPSTSSS
HCCCHHHCCCCCCCC		36.2628152594
273PhosphorylationGLRRTLPSTSSSGSK
CHHHCCCCCCCCCCC		43.9921955146
273 (in isoform 5)Phosphorylation-43.9924719451
274PhosphorylationLRRTLPSTSSSGSKR
HHHCCCCCCCCCCCC		30.5928152594
275O-linked_GlycosylationRRTLPSTSSSGSKRH
HHCCCCCCCCCCCCC		27.1830059200
275PhosphorylationRRTLPSTSSSGSKRH
HHCCCCCCCCCCCCC		27.1825159151
276PhosphorylationRTLPSTSSSGSKRHK
HCCCCCCCCCCCCCC		38.5123401153
277PhosphorylationTLPSTSSSGSKRHKS
CCCCCCCCCCCCCCC		47.0225159151
279PhosphorylationPSTSSSGSKRHKSGS
CCCCCCCCCCCCCCC		28.5925159151
280AcetylationSTSSSGSKRHKSGSM
CCCCCCCCCCCCCCC		63.1526051181
284PhosphorylationSGSKRHKSGSMEEDV
CCCCCCCCCCCCCCC		29.9423927012
284 (in isoform 5)Phosphorylation-29.9424719451
286PhosphorylationSKRHKSGSMEEDVDT
CCCCCCCCCCCCCCC		30.0623927012
286 (in isoform 5)Phosphorylation-30.0624719451
293PhosphorylationSMEEDVDTSPGGDYY
CCCCCCCCCCCCCCC		36.3530278072
293 (in isoform 5)Phosphorylation-36.3524719451
294PhosphorylationMEEDVDTSPGGDYYT
CCCCCCCCCCCCCCC		19.6523927012
294 (in isoform 5)Phosphorylation-19.6524719451
299PhosphorylationDTSPGGDYYTSPSSP
CCCCCCCCCCCCCCC		16.3630278072
300PhosphorylationTSPGGDYYTSPSSPT
CCCCCCCCCCCCCCC		12.8923927012
301PhosphorylationSPGGDYYTSPSSPTS
CCCCCCCCCCCCCCC		28.1223927012
302PhosphorylationPGGDYYTSPSSPTSS
CCCCCCCCCCCCCCC		13.4823927012
304PhosphorylationGDYYTSPSSPTSSSR
CCCCCCCCCCCCCCC		49.0323401153
304 (in isoform 5)Phosphorylation-49.0324719451
305PhosphorylationDYYTSPSSPTSSSRN
CCCCCCCCCCCCCCC		35.2623927012
307PhosphorylationYTSPSSPTSSSRNWT
CCCCCCCCCCCCCCC		43.0930278072
308PhosphorylationTSPSSPTSSSRNWTE
CCCCCCCCCCCCCCC		29.6930278072
309PhosphorylationSPSSPTSSSRNWTED
CCCCCCCCCCCCCCC		35.4830278072
310PhosphorylationPSSPTSSSRNWTEDM
CCCCCCCCCCCCCCC		29.4230278072
314PhosphorylationTSSSRNWTEDMEGGI
CCCCCCCCCCCCCCC		26.1722167270
322PhosphorylationEDMEGGISSPVKKTE
CCCCCCCCCCCCCCC		31.6822167270
323PhosphorylationDMEGGISSPVKKTEM
CCCCCCCCCCCCCCC		31.6222167270
323 (in isoform 5)Phosphorylation-31.6224719451
328PhosphorylationISSPVKKTEMDKSPF
CCCCCCCCCCCCCCC		30.7230266825
333PhosphorylationKKTEMDKSPFNSPSP
CCCCCCCCCCCCCCC		30.3829255136
337PhosphorylationMDKSPFNSPSPQDSP
CCCCCCCCCCCCCCC		27.4329255136
339PhosphorylationKSPFNSPSPQDSPRL
CCCCCCCCCCCCCCH		34.7129255136
339 (in isoform 5)Phosphorylation-34.7124719451
343PhosphorylationNSPSPQDSPRLSSFT
CCCCCCCCCCHHHHH		13.4829255136
343 (in isoform 5)Phosphorylation-13.4824719451
345MethylationPSPQDSPRLSSFTQH
CCCCCCCCHHHHHHC		51.67115384105
347PhosphorylationPQDSPRLSSFTQHHR
CCCCCCHHHHHHCCC		25.3727251275
348PhosphorylationQDSPRLSSFTQHHRP
CCCCCHHHHHHCCCC		36.5823401153
348 (in isoform 5)Phosphorylation-36.5824719451
350PhosphorylationSPRLSSFTQHHRPVI
CCCHHHHHHCCCCEE		29.0128348404
361PhosphorylationRPVIAVHSGIARSPH
CCEEEEECCCCCCCC		25.8723312004
365Asymmetric dimethylarginineAVHSGIARSPHPSSA
EEECCCCCCCCCCCC		49.12-
365MethylationAVHSGIARSPHPSSA
EEECCCCCCCCCCCC		49.1224129315
366PhosphorylationVHSGIARSPHPSSAL
EECCCCCCCCCCCCC		20.6625159151
370PhosphorylationIARSPHPSSALHFPT
CCCCCCCCCCCCCCC		25.8028152594
371PhosphorylationARSPHPSSALHFPTT
CCCCCCCCCCCCCCC		39.0228152594
377PhosphorylationSSALHFPTTSILPQT
CCCCCCCCCCCCCCC		32.0328450419
378PhosphorylationSALHFPTTSILPQTA
CCCCCCCCCCCCCCC		17.6328450419
379PhosphorylationALHFPTTSILPQTAS
CCCCCCCCCCCCCCC		25.3028450419
395Asymmetric dimethylarginineYFPHTAIRYPPHLNP
CCCCCCCCCCCCCCC		35.13-
395MethylationYFPHTAIRYPPHLNP
CCCCCCCCCCCCCCC		35.1324129315
396PhosphorylationFPHTAIRYPPHLNPQ
CCCCCCCCCCCCCCC		18.2729632367
427PhosphorylationQPGPLNGSGQLKMPS
CCCCCCCCCCCCCCH		23.4620886841
434PhosphorylationSGQLKMPSHCLSAQM
CCCCCCCHHHEEHHH		24.2723186163
438PhosphorylationKMPSHCLSAQMLAPP
CCCHHHEEHHHCCCC		23.1123917254
451MethylationPPPPGLPRLALPPAT
CCCCCCCCCCCCCCC		37.3224129315
458PhosphorylationRLALPPATKPATTSE
CCCCCCCCCCCCCCC		43.2523186163
459AcetylationLALPPATKPATTSEG
CCCCCCCCCCCCCCC		34.4626051181
460 (in isoform 2)Phosphorylation-30.4024719451
462PhosphorylationPPATKPATTSEGGAT
CCCCCCCCCCCCCCC		39.1125850435
463PhosphorylationPATKPATTSEGGATS
CCCCCCCCCCCCCCC		27.2125850435
463 (in isoform 2)Phosphorylation-27.2124719451
464PhosphorylationATKPATTSEGGATSP
CCCCCCCCCCCCCCC		29.8625850435
464 (in isoform 2)Phosphorylation-29.8624719451
469PhosphorylationTTSEGGATSPTSPSY
CCCCCCCCCCCCCCC		38.2126657352
470PhosphorylationTSEGGATSPTSPSYS
CCCCCCCCCCCCCCC		26.1630576142
472PhosphorylationEGGATSPTSPSYSPP
CCCCCCCCCCCCCCC		53.7025159151
473PhosphorylationGGATSPTSPSYSPPD
CCCCCCCCCCCCCCC		18.4225159151
475PhosphorylationATSPTSPSYSPPDTS
CCCCCCCCCCCCCCC		37.7025850435
476PhosphorylationTSPTSPSYSPPDTSP
CCCCCCCCCCCCCCC		28.6929116813
477PhosphorylationSPTSPSYSPPDTSPA
CCCCCCCCCCCCCCC		34.0025850435
481PhosphorylationPSYSPPDTSPANRSF
CCCCCCCCCCCCCCC		42.2424275569
482PhosphorylationSYSPPDTSPANRSFV
CCCCCCCCCCCCCCC		29.4227732954
487PhosphorylationDTSPANRSFVGLGPR
CCCCCCCCCCCCCCC		24.888710515
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NFIC_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 NFIC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LLPH_HUMANLLPHphysical
16189514
TPD55_HUMANTPD52L3physical
16189514
ZCH14_HUMANZCCHC14physical
16189514
ZKSC7_HUMANZKSCAN7physical
16189514
TKTL2_HUMANTKTL2physical
16189514
SMAD3_HUMANSMAD3physical
22195013
SMUF1_HUMANSMURF1physical
22195013
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 NFIC_HUMAN

loading...

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-333, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, 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-294; SER-305; SER-323;SER-333 AND SER-339, AND MASS SPECTROMETRY.
"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-323, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-305; SER-339AND SER-343, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-339, ANDMASS SPECTROMETRY.
"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-4; SER-194; SER-323;SER-333 AND SER-339, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-333 ANDSER-339, AND MASS SPECTROMETRY.

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