NFIB_MOUSE - dbPTM
NFIB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NFIB_MOUSE
UniProt AC P97863
Protein Name Nuclear factor 1 B-type
Gene Name Nfib
Organism Mus musculus (Mouse).
Sequence Length 570
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 MMYSPICLTQDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLSEKPEIKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLMKSPHCTNPALCVQPHHITVSVKELDLFLAYYVQEQDSGQSGSPSHSDPAKNPPGYLEDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSQPYYHDMNSGVNLQRSLSSPPSSKRPKTISIDENMEPSPTGDFYPSPNSPAAGSRTWHERDQDMSSPTTMKKPEKPLFSSTSPQDSSPRLSTFPQHHHPGIPGVAHSVISTRTPPPPSPLPFPTQAILPPAPSSYFSHPTIRYPPHLNPQDTLKNYVPSYDPSSPQTSQPNSSGQVVGKVPGHFTPVLAPSPHPSAVRPVTLTMTDTKPITTSTEGEAASPTATTYTASGTSQANRYVGLSPRDPSFLHQQQLRICDWTMNQNGRHLYPSTSEDTLGITWQSPGTWASLVPFQVSNRTPILPANVQNYGLNIIGEPFLQAETSN
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
3Phosphorylation-----MMYSPICLTQ
-----CCCCCEECCC		15.2523984901
4Phosphorylation----MMYSPICLTQD
----CCCCCEECCCC		7.0126643407
9PhosphorylationMYSPICLTQDEFHPF
CCCCEECCCCCCHHH		29.5727717184
63PhosphorylationAVKDELLSEKPEIKQ
HHHHHHHHCCHHHHH		57.0817203969
183PhosphorylationLDLFLAYYVQEQDSG
HHHEEEEECCCCCCC		7.0523140645
189PhosphorylationYYVQEQDSGQSGSPS
EECCCCCCCCCCCCC		38.1326643407
192PhosphorylationQEQDSGQSGSPSHSD
CCCCCCCCCCCCCCC		44.7726643407
194PhosphorylationQDSGQSGSPSHSDPA
CCCCCCCCCCCCCCC		28.6026643407
196PhosphorylationSGQSGSPSHSDPAKN
CCCCCCCCCCCCCCC		37.0026643407
198PhosphorylationQSGSPSHSDPAKNPP
CCCCCCCCCCCCCCC		50.0226643407
215PhosphorylationLEDSFVKSGVFNVSE
CCCHHHCCCCCCHHH		34.5825338131
221PhosphorylationKSGVFNVSELVRVSR
CCCCCCHHHHEEEEC		26.73-
246PhosphorylationFPIGEIPSQPYYHDM
CCCCCCCCCCCCCCC		49.82-
262PhosphorylationSGVNLQRSLSSPPSS
CCCCCCCCCCCCCCC		21.4623737553
264PhosphorylationVNLQRSLSSPPSSKR
CCCCCCCCCCCCCCC		41.8826824392
265PhosphorylationNLQRSLSSPPSSKRP
CCCCCCCCCCCCCCC		46.2327742792
268PhosphorylationRSLSSPPSSKRPKTI
CCCCCCCCCCCCCEE		52.4523737553
269PhosphorylationSLSSPPSSKRPKTIS
CCCCCCCCCCCCEEE		38.1623737553
274PhosphorylationPSSKRPKTISIDENM
CCCCCCCEEEECCCC		23.7327087446
276PhosphorylationSKRPKTISIDENMEP
CCCCCEEEECCCCCC		29.2623684622
281OxidationTISIDENMEPSPTGD
EEEECCCCCCCCCCC		8.2417242355
284PhosphorylationIDENMEPSPTGDFYP
ECCCCCCCCCCCCCC		23.0723684622
286PhosphorylationENMEPSPTGDFYPSP
CCCCCCCCCCCCCCC		54.4427087446
290PhosphorylationPSPTGDFYPSPNSPA
CCCCCCCCCCCCCCC		13.9327087446
292PhosphorylationPTGDFYPSPNSPAAG
CCCCCCCCCCCCCCC		25.9027087446
295PhosphorylationDFYPSPNSPAAGSRT
CCCCCCCCCCCCCCC		21.2127087446
300PhosphorylationPNSPAAGSRTWHERD
CCCCCCCCCCCHHHC		23.0822942356
302PhosphorylationSPAAGSRTWHERDQD
CCCCCCCCCHHHCCC		32.6325777480
311PhosphorylationHERDQDMSSPTTMKK
HHHCCCCCCCCCCCC		41.2623429704
312PhosphorylationERDQDMSSPTTMKKP
HHCCCCCCCCCCCCC		21.4525521595
314PhosphorylationDQDMSSPTTMKKPEK
CCCCCCCCCCCCCCC		41.2823429704
315PhosphorylationQDMSSPTTMKKPEKP
CCCCCCCCCCCCCCC		30.3123737553
318AcetylationSSPTTMKKPEKPLFS
CCCCCCCCCCCCCCC		47.8122826441
321AcetylationTTMKKPEKPLFSSTS
CCCCCCCCCCCCCCC		56.3923806337
325PhosphorylationKPEKPLFSSTSPQDS
CCCCCCCCCCCCCCC		40.1525168779
326PhosphorylationPEKPLFSSTSPQDSS
CCCCCCCCCCCCCCC		26.1027742792
327PhosphorylationEKPLFSSTSPQDSSP
CCCCCCCCCCCCCCC		43.1426824392
328PhosphorylationKPLFSSTSPQDSSPR
CCCCCCCCCCCCCCC		23.6327087446
332PhosphorylationSSTSPQDSSPRLSTF
CCCCCCCCCCCCCCC		36.6726824392
333PhosphorylationSTSPQDSSPRLSTFP
CCCCCCCCCCCCCCC		23.4826824392
335MethylationSPQDSSPRLSTFPQH
CCCCCCCCCCCCCCC		43.1324129315
335Asymmetric dimethylarginineSPQDSSPRLSTFPQH
CCCCCCCCCCCCCCC		43.13-
359PhosphorylationHSVISTRTPPPPSPL
CCEECCCCCCCCCCC		39.9927180971
364PhosphorylationTRTPPPPSPLPFPTQ
CCCCCCCCCCCCCCC		44.8626643407
370PhosphorylationPSPLPFPTQAILPPA
CCCCCCCCCCCCCCC		30.8926643407
388Asymmetric dimethylarginineYFSHPTIRYPPHLNP
HCCCCCCCCCCCCCH		40.14-
388MethylationYFSHPTIRYPPHLNP
HCCCCCCCCCCCCCH		40.1424129315
402 (in isoform 3)Phosphorylation-16.4923737553
402PhosphorylationPQDTLKNYVPSYDPS
HHHHHHHCCCCCCCC		16.4925619855
405 (in isoform 3)Phosphorylation-31.9323737553
405PhosphorylationTLKNYVPSYDPSSPQ
HHHHCCCCCCCCCCC		31.9325619855
406 (in isoform 3)Phosphorylation-26.2923737553
406PhosphorylationLKNYVPSYDPSSPQT
HHHCCCCCCCCCCCC		26.2925619855
409PhosphorylationYVPSYDPSSPQTSQP
CCCCCCCCCCCCCCC		52.3225619855
409 (in isoform 3)Phosphorylation-52.3223737553
409 (in isoform 2)Phosphorylation-52.3225338131
410PhosphorylationVPSYDPSSPQTSQPN
CCCCCCCCCCCCCCC		26.8125619855
410 (in isoform 3)Phosphorylation-26.8123737553
410 (in isoform 2)Phosphorylation-26.8129514104
413PhosphorylationYDPSSPQTSQPNSSG
CCCCCCCCCCCCCCC		32.4825619855
413 (in isoform 3)Phosphorylation-32.4823737553
414 (in isoform 3)Phosphorylation-38.0923737553
414PhosphorylationDPSSPQTSQPNSSGQ
CCCCCCCCCCCCCCC		38.0925619855
416 (in isoform 3)Phosphorylation-42.3024453211
418 (in isoform 3)Phosphorylation-42.3923737553
418PhosphorylationPQTSQPNSSGQVVGK
CCCCCCCCCCCEEEC		42.3925619855
419PhosphorylationQTSQPNSSGQVVGKV
CCCCCCCCCCEEECC		39.6325619855
431PhosphorylationGKVPGHFTPVLAPSP
ECCCCCCCCEECCCC		13.5526370283
437PhosphorylationFTPVLAPSPHPSAVR
CCCEECCCCCCCCCC		30.1826370283
483PhosphorylationGTSQANRYVGLSPRD
CCCHHCCCCCCCCCC		9.9322817900
487PhosphorylationANRYVGLSPRDPSFL
HCCCCCCCCCCHHHH		16.3827180971
568PhosphorylationEPFLQAETSN-----
CCCCCCCCCC-----		36.2626643407
569PhosphorylationPFLQAETSN------
CCCCCCCCC------		31.8627180971
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 NFIB_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NFIB_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 NFIB_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NFIB_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NFIB_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-264; SER-292 ANDSER-295, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND MASSSPECTROMETRY.

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