NFIA_HUMAN - dbPTM
NFIA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NFIA_HUMAN
UniProt AC Q12857
Protein Name Nuclear factor 1 A-type
Gene Name NFIA
Organism Homo sapiens (Human).
Sequence Length 509
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 MYSPLCLTQDEFHPFIEALLPHVRAFAYTWFNLQARKRKYFKKHEKRMSKEEERAVKDELLSEKPEVKQKWASRLLAKLRKDIRPEYREDFVLTVTGKKPPCCVLSNPDQKGKMRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLVKSPQCSNPGLCVQPHHIGVSVKELDLYLAYFVHAADSSQSESPSQPSDADIKDQPENGHLGFQDSFVTSGVFSVTELVRVSQTPIAAGTGPNFSLSDLESSSYYSMSPGAMRRSLPSTSSTSSTKRLKSVEDEMDSPGEEPFYTGQGRSPGSGSQSSGWHEVEPGMPSPTTLKKSEKSGFSSPSPSQTSSLGTAFTQHHRPVITGPRASPHATPSTLHFPTSPIIQQPGPYFSHPAIRYHPQETLKEFVQLVCPDAGQQAGQVGFLNPNGSSQGKVHNPFLPTPMLPPPPPPPMARPVPLPVPDTKPPTTSTEGGAASPTSPTYSTPSTSPANRFVSVGPRDPSFVNIPQQTQSWYLG
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
2Phosphorylation------MYSPLCLTQ
------CCCCCCCCC		20.9923090842
3Phosphorylation-----MYSPLCLTQD
-----CCCCCCCCCC		15.3125849741
3 (in isoform 2)Phosphorylation-15.3124719451
40PhosphorylationLQARKRKYFKKHEKR
HHHHHHHHHHHHHHH		25.3522817900
47 (in isoform 4)Phosphorylation-31.4627642862
48 (in isoform 4)Phosphorylation-11.2727642862
56UbiquitinationSKEEERAVKDELLSE
CHHHHHHHHHHHHHC		11.4129967540
57AcetylationKEEERAVKDELLSEK
HHHHHHHHHHHHHCC		44.4926051181
62PhosphorylationAVKDELLSEKPEVKQ
HHHHHHHHCCHHHHH		57.0824719451
64AcetylationKDELLSEKPEVKQKW
HHHHHHCCHHHHHHH		43.0026051181
64UbiquitinationKDELLSEKPEVKQKW
HHHHHHCCHHHHHHH		43.0029967540
109UbiquitinationCCVLSNPDQKGKMRR
EEEECCCCCCCCCCH		68.0529967540
145PhosphorylationKGIPLESTDGERLVK
CCCCCCCCCCCHHCC		38.35-
189PhosphorylationFVHAADSSQSESPSQ
HHHHHCCCCCCCCCC		37.9729802988
191PhosphorylationHAADSSQSESPSQPS
HHHCCCCCCCCCCCC		41.8325159151
193PhosphorylationADSSQSESPSQPSDA
HCCCCCCCCCCCCCC		34.7926657352
195PhosphorylationSSQSESPSQPSDADI
CCCCCCCCCCCCCCC		65.0928348404
232PhosphorylationVTELVRVSQTPIAAG
HHHEEEECCCCCCCC		20.1330576142
234PhosphorylationELVRVSQTPIAAGTG
HEEEECCCCCCCCCC		14.7920068231
238 (in isoform 4)Phosphorylation-19.4627251275
240PhosphorylationQTPIAAGTGPNFSLS
CCCCCCCCCCCCCHH		44.7518669648
245PhosphorylationAGTGPNFSLSDLESS
CCCCCCCCHHHHCCC		33.3422199227
247PhosphorylationTGPNFSLSDLESSSY
CCCCCCHHHHCCCCC		38.6622199227
251PhosphorylationFSLSDLESSSYYSMS
CCHHHHCCCCCEECC		31.7022199227
252PhosphorylationSLSDLESSSYYSMSP
CHHHHCCCCCEECCC		17.0022199227
253PhosphorylationLSDLESSSYYSMSPG
HHHHCCCCCEECCCC		37.0522199227
254PhosphorylationSDLESSSYYSMSPGA
HHHCCCCCEECCCCH		11.0822199227
255PhosphorylationDLESSSYYSMSPGAM
HHCCCCCEECCCCHH		10.3922199227
256PhosphorylationLESSSYYSMSPGAMR
HCCCCCEECCCCHHC		12.4525159151
258PhosphorylationSSSYYSMSPGAMRRS
CCCCEECCCCHHCCC		17.7828176443
258 (in isoform 2)Phosphorylation-17.7824719451
265PhosphorylationSPGAMRRSLPSTSST
CCCHHCCCCCCCCCC		33.9823927012
265 (in isoform 2)Phosphorylation-33.9824719451
268PhosphorylationAMRRSLPSTSSTSST
HHCCCCCCCCCCCCC		46.3323927012
268 (in isoform 2)Phosphorylation-46.3324719451
269PhosphorylationMRRSLPSTSSTSSTK
HCCCCCCCCCCCCCC		25.4226657352
270O-linked_GlycosylationRRSLPSTSSTSSTKR
CCCCCCCCCCCCCCC		35.6430059200
270PhosphorylationRRSLPSTSSTSSTKR
CCCCCCCCCCCCCCC		35.6420044836
271PhosphorylationRSLPSTSSTSSTKRL
CCCCCCCCCCCCCCH		32.1823927012
272PhosphorylationSLPSTSSTSSTKRLK
CCCCCCCCCCCCCHH		26.8520044836
273PhosphorylationLPSTSSTSSTKRLKS
CCCCCCCCCCCCHHC		37.6523927012
274PhosphorylationPSTSSTSSTKRLKSV
CCCCCCCCCCCHHCC		37.7323927012
275PhosphorylationSTSSTSSTKRLKSVE
CCCCCCCCCCHHCCC		21.6823927012
276AcetylationTSSTSSTKRLKSVED
CCCCCCCCCHHCCCC		58.6525953088
276UbiquitinationTSSTSSTKRLKSVED
CCCCCCCCCHHCCCC		58.65-
279PhosphorylationTSSTKRLKSVEDEMD
CCCCCCHHCCCCCCC		57.3933259812
280PhosphorylationSSTKRLKSVEDEMDS
CCCCCHHCCCCCCCC		35.0222167270
280 (in isoform 2)Phosphorylation-35.0224719451
285 (in isoform 4)Phosphorylation-10.7927251275
287PhosphorylationSVEDEMDSPGEEPFY
CCCCCCCCCCCCCCC		33.2322167270
287 (in isoform 2)Phosphorylation-33.2324719451
294PhosphorylationSPGEEPFYTGQGRSP
CCCCCCCCCCCCCCC		22.2222167270
295PhosphorylationPGEEPFYTGQGRSPG
CCCCCCCCCCCCCCC		24.3322167270
300PhosphorylationFYTGQGRSPGSGSQS
CCCCCCCCCCCCCCC		40.2022167270
300 (in isoform 2)Phosphorylation-40.2024719451
303PhosphorylationGQGRSPGSGSQSSGW
CCCCCCCCCCCCCCC		38.3630278072
303 (in isoform 4)Phosphorylation-38.3627251275
305PhosphorylationGRSPGSGSQSSGWHE
CCCCCCCCCCCCCEE		28.6917525332
307PhosphorylationSPGSGSQSSGWHEVE
CCCCCCCCCCCEECC		32.3030278072
308PhosphorylationPGSGSQSSGWHEVEP
CCCCCCCCCCEECCC		37.9630278072
310 (in isoform 4)Phosphorylation-6.0927251275
313 (in isoform 4)Phosphorylation-7.5127251275
314 (in isoform 4)Phosphorylation-32.9027251275
317 (in isoform 4)Phosphorylation-4.3127251275
318 (in isoform 4)Phosphorylation-42.9727251275
319PhosphorylationEVEPGMPSPTTLKKS
ECCCCCCCCCCCCHH		26.4523401153
319 (in isoform 2)Phosphorylation-26.4524719451
319 (in isoform 4)Phosphorylation-26.4527251275
321PhosphorylationEPGMPSPTTLKKSEK
CCCCCCCCCCCHHHH		49.4523927012
322PhosphorylationPGMPSPTTLKKSEKS
CCCCCCCCCCHHHHC		39.7123927012
325 (in isoform 4)Phosphorylation-67.9427642862
328AcetylationTTLKKSEKSGFSSPS
CCCCHHHHCCCCCCC		64.0726051181
329PhosphorylationTLKKSEKSGFSSPSP
CCCHHHHCCCCCCCH		40.8124732914
332PhosphorylationKSEKSGFSSPSPSQT
HHHHCCCCCCCHHHC		44.8825159151
332 (in isoform 4)Phosphorylation-44.8827642862
333PhosphorylationSEKSGFSSPSPSQTS
HHHCCCCCCCHHHCC		27.4323927012
335PhosphorylationKSGFSSPSPSQTSSL
HCCCCCCCHHHCCCC		38.8525159151
335 (in isoform 2)Phosphorylation-38.8524719451
337PhosphorylationGFSSPSPSQTSSLGT
CCCCCCHHHCCCCCC		50.8828152594
339PhosphorylationSSPSPSQTSSLGTAF
CCCCHHHCCCCCCHH		25.3128152594
339 (in isoform 4)Phosphorylation-25.3127642862
340PhosphorylationSPSPSQTSSLGTAFT
CCCHHHCCCCCCHHH		18.8728152594
341PhosphorylationPSPSQTSSLGTAFTQ
CCHHHCCCCCCHHHC		33.9228152594
344PhosphorylationSQTSSLGTAFTQHHR
HHCCCCCCHHHCCCC		24.7224732914
345 (in isoform 4)Phosphorylation-12.0527251275
347PhosphorylationSSLGTAFTQHHRPVI
CCCCCHHHCCCCCCC		25.2424732914
355PhosphorylationQHHRPVITGPRASPH
CCCCCCCCCCCCCCC		41.1724732914
360PhosphorylationVITGPRASPHATPST
CCCCCCCCCCCCCCC		20.6323927012
360 (in isoform 2)Phosphorylation-20.6324719451
364PhosphorylationPRASPHATPSTLHFP
CCCCCCCCCCCCCCC		18.1023927012
364 (in isoform 2)Phosphorylation-18.1024719451
364 (in isoform 4)Phosphorylation-18.1027251275
366PhosphorylationASPHATPSTLHFPTS
CCCCCCCCCCCCCCC		38.9724732914
367O-linked_GlycosylationSPHATPSTLHFPTSP
CCCCCCCCCCCCCCC		26.0030059200
367PhosphorylationSPHATPSTLHFPTSP
CCCCCCCCCCCCCCC		26.0023927012
372PhosphorylationPSTLHFPTSPIIQQP
CCCCCCCCCCCCCCC		46.3123927012
372 (in isoform 2)Phosphorylation-46.3124719451
373O-linked_GlycosylationSTLHFPTSPIIQQPG
CCCCCCCCCCCCCCC		17.8430059200
373PhosphorylationSTLHFPTSPIIQQPG
CCCCCCCCCCCCCCC		17.8425159151
378 (in isoform 4)Phosphorylation-34.2127251275
380 (in isoform 4)Phosphorylation-25.7927251275
382PhosphorylationIIQQPGPYFSHPAIR
CCCCCCCCCCCCHHH		24.5124732914
382 (in isoform 4)Phosphorylation-24.5127251275
384PhosphorylationQQPGPYFSHPAIRYH
CCCCCCCCCCHHHCC		23.7924732914
389Asymmetric dimethylarginineYFSHPAIRYHPQETL
CCCCCHHHCCCHHHH		26.30-
389MethylationYFSHPAIRYHPQETL
CCCCCHHHCCCHHHH		26.3054548547
405 (in isoform 4)Phosphorylation-27.3227251275
417 (in isoform 4)Phosphorylation-9.5427251275
418 (in isoform 4)Phosphorylation-26.2327251275
422PhosphorylationGFLNPNGSSQGKVHN
EEECCCCCCCCCCCC		26.5727251275
423PhosphorylationFLNPNGSSQGKVHNP
EECCCCCCCCCCCCC		44.3327251275
456 (in isoform 2)Phosphorylation-39.1023663014
460 (in isoform 2)Phosphorylation-41.7423663014
461 (in isoform 2)Phosphorylation-39.1523663014
462 (in isoform 2)Phosphorylation-27.2623663014
463 (in isoform 2)Phosphorylation-36.2423663014
468 (in isoform 4)Phosphorylation-21.2227251275
469PhosphorylationSTEGGAASPTSPTYS
CCCCCCCCCCCCCCC		28.3324275569
469 (in isoform 2)Phosphorylation-28.3323663014
471PhosphorylationEGGAASPTSPTYSTP
CCCCCCCCCCCCCCC		44.8614702039
471 (in isoform 2)Phosphorylation-44.8623663014
472PhosphorylationGGAASPTSPTYSTPS
CCCCCCCCCCCCCCC		20.7320068231
472 (in isoform 2)Phosphorylation-20.7323663014
474PhosphorylationAASPTSPTYSTPSTS
CCCCCCCCCCCCCCC		29.8524275569
475PhosphorylationASPTSPTYSTPSTSP
CCCCCCCCCCCCCCC		17.5824275569
476PhosphorylationSPTSPTYSTPSTSPA
CCCCCCCCCCCCCCC		36.0024275569
480PhosphorylationPTYSTPSTSPANRFV
CCCCCCCCCCCCCCE		39.6824275569
481PhosphorylationTYSTPSTSPANRFVS
CCCCCCCCCCCCCEE		26.7624275569
495PhosphorylationSVGPRDPSFVNIPQQ
EECCCCHHHCCCCHH		46.2227251275
496 (in isoform 2)Phosphorylation-6.2426714015
497 (in isoform 2)Phosphorylation-8.1326714015
540 (in isoform 4)Phosphorylation-27251275
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 NFIA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NFIA_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 NFIA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAP18_HUMANSAP18physical
22939629
PCDA2_HUMANPCDHA2physical
22939629
NOP2_HUMANNOP2physical
22939629
TRA2A_HUMANTRA2Aphysical
22939629
TPBG_HUMANTPBGphysical
22939629
SRSF7_HUMANSRSF7physical
22939629
NOP56_HUMANNOP56physical
22939629
RRS1_HUMANRRS1physical
22939629
RS13_HUMANRPS13physical
22939629
SON_HUMANSONphysical
22939629
SRS10_HUMANSRSF10physical
22939629
SPB1_HUMANFTSJ3physical
22939629
RRP7A_HUMANRRP7Aphysical
22939629
UT14A_HUMANUTP14Aphysical
22939629
ZN326_HUMANZNF326physical
22939629
RS6_HUMANRPS6physical
22939629
RS24_HUMANRPS24physical
22939629
SURF4_HUMANSURF4physical
22939629
TRI55_HUMANTRIM55physical
22939629
VTNC_HUMANVTNphysical
22939629
RBM25_HUMANRBM25physical
22939629
SRSF3_HUMANSRSF3physical
22939629
TRA2B_HUMANTRA2Bphysical
22939629
RS11_HUMANRPS11physical
22939629
RL37A_HUMANRPL37Aphysical
22939629
SMAD4_HUMANSMAD4physical
18215124
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 NFIA_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-280 AND SER-287, ANDMASS SPECTROMETRY.
"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-258; SER-265; SER-280;SER-287; SER-300 AND SER-319, AND MASS SPECTROMETRY.
"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-287, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300 AND SER-305, 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-300, AND MASSSPECTROMETRY.
"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-287, AND MASSSPECTROMETRY.

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