NFX1_HUMAN - dbPTM
NFX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NFX1_HUMAN
UniProt AC Q12986
Protein Name Transcriptional repressor NF-X1
Gene Name NFX1
Organism Homo sapiens (Human).
Sequence Length 1120
Subcellular Localization Nucleus.
Protein Description Binds to the X-box motif of MHC class II genes and represses their expression. May play an important role in regulating the duration of an inflammatory response by limiting the period in which MHC class II molecules are induced by interferon-gamma. Isoform 3 binds to the X-box motif of TERT promoter and represses its expression. Together with PABPC1 or PABPC4, isoform 1 acts as a coactivator for TERT expression. Mediates E2-dependent ubiquitination..
Protein Sequence MAEAPPVSGTFKFNTDAAEFIPQEKKNSGLNCGTQRRLDSNRIGRRNYSSPPPCHLSRQVPYDEISAVHQHSYHPSGSKPKSQQTSFQSSPCNKSPKSHGLQNQPWQKLRNEKHHIRVKKAQSLAEQTSDTAGLESSTRSESGTDLREHSPSESEKEVVGADPRGAKPKKATQFVYSYGRGPKVKGKLKCEWSNRTTPKPEDAGPESTKPVGVFHPDSSEASSRKGVLDGYGARRNEQRRYPQKRPPWEVEGARPRPGRNPPKQEGHRHTNAGHRNNMGPIPKDDLNERPAKSTCDSENLAVINKSSRRVDQEKCTVRRQDPQVVSPFSRGKQNHVLKNVETHTGSLIEQLTTEKYECMVCCELVRVTAPVWSCQSCYHVFHLNCIKKWARSPASQADGQSGWRCPACQNVSAHVPNTYTCFCGKVKNPEWSRNEIPHSCGEVCRKKQPGQDCPHSCNLLCHPGPCPPCPAFMTKTCECGRTRHTVRCGQAVSVHCSNPCENILNCGQHQCAELCHGGQCQPCQIILNQVCYCGSTSRDVLCGTDVGKSDGFGDFSCLKICGKDLKCGNHTCSQVCHPQPCQQCPRLPQLVRCCPCGQTPLSQLLELGSSSRKTCMDPVPSCGKVCGKPLPCGSLDFIHTCEKLCHEGDCGPCSRTSVISCRCSFRTKELPCTSLKSEDATFMCDKRCNKKRLCGRHKCNEICCVDKEHKCPLICGRKLRCGLHRCEEPCHRGNCQTCWQASFDELTCHCGASVIYPPVPCGTRPPECTQTCARVHECDHPVYHSCHSEEKCPPCTFLTQKWCMGKHEFRSNIPCHLVDISCGLPCSATLPCGMHKCQRLCHKGECLVDEPCKQPCTTPRADCGHPCMAPCHTSSPCPVTACKAKVELQCECGRRKEMVICSEASSTYQRIAAISMASKITDMQLGGSVEISKLITKKEVHQARLECDEECSALERKKRLAEAFHISEDSDPFNIRSSGSKFSDSLKEDARKDLKFVSDVEKEMETLVEAVNKGKNSKKSHSFPPMNRDHRRIIHDLAQVYGLESVSYDSEPKRNVVVTAIRGKSVCPPTTLTGVLEREMQARPPPPIPHHRHQSDKNPGSSNLQKITKEPIIDYFDVQD
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
8PhosphorylationMAEAPPVSGTFKFNT
CCCCCCCCCEEEECC
37.5824719451
25UbiquitinationAEFIPQEKKNSGLNC
HHHCCHHHCCCCCCC
52.5929967540
34PhosphorylationNSGLNCGTQRRLDSN
CCCCCCCCCCCCCCC
22.54-
48PhosphorylationNRIGRRNYSSPPPCH
CCCCCCCCCCCCCCC
14.5522167270
49PhosphorylationRIGRRNYSSPPPCHL
CCCCCCCCCCCCCCC
39.6622167270
50PhosphorylationIGRRNYSSPPPCHLS
CCCCCCCCCCCCCCC
30.9422167270
57PhosphorylationSPPPCHLSRQVPYDE
CCCCCCCCCCCCHHH
9.3023927012
62PhosphorylationHLSRQVPYDEISAVH
CCCCCCCHHHHHHHE
27.6126074081
82PhosphorylationPSGSKPKSQQTSFQS
CCCCCCCCCCCCCCC
35.7323927012
85PhosphorylationSKPKSQQTSFQSSPC
CCCCCCCCCCCCCCC
24.7128450419
86PhosphorylationKPKSQQTSFQSSPCN
CCCCCCCCCCCCCCC
19.5628450419
89PhosphorylationSQQTSFQSSPCNKSP
CCCCCCCCCCCCCCC
33.9525159151
90PhosphorylationQQTSFQSSPCNKSPK
CCCCCCCCCCCCCCC
23.7625159151
95PhosphorylationQSSPCNKSPKSHGLQ
CCCCCCCCCCCCCCC
24.4623927012
97UbiquitinationSPCNKSPKSHGLQNQ
CCCCCCCCCCCCCCC
63.2729967540
98PhosphorylationPCNKSPKSHGLQNQP
CCCCCCCCCCCCCCH
26.6027174698
108UbiquitinationLQNQPWQKLRNEKHH
CCCCHHHHHHCCHHH
45.6132015554
120UbiquitinationKHHIRVKKAQSLAEQ
HHHHHHHHHHHHHHH
49.1229967540
123PhosphorylationIRVKKAQSLAEQTSD
HHHHHHHHHHHHCCC
34.1125159151
128PhosphorylationAQSLAEQTSDTAGLE
HHHHHHHCCCCCCCC
21.7827732954
129PhosphorylationQSLAEQTSDTAGLES
HHHHHHCCCCCCCCC
32.4327732954
131PhosphorylationLAEQTSDTAGLESST
HHHHCCCCCCCCCCC
23.5327732954
136PhosphorylationSDTAGLESSTRSESG
CCCCCCCCCCCCCCC
41.8925159151
137PhosphorylationDTAGLESSTRSESGT
CCCCCCCCCCCCCCC
20.6125159151
138PhosphorylationTAGLESSTRSESGTD
CCCCCCCCCCCCCCC
47.7125159151
140PhosphorylationGLESSTRSESGTDLR
CCCCCCCCCCCCCHH
35.8823403867
142PhosphorylationESSTRSESGTDLREH
CCCCCCCCCCCHHHC
48.5223401153
144PhosphorylationSTRSESGTDLREHSP
CCCCCCCCCHHHCCC
40.9325159151
150PhosphorylationGTDLREHSPSESEKE
CCCHHHCCCCHHHHH
25.9329255136
152PhosphorylationDLREHSPSESEKEVV
CHHHCCCCHHHHHCC
57.6923927012
154PhosphorylationREHSPSESEKEVVGA
HHCCCCHHHHHCCCC
59.3025159151
172PhosphorylationGAKPKKATQFVYSYG
CCCCCCCCCCEEECC
31.2721945579
176PhosphorylationKKATQFVYSYGRGPK
CCCCCCEEECCCCCC
9.4721945579
177PhosphorylationKATQFVYSYGRGPKV
CCCCCEEECCCCCCC
18.7921945579
178PhosphorylationATQFVYSYGRGPKVK
CCCCEEECCCCCCCC
7.9921945579
193PhosphorylationGKLKCEWSNRTTPKP
CEEEEEECCCCCCCC
8.3027251275
197PhosphorylationCEWSNRTTPKPEDAG
EEECCCCCCCCCCCC
26.5228555341
199UbiquitinationWSNRTTPKPEDAGPE
ECCCCCCCCCCCCCC
59.9729967540
209UbiquitinationDAGPESTKPVGVFHP
CCCCCCCCCCEEECC
47.1629967540
218PhosphorylationVGVFHPDSSEASSRK
CEEECCCCCCHHHCC
34.2327732954
219PhosphorylationGVFHPDSSEASSRKG
EEECCCCCCHHHCCC
44.5627732954
222PhosphorylationHPDSSEASSRKGVLD
CCCCCCHHHCCCCCC
26.9927732954
223PhosphorylationPDSSEASSRKGVLDG
CCCCCHHHCCCCCCC
45.0927732954
225UbiquitinationSSEASSRKGVLDGYG
CCCHHHCCCCCCCCC
56.1533845483
231PhosphorylationRKGVLDGYGARRNEQ
CCCCCCCCCCCCCCC
13.79-
283UbiquitinationNNMGPIPKDDLNERP
CCCCCCCHHHCCCCC
65.6729967540
292MethylationDLNERPAKSTCDSEN
HCCCCCCCCCCCHHC
49.3223644510
294PhosphorylationNERPAKSTCDSENLA
CCCCCCCCCCHHCEE
21.4528555341
305UbiquitinationENLAVINKSSRRVDQ
HCEEEEECCCCCCCH
38.3932015554
314UbiquitinationSRRVDQEKCTVRRQD
CCCCCHHHCCCCCCC
29.5824816145
316PhosphorylationRVDQEKCTVRRQDPQ
CCCHHHCCCCCCCCC
28.28-
326PhosphorylationRQDPQVVSPFSRGKQ
CCCCCCCCCCCCCCC
22.7519664994
329PhosphorylationPQVVSPFSRGKQNHV
CCCCCCCCCCCCCCE
43.4330266825
342PhosphorylationHVLKNVETHTGSLIE
CEECCCCHHHCCHHH
22.0627251275
344PhosphorylationLKNVETHTGSLIEQL
ECCCCHHHCCHHHHH
35.5727251275
346PhosphorylationNVETHTGSLIEQLTT
CCCHHHCCHHHHHHC
27.5920873877
392PhosphorylationCIKKWARSPASQADG
HHHHHHCCHHHHCCC
19.6425159151
427UbiquitinationTCFCGKVKNPEWSRN
ECCCCCCCCCCCCCC
70.9832015554
548UbiquitinationLCGTDVGKSDGFGDF
EECCCCCCCCCCCCC
45.2632015554
559UbiquitinationFGDFSCLKICGKDLK
CCCCHHEEEECCCCC
40.0332015554
599PhosphorylationRCCPCGQTPLSQLLE
CCCCCCCCCHHHHHH
16.10-
602PhosphorylationPCGQTPLSQLLELGS
CCCCCCHHHHHHHCC
21.71-
609PhosphorylationSQLLELGSSSRKTCM
HHHHHHCCCCCCCCC
37.45-
613UbiquitinationELGSSSRKTCMDPVP
HHCCCCCCCCCCCCC
48.2829967540
628UbiquitinationSCGKVCGKPLPCGSL
CCCCCCCCCCCCCCC
37.9532015554
634PhosphorylationGKPLPCGSLDFIHTC
CCCCCCCCCHHHHHH
31.3327251275
664PhosphorylationSVISCRCSFRTKELP
EEEEEEEEEECCCCC
9.83-
668UbiquitinationCRCSFRTKELPCTSL
EEEEEECCCCCCCCC
53.6629967540
676UbiquitinationELPCTSLKSEDATFM
CCCCCCCCCCCCCEE
52.1232015554
677PhosphorylationLPCTSLKSEDATFMC
CCCCCCCCCCCCEEC
46.10-
681PhosphorylationSLKSEDATFMCDKRC
CCCCCCCCEECCCCC
24.99-
686AcetylationDATFMCDKRCNKKRL
CCCEECCCCCCCCCC
54.6527452117
686UbiquitinationDATFMCDKRCNKKRL
CCCEECCCCCCCCCC
54.6532015554
690UbiquitinationMCDKRCNKKRLCGRH
ECCCCCCCCCCCCCC
42.78-
691UbiquitinationCDKRCNKKRLCGRHK
CCCCCCCCCCCCCCC
36.29-
710UbiquitinationCCVDKEHKCPLICGR
EECCCCCCCCEECCC
38.3429967540
711UbiquitinationCVDKEHKCPLICGRK
ECCCCCCCCEECCCE
3.4129967540
783PhosphorylationHECDHPVYHSCHSEE
HCCCCCCCCCCCCCC
7.77-
785PhosphorylationCDHPVYHSCHSEEKC
CCCCCCCCCCCCCCC
8.8828555341
788PhosphorylationPVYHSCHSEEKCPPC
CCCCCCCCCCCCCCC
52.3429449344
811PhosphorylationMGKHEFRSNIPCHLV
CCCCHHHHCCCEEEE
44.4222210691
812 (in isoform 3)Phosphorylation-37.66-
818UbiquitinationSNIPCHLVDISCGLP
HCCCEEEEEECCCCC
2.4629967540
853UbiquitinationCLVDEPCKQPCTTPR
CCCCCCCCCCCCCCC
68.9132015554
854UbiquitinationLVDEPCKQPCTTPRA
CCCCCCCCCCCCCCC
45.0432015554
857PhosphorylationEPCKQPCTTPRADCG
CCCCCCCCCCCCCCC
46.6627251275
858PhosphorylationPCKQPCTTPRADCGH
CCCCCCCCCCCCCCC
19.9327251275
885UbiquitinationPVTACKAKVELQCEC
CCCCCEEEEEEEEEC
23.0321906983
885 (in isoform 1)Ubiquitination-23.0321906983
885 (in isoform 2)Ubiquitination-23.0321906983
907PhosphorylationICSEASSTYQRIAAI
EEECCCCHHHHHHHH
22.60-
928PhosphorylationTDMQLGGSVEISKLI
CCCCCCCCEEEHHCC
18.1228555341
967PhosphorylationLAEAFHISEDSDPFN
HHHHHCCCCCCCCCC
27.1224719451
977PhosphorylationSDPFNIRSSGSKFSD
CCCCCCCCCCCCCCH
34.9425627689
978PhosphorylationDPFNIRSSGSKFSDS
CCCCCCCCCCCCCHH
36.9225159151
980PhosphorylationFNIRSSGSKFSDSLK
CCCCCCCCCCCHHHH
32.2624719451
981AcetylationNIRSSGSKFSDSLKE
CCCCCCCCCCHHHHH
53.037705889
981UbiquitinationNIRSSGSKFSDSLKE
CCCCCCCCCCHHHHH
53.0329967540
982UbiquitinationIRSSGSKFSDSLKED
CCCCCCCCCHHHHHH
11.9829967540
983PhosphorylationRSSGSKFSDSLKEDA
CCCCCCCCHHHHHHH
29.9927251275
985PhosphorylationSGSKFSDSLKEDARK
CCCCCCHHHHHHHHH
39.8927251275
995UbiquitinationEDARKDLKFVSDVEK
HHHHHHHCHHHHHHH
54.5829967540
996UbiquitinationDARKDLKFVSDVEKE
HHHHHHCHHHHHHHH
9.1629967540
1013UbiquitinationTLVEAVNKGKNSKKS
HHHHHHHCCCCCCCC
65.7429967540
1014UbiquitinationLVEAVNKGKNSKKSH
HHHHHHCCCCCCCCC
29.2229967540
1041PhosphorylationIHDLAQVYGLESVSY
HHHHHHHHCCCCCCC
12.1518187866
1045PhosphorylationAQVYGLESVSYDSEP
HHHHCCCCCCCCCCC
22.7718187866
1047PhosphorylationVYGLESVSYDSEPKR
HHCCCCCCCCCCCCC
32.2818187866
1095PhosphorylationIPHHRHQSDKNPGSS
CCCCCCCCCCCCCCC
44.4123401153
1097UbiquitinationHHRHQSDKNPGSSNL
CCCCCCCCCCCCCCH
71.0029967540
1098UbiquitinationHRHQSDKNPGSSNLQ
CCCCCCCCCCCCCHH
51.6729967540
1106UbiquitinationPGSSNLQKITKEPII
CCCCCHHHHHCCCEE
56.3529967540
1107UbiquitinationGSSNLQKITKEPIID
CCCCHHHHHCCCEEC
4.2529967540
1115PhosphorylationTKEPIIDYFDVQD--
HCCCEECCCCCCC--
7.4128796482

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 NFX1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NFX1_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 NFX1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAML3_HUMANMAML3physical
20211142
SIN3A_HUMANSIN3Aphysical
18505829
USP9X_HUMANUSP9Xphysical
17267499
PABP1_HUMANPABPC1physical
17267499
EF1A2_HUMANEEF1A2physical
17267499
MATR3_HUMANMATR3physical
17267499
PABP3_HUMANPABPC3physical
17267499
HNRPM_HUMANHNRNPMphysical
17267499
HNRPU_HUMANHNRNPUphysical
17267499
RL13_HUMANRPL13physical
17267499
SRSF4_HUMANSRSF4physical
17267499
H2A1B_HUMANHIST1H2AEphysical
17267499
RL7A_HUMANRPL7Aphysical
17267499
F208B_HUMANFAM208Bphysical
17267499
LARP1_HUMANLARP1physical
17267499
DDX5_HUMANDDX5physical
17267499
DMD_HUMANDMDphysical
17267499
NUCL_HUMANNCLphysical
17267499
RL13A_HUMANRPL13Aphysical
17267499
RL17_HUMANRPL17physical
17267499
RL22_HUMANRPL22physical
17267499
RL3_HUMANRPL3physical
17267499
RL6_HUMANRPL6physical
17267499
ROA2_HUMANHNRNPA2B1physical
17267499
HNRH1_HUMANHNRNPH1physical
17267499
RS19_HUMANRPS19physical
17267499
RS3A_HUMANRPS3Aphysical
17267499
SRSF3_HUMANSRSF3physical
17267499
APCL_HUMANAPC2physical
17267499
YBOX1_HUMANYBX1physical
17267499

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 NFX1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-50, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, 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-50, 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-49 AND SER-50, AND MASSSPECTROMETRY.
"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 TYR-1041, AND MASSSPECTROMETRY.

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