ERF_HUMAN - dbPTM
ERF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERF_HUMAN
UniProt AC P50548
Protein Name ETS domain-containing transcription factor ERF
Gene Name ERF
Organism Homo sapiens (Human).
Sequence Length 548
Subcellular Localization Nucleus.
Protein Description Potent transcriptional repressor that binds to the H1 element of the Ets2 promoter. May regulate other genes involved in cellular proliferation. Required for extraembryonic ectoderm differentiation, ectoplacental cone cavity closure, and chorioallantoic attachment (By similarity). May be important for regulating trophoblast stem cell differentiation (By similarity)..
Protein Sequence MKTPADTGFAFPDWAYKPESSPGSRQIQLWHFILELLRKEEYQGVIAWQGDYGEFVIKDPDEVARLWGVRKCKPQMNYDKLSRALRYYYNKRILHKTKGKRFTYKFNFNKLVLVNYPFIDVGLAGGAVPQSAPPVPSGGSHFRFPPSTPSEVLSPTEDPRSPPACSSSSSSLFSAVVARRLGRGSVSDCSDGTSELEEPLGEDPRARPPGPPDLGAFRGPPLARLPHDPGVFRVYPRPRGGPEPLSPFPVSPLAGPGSLLPPQLSPALPMTPTHLAYTPSPTLSPMYPSGGGGPSGSGGGSHFSFSPEDMKRYLQAHTQSVYNYHLSPRAFLHYPGLVVPQPQRPDKCPLPPMAPETPPVPSSASSSSSSSSSPFKFKLQPPPLGRRQRAAGEKAVAGADKSGGSAGGLAEGAGALAPPPPPPQIKVEPISEGESEEVEVTDISDEDEEDGEVFKTPRAPPAPPKPEPGEAPGASQCMPLKLRFKRRWSEDCRLEGGGGPAGGFEDEGEDKKVRGEGPGEAGGPLTPRRVSSDLQHATAQLSLEHRDS
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
2Ubiquitination------MKTPADTGF
------CCCCCCCCC		64.32-
2Methylation------MKTPADTGF
------CCCCCCCCC		64.32-
3Phosphorylation-----MKTPADTGFA
-----CCCCCCCCCC		23.5523401153
7Phosphorylation-MKTPADTGFAFPDW
-CCCCCCCCCCCCCC		35.9823927012
16PhosphorylationFAFPDWAYKPESSPG
CCCCCCCCCCCCCCC		23.8723927012
17UbiquitinationAFPDWAYKPESSPGS
CCCCCCCCCCCCCCH		34.26-
20PhosphorylationDWAYKPESSPGSRQI
CCCCCCCCCCCHHHH		50.8122167270
21PhosphorylationWAYKPESSPGSRQIQ
CCCCCCCCCCHHHHH		31.4522167270
24PhosphorylationKPESSPGSRQIQLWH
CCCCCCCHHHHHHHH		25.1322167270
30UbiquitinationGSRQIQLWHFILELL
CHHHHHHHHHHHHHH		2.83-
71UbiquitinationARLWGVRKCKPQMNY
HHHHCCCCCCCCCCH		44.17-
73UbiquitinationLWGVRKCKPQMNYDK
HHCCCCCCCCCCHHH		41.12-
80UbiquitinationKPQMNYDKLSRALRY
CCCCCHHHHHHHHHH		37.69-
105UbiquitinationKGKRFTYKFNFNKLV
CCCCEEEEECCCEEE		30.6721890473
105UbiquitinationKGKRFTYKFNFNKLV
CCCCEEEEECCCEEE		30.6721890473
131PhosphorylationAGGAVPQSAPPVPSG
CCCCCCCCCCCCCCC		36.3530183078
137PhosphorylationQSAPPVPSGGSHFRF
CCCCCCCCCCCCCCC		56.8929514088
140PhosphorylationPPVPSGGSHFRFPPS
CCCCCCCCCCCCCCC		23.9929514088
147PhosphorylationSHFRFPPSTPSEVLS
CCCCCCCCCHHHCCC		53.8626503892
148PhosphorylationHFRFPPSTPSEVLSP
CCCCCCCCHHHCCCC		36.2930266825
150PhosphorylationRFPPSTPSEVLSPTE
CCCCCCHHHCCCCCC		40.1929255136
154PhosphorylationSTPSEVLSPTEDPRS
CCHHHCCCCCCCCCC		34.6426503892
156PhosphorylationPSEVLSPTEDPRSPP
HHHCCCCCCCCCCCC		50.0429255136
161PhosphorylationSPTEDPRSPPACSSS
CCCCCCCCCCCCCCC		40.3927794612
166PhosphorylationPRSPPACSSSSSSLF
CCCCCCCCCCHHHHH		35.0523663014
167PhosphorylationRSPPACSSSSSSLFS
CCCCCCCCCHHHHHH		33.8423663014
168PhosphorylationSPPACSSSSSSLFSA
CCCCCCCCHHHHHHH		20.2523663014
169PhosphorylationPPACSSSSSSLFSAV
CCCCCCCHHHHHHHH		26.3723663014
170PhosphorylationPACSSSSSSLFSAVV
CCCCCCHHHHHHHHH		32.7723663014
171PhosphorylationACSSSSSSLFSAVVA
CCCCCHHHHHHHHHH		35.0723663014
174PhosphorylationSSSSSLFSAVVARRL
CCHHHHHHHHHHHHH		26.0023663014
183MethylationVVARRLGRGSVSDCS
HHHHHHCCCCCCCCC		38.51-
185PhosphorylationARRLGRGSVSDCSDG
HHHHCCCCCCCCCCC		19.6523401153
187PhosphorylationRLGRGSVSDCSDGTS
HHCCCCCCCCCCCCC		34.3029255136
190PhosphorylationRGSVSDCSDGTSELE
CCCCCCCCCCCCCCC		44.0323927012
193PhosphorylationVSDCSDGTSELEEPL
CCCCCCCCCCCCCCC		24.8223927012
194PhosphorylationSDCSDGTSELEEPLG
CCCCCCCCCCCCCCC		45.7923927012
218MethylationPPDLGAFRGPPLARL
CCCCCCCCCCCCCCC		57.06-
224MethylationFRGPPLARLPHDPGV
CCCCCCCCCCCCCCC		57.33-
233MethylationPHDPGVFRVYPRPRG
CCCCCCEEEECCCCC		25.34-
246PhosphorylationRGGPEPLSPFPVSPL
CCCCCCCCCCCCCCC		34.9022817900
251PhosphorylationPLSPFPVSPLAGPGS
CCCCCCCCCCCCCCC		17.9022817900
313PhosphorylationSPEDMKRYLQAHTQS
CHHHHHHHHHHHHHH		9.5423403867
318PhosphorylationKRYLQAHTQSVYNYH
HHHHHHHHHHHHHHC		26.0928152594
319AcetylationRYLQAHTQSVYNYHL
HHHHHHHHHHHHHCC		22.49-
320PhosphorylationYLQAHTQSVYNYHLS
HHHHHHHHHHHHCCC		27.9428152594
322PhosphorylationQAHTQSVYNYHLSPR
HHHHHHHHHHCCCCC		18.4323403867
324PhosphorylationHTQSVYNYHLSPRAF
HHHHHHHHCCCCCCC		6.1023927012
327PhosphorylationSVYNYHLSPRAFLHY
HHHHHCCCCCCCCCC		10.0623401153
329MethylationYNYHLSPRAFLHYPG
HHHCCCCCCCCCCCC		34.30-
334PhosphorylationSPRAFLHYPGLVVPQ
CCCCCCCCCCCCCCC		10.9227642862
357PhosphorylationLPPMAPETPPVPSSA
CCCCCCCCCCCCCCC		31.6525850435
362PhosphorylationPETPPVPSSASSSSS
CCCCCCCCCCCCCCC		38.4825850435
363PhosphorylationETPPVPSSASSSSSS
CCCCCCCCCCCCCCC		26.5427251275
365PhosphorylationPPVPSSASSSSSSSS
CCCCCCCCCCCCCCC		32.4727251275
366PhosphorylationPVPSSASSSSSSSSS
CCCCCCCCCCCCCCC		33.6827251275
367PhosphorylationVPSSASSSSSSSSSP
CCCCCCCCCCCCCCC		31.5725850435
368PhosphorylationPSSASSSSSSSSSPF
CCCCCCCCCCCCCCC		35.8725850435
369PhosphorylationSSASSSSSSSSSPFK
CCCCCCCCCCCCCCC		35.8725850435
370PhosphorylationSASSSSSSSSSPFKF
CCCCCCCCCCCCCCE		35.8725850435
371PhosphorylationASSSSSSSSSPFKFK
CCCCCCCCCCCCCEE		36.4627251275
372PhosphorylationSSSSSSSSSPFKFKL
CCCCCCCCCCCCEEC		43.9327251275
373PhosphorylationSSSSSSSSPFKFKLQ
CCCCCCCCCCCEECC		35.9825850435
376MethylationSSSSSPFKFKLQPPP
CCCCCCCCEECCCCC		45.00-
378SumoylationSSSPFKFKLQPPPLG
CCCCCCEECCCCCCC		46.96-
378SumoylationSSSPFKFKLQPPPLG
CCCCCCEECCCCCCC		46.96-
394AcetylationRQRAAGEKAVAGADK
HHHHCHHHCCCCCCC		47.4423749302
402PhosphorylationAVAGADKSGGSAGGL
CCCCCCCCCCCCCHH		49.2728555341
405PhosphorylationGADKSGGSAGGLAEG
CCCCCCCCCCHHHCC		27.5428387310
431PhosphorylationQIKVEPISEGESEEV
CCEEEECCCCCCCEE		50.7127422710
435PhosphorylationEPISEGESEEVEVTD
EECCCCCCCEEEEEE		50.3327422710
441PhosphorylationESEEVEVTDISDEDE
CCCEEEEEECCCCCC		17.7025072903
444PhosphorylationEVEVTDISDEDEEDG
EEEEEECCCCCCCCC		37.4425072903
456PhosphorylationEDGEVFKTPRAPPAP
CCCCEECCCCCCCCC		13.4221406692
465SumoylationRAPPAPPKPEPGEAP
CCCCCCCCCCCCCCC		62.04-
465SumoylationRAPPAPPKPEPGEAP
CCCCCCCCCCCCCCC		62.0428112733
475PhosphorylationPGEAPGASQCMPLKL
CCCCCCCCCCCCCEE		29.8128555341
481SumoylationASQCMPLKLRFKRRW
CCCCCCCEECEEECC		31.5728112733
489PhosphorylationLRFKRRWSEDCRLEG
ECEEECCCCCCCCCC		23.0323401153
512SumoylationEDEGEDKKVRGEGPG
CCCCCCCCCCCCCCC		49.8728112733
512SumoylationEDEGEDKKVRGEGPG
CCCCCCCCCCCCCCC		49.87-
526PhosphorylationGEAGGPLTPRRVSSD
CCCCCCCCCCCCCHH		20.2019664994
531PhosphorylationPLTPRRVSSDLQHAT
CCCCCCCCHHHHHHH		19.1429255136
532PhosphorylationLTPRRVSSDLQHATA
CCCCCCCHHHHHHHH		39.2129255136
538PhosphorylationSSDLQHATAQLSLEH
CHHHHHHHHHHHHHC		16.8923927012
542PhosphorylationQHATAQLSLEHRDS-
HHHHHHHHHHCCCC-		21.4523927012
548PhosphorylationLSLEHRDS-------
HHHHCCCC-------		41.9223927012
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
161SPhosphorylationKinaseMAPK1P28482
GPS
246SPhosphorylationKinaseMAPK1P28482
GPS
251SPhosphorylationKinaseMAPK1P28482
GPS
526TPhosphorylationKinaseMK01P28482
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
526TPhosphorylation

7588608
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 ERF_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPOP_HUMANSPOPphysical
26344095
MARF1_HUMANKIAA0430physical
27173435
PAN2_HUMANPAN2physical
27173435
NISCH_HUMANNISCHphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
600775Craniosynostosis 4 (CRS4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERF_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-431; SER-444 ANDTHR-526, AND MASS 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 THR-3; THR-7; TYR-16;SER-20; SER-21; THR-148; SER-171; SER-185; SER-187; SER-190; SER-327;SER-431; SER-435; THR-441; SER-444; THR-526; SER-531 AND SER-548, 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-21; SER-185; SER-187;SER-190 AND SER-531, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526, AND MASSSPECTROMETRY.
"ERF: an ETS domain protein with strong transcriptional repressoractivity, can suppress ets-associated tumorigenesis and is regulatedby phosphorylation during cell cycle and mitogenic stimulation.";
Sgouras D.N., Athanasiou M.A., Beal G.J. Jr., Fisher R.J., Blair D.G.,Mavrothalassitis G.J.;
EMBO J. 14:4781-4793(1995).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-526, ANDMUTAGENESIS OF THR-526.

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