ELF2_HUMAN - dbPTM
ELF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELF2_HUMAN
UniProt AC Q15723
Protein Name ETS-related transcription factor Elf-2
Gene Name ELF2 {ECO:0000312|EMBL:AAF67195.1}
Organism Homo sapiens (Human).
Sequence Length 593
Subcellular Localization Nucleus.
Protein Description Isoform 1 transcriptionally activates the LYN and BLK promoters and acts synergistically with RUNX1 to transactivate the BLK promoter.; Isoform 2 may function in repression of RUNX1-mediated transactivation..
Protein Sequence MTSAVVDSGGTILELSSNGVENQEESEKVSEYPAVIVEPVPSARLEQGYAAQVLVYDDETYMMQDVAEEQEVETENVETVEASVHSSNAHCTDKTIEAAEALLHMESPTCLRDSRSPVEVFVPPCVSTPEFIHAAMRPDVITETVVEVSTEESEPMDTSPIPTSPDSHEPMKKKKVGRKPKTQQSPISNGSPELGIKKKPREGKGNTTYLWEFLLDLLQDKNTCPRYIKWTQREKGIFKLVDSKAVSKLWGKHKNKPDMNYETMGRALRYYYQRGILAKVEGQRLVYQFKDMPKNIVVIDDDKSETCNEDLAGTTDEKSLERVSLSAESLLKAASSVRSGKNSSPINCSRAEKGVARVVNITSPGHDASSRSPTTTASVSATAAPRTVRVAMQVPVVMTSLGQKISTVAVQSVNAGAPLITSTSPTTATSPKVVIQTIPTVMPASTENGDKITMQPAKIITIPATQLAQCQLQTKSNLTGSGSINIVGTPLAVRALTPVSIAHGTPVMRLSMPTQQASGQTPPRVISAVIKGPEVKSEAVAKKQEHDVKTLQLVEEKPADGNKTVTHVVVVSAPSAIALPVTMKTEGLVTCEK
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
3 (in isoform 2)Phosphorylation-20.1226714015
3 (in isoform 3)Phosphorylation-20.1226714015
3 (in isoform 4)Phosphorylation-20.1226714015
4 (in isoform 2)Phosphorylation-9.0026714015
4 (in isoform 3)Phosphorylation-9.0026714015
4 (in isoform 4)Phosphorylation-9.0026714015
8PhosphorylationMTSAVVDSGGTILEL
CCEEEECCCCEEEEE		27.7527251275
11PhosphorylationAVVDSGGTILELSSN
EEECCCCEEEEECCC		26.3927251275
16PhosphorylationGGTILELSSNGVENQ
CCEEEEECCCCCCCH		16.6327251275
17PhosphorylationGTILELSSNGVENQE
CEEEEECCCCCCCHH		50.6727251275
47 (in isoform 2)Phosphorylation-55.5825849741
54 (in isoform 2)Phosphorylation-1.6428111955
56 (in isoform 2)Phosphorylation-17.3224719451
95PhosphorylationNAHCTDKTIEAAEAL
CCCCCHHHHHHHHHH		27.1923312004
107PhosphorylationEALLHMESPTCLRDS
HHHHCCCCCCCCCCC		20.2430266825
107 (in isoform 1)Phosphorylation-20.2425849741
109PhosphorylationLLHMESPTCLRDSRS
HHCCCCCCCCCCCCC		33.1930266825
114PhosphorylationSPTCLRDSRSPVEVF
CCCCCCCCCCCCEEE		28.3728102081
114 (in isoform 1)Phosphorylation-28.3728111955
116PhosphorylationTCLRDSRSPVEVFVP
CCCCCCCCCCEEECC		36.9324275569
116 (in isoform 1)Phosphorylation-36.9324719451
125 (in isoform 2)Ubiquitination-2.8621890473
137 (in isoform 3)Ubiquitination-21.3821890473
142PhosphorylationAMRPDVITETVVEVS
HHCCCEEEEEEEEEE		26.00-
150 (in isoform 4)Ubiquitination-49.2821890473
153PhosphorylationVEVSTEESEPMDTSP
EEEECCCCCCCCCCC		40.54-
158PhosphorylationEESEPMDTSPIPTSP
CCCCCCCCCCCCCCC		30.10-
163PhosphorylationMDTSPIPTSPDSHEP
CCCCCCCCCCCCCCC		54.3224275569
167 (in isoform 2)Ubiquitination-32.8921890473
170PhosphorylationTSPDSHEPMKKKKVG
CCCCCCCCCCCCCCC		34.1719651622
173PhosphorylationDSHEPMKKKKVGRKP
CCCCCCCCCCCCCCC		52.1219651622
176PhosphorylationEPMKKKKVGRKPKTQ
CCCCCCCCCCCCCCC		14.2319651622
179PhosphorylationKKKKVGRKPKTQQSP
CCCCCCCCCCCCCCC		44.9619413330
179 (in isoform 3)Ubiquitination-44.9621890473
182PhosphorylationKVGRKPKTQQSPISN
CCCCCCCCCCCCCCC		40.1323927012
185PhosphorylationRKPKTQQSPISNGSP
CCCCCCCCCCCCCCC		17.8730266825
185 (in isoform 1)Ubiquitination-17.8721890473
188PhosphorylationKTQQSPISNGSPELG
CCCCCCCCCCCCCCC		38.2230266825
191PhosphorylationQSPISNGSPELGIKK
CCCCCCCCCCCCCCC		21.3223927012
197UbiquitinationGSPELGIKKKPREGK
CCCCCCCCCCCCCCC		53.60-
197 (in isoform 5)Ubiquitination-53.6021890473
198UbiquitinationSPELGIKKKPREGKG
CCCCCCCCCCCCCCC		67.12-
227 (in isoform 1)Ubiquitination-7.6221890473
229UbiquitinationNTCPRYIKWTQREKG
CCCHHHCCCHHHCCC		34.94-
239UbiquitinationQREKGIFKLVDSKAV
HHCCCEEEEECHHHH		45.76-
239 (in isoform 5)Ubiquitination-45.7621890473
243UbiquitinationGIFKLVDSKAVSKLW
CEEEEECHHHHHHHH		18.29-
248UbiquitinationVDSKAVSKLWGKHKN
ECHHHHHHHHHCCCC		41.48-
256UbiquitinationLWGKHKNKPDMNYET
HHHCCCCCCCCCHHH		47.39-
261PhosphorylationKNKPDMNYETMGRAL
CCCCCCCHHHHHHHH		13.21-
269MethylationETMGRALRYYYQRGI
HHHHHHHHHHHHCCC		19.20-
270PhosphorylationTMGRALRYYYQRGIL
HHHHHHHHHHHCCCC		13.8428270605
271PhosphorylationMGRALRYYYQRGILA
HHHHHHHHHHCCCCC		6.1628270605
272PhosphorylationGRALRYYYQRGILAK
HHHHHHHHHCCCCCE		5.2528270605
279SumoylationYQRGILAKVEGQRLV
HHCCCCCEEECEEEE		37.06-
279UbiquitinationYQRGILAKVEGQRLV
HHCCCCCEEECEEEE		37.06-
287PhosphorylationVEGQRLVYQFKDMPK
EECEEEEEEECCCCC		16.90-
290UbiquitinationQRLVYQFKDMPKNIV
EEEEEEECCCCCCEE		37.28-
294UbiquitinationYQFKDMPKNIVVIDD
EEECCCCCCEEEECC		53.31-
304PhosphorylationVVIDDDKSETCNEDL
EEECCCCCCCCCCCC		45.1725849741
306PhosphorylationIDDDKSETCNEDLAG
ECCCCCCCCCCCCCC		27.9328348404
314PhosphorylationCNEDLAGTTDEKSLE
CCCCCCCCCCHHHHH		26.0118669648
315PhosphorylationNEDLAGTTDEKSLER
CCCCCCCCCHHHHHH		41.0423312004
318UbiquitinationLAGTTDEKSLERVSL
CCCCCCHHHHHHHCC		64.25-
319PhosphorylationAGTTDEKSLERVSLS
CCCCCHHHHHHHCCC		33.1523312004
324PhosphorylationEKSLERVSLSAESLL
HHHHHHHCCCHHHHH		23.8730108239
326PhosphorylationSLERVSLSAESLLKA
HHHHHCCCHHHHHHH		23.6023917254
329PhosphorylationRVSLSAESLLKAASS
HHCCCHHHHHHHHHH		38.4230108239
332UbiquitinationLSAESLLKAASSVRS
CCHHHHHHHHHHHHC		47.39-
341AcetylationASSVRSGKNSSPINC
HHHHHCCCCCCCCCC		55.7026051181
343PhosphorylationSVRSGKNSSPINCSR
HHHCCCCCCCCCCCH		40.7627794612
344PhosphorylationVRSGKNSSPINCSRA
HHCCCCCCCCCCCHH		38.9125159151
351PhosphorylationSPINCSRAEKGVARV
CCCCCCHHHHCEEEE		13.4218669648
360PhosphorylationKGVARVVNITSPGHD
HCEEEEEECCCCCCC		29.0318669648
362UbiquitinationVARVVNITSPGHDAS
EEEEEECCCCCCCCC		24.54-
362PhosphorylationVARVVNITSPGHDAS
EEEEEECCCCCCCCC		24.5421712546
363PhosphorylationARVVNITSPGHDASS
EEEEECCCCCCCCCC		25.7025159151
369PhosphorylationTSPGHDASSRSPTTT
CCCCCCCCCCCCCCE		32.1323403867
370O-linked_GlycosylationSPGHDASSRSPTTTA
CCCCCCCCCCCCCEE		38.2030059200
370PhosphorylationSPGHDASSRSPTTTA
CCCCCCCCCCCCCEE		38.2021712546
372O-linked_GlycosylationGHDASSRSPTTTASV
CCCCCCCCCCCEEEE		28.6630059200
372PhosphorylationGHDASSRSPTTTASV
CCCCCCCCCCCEEEE		28.6630266825
374O-linked_GlycosylationDASSRSPTTTASVSA
CCCCCCCCCEEEEEC		37.7230059200
374PhosphorylationDASSRSPTTTASVSA
CCCCCCCCCEEEEEC		37.7230266825
375O-linked_GlycosylationASSRSPTTTASVSAT
CCCCCCCCEEEEECC		24.6130059200
375PhosphorylationASSRSPTTTASVSAT
CCCCCCCCEEEEECC		24.6130266825
376O-linked_GlycosylationSSRSPTTTASVSATA
CCCCCCCEEEEECCC		21.2930059200
376PhosphorylationSSRSPTTTASVSATA
CCCCCCCEEEEECCC		21.2930266825
378O-linked_GlycosylationRSPTTTASVSATAAP
CCCCCEEEEECCCCC		17.9530059200
378PhosphorylationRSPTTTASVSATAAP
CCCCCEEEEECCCCC		17.9530108239
380O-linked_GlycosylationPTTTASVSATAAPRT
CCCEEEEECCCCCCC		19.8730059200
380PhosphorylationPTTTASVSATAAPRT
CCCEEEEECCCCCCC		19.8730108239
382O-linked_GlycosylationTTASVSATAAPRTVR
CEEEEECCCCCCCEE		18.8230059200
382PhosphorylationTTASVSATAAPRTVR
CEEEEECCCCCCCEE		18.8230108239
400O-linked_GlycosylationQVPVVMTSLGQKIST
ECCEEEECCCCCEEE		16.6530059200
406O-linked_GlycosylationTSLGQKISTVAVQSV
ECCCCCEEEEEEEEC		24.7030059200
410PhosphorylationQKISTVAVQSVNAGA
CCEEEEEEEECCCCC		3.6620068231
412PhosphorylationISTVAVQSVNAGAPL
EEEEEEEECCCCCCE		15.6720068231
414PhosphorylationTVAVQSVNAGAPLIT
EEEEEECCCCCCEEE		37.5919413330
415PhosphorylationVAVQSVNAGAPLITS
EEEEECCCCCCEEEE		17.2318669648
417PhosphorylationVQSVNAGAPLITSTS
EEECCCCCCEEEECC		8.0419413330
418PhosphorylationQSVNAGAPLITSTSP
EECCCCCCEEEECCC		24.3119413330
421O-linked_GlycosylationNAGAPLITSTSPTTA
CCCCCEEEECCCCCC		33.3730059200
421PhosphorylationNAGAPLITSTSPTTA
CCCCCEEEECCCCCC		33.3728450419
422O-linked_GlycosylationAGAPLITSTSPTTAT
CCCCEEEECCCCCCC		21.6430059200
422PhosphorylationAGAPLITSTSPTTAT
CCCCEEEECCCCCCC		21.6425159151
423O-linked_GlycosylationGAPLITSTSPTTATS
CCCEEEECCCCCCCC		30.0330059200
423PhosphorylationGAPLITSTSPTTATS
CCCEEEECCCCCCCC		30.0325159151
424O-linked_GlycosylationAPLITSTSPTTATSP
CCEEEECCCCCCCCC		21.7330059200
424PhosphorylationAPLITSTSPTTATSP
CCEEEECCCCCCCCC		21.7325159151
426PhosphorylationLITSTSPTTATSPKV
EEEECCCCCCCCCCE		28.9119413330
427O-linked_GlycosylationITSTSPTTATSPKVV
EEECCCCCCCCCCEE		31.1830059200
427PhosphorylationITSTSPTTATSPKVV
EEECCCCCCCCCCEE		31.1828348404
429PhosphorylationSTSPTTATSPKVVIQ
ECCCCCCCCCCEEEE		43.3925159151
430PhosphorylationTSPTTATSPKVVIQT
CCCCCCCCCCEEEEE		21.9125159151
442UbiquitinationIQTIPTVMPASTENG
EEECCCCCCCCCCCC		2.23-
451UbiquitinationASTENGDKITMQPAK
CCCCCCCCCEECCCE		41.28-
461PhosphorylationMQPAKIITIPATQLA
ECCCEEEEEEHHHHH		25.1219413330
468UbiquitinationTIPATQLAQCQLQTK
EEEHHHHHHCCCCCC		9.78-
479PhosphorylationLQTKSNLTGSGSINI
CCCCCCCCCCCCEEE		33.2922210691
489PhosphorylationGSINIVGTPLAVRAL
CCEEECCCCEEEEEC		12.3025159151
494MethylationVGTPLAVRALTPVSI
CCCCEEEEECCCEEE		20.4824129315
497O-linked_GlycosylationPLAVRALTPVSIAHG
CEEEEECCCEEECCC		22.2130059200
497PhosphorylationPLAVRALTPVSIAHG
CEEEEECCCEEECCC		22.2125159151
500O-linked_GlycosylationVRALTPVSIAHGTPV
EEECCCEEECCCCCE		18.4330059200
500PhosphorylationVRALTPVSIAHGTPV
EEECCCEEECCCCCE		18.4328450419
505O-linked_GlycosylationPVSIAHGTPVMRLSM
CEEECCCCCEEEEEC		11.6630059200
505PhosphorylationPVSIAHGTPVMRLSM
CEEECCCCCEEEEEC		11.6622199227
509MethylationAHGTPVMRLSMPTQQ
CCCCCEEEEECCCCC		24.68-
509PhosphorylationAHGTPVMRLSMPTQQ
CCCCCEEEEECCCCC		24.6819413330
511PhosphorylationGTPVMRLSMPTQQAS
CCCEEEEECCCCCCC		16.6122199227
514PhosphorylationVMRLSMPTQQASGQT
EEEEECCCCCCCCCC		25.3530576142
518PhosphorylationSMPTQQASGQTPPRV
ECCCCCCCCCCCCCE		27.3930266825
521PhosphorylationTQQASGQTPPRVISA
CCCCCCCCCCCEEEE		38.4930266825
527PhosphorylationQTPPRVISAVIKGPE
CCCCCEEEEEEECHH		17.3927251275
531AcetylationRVISAVIKGPEVKSE
CEEEEEEECHHHCCH		62.9125953088
531UbiquitinationRVISAVIKGPEVKSE
CEEEEEEECHHHCCH		62.91-
536SumoylationVIKGPEVKSEAVAKK
EEECHHHCCHHHHHH		40.70-
536SumoylationVIKGPEVKSEAVAKK
EEECHHHCCHHHHHH		40.7025218447
549SumoylationKKQEHDVKTLQLVEE
HHCCCCCEEEEEEEE		49.96-
557UbiquitinationTLQLVEEKPADGNKT
EEEEEEECCCCCCCE		31.81-
564O-linked_GlycosylationKPADGNKTVTHVVVV
CCCCCCCEEEEEEEE		34.3430059200
566O-linked_GlycosylationADGNKTVTHVVVVSA
CCCCCEEEEEEEEEC		17.7430059200
572O-linked_GlycosylationVTHVVVVSAPSAIAL
EEEEEEEECCCCEEC		23.8930059200
575O-linked_GlycosylationVVVVSAPSAIALPVT
EEEEECCCCEECCEE		31.8330059200
582O-linked_GlycosylationSAIALPVTMKTEGLV
CCEECCEEEECCCCE		15.8330059200
582PhosphorylationSAIALPVTMKTEGLV
CCEECCEEEECCCCE		15.83-
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 ELF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELF2_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 ELF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZBT32_HUMANZBTB32physical
20211142
A4_HUMANAPPphysical
21832049
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 ELF2_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-191, 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 THR-182; SER-185; SER-191;THR-426; THR-429; SER-430 AND THR-521, 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 SER-363 AND SER-372, ANDMASS 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-191, AND MASSSPECTROMETRY.

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