ELF4_HUMAN - dbPTM
ELF4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELF4_HUMAN
UniProt AC Q99607
Protein Name ETS-related transcription factor Elf-4
Gene Name ELF4 {ECO:0000312|EMBL:CAI42882.1}
Organism Homo sapiens (Human).
Sequence Length 663
Subcellular Localization Nucleus, PML body . Accumulation into PML nuclear bodies is mediated by PML.
Protein Description Transcriptional activator that binds to DNA sequences containing the consensus 5'-WGGA-3'. Transactivates promoters of the hematopoietic growth factor genes CSF2, IL3, IL8, and of the bovine lysozyme gene. Acts synergistically with RUNX1 to transactivate the IL3 promoter (By similarity). Also transactivates the PRF1 promoter in natural killer (NK) cells. Plays a role in the development and function of NK and NK T-cells and in innate immunity. Controls the proliferation and homing of CD8+ T-cells via the Kruppel-like factors KLF4 and KLF2 (By similarity). Controls cell senescence in a p53-dependent manner. Can also promote cellular transformation through inhibition of the p16 pathway..
Protein Sequence MAITLQPSDLIFEFASNGMDDDIHQLEDPSVFPAVIVEQVPYPDLLHLYSGLELDDVHNGIITDGTLCMTQDQILEGSFLLTDDNEATSHTMSTAEVLLNMESPSDILDEKQIFSTSEMLPDSDPAPAVTLPNYLFPASEPDALNRAGDTSDQEGHSLEEKASREESAKKTGKSKKRIRKTKGNRSTSPVTDPSIPIRKKSKDGKGSTIYLWEFLLALLQDRNTCPKYIKWTQREKGIFKLVDSKAVSKLWGKQKNKPDMNYETMGRALRYYYQRGILAKVEGQRLVYQFKEMPKDLVVIEDEDESSEATAAPPQASTASVASASTTRRTSSRVSSRSAPQGKGSSSWEKPKIQHVGLQPSASLELGPSLDEEIPTTSTMLVSPAEGQVKLTKAVSASSVPSNIHLGVAPVGSGSALTLQTIPLTTVLTNGPPASTTAPTQLVLQSVPAASTFKDTFTLQASFPLNASFQDSQVAAPGAPLILSGLPQLLAGANRPTNPAPPTVTGAGPAGPSSQPPGTVIAAFIRTSGTTAAPRVKEGPLRSSSYVQGMVTGAPMEGLLVPEETLRELLRDQAHLQPLPTQVVSRGSHNPSLLGNQTLSPPSRPTVGLTPVAELELSSGSGSLLMAEPSVTTSGSLLTRSPTPAPFSPFNPTSLIKMEPHDI
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
111SumoylationPSDILDEKQIFSTSE
HHHHCCHHHCCCCCC		48.65-
150PhosphorylationALNRAGDTSDQEGHS
HHHCCCCCCCHHCCC		33.0322167270
151PhosphorylationLNRAGDTSDQEGHSL
HHCCCCCCCHHCCCH		41.8722167270
157PhosphorylationTSDQEGHSLEEKASR
CCCHHCCCHHHHHHH		48.6223927012
159UbiquitinationDQEGHSLEEKASREE
CHHCCCHHHHHHHHH		61.5422817900
163PhosphorylationHSLEEKASREESAKK
CCHHHHHHHHHHHHH		51.8223312004
163UbiquitinationHSLEEKASREESAKK
CCHHHHHHHHHHHHH		51.8221890473
167O-linked_GlycosylationEKASREESAKKTGKS
HHHHHHHHHHHHCCC		40.4130379171
168UbiquitinationKASREESAKKTGKSK
HHHHHHHHHHHCCCH		22.2022817900
172UbiquitinationEESAKKTGKSKKRIR
HHHHHHHCCCHHHHH		40.9121890473
177UbiquitinationKTGKSKKRIRKTKGN
HHCCCHHHHHCCCCC		37.3722817900
186PhosphorylationRKTKGNRSTSPVTDP
HCCCCCCCCCCCCCC		36.9223401153
187PhosphorylationKTKGNRSTSPVTDPS
CCCCCCCCCCCCCCC		33.5429255136
188PhosphorylationTKGNRSTSPVTDPSI
CCCCCCCCCCCCCCC		20.7229255136
191PhosphorylationNRSTSPVTDPSIPIR
CCCCCCCCCCCCCCC		45.6430266825
194PhosphorylationTSPVTDPSIPIRKKS
CCCCCCCCCCCCCCC		43.7523927012
203UbiquitinationPIRKKSKDGKGSTIY
CCCCCCCCCCCCHHH		71.7422505724
212UbiquitinationKGSTIYLWEFLLALL
CCCHHHHHHHHHHHH		4.1922505724
214UbiquitinationSTIYLWEFLLALLQD
CHHHHHHHHHHHHHC		4.6021890473
218UbiquitinationLWEFLLALLQDRNTC
HHHHHHHHHHCCCCC		4.4422817900
223UbiquitinationLALLQDRNTCPKYIK
HHHHHCCCCCHHHCC		55.0821890473
227UbiquitinationQDRNTCPKYIKWTQR
HCCCCCHHHCCCHHH		62.8522817900
230UbiquitinationNTCPKYIKWTQREKG
CCCHHHCCCHHHHCC		40.89-
232PhosphorylationCPKYIKWTQREKGIF
CHHHCCCHHHHCCCE		16.85-
236UbiquitinationIKWTQREKGIFKLVD
CCCHHHHCCCEEECC		60.5422817900
240UbiquitinationQREKGIFKLVDSKAV
HHHCCCEEECCHHHH		45.7621890473
245UbiquitinationIFKLVDSKAVSKLWG
CEEECCHHHHHHHHC		48.6322817900
249UbiquitinationVDSKAVSKLWGKQKN
CCHHHHHHHHCCCCC		41.48-
257UbiquitinationLWGKQKNKPDMNYET
HHCCCCCCCCCCHHH		49.80-
262PhosphorylationKNKPDMNYETMGRAL
CCCCCCCHHHHHHHH		13.21-
270MethylationETMGRALRYYYQRGI
HHHHHHHHHHHHCCC		19.20-
271PhosphorylationTMGRALRYYYQRGIL
HHHHHHHHHHHCCCC		13.8428270605
272PhosphorylationMGRALRYYYQRGILA
HHHHHHHHHHCCCCC		6.1628270605
273PhosphorylationGRALRYYYQRGILAK
HHHHHHHHHCCCCCE		5.2528270605
280SumoylationYQRGILAKVEGQRLV
HHCCCCCEEECEEEE		37.06-
280SumoylationYQRGILAKVEGQRLV
HHCCCCCEEECEEEE		37.06-
280UbiquitinationYQRGILAKVEGQRLV
HHCCCCCEEECEEEE		37.0622505724
291UbiquitinationQRLVYQFKEMPKDLV
EEEEEEEECCCCCEE		37.2621890473
295UbiquitinationYQFKEMPKDLVVIED
EEEECCCCCEEEEEC		63.4822817900
330O-linked_GlycosylationSASTTRRTSSRVSSR
CCCCCCCCCCCCCCC		27.9730379171
330PhosphorylationSASTTRRTSSRVSSR
CCCCCCCCCCCCCCC		27.9729083192
331PhosphorylationASTTRRTSSRVSSRS
CCCCCCCCCCCCCCC		17.8429083192
332PhosphorylationSTTRRTSSRVSSRSA
CCCCCCCCCCCCCCC		35.7729083192
335PhosphorylationRRTSSRVSSRSAPQG
CCCCCCCCCCCCCCC		20.9429083192
336PhosphorylationRTSSRVSSRSAPQGK
CCCCCCCCCCCCCCC		27.6529083192
338PhosphorylationSSRVSSRSAPQGKGS
CCCCCCCCCCCCCCC		46.3729083192
361PhosphorylationQHVGLQPSASLELGP
EEEECCCCCEEECCC		19.9628348404
363PhosphorylationVGLQPSASLELGPSL
EECCCCCEEECCCCC		27.0628348404
369PhosphorylationASLELGPSLDEEIPT
CEEECCCCCCCCCCC		46.80-
513PhosphorylationGAGPAGPSSQPPGTV
CCCCCCCCCCCCCCE		40.4622210691
527PhosphorylationVIAAFIRTSGTTAAP
EEEEEEECCCCCCCC		27.0520068231
528PhosphorylationIAAFIRTSGTTAAPR
EEEEEECCCCCCCCC		25.0520068231
530PhosphorylationAFIRTSGTTAAPRVK
EEEECCCCCCCCCCC		17.0220068231
531PhosphorylationFIRTSGTTAAPRVKE
EEECCCCCCCCCCCC		25.0920068231
537UbiquitinationTTAAPRVKEGPLRSS
CCCCCCCCCCCCCCC		59.23-
543PhosphorylationVKEGPLRSSSYVQGM
CCCCCCCCCCCCCCC		31.1728450419
544PhosphorylationKEGPLRSSSYVQGMV
CCCCCCCCCCCCCCC		21.1828450419
545PhosphorylationEGPLRSSSYVQGMVT
CCCCCCCCCCCCCCC		30.4826657352
546PhosphorylationGPLRSSSYVQGMVTG
CCCCCCCCCCCCCCC		9.9528450419
552PhosphorylationSYVQGMVTGAPMEGL
CCCCCCCCCCCCCCC		20.8027080861
636PhosphorylationPSVTTSGSLLTRSPT
CCEECCCCCCCCCCC		21.7024719451
641PhosphorylationSGSLLTRSPTPAPFS
CCCCCCCCCCCCCCC		28.0828731282
643PhosphorylationSLLTRSPTPAPFSPF
CCCCCCCCCCCCCCC		33.0721712546
648PhosphorylationSPTPAPFSPFNPTSL
CCCCCCCCCCCCCHH		27.7626055452
653PhosphorylationPFSPFNPTSLIKMEP
CCCCCCCCHHEECCC		36.9523403867
654PhosphorylationFSPFNPTSLIKMEPH
CCCCCCCHHEECCCC		29.3823403867
657SumoylationFNPTSLIKMEPHDI-
CCCCHHEECCCCCC-		42.37-
657SumoylationFNPTSLIKMEPHDI-
CCCCHHEECCCCCC-		42.37-
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
369SPhosphorylationKinaseHIPK2Q9H2X6
PSP
641SPhosphorylationKinaseMAPK8P45983
GPS
643TPhosphorylationKinaseCDK2P24941
PSP
648SPhosphorylationKinaseCDK2P24941
PSP
-KUbiquitinationE3 ubiquitin ligaseSKP2Q13309
PMID:16581786
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELF4_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 ELF4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PML_HUMANPMLphysical
14976184
SET_HUMANSETphysical
21988832
NPM_HUMANNPM1physical
23393136
MDM2_HUMANMDM2physical
25081543
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 ELF4_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-648, 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-187 AND SER-188, 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-151; THR-643 ANDSER-648, AND MASS SPECTROMETRY.

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