ELF1_HUMAN - dbPTM
ELF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELF1_HUMAN
UniProt AC P32519
Protein Name ETS-related transcription factor Elf-1
Gene Name ELF1
Organism Homo sapiens (Human).
Sequence Length 619
Subcellular Localization Nucleus.
Protein Description Transcription factor that activates the LYN and BLK promoters. Appears to be required for the T-cell-receptor-mediated trans activation of HIV-2 gene expression. Binds specifically to two purine-rich motifs in the HIV-2 enhancer..
Protein Sequence MAAVVQQNDLVFEFASNVMEDERQLGDPAIFPAVIVEHVPGADILNSYAGLACVEEPNDMITESSLDVAEEEIIDDDDDDITLTVEASCHDGDETIETIEAAEALLNMDSPGPMLDEKRINNNIFSSPEDDMVVAPVTHVSVTLDGIPEVMETQQVQEKYADSPGASSPEQPKRKKGRKTKPPRPDSPATTPNISVKKKNKDGKGNTIYLWEFLLALLQDKATCPKYIKWTQREKGIFKLVDSKAVSRLWGKHKNKPDMNYETMGRALRYYYQRGILAKVEGQRLVYQFKEMPKDLIYINDEDPSSSIESSDPSLSSSATSNRNQTSRSRVSSSPGVKGGATTVLKPGNSKAAKPKDPVEVAQPSEVLRTVQPTQSPYPTQLFRTVHVVQPVQAVPEGEAARTSTMQDETLNSSVQSIRTIQAPTQVPVVVSPRNQQLHTVTLQTVPLTTVIASTDPSAGTGSQKFILQAIPSSQPMTVLKENVMLQSQKAGSPPSIVLGPAQVQQVLTSNVQTICNGTVSVASSPSFSATAPVVTFSPRSSQLVAHPPGTVITSVIKTQETKTLTQEVEKKESEDHLKENTEKTEQQPQPYVMVVSSSNGFTSQVAMKQNELLEPNSF
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
110PhosphorylationEALLNMDSPGPMLDE
HHHHCCCCCCCCCCH		22.4626074081
126PhosphorylationRINNNIFSSPEDDMV
HCCCCCCCCCCCCEE		40.9825627689
127PhosphorylationINNNIFSSPEDDMVV
CCCCCCCCCCCCEEE		22.8925627689
160PhosphorylationTQQVQEKYADSPGAS
HHHHHHHHCCCCCCC		18.1923927012
163PhosphorylationVQEKYADSPGASSPE
HHHHHCCCCCCCCCC		19.6429255136
167PhosphorylationYADSPGASSPEQPKR
HCCCCCCCCCCCCCC		52.9529255136
168PhosphorylationADSPGASSPEQPKRK
CCCCCCCCCCCCCCC		31.7429255136
180PhosphorylationKRKKGRKTKPPRPDS
CCCCCCCCCCCCCCC		47.6323927012
187PhosphorylationTKPPRPDSPATTPNI
CCCCCCCCCCCCCCE		21.0825159151
190PhosphorylationPRPDSPATTPNISVK
CCCCCCCCCCCEEEE		46.2825159151
191PhosphorylationRPDSPATTPNISVKK
CCCCCCCCCCEEEEE		19.2223401153
195PhosphorylationPATTPNISVKKKNKD
CCCCCCEEEEEECCC		34.2323401153
197UbiquitinationTTPNISVKKKNKDGK
CCCCEEEEEECCCCC		51.76-
226UbiquitinationQDKATCPKYIKWTQR
HCCCCCHHHCCCHHH		62.85-
229UbiquitinationATCPKYIKWTQREKG
CCCHHHCCCHHHCCC		40.89-
231PhosphorylationCPKYIKWTQREKGIF
CHHHCCCHHHCCCEE		16.8522817900
239UbiquitinationQREKGIFKLVDSKAV
HHCCCEEEEECHHHH		45.7621890473
239UbiquitinationQREKGIFKLVDSKAV
HHCCCEEEEECHHHH		45.7621890473
244UbiquitinationIFKLVDSKAVSRLWG
EEEEECHHHHHHHHC		48.63-
256UbiquitinationLWGKHKNKPDMNYET
HHCCCCCCCCCCHHH		47.39-
261PhosphorylationKNKPDMNYETMGRAL
CCCCCCCHHHHHHHH		13.21-
269MethylationETMGRALRYYYQRGI
HHHHHHHHHHHHCCC		19.20-
270PhosphorylationTMGRALRYYYQRGIL
HHHHHHHHHHHCCCC		13.8428270605
271PhosphorylationMGRALRYYYQRGILA
HHHHHHHHHHCCCCC		6.1628270605
272PhosphorylationGRALRYYYQRGILAK
HHHHHHHHHCCCCCE		5.2528270605
279SumoylationYQRGILAKVEGQRLV
HHCCCCCEEECCEEE		37.06-
279SumoylationYQRGILAKVEGQRLV
HHCCCCCEEECCEEE		37.06-
279UbiquitinationYQRGILAKVEGQRLV
HHCCCCCEEECCEEE		37.06-
290UbiquitinationQRLVYQFKEMPKDLI
CEEEEEEECCCCCEE		37.2621890473
290UbiquitinationQRLVYQFKEMPKDLI
CEEEEEEECCCCCEE		37.2621890473
305PhosphorylationYINDEDPSSSIESSD
EECCCCCCCCCCCCC		49.3827690223
306PhosphorylationINDEDPSSSIESSDP
ECCCCCCCCCCCCCC		40.5030576142
307PhosphorylationNDEDPSSSIESSDPS
CCCCCCCCCCCCCCC		34.4130576142
310PhosphorylationDPSSSIESSDPSLSS
CCCCCCCCCCCCCCC		38.0727690223
311PhosphorylationPSSSIESSDPSLSSS
CCCCCCCCCCCCCCC		40.5327690223
317PhosphorylationSSDPSLSSSATSNRN
CCCCCCCCCCCCCCC		29.3225627689
318PhosphorylationSDPSLSSSATSNRNQ
CCCCCCCCCCCCCCC		31.9925627689
329PhosphorylationNRNQTSRSRVSSSPG
CCCCCCCCHHCCCCC		36.4830576142
332PhosphorylationQTSRSRVSSSPGVKG
CCCCCHHCCCCCCCC		24.8026055452
333PhosphorylationTSRSRVSSSPGVKGG
CCCCHHCCCCCCCCC		37.3823401153
334PhosphorylationSRSRVSSSPGVKGGA
CCCHHCCCCCCCCCC		20.4026055452
342PhosphorylationPGVKGGATTVLKPGN
CCCCCCCEEEECCCC		22.2528122231
343PhosphorylationGVKGGATTVLKPGNS
CCCCCCEEEECCCCC		24.2528122231
346AcetylationGGATTVLKPGNSKAA
CCCEEEECCCCCCCC		46.6823749302
350PhosphorylationTVLKPGNSKAAKPKD
EEECCCCCCCCCCCC		29.5923312004
351AcetylationVLKPGNSKAAKPKDP
EECCCCCCCCCCCCC		57.2625953088
354AcetylationPGNSKAAKPKDPVEV
CCCCCCCCCCCCCCC		58.4225953088
354UbiquitinationPGNSKAAKPKDPVEV
CCCCCCCCCCCCCCC		58.42-
370PhosphorylationQPSEVLRTVQPTQSP
CHHHHHHCCCCCCCC		21.2328450419
374PhosphorylationVLRTVQPTQSPYPTQ
HHHCCCCCCCCCCCE		25.2928450419
376PhosphorylationRTVQPTQSPYPTQLF
HCCCCCCCCCCCEEE		28.9525159151
378PhosphorylationVQPTQSPYPTQLFRT
CCCCCCCCCCEEEEE		24.9428450419
380PhosphorylationPTQSPYPTQLFRTVH
CCCCCCCCEEEEEEE		31.8728450419
403O-linked_GlycosylationPEGEAARTSTMQDET
CCCCCCCCCCCCHHH		24.6730059200
404O-linked_GlycosylationEGEAARTSTMQDETL
CCCCCCCCCCCHHHH		19.1430059200
405O-linked_GlycosylationGEAARTSTMQDETLN
CCCCCCCCCCHHHHH		20.4530059200
406SulfoxidationEAARTSTMQDETLNS
CCCCCCCCCHHHHHH		4.7821406390
413O-linked_GlycosylationMQDETLNSSVQSIRT
CCHHHHHHHHHHHEE		34.6930059200
413PhosphorylationMQDETLNSSVQSIRT
CCHHHHHHHHHHHEE		34.6927251275
414PhosphorylationQDETLNSSVQSIRTI
CHHHHHHHHHHHEEE		24.0928555341
420PhosphorylationSSVQSIRTIQAPTQV
HHHHHHEEEECCCCC		18.7729396449
425PhosphorylationIRTIQAPTQVPVVVS
HEEEECCCCCCEEEC		45.2626657352
432PhosphorylationTQVPVVVSPRNQQLH
CCCCEEECCCCCEEE		13.4125159151
440PhosphorylationPRNQQLHTVTLQTVP
CCCCEEEEEEEEECC		24.6324043423
442PhosphorylationNQQLHTVTLQTVPLT
CCEEEEEEEEECCCE		17.8224043423
445PhosphorylationLHTVTLQTVPLTTVI
EEEEEEEECCCEEEE		27.4924043423
449PhosphorylationTLQTVPLTTVIASTD
EEEECCCEEEEEECC		16.9724043423
450PhosphorylationLQTVPLTTVIASTDP
EEECCCEEEEEECCC		20.0024043423
454PhosphorylationPLTTVIASTDPSAGT
CCEEEEEECCCCCCC		23.4024043423
455PhosphorylationLTTVIASTDPSAGTG
CEEEEEECCCCCCCC		42.7924043423
458PhosphorylationVIASTDPSAGTGSQK
EEEECCCCCCCCCCE		41.9824043423
461PhosphorylationSTDPSAGTGSQKFIL
ECCCCCCCCCCEEEE		33.1224043423
463PhosphorylationDPSAGTGSQKFILQA
CCCCCCCCCEEEEEE		29.9922817901
473O-linked_GlycosylationFILQAIPSSQPMTVL
EEEEECCCCCCCEEE		35.1830059200
473PhosphorylationFILQAIPSSQPMTVL
EEEEECCCCCCCEEE		35.1827251275
474O-linked_GlycosylationILQAIPSSQPMTVLK
EEEECCCCCCCEEEE		32.7130059200
474PhosphorylationILQAIPSSQPMTVLK
EEEECCCCCCCEEEE		32.7117525332
478O-linked_GlycosylationIPSSQPMTVLKENVM
CCCCCCCEEEEHHHH		29.3930059200
478PhosphorylationIPSSQPMTVLKENVM
CCCCCCCEEEEHHHH		29.3927251275
481UbiquitinationSQPMTVLKENVMLQS
CCCCEEEEHHHHHCC		42.79-
488O-linked_GlycosylationKENVMLQSQKAGSPP
EHHHHHCCCCCCCCC		29.6830059200
493O-linked_GlycosylationLQSQKAGSPPSIVLG
HCCCCCCCCCEEEEC		38.2030059200
509O-linked_GlycosylationAQVQQVLTSNVQTIC
HHHHHHHHCCCCEEE		21.2830059200
510O-linked_GlycosylationQVQQVLTSNVQTICN
HHHHHHHCCCCEEEC		30.7330059200
514O-linked_GlycosylationVLTSNVQTICNGTVS
HHHCCCCEEECCEEE		24.1830059200
519O-linked_GlycosylationVQTICNGTVSVASSP
CCEEECCEEEECCCC		8.8030059200
521O-linked_GlycosylationTICNGTVSVASSPSF
EEECCEEEECCCCCC		16.2930059200
525O-linked_GlycosylationGTVSVASSPSFSATA
CEEEECCCCCCCCCC		18.1530059200
527O-linked_GlycosylationVSVASSPSFSATAPV
EEECCCCCCCCCCCE		33.5130059200
529O-linked_GlycosylationVASSPSFSATAPVVT
ECCCCCCCCCCCEEE		29.1030059200
531O-linked_GlycosylationSSPSFSATAPVVTFS
CCCCCCCCCCEEEEC		30.2330059200
536O-linked_GlycosylationSATAPVVTFSPRSSQ
CCCCCEEEECCCHHH		20.7330059200
536PhosphorylationSATAPVVTFSPRSSQ
CCCCCEEEECCCHHH		20.7326074081
538PhosphorylationTAPVVTFSPRSSQLV
CCCEEEECCCHHHEE		15.2726074081
541PhosphorylationVVTFSPRSSQLVAHP
EEEECCCHHHEEECC		26.3126074081
542PhosphorylationVTFSPRSSQLVAHPP
EEECCCHHHEEECCC		28.9026074081
547 (in isoform 2)Ubiquitination-22.9320972266
554PhosphorylationHPPGTVITSVIKTQE
CCCCCEEEEEEECHH		16.7722210691
555PhosphorylationPPGTVITSVIKTQET
CCCCEEEEEEECHHC		15.6622210691
558AcetylationTVITSVIKTQETKTL
CEEEEEEECHHCHHH		41.8425953088
559PhosphorylationVITSVIKTQETKTLT
EEEEEEECHHCHHHH		22.10-
562PhosphorylationSVIKTQETKTLTQEV
EEEECHHCHHHHHHH		21.3622210691
564PhosphorylationIKTQETKTLTQEVEK
EECHHCHHHHHHHHH		42.3222210691
566PhosphorylationTQETKTLTQEVEKKE
CHHCHHHHHHHHHHH		28.1017525332
571UbiquitinationTLTQEVEKKESEDHL
HHHHHHHHHHCHHHH		68.002097226
618PhosphorylationNELLEPNSF------
CCCCCCCCC------		42.9430576142
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
-KUbiquitinationE3 ubiquitin ligasePJA1Q8NG27
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELF1_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 ELF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NFKB1_HUMANNFKB1physical
7862168
REL_HUMANRELphysical
7862168
NFKB1_HUMANNFKB1physical
9094628
HXC13_HUMANHOXC13physical
18692240
HPBP1_HUMANHSPBP1physical
28514442
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 ELF1_HUMAN

loading...

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 TYR-160; SER-163; SER-167;SER-187 AND SER-432, AND MASS SPECTROMETRY.
"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-167, 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 TYR-160; SER-163 ANDSER-168, 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-163; SER-168 ANDSER-432, 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-432, 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-474 AND THR-566, ANDMASS 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 SER-432, 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-168, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory