ELK1_HUMAN - dbPTM
ELK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELK1_HUMAN
UniProt AC P19419
Protein Name ETS domain-containing protein Elk-1
Gene Name ELK1
Organism Homo sapiens (Human).
Sequence Length 428
Subcellular Localization Nucleus.
Protein Description Transcription factor that binds to purine-rich DNA sequences. Forms a ternary complex with SRF and the ETS and SRF motifs of the serum response element (SRE) on the promoter region of immediate early genes such as FOS and IER2. Induces target gene transcription upon JNK-signaling pathway stimulation (By similarity)..
Protein Sequence MDPSVTLWQFLLQLLREQGNGHIISWTSRDGGEFKLVDAEEVARLWGLRKNKTNMNYDKLSRALRYYYDKNIIRKVSGQKFVYKFVSYPEVAGCSTEDCPPQPEVSVTSTMPNVAPAAIHAAPGDTVSGKPGTPKGAGMAGPGGLARSSRNEYMRSGLYSTFTIQSLQPQPPPHPRPAVVLPSAAPAGAAAPPSGSRSTSPSPLEACLEAEEAGLPLQVILTPPEAPNLKSEELNVEPGLGRALPPEVKVEGPKEELEVAGERGFVPETTKAEPEVPPQEGVPARLPAVVMDTAGQAGGHAASSPEISQPQKGRKPRDLELPLSPSLLGGPGPERTPGSGSGSGLQAPGPALTPSLLPTHTLTPVLLTPSSLPPSIHFWSTLSPIAPRSPAKLSFQFPSSGSAQVHIPSISVDGLSTPVVLSPGPQKP
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
57PhosphorylationKNKTNMNYDKLSRAL
CCCCCCCHHHHHHHH		12.0425884760
59UbiquitinationKTNMNYDKLSRALRY
CCCCCHHHHHHHHHH		37.69-
106PhosphorylationCPPQPEVSVTSTMPN
CCCCCCEEEECCCCC		20.3028348404
126PhosphorylationIHAAPGDTVSGKPGT
EEECCCCCCCCCCCC		23.6122210691
128PhosphorylationAAPGDTVSGKPGTPK
ECCCCCCCCCCCCCC		43.1028348404
133PhosphorylationTVSGKPGTPKGAGMA
CCCCCCCCCCCCCCC		30.2928348404
153PhosphorylationARSSRNEYMRSGLYS
HCCCCCHHHHHCCCE		11.0229978859
156PhosphorylationSRNEYMRSGLYSTFT
CCCHHHHHCCCEEEE		19.3429978859
159PhosphorylationEYMRSGLYSTFTIQS
HHHHHCCCEEEEEEE		14.8029978859
160PhosphorylationYMRSGLYSTFTIQSL
HHHHCCCEEEEEEEC		23.3029978859
161PhosphorylationMRSGLYSTFTIQSLQ
HHHCCCEEEEEEECC		15.9629978859
163PhosphorylationSGLYSTFTIQSLQPQ
HCCCEEEEEEECCCC		20.4229978859
166PhosphorylationYSTFTIQSLQPQPPP
CEEEEEEECCCCCCC		25.7329978859
183PhosphorylationRPAVVLPSAAPAGAA
CCEEECCCCCCCCCC		32.6623312004
194PhosphorylationAGAAAPPSGSRSTSP
CCCCCCCCCCCCCCC		48.6330266825
196PhosphorylationAAAPPSGSRSTSPSP
CCCCCCCCCCCCCCH		27.6530266825
198PhosphorylationAPPSGSRSTSPSPLE
CCCCCCCCCCCCHHH		34.6323663014
199PhosphorylationPPSGSRSTSPSPLEA
CCCCCCCCCCCHHHH		43.4723663014
200PhosphorylationPSGSRSTSPSPLEAC
CCCCCCCCCCHHHHH		25.3223663014
202PhosphorylationGSRSTSPSPLEACLE
CCCCCCCCHHHHHHH		41.7123663014
222PhosphorylationLPLQVILTPPEAPNL
CCEEEEECCCCCCCC		26.1826074081
230SumoylationPPEAPNLKSEELNVE
CCCCCCCCCHHCCCC		63.5615210726
230SumoylationPPEAPNLKSEELNVE
CCCCCCCCCHHCCCC		63.56-
249SumoylationRALPPEVKVEGPKEE
CCCCCCCEEECCHHH		32.67-
249SumoylationRALPPEVKVEGPKEE
CCCCCCCEEECCHHH		32.6712887893
254SumoylationEVKVEGPKEELEVAG
CCEEECCHHHHHHCC		74.75-
254SumoylationEVKVEGPKEELEVAG
CCEEECCHHHHHHCC		74.7515210726
270O-linked_GlycosylationRGFVPETTKAEPEVP
CCCCCCCCCCCCCCC		26.9628657654
293PhosphorylationLPAVVMDTAGQAGGH
CCEEEEECCCCCCCC		18.0029978859
303PhosphorylationQAGGHAASSPEISQP
CCCCCCCCCCCCCCC		47.4025159151
304PhosphorylationAGGHAASSPEISQPQ
CCCCCCCCCCCCCCC		23.0929116813
308PhosphorylationAASSPEISQPQKGRK
CCCCCCCCCCCCCCC		33.8629978859
312AcetylationPEISQPQKGRKPRDL
CCCCCCCCCCCCCCC		68.3325953088
324PhosphorylationRDLELPLSPSLLGGP
CCCCCCCCHHHCCCC		15.5430266825
326PhosphorylationLELPLSPSLLGGPGP
CCCCCCHHHCCCCCC		32.6130266825
336PhosphorylationGGPGPERTPGSGSGS
CCCCCCCCCCCCCCC		30.277889942
353PhosphorylationQAPGPALTPSLLPTH
CCCCCCCCCHHCCCC		16.9710637505
363PhosphorylationLLPTHTLTPVLLTPS
HCCCCCCCCEEECCC		16.7110637505
368PhosphorylationTLTPVLLTPSSLPPS
CCCCEEECCCCCCCC		19.5710637505
383PhosphorylationIHFWSTLSPIAPRSP
EEECEECCCCCCCCC		17.8520675591
389PhosphorylationLSPIAPRSPAKLSFQ
CCCCCCCCCCEEEEE		28.3110637505
411PhosphorylationQVHIPSISVDGLSTP
EEECCEEEECCCCCC		20.6329523821
416PhosphorylationSISVDGLSTPVVLSP
EEEECCCCCCEEECC		35.8729523821
417PhosphorylationISVDGLSTPVVLSPG
EEECCCCCCEEECCC		25.7410637505
422PhosphorylationLSTPVVLSPGPQKP-
CCCCEEECCCCCCC-		19.0525159151
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
324SPhosphorylationKinaseMAPK1P28482
Uniprot
336TPhosphorylationKinaseMAPK1P28482
Uniprot
353TPhosphorylationKinaseMAPK1P28482
Uniprot
363TPhosphorylationKinaseMAPK1P28482
Uniprot
368TPhosphorylationKinaseMAPK1P28482
Uniprot
383SPhosphorylationKinaseERK2P28482
PSP
383SPhosphorylationKinaseMAPK14Q16539
GPS
383SPhosphorylationKinaseMAPK8P45983
Uniprot
383SPhosphorylationKinaseMAPK3Q63844
GPS
383SPhosphorylationKinaseMK03P27361
PhosphoELM
383SPhosphorylationKinaseERK2P63085
PSP
383SPhosphorylationKinaseRPS6KA5O75582
GPS
389SPhosphorylationKinaseMAPK3P27361
GPS
389SPhosphorylationKinaseMAPK14Q16539
GPS
389SPhosphorylationKinaseMAPK1P28482
Uniprot
417TPhosphorylationKinaseMAPK1P28482
Uniprot
417TPhosphorylationKinasePRP4O43172
PhosphoELM
417TPhosphorylationKinasePRPF4BQ13523
GPS
422SPhosphorylationKinaseMAPK1P28482
Uniprot
-KUbiquitinationE3 ubiquitin ligaseFBXO25Q8TCJ0
PMID:23940030
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
383SPhosphorylation

7889942
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 ELK1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EP300_HUMANEP300genetic
12514134
EP300_HUMANEP300physical
12514134
FLI1_HUMANFLI1physical
9010223
SRF_HUMANSRFphysical
9010223
EWS_HUMANEWSR1physical
9010223
MK01_HUMANMAPK1physical
8586671
EMX1_HUMANEMX1physical
20211142
HXB13_HUMANHOXB13physical
20211142
KLF4_HUMANKLF4physical
18768922
SIN3A_MOUSESin3aphysical
11283259
HDAC1_HUMANHDAC1physical
11283259
PADI4_HUMANPADI4physical
21655091
MD2L2_HUMANMAD2L2physical
17296730
SYUA_HUMANSNCAphysical
11279280
A4_HUMANAPPphysical
21832049
UBC9_HUMANUBE2Iphysical
17036045
FBX25_HUMANFBXO25physical
23940030
ELK1_HUMANELK1physical
23940030
STR3N_HUMANSTARD3NLphysical
21988832
UBC9_HUMANUBE2Iphysical
23395904
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 ELK1_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-324 AND SER-422, ANDMASS SPECTROMETRY.
"ERK activation induces phosphorylation of Elk-1 at multiple S/T-Pmotifs to high stoichiometry.";
Cruzalegui F.H., Cano E., Treisman R.;
Oncogene 18:7948-7957(1999).
Cited for: PHOSPHORYLATION AT THR-353; THR-363; THR-368; SER-383; SER-389 ANDTHR-417.
"ERK phosphorylation potentiates Elk-1-mediated ternary complexformation and transactivation.";
Gille H., Kortenjann M., Thomae O., Moomaw C., Slaughter C.,Cobb M.H., Shaw P.E.;
EMBO J. 14:951-962(1995).
Cited for: PROTEIN SEQUENCE OF 318-331; 336-364 AND 380-408, PHOSPHORYLATION ATSER-324; THR-336; SER-383; SER-389 AND SER-422, AND MUTAGENESIS OFSER-324; THR-336; THR-353; THR-363; THR-368; SER-383; SER-389; THR-417AND SER-422.
Sumoylation
ReferencePubMed
"SUMOylation regulates nucleo-cytoplasmic shuttling of Elk-1.";
Salinas S., Briancon-Marjollet A., Bossis G., Lopez M.-A.,Piechaczyk M., Jariel-Encontre I., Debant A., Hipskind R.A.;
J. Cell Biol. 165:767-773(2004).
Cited for: SUMOYLATION AT LYS-230; LYS-249 AND LYS-254, AND MUTAGENESIS OFLYS-230; LYS-249 AND LYS-254.
"Dynamic interplay of the SUMO and ERK pathways in regulating Elk-1transcriptional activity.";
Yang S.-H., Jaffray E., Hay R.T., Sharrocks A.D.;
Mol. Cell 12:63-74(2003).
Cited for: SUMOYLATION AT LYS-249, AND MUTAGENESIS OF LYS-230 AND LYS-249.

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