ELK4_HUMAN - dbPTM
ELK4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELK4_HUMAN
UniProt AC P28324
Protein Name ETS domain-containing protein Elk-4
Gene Name ELK4
Organism Homo sapiens (Human).
Sequence Length 431
Subcellular Localization Nucleus.
Protein Description Involved in both transcriptional activation and repression. Interaction with SIRT7 leads to recruitment and stabilization of SIRT7 at promoters, followed by deacetylation of histone H3 at 'Lys-18' (H3K18Ac) and subsequent transcription repression. Forms a ternary complex with the serum response factor (SRF). Requires DNA-bound SRF for ternary complex formation and makes extensive DNA contacts to the 5'side of SRF, but does not bind DNA autonomously..
Protein Sequence MDSAITLWQFLLQLLQKPQNKHMICWTSNDGQFKLLQAEEVARLWGIRKNKPNMNYDKLSRALRYYYVKNIIKKVNGQKFVYKFVSYPEILNMDPMTVGRIEGDCESLNFSEVSSSSKDVENGGKDKPPQPGAKTSSRNDYIHSGLYSSFTLNSLNSSNVKLFKLIKTENPAEKLAEKKSPQEPTPSVIKFVTTPSKKPPVEPVAATISIGPSISPSSEETIQALETLVSPKLPSLEAPTSASNVMTAFATTPPISSIPPLQEPPRTPSPPLSSHPDIDTDIDSVASQPMELPENLSLEPKDQDSVLLEKDKVNNSSRSKKPKGLELAPTLVITSSDPSPLGILSPSLPTASLTPAFFSQTPIILTPSPLLSSIHFWSTLSPVAPLSPARLQGANTLFQFPSVLNSHGPFTLSGLDGPSTPGPFSPDLQKT
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
56PhosphorylationKNKPNMNYDKLSRAL
CCCCCCCHHHHHHHH
12.0420049867
107PhosphorylationRIEGDCESLNFSEVS
EEECCHHHCCHHHHC
34.64-
111PhosphorylationDCESLNFSEVSSSSK
CHHHCCHHHHCCCCC
35.6927251275
114PhosphorylationSLNFSEVSSSSKDVE
HCCHHHHCCCCCCHH
22.0527251275
125AcetylationKDVENGGKDKPPQPG
CCHHCCCCCCCCCCC
65.0726051181
135PhosphorylationPPQPGAKTSSRNDYI
CCCCCCCCCCCCCCC
31.25-
137PhosphorylationQPGAKTSSRNDYIHS
CCCCCCCCCCCCCCC
40.09-
164SumoylationSSNVKLFKLIKTENP
CCCEEEEEEEECCCH
60.79-
164SumoylationSSNVKLFKLIKTENP
CCCEEEEEEEECCCH
60.79-
167SumoylationVKLFKLIKTENPAEK
EEEEEEEECCCHHHH
61.29-
167SumoylationVKLFKLIKTENPAEK
EEEEEEEECCCHHHH
61.2928112733
178UbiquitinationPAEKLAEKKSPQEPT
HHHHHHHCCCCCCCC
53.60-
180PhosphorylationEKLAEKKSPQEPTPS
HHHHHCCCCCCCCCC
42.7730266825
185PhosphorylationKKSPQEPTPSVIKFV
CCCCCCCCCCCEEEE
27.6923403867
187PhosphorylationSPQEPTPSVIKFVTT
CCCCCCCCCEEEEEC
38.6623403867
193PhosphorylationPSVIKFVTTPSKKPP
CCCEEEEECCCCCCC
35.8027251275
194PhosphorylationSVIKFVTTPSKKPPV
CCEEEEECCCCCCCC
21.9129396449
207PhosphorylationPVEPVAATISIGPSI
CCCCEEEEEEECCCC
12.9127080861
209PhosphorylationEPVAATISIGPSISP
CCEEEEEEECCCCCC
19.6927080861
213PhosphorylationATISIGPSISPSSEE
EEEEECCCCCCCHHH
30.4130108239
215PhosphorylationISIGPSISPSSEETI
EEECCCCCCCHHHHH
24.0625159151
217PhosphorylationIGPSISPSSEETIQA
ECCCCCCCHHHHHHH
43.5226657352
218PhosphorylationGPSISPSSEETIQAL
CCCCCCCHHHHHHHH
42.7230108239
221PhosphorylationISPSSEETIQALETL
CCCCHHHHHHHHHHH
17.8430108239
227PhosphorylationETIQALETLVSPKLP
HHHHHHHHHHCCCCC
33.0527080861
230PhosphorylationQALETLVSPKLPSLE
HHHHHHHCCCCCCCC
21.3025159151
235O-linked_GlycosylationLVSPKLPSLEAPTSA
HHCCCCCCCCCCCCC
49.64OGP
305PhosphorylationLEPKDQDSVLLEKDK
CCCCCCCCEEEEECC
14.7225159151
310UbiquitinationQDSVLLEKDKVNNSS
CCCEEEEECCCCCCC
63.92-
316PhosphorylationEKDKVNNSSRSKKPK
EECCCCCCCCCCCCC
23.1721712546
320AcetylationVNNSSRSKKPKGLEL
CCCCCCCCCCCCCCC
72.497926731
378PhosphorylationLSSIHFWSTLSPVAP
HHHHHHHHCCCCCCC
20.6626074081
379PhosphorylationSSIHFWSTLSPVAPL
HHHHHHHCCCCCCCC
23.1126074081
381PhosphorylationIHFWSTLSPVAPLSP
HHHHHCCCCCCCCCH
19.8826074081
385 (in isoform 2)Phosphorylation-33.3427174698
386 (in isoform 2)Phosphorylation-7.4527174698
387PhosphorylationLSPVAPLSPARLQGA
CCCCCCCCHHHHCCC
18.5626074081
419PhosphorylationLSGLDGPSTPGPFSP
ECCCCCCCCCCCCCC
53.41-
420PhosphorylationSGLDGPSTPGPFSPD
CCCCCCCCCCCCCCC
35.08-
425PhosphorylationPSTPGPFSPDLQKT-
CCCCCCCCCCCCCC-
22.1926074081

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
194TPhosphorylationKinaseCDK2P24941
PSP
361TPhosphorylationKinaseMAPK8P45983
GPS
366TPhosphorylationKinaseMAPK8P45983
GPS
381SPhosphorylationKinaseERK1P27361
PSP
381SPhosphorylationKinaseMAPK8P45983
GPS
381SPhosphorylationKinaseP38AQ16539
PSP
387SPhosphorylationKinaseCDK2P24941
PSP
387SPhosphorylationKinaseERK1P27361
PSP
387SPhosphorylationKinaseMAPK8P45983
GPS
387SPhosphorylationKinaseP38AQ16539
PSP
420TPhosphorylationKinaseMAPK8P45983
GPS
425SPhosphorylationKinaseMAPK8P45983
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELK4_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 ELK4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRF_HUMANSRFphysical
11406578
SIR7_HUMANSIRT7physical
28655758

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 ELK4_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP