ELK1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ELK1_MOUSE
• UniProt AC: P41969
• Protein Name: ETS domain-containing protein Elk-1
• Gene Name: Elk1 {ECO:0000312|MGI:MGI:101833}
• Organism: Mus musculus (Mouse).
• Sequence Length: 429
• 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 (By similarity). Induces target gene transcription upon JNK-signaling pathway stimulation (By similarity)..
• Protein Sequence: MDPSVTLWQFLLQLLREQGNGHIISWTSRDGGEFKLVDAEEVARLWGLRKNKTNMNYDKLSRALRYYYDKNIIRKVSGQKFVYKFVSYPEVAGCSTEDCPPQPEVSVTSAIAMAPATVHAGPGDTATGKPGTPKGAGMTGQGGLARSSRNEYMRSGLYSTFTIQSLQPQPQPPIPPRPASVLPNTTPAGVPAPASGSRSTSPNPLEACLEAEEAGLPLQVILTPPEAPNQKSEELSLDPSFGHPQPPEVKVEGPKEELEAARAGGFSSEAVKAEPEVSASEGLLARLPAILTENTAQVCGLSTSTTEITQPQKGRKPRDLELPLSPSLLGGQGPERTPGSGTSSGLQAPGPALTPSLLPTHTLTPVLLTPSSLPPSIHFWSTLSPIAPRSPAKLSFQFPSSGSAQVHIPSISVDGLSTPVVLSPGPQKP

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
66	Phosphorylation	KLSRALRYYYDKNII HHHHHHHHHHHHCCH	13.76	-
67	Phosphorylation	LSRALRYYYDKNIIR HHHHHHHHHHHCCHH	9.96	-
195	Phosphorylation	AGVPAPASGSRSTSP CCCCCCCCCCCCCCC	35.92	29233185
197	Phosphorylation	VPAPASGSRSTSPNP CCCCCCCCCCCCCCH	22.14	29233185
201	Phosphorylation	ASGSRSTSPNPLEAC CCCCCCCCCCHHHHH	24.75	29899451
325	Phosphorylation	RDLELPLSPSLLGGQ CCCCCCCCHHHCCCC	15.54	29514104
327	Phosphorylation	LELPLSPSLLGGQGP CCCCCCHHHCCCCCC	32.61	28066266
337	Phosphorylation	GGQGPERTPGSGTSS CCCCCCCCCCCCCCC	30.27	22817900
354	Phosphorylation	QAPGPALTPSLLPTH CCCCCCCCCHHCCCC	16.97	-
364	Phosphorylation	LLPTHTLTPVLLTPS HCCCCCCCCEEECCC	16.71	-
369	Phosphorylation	TLTPVLLTPSSLPPS CCCCEEECCCCCCCC	19.57	-
384	Phosphorylation	IHFWSTLSPIAPRSP EEECEECCCCCCCCC	17.85	15102857
390	Phosphorylation	LSPIAPRSPAKLSFQ CCCCCCCCCCEEEEE	28.31	22817900
418	Phosphorylation	ISVDGLSTPVVLSPG EEECCCCCCEEECCC	25.74	-
423	Phosphorylation	LSTPVVLSPGPQKP- CCCCEEECCCCCCC-	19.05	22817900

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
325	S	Phosphorylation	Kinase	MAPK3	Q63844	GPS
325	S	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
337	T	Phosphorylation	Kinase	MAPK3	Q63844	GPS
337	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
337	T	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
354	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
354	T	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
364	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
364	T	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
369	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
369	T	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
384	S	Phosphorylation	Kinase	MAPK8	Q91Y86	Uniprot
384	S	Phosphorylation	Kinase	MAPK3	Q63844	GPS
384	S	Phosphorylation	Kinase	MK01	P63085	PhosphoELM
384	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
390	S	Phosphorylation	Kinase	MK01	P63085	PhosphoELM
390	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
390	S	Phosphorylation	Kinase	MAPK3	Q63844	GPS
418	T	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
418	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
423	S	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
423	S	Phosphorylation	Kinase	MAPK3	Q63844	GPS
423	S	Phosphorylation	Kinase	MAPK1	P28482	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ELK1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ELK1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ELK1_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.