dbPTM

ELK3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ELK3_HUMAN
UniProt AC	P41970
Protein Name	ETS domain-containing protein Elk-3
Gene Name	ELK3
Organism	Homo sapiens (Human).
Sequence Length	407
Subcellular Localization	Nucleus.
Protein Description	May be a negative regulator of transcription, but can activate transcription when coexpressed with Ras, Src or Mos. Forms a ternary complex with the serum response factor and the ETS and SRF motifs of the Fos serum response element..
Protein Sequence	MESAITLWQFLLQLLLDQKHEHLICWTSNDGEFKLLKAEEVAKLWGLRKNKTNMNYDKLSRALRYYYDKNIIKKVIGQKFVYKFVSFPEILKMDPHAVEISRESLLLQDSDCKASPEGREAHKHGLAALRSTSRNEYIHSGLYSSFTINSLQNPPDAFKAIKTEKLEEPPEDSPPVEEVRTVIRFVTNKTDKHVTRPVVSLPSTSEAAAASAFLASSVSAKISSLMLPNAASISSASPFSSRSPSLSPNSPLPSEHRSLFLEAACHDSDSLEPLNLSSGSKTKSPSLPPKAKKPKGLEISAPPLVLSGTDIGSIALNSPALPSGSLTPAFFTAQTPNGLLLTPSPLLSSIHFWSSLSPVAPLSPARLQGPSTLFQFPTLLNGHMPVPIPSLDRAASPVLLSSNSQKS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MESAITLWQF -----CHHHHHHHHH	24.55	27732954
6	Phosphorylation	--MESAITLWQFLLQ --CHHHHHHHHHHHH	22.97	27732954
56	Phosphorylation	KNKTNMNYDKLSRAL CCCCCCCHHHHHHHH	12.04	-
58	Ubiquitination	KTNMNYDKLSRALRY CCCCCHHHHHHHHHH	37.69	-
83	Ubiquitination	IGQKFVYKFVSFPEI HCCCHHEEECCHHHH	33.71	-
92	Ubiquitination	VSFPEILKMDPHAVE CCHHHHHCCCHHHHH	47.09	21906983
92	Sumoylation	VSFPEILKMDPHAVE CCHHHHHCCCHHHHH	47.09	28112733
104	Phosphorylation	AVEISRESLLLQDSD HHHCCHHHHHCCCCC	24.17	23403867
110	Phosphorylation	ESLLLQDSDCKASPE HHHHCCCCCCCCCCC	31.76	30266825
113	Ubiquitination	LLQDSDCKASPEGRE HCCCCCCCCCCCHHH	57.81	-
115	Phosphorylation	QDSDCKASPEGREAH CCCCCCCCCCHHHHH	14.69	23401153
131	Phosphorylation	HGLAALRSTSRNEYI HHHHHHHCCCCCCCC	31.42	27251275
132	Phosphorylation	GLAALRSTSRNEYIH HHHHHHCCCCCCCCC	25.85	27251275
133	Phosphorylation	LAALRSTSRNEYIHS HHHHHCCCCCCCCCC	34.06	27251275
137	Phosphorylation	RSTSRNEYIHSGLYS HCCCCCCCCCCCCCC	13.90	29978859
140	Phosphorylation	SRNEYIHSGLYSSFT CCCCCCCCCCCCCCE	22.42	29978859
143	Phosphorylation	EYIHSGLYSSFTINS CCCCCCCCCCCEECC	13.04	29978859
144	Phosphorylation	YIHSGLYSSFTINSL CCCCCCCCCCEECCC	24.82	29978859
145	Phosphorylation	IHSGLYSSFTINSLQ CCCCCCCCCEECCCC	16.92	29978859
147	Phosphorylation	SGLYSSFTINSLQNP CCCCCCCEECCCCCC	22.61	29978859
150	Phosphorylation	YSSFTINSLQNPPDA CCCCEECCCCCCCHH	27.73	29978859
162	Sumoylation	PDAFKAIKTEKLEEP CHHHHHHHHHCCCCC	56.33	-
162	Sumoylation	PDAFKAIKTEKLEEP CHHHHHHHHHCCCCC	56.33	-
165	Sumoylation	FKAIKTEKLEEPPED HHHHHHHCCCCCCCC	67.44	28112733
165	Ubiquitination	FKAIKTEKLEEPPED HHHHHHHCCCCCCCC	67.44	-
173	Phosphorylation	LEEPPEDSPPVEEVR CCCCCCCCCCHHHHH	29.46	23401153
189	Acetylation	VIRFVTNKTDKHVTR HHHHHHCCCCCCCCC	49.05	18584403
195	O-linked_Glycosylation	NKTDKHVTRPVVSLP CCCCCCCCCCEECCC	29.04	29351928
200	O-linked_Glycosylation	HVTRPVVSLPSTSEA CCCCCEECCCCHHHH	34.49	29351928
203	O-linked_Glycosylation	RPVVSLPSTSEAAAA CCEECCCCHHHHHHH	50.27	29351928
204	O-linked_Glycosylation	PVVSLPSTSEAAAAS CEECCCCHHHHHHHH	28.75	29351928
205	O-linked_Glycosylation	VVSLPSTSEAAAASA EECCCCHHHHHHHHH	29.58	29351928
211	O-linked_Glycosylation	TSEAAAASAFLASSV HHHHHHHHHHHHHHH	18.15	29351928
240	Phosphorylation	ISSASPFSSRSPSLS CCCCCCCCCCCCCCC	28.38	24247654
243	Phosphorylation	ASPFSSRSPSLSPNS CCCCCCCCCCCCCCC	22.31	30266825
245	Phosphorylation	PFSSRSPSLSPNSPL CCCCCCCCCCCCCCC	42.60	30266825
247	Phosphorylation	SSRSPSLSPNSPLPS CCCCCCCCCCCCCCH	26.77	30266825
250	Phosphorylation	SPSLSPNSPLPSEHR CCCCCCCCCCCHHHH	31.06	30266825
254	Phosphorylation	SPNSPLPSEHRSLFL CCCCCCCHHHHHHHH	54.43	27732954
258	Phosphorylation	PLPSEHRSLFLEAAC CCCHHHHHHHHHHHC	25.94	27732954
268	Phosphorylation	LEAACHDSDSLEPLN HHHHCCCCCCCCCCC	12.87	27732954
270	Phosphorylation	AACHDSDSLEPLNLS HHCCCCCCCCCCCCC	38.29	27732954
282	Phosphorylation	NLSSGSKTKSPSLPP CCCCCCCCCCCCCCC	38.15	23403867
284	Phosphorylation	SSGSKTKSPSLPPKA CCCCCCCCCCCCCCC	25.59	26657352
286	Phosphorylation	GSKTKSPSLPPKAKK CCCCCCCCCCCCCCC	61.67	23403867
357	Phosphorylation	IHFWSSLSPVAPLSP HHHHHCCCCCCCCCH	21.19	11042694
363	Phosphorylation	LSPVAPLSPARLQGP CCCCCCCCHHHHCCC	18.56	11042694
396	Phosphorylation	PSLDRAASPVLLSSN CCCCCCCCCEEECCC	17.98	29255136
401	Phosphorylation	AASPVLLSSNSQKS- CCCCEEECCCCCCC-	24.26	30266825
402	Phosphorylation	ASPVLLSSNSQKS-- CCCEEECCCCCCC--	40.23	23403867
404	Phosphorylation	PVLLSSNSQKS---- CEEECCCCCCC----	40.72	23403867
407	Phosphorylation	LSSNSQKS------- ECCCCCCC-------	37.50	23403867

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
357	S	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS
357	S	Phosphorylation	Kinase	JNK_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ELK3_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 ELK3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
TFE2_HUMAN	TCF3	physical	8918463
A4_HUMAN	APP	physical	21832049

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 ELK3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396, AND MASSSPECTROMETRY.	19007248 [Abstract]
"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-245, AND MASSSPECTROMETRY.	15302935 [Abstract]