ELAV3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ELAV3_HUMAN
• UniProt AC: Q14576
• Protein Name: ELAV-like protein 3
• Gene Name: ELAVL3
• Organism: Homo sapiens (Human).
• Sequence Length: 367
• Protein Description: Binds to AU-rich sequences (AREs) of target mRNAs, including VEGF mRNA. May also bind poly-A tracts via RRM 3 (By similarity). May be involved in neuronal differentiation and maintenance..
• Protein Sequence: MVTQILGAMESQVGGGPAGPALPNGPLLGTNGATDDSKTNLIVNYLPQNMTQDEFKSLFGSIGDIESCKLVRDKITGQSLGYGFVNYSDPNDADKAINTLNGLKLQTKTIKVSYARPSSASIRDANLYVSGLPKTMSQKEMEQLFSQYGRIITSRILVDQVTGVSRGVGFIRFDKRIEAEEAIKGLNGQKPLGAAEPITVKFANNPSQKTGQALLTHLYQSSARRYAGPLHHQTQRFRLDNLLNMAYGVKSPLSLIARFSPIAIDGMSGLAGVGLSGGAAGAGWCIFVYNLSPEADESVLWQLFGPFGAVTNVKVIRDFTTNKCKGFGFVTMTNYDEAAMAIASLNGYRLGERVLQVSFKTSKQHKA

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
68	Ubiquitination	SIGDIESCKLVRDKI CCCCHHHCEEEEECC	2.28	22817900
69	Ubiquitination	IGDIESCKLVRDKIT CCCHHHCEEEEECCC	60.33	22817900
73	Ubiquitination	ESCKLVRDKITGQSL HHCEEEEECCCCCCC	38.95	22817900
74	Ubiquitination	SCKLVRDKITGQSLG HCEEEEECCCCCCCE	31.44	22817900
74 (in isoform 2)	Ubiquitination	-	31.44	-
104	Ubiquitination	INTLNGLKLQTKTIK HHHHHCCEEEEEEEE	39.69	32142685
108	Ubiquitination	NGLKLQTKTIKVSYA HCCEEEEEEEEEEEE	34.98	32142685
110	Ubiquitination	LKLQTKTIKVSYARP CEEEEEEEEEEEECC	4.40	21890473
111	Ubiquitination	KLQTKTIKVSYARPS EEEEEEEEEEEECCC	30.29	21890473
113	Phosphorylation	QTKTIKVSYARPSSA EEEEEEEEEECCCCC	14.20	24117733
114	Phosphorylation	TKTIKVSYARPSSAS EEEEEEEEECCCCCC	15.04	32142685
118	Phosphorylation	KVSYARPSSASIRDA EEEEECCCCCCCCCC	32.74	24117733
119	Phosphorylation	VSYARPSSASIRDAN EEEECCCCCCCCCCC	28.81	24117733
121	Phosphorylation	YARPSSASIRDANLY EECCCCCCCCCCCEE	21.80	24117733
133	Ubiquitination	NLYVSGLPKTMSQKE CEEECCCCCCCCHHH	33.33	23503661
134	Ubiquitination	LYVSGLPKTMSQKEM EEECCCCCCCCHHHH	63.00	23503661
137	Phosphorylation	SGLPKTMSQKEMEQL CCCCCCCCHHHHHHH	43.25	-
138	Ubiquitination	GLPKTMSQKEMEQLF CCCCCCCHHHHHHHH	34.60	23503661
139 (in isoform 2)	Ubiquitination	-	52.28	-
139	Ubiquitination	LPKTMSQKEMEQLFS CCCCCCHHHHHHHHH	52.28	23503661
153	Phosphorylation	SQYGRIITSRILVDQ HHHHHHHHHHHHHHH	15.02	24719451
154	Phosphorylation	QYGRIITSRILVDQV HHHHHHHHHHHHHHH	13.60	24719451
208	Ubiquitination	KFANNPSQKTGQALL EECCCCCHHHHHHHH	48.89	23503661
209 (in isoform 2)	Ubiquitination	-	59.98	-
209	Ubiquitination	FANNPSQKTGQALLT ECCCCCHHHHHHHHH	59.98	32142685
210	Phosphorylation	ANNPSQKTGQALLTH CCCCCHHHHHHHHHH	27.21	29978859
216	Phosphorylation	KTGQALLTHLYQSSA HHHHHHHHHHHHHHH	15.64	29978859
219	Phosphorylation	QALLTHLYQSSARRY HHHHHHHHHHHHHHH	9.95	29978859
221	Phosphorylation	LLTHLYQSSARRYAG HHHHHHHHHHHHHCC	16.65	29978859
222	Phosphorylation	LTHLYQSSARRYAGP HHHHHHHHHHHHCCC	15.40	29978859
226	Phosphorylation	YQSSARRYAGPLHHQ HHHHHHHHCCCCCCC	15.45	-
234	Phosphorylation	AGPLHHQTQRFRLDN CCCCCCCCHHHHHHH	19.84	-
251	Phosphorylation	NMAYGVKSPLSLIAR HHHHCCCCHHHHHHH	28.77	27732954
254	Phosphorylation	YGVKSPLSLIARFSP HCCCCHHHHHHHCCC	22.55	27732954
331	Phosphorylation	CKGFGFVTMTNYDEA CCCEEEEEEECHHHH	18.93	-
344	Phosphorylation	EAAMAIASLNGYRLG HHHHHHHHHCCCCCC	19.09	-
358	Phosphorylation	GERVLQVSFKTSKQH CCEEEEEEEECCCCC	14.20	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ELAV3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ELAV3_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ELAV3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EWS_HUMAN	EWSR1	physical	16189514
PEX14_HUMAN	PEX14	physical	26344197

Drug and Disease Associations

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