ELAV1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ELAV1_MOUSE
• UniProt AC: P70372
• Protein Name: ELAV-like protein 1
• Gene Name: Elavl1
• Organism: Mus musculus (Mouse).
• Sequence Length: 326
• Subcellular Localization: Cytoplasm . Nucleus . Translocates into the cytoplasm following phosphorylation by MAPKAPK2. Likewise, phosphorylation by PRKCD promotes translocation from the nucleus into the cytoplasm, where it is associated with free and cytoskeleton-bound polyso
• Protein Description: RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability. Involved in embryonic stem cells (ESCs) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESCs differentiation. [PubMed: 24394384 Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs. Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, binds to a core element of 27 nucleotides that contain AUUUA, AUUUUA, and AUUUUUA motifs. Binds preferentially to the 5'-UUUU[AG]UUU-3' motif in vitro (By similarity With ZNF385A, binds the 3'-UTR of p53/TP53 mRNA to control their nuclear export induced by CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the CDKN2A anti-proliferative activity. May also bind with ZNF385A the CCNB1 mRNA]
• Protein Sequence: MSNGYEDHMAEDCRDDIGRTNLIVNYLPQNMTQEELRSLFSSIGEVESAKLIRDKVAGHSLGYGFVNYVTAKDAERAISTLNGLRLQSKTIKVSYARPSSEVIKDANLYISGLPRTMTQKDVEDMFSRFGRIINSRVLVDQTTGLSRGVAFIRFDKRSEAEEAITSFNGHKPPGSSEPITVKFAANPNQNKNMALLSQLYHSPARRFGGPVHHQAQRFRFSPMGVDHMSGISGVNVPGNASSGWCIFIYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYEEAAMAIASLNGYRLGDKILQVSFKTNKSHK

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
2	Phosphorylation	------MSNGYEDHM ------CCCCCHHHC	38.67	23527152
2	Acetylation	------MSNGYEDHM ------CCCCCHHHC	38.67	-
5	Phosphorylation	---MSNGYEDHMAED ---CCCCCHHHCHHH	23.57	26643407
32	Phosphorylation	NYLPQNMTQEELRSL HCCCCCCCHHHHHHH	40.14	30635358
50	Ubiquitination	IGEVESAKLIRDKVA HHHHHHHHHHHHHHH	54.44	22790023
55	Acetylation	SAKLIRDKVAGHSLG HHHHHHHHHHCCCCC	24.92	23806337
55	Ubiquitination	SAKLIRDKVAGHSLG HHHHHHHHHHCCCCC	24.92	22790023
63	Phosphorylation	VAGHSLGYGFVNYVT HHCCCCCCCCEEEEE	16.81	29514104
72	Ubiquitination	FVNYVTAKDAERAIS CEEEEEHHHHHHHHH	48.37	22790023
79	Phosphorylation	KDAERAISTLNGLRL HHHHHHHHHHHCCEE	26.34	-
80	Phosphorylation	DAERAISTLNGLRLQ HHHHHHHHHHCCEEC	20.37	-
89	Ubiquitination	NGLRLQSKTIKVSYA HCCEECCEEEEEEEE	41.11	27667366
92	Ubiquitination	RLQSKTIKVSYARPS EECCEEEEEEEECCC	30.29	22790023
94	Phosphorylation	QSKTIKVSYARPSSE CCEEEEEEEECCCCH	14.20	22817900
95	Phosphorylation	SKTIKVSYARPSSEV CEEEEEEEECCCCHH	15.04	22817900
99	Phosphorylation	KVSYARPSSEVIKDA EEEEECCCCHHHCCC	33.31	29176673
100	Phosphorylation	VSYARPSSEVIKDAN EEEECCCCHHHCCCC	38.27	29176673
104	Ubiquitination	RPSSEVIKDANLYIS CCCCHHHCCCCEEEC	56.83	22790023
111	Phosphorylation	KDANLYISGLPRTMT CCCCEEECCCCCCCC	22.26	25338131
120	Ubiquitination	LPRTMTQKDVEDMFS CCCCCCHHHHHHHHH	55.35	22790023
127	Phosphorylation	KDVEDMFSRFGRIIN HHHHHHHHHHHHHHC	21.77	22324799
146	Phosphorylation	VDQTTGLSRGVAFIR EECCCCCCCCEEEEE	28.47	19854140
158	Phosphorylation	FIRFDKRSEAEEAIT EEEEECCHHHHHHHH	47.07	-
166	Phosphorylation	EAEEAITSFNGHKPP HHHHHHHHCCCCCCC	15.59	25890499
191	Acetylation	AANPNQNKNMALLSQ ECCCCCCCCHHHHHH	38.03	23806337
191	Ubiquitination	AANPNQNKNMALLSQ ECCCCCCCCHHHHHH	38.03	22790023
197	Phosphorylation	NKNMALLSQLYHSPA CCCHHHHHHHHCCHH	20.99	21149613
200	Phosphorylation	MALLSQLYHSPARRF HHHHHHHHCCHHHHC	7.82	21082442
202	Phosphorylation	LLSQLYHSPARRFGG HHHHHHCCHHHHCCC	13.49	26824392
206	Dimethylation	LYHSPARRFGGPVHH HHCCHHHHCCCCCCH	36.35	-
206	Methylation	LYHSPARRFGGPVHH HHCCHHHHCCCCCCH	36.35	24129315
217	Methylation	PVHHQAQRFRFSPMG CCCHHHHCCCCCCCC	27.94	24129315
217	Dimethylation	PVHHQAQRFRFSPMG CCCHHHHCCCCCCCC	27.94	-
219	Methylation	HHQAQRFRFSPMGVD CHHHHCCCCCCCCCC	33.07	18967409
221	Phosphorylation	QAQRFRFSPMGVDHM HHHCCCCCCCCCCCC	15.10	-
283	Ubiquitination	IRDFNTNKCKGFGFV EEECCCCCCCCEEEE	34.97	-
318	Phosphorylation	GDKILQVSFKTNKSH CCEEEEEEEECCCCC	14.20	19854140
320	Ubiquitination	KILQVSFKTNKSHK- EEEEEEEECCCCCC-	43.62	22790023
323	Ubiquitination	QVSFKTNKSHK---- EEEEECCCCCC----	60.20	-

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

Oops, there are no upstream regulatory protein records of ELAV1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
217	R	Methylation	Methylated at Arg-217 by CARM1 in T-cells in response to LPS challenge.	12237300

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ELAV1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ELAV2_HUMAN	ELAVL2	physical	26496610
RENT1_HUMAN	UPF1	physical	26496610
RU17_HUMAN	SNRNP70	physical	26496610
UBP24_HUMAN	USP24	physical	26496610
RM27_HUMAN	MRPL27	physical	26496610
CARL1_HUMAN	LRRC16A	physical	26496610
SPTCS_HUMAN	SPG11	physical	26496610
CE128_HUMAN	CEP128	physical	26496610

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Methylation

"Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizingprotein, by CARM1. Coactivator-associated argininemethyltransferase.";
Li H., Park S., Kilburn B., Jelinek M.A., Henschen-Edman A.,Aswad D.W., Stallcup M.R., Laird-Offringa I.A.;
J. Biol. Chem. 277:44623-44630(2002).
Cited for: METHYLATION AT ARG-217.
PubMed: 12237300