dbPTM

ELAV4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ELAV4_HUMAN
UniProt AC	P26378
Protein Name	ELAV-like protein 4
Gene Name	ELAVL4
Organism	Homo sapiens (Human).
Sequence Length	380
Subcellular Localization
Protein Description	May play a role in neuron-specific RNA processing. Protects CDKN1A mRNA from decay by binding to its 3'-UTR (By similarity). Binds to AU-rich sequences (AREs) of target mRNAs, including VEGF and FOS mRNA..
Protein Sequence	MVMIISTMEPQVSNGPTSNTSNGPSSNNRNCPSPMQTGATTDDSKTNLIVNYLPQNMTQEEFRSLFGSIGEIESCKLVRDKITGQSLGYGFVNYIDPKDAEKAINTLNGLRLQTKTIKVSYARPSSASIRDANLYVSGLPKTMTQKELEQLFSQYGRIITSRILVDQVTGVSRGVGFIRFDKRIEAEEAIKGLNGQKPSGATEPITVKFANNPSQKSSQALLSQLYQSPNRRYPGPLHHQAQRFRLDNLLNMAYGVKRLMSGPVPPSACPPRFSPITIDGMTSLVGMNIPGHTGTGWCIFVYNLSPDSDESVLWQLFGPFGAVNNVKVIRDFNTNKCKGFGFVTMTNYDEAAMAIASLNGYRLGDRVLQVSFKTNKAHKS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MVMIISTMEPQVS --CEEEEEECCCCCC	15.69	18669648
7	Phosphorylation	-MVMIISTMEPQVSN -CEEEEEECCCCCCC	18.36	-
11	Phosphorylation	IISTMEPQVSNGPTS EEEECCCCCCCCCCC	37.65	20068231
12	Phosphorylation	ISTMEPQVSNGPTSN EEECCCCCCCCCCCC	7.60	20068231
13 (in isoform 4)	Phosphorylation	-	30.71	22210691
17	Phosphorylation	PQVSNGPTSNTSNGP CCCCCCCCCCCCCCC	35.69	20068231
18	Phosphorylation	QVSNGPTSNTSNGPS CCCCCCCCCCCCCCC	41.04	18669648
18	Phosphorylation	QVSNGPTSNTSNGPS CCCCCCCCCCCCCCC	41.04	20068231
20 (in isoform 4)	Phosphorylation	-	24.28	22210691
21	Phosphorylation	NGPTSNTSNGPSSNN CCCCCCCCCCCCCCC	44.00	18669648
21 (in isoform 4)	Phosphorylation	-	44.00	22210691
22	Phosphorylation	GPTSNTSNGPSSNNR CCCCCCCCCCCCCCC	65.44	20068231
23	Phosphorylation	PTSNTSNGPSSNNRN CCCCCCCCCCCCCCC	24.20	20068231
25	Phosphorylation	SNTSNGPSSNNRNCP CCCCCCCCCCCCCCC	47.28	20068231
25	Phosphorylation	SNTSNGPSSNNRNCP CCCCCCCCCCCCCCC	47.28	18669648
26	Phosphorylation	NTSNGPSSNNRNCPS CCCCCCCCCCCCCCC	41.06	20068231
26	Phosphorylation	NTSNGPSSNNRNCPS CCCCCCCCCCCCCCC	41.06	20068231
30	Phosphorylation	GPSSNNRNCPSPMQT CCCCCCCCCCCCCCC	44.14	20068231
31	Phosphorylation	PSSNNRNCPSPMQTG CCCCCCCCCCCCCCC	2.97	20068231
33	Phosphorylation	SNNRNCPSPMQTGAT CCCCCCCCCCCCCCC	34.89	28450419
37	Phosphorylation	NCPSPMQTGATTDDS CCCCCCCCCCCCCCC	23.64	22210691
38	Phosphorylation	CPSPMQTGATTDDSK CCCCCCCCCCCCCCC	12.20	-
40	Phosphorylation	SPMQTGATTDDSKTN CCCCCCCCCCCCCCC	31.91	27732954
41	Phosphorylation	PMQTGATTDDSKTNL CCCCCCCCCCCCCCE	36.96	27732954
52	Phosphorylation	KTNLIVNYLPQNMTQ CCCEEEECCCCCCCH	14.63	22210691
64	Phosphorylation	MTQEEFRSLFGSIGE CCHHHHHHHHCCCCC	33.11	22210691
69	Phosphorylation	FRSLFGSIGEIESCK HHHHHCCCCCHHHCE	6.17	27251275
81 (in isoform 2)	Ubiquitination	-	31.44	21890473
81	Ubiquitination	SCKLVRDKITGQSLG HCEEECCCCCCCCCC	31.44	-
81 (in isoform 4)	Ubiquitination	-	31.44	21890473
81 (in isoform 1)	Ubiquitination	-	31.44	21890473
86	Ubiquitination	RDKITGQSLGYGFVN CCCCCCCCCCCEECE	25.71	21890473
98 (in isoform 3)	Ubiquitination	-	66.86	21890473
102 (in isoform 1)	Ubiquitination	-	57.18	21890473
102 (in isoform 2)	Ubiquitination	-	57.18	21890473
102 (in isoform 4)	Ubiquitination	-	57.18	21890473
102	Ubiquitination	IDPKDAEKAINTLNG CCHHHHHHHHHHHHC	57.18	-
106	Phosphorylation	DAEKAINTLNGLRLQ HHHHHHHHHHCCEEE	18.58	-
107	Ubiquitination	AEKAINTLNGLRLQT HHHHHHHHHCCEEEE	4.07	21890473
118	Ubiquitination	RLQTKTIKVSYARPS EEEEEEEEEEEECCC	30.29	-
118	Malonylation	RLQTKTIKVSYARPS EEEEEEEEEEEECCC	30.29	26320211
119 (in isoform 3)	Ubiquitination	-	4.71	21890473
120	Phosphorylation	QTKTIKVSYARPSSA EEEEEEEEEECCCCC	14.20	24117733
121	Phosphorylation	TKTIKVSYARPSSAS EEEEEEEEECCCCCC	15.04	-
125	Phosphorylation	KVSYARPSSASIRDA EEEEECCCCCCCCCC	32.74	24117733
126	Phosphorylation	VSYARPSSASIRDAN EEEECCCCCCCCCCC	28.81	24117733
128	Phosphorylation	YARPSSASIRDANLY EECCCCCCCCCCCEE	21.80	24117733
142	Phosphorylation	YVSGLPKTMTQKELE EECCCCCCCCHHHHH	24.42	30631047
144	Phosphorylation	SGLPKTMTQKELEQL CCCCCCCCHHHHHHH	41.54	30622161
146 (in isoform 2)	Ubiquitination	-	55.91	-
153	Phosphorylation	KELEQLFSQYGRIIT HHHHHHHHHHHHHHH	30.96	30622161
155	Phosphorylation	LEQLFSQYGRIITSR HHHHHHHHHHHHHHH	13.74	30622161
160	Phosphorylation	SQYGRIITSRILVDQ HHHHHHHHHHHHHHH	15.02	24719451
161	Phosphorylation	QYGRIITSRILVDQV HHHHHHHHHHHHHHH	13.60	24719451
178	Phosphorylation	VSRGVGFIRFDKRIE CCCCCCEEEECCCCC	3.36	24719451
216 (in isoform 2)	Ubiquitination	-	57.31	-
217	Phosphorylation	ANNPSQKSSQALLSQ CCCCCHHHHHHHHHH	21.75	24043423
218	Phosphorylation	NNPSQKSSQALLSQL CCCCHHHHHHHHHHH	26.89	24043423
221	Ubiquitination	SQKSSQALLSQLYQS CHHHHHHHHHHHHCC	3.52	-
223	Phosphorylation	KSSQALLSQLYQSPN HHHHHHHHHHHCCCC	20.99	24076635
226	Phosphorylation	QALLSQLYQSPNRRY HHHHHHHHCCCCCCC	10.17	25884760
228	Phosphorylation	LLSQLYQSPNRRYPG HHHHHHCCCCCCCCC	15.58	22496350
233	Phosphorylation	YQSPNRRYPGPLHHQ HCCCCCCCCCCCCHH	14.87	24719451
243	Methylation	PLHHQAQRFRLDNLL CCCHHHHHHHHHHHH	22.97	16508003
248	Methylation	AQRFRLDNLLNMAYG HHHHHHHHHHHHHHH	51.52	16508003
250	Phosphorylation	RFRLDNLLNMAYGVK HHHHHHHHHHHHHHH	5.30	24719451
254	Phosphorylation	DNLLNMAYGVKRLMS HHHHHHHHHHHHHHC	16.22	24719451
257 (in isoform 2)	Ubiquitination	-	35.14	-
264	Phosphorylation	KRLMSGPVPPSACPP HHHHCCCCCCCCCCC	14.37	27251275
271	Phosphorylation	VPPSACPPRFSPITI CCCCCCCCCCCCEEE	50.24	24719451
336	Acetylation	IRDFNTNKCKGFGFV EEECCCCCCCCEEEE	34.97	25953088
336	Ubiquitination	IRDFNTNKCKGFGFV EEECCCCCCCCEEEE	34.97	-
344	Phosphorylation	CKGFGFVTMTNYDEA CCCEEEEEECCHHHH	18.93	-
357	Phosphorylation	EAAMAIASLNGYRLG HHHHHHHHHCCCCCC	19.09	-
359 (in isoform 2)	Ubiquitination	-	42.85	-
378	Ubiquitination	SFKTNKAHKS----- EEECCCCCCC-----	32.28	-

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
Oops, there are no upstream regulatory protein records of ELAV4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
248	R	Methylation		16508003
Methylation at Arg-248 by CARM1 weakens protective binding to the 3'UTR of CDKN1A mRNA and down-regulates CDKN1A protein expression, thereby maintaining cells in a proliferative state (By similarity).

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 ELAV4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EWS_HUMAN	EWSR1	physical	16189514
NXF1_HUMAN	NXF1	physical	15358174
P20L1_HUMAN	PHF20L1	physical	21988832
HNRH1_MOUSE	Hnrnph1	physical	15086518
SFPQ_MOUSE	Sfpq	physical	15086518
G3BP1_MOUSE	G3bp1	physical	15086518
IF2B1_MOUSE	Igf2bp1	physical	15086518
IF2B1_HUMAN	IGF2BP1	physical	15086518

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 ELAV4_HUMAN

Related Literatures of Post-Translational Modification

Methylation
Reference	PubMed
"CARM1 regulates proliferation of PC12 cells by methylating HuD."; Fujiwara T., Mori Y., Chu D.L., Koyama Y., Miyata S., Tanaka H.,Yachi K., Kubo T., Yoshikawa H., Tohyama M.; Mol. Cell. Biol. 26:2273-2285(2006). Cited for: METHYLATION AT ARG-243.	16508003 [Abstract]

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