CELF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CELF2_HUMAN
• UniProt AC: O95319
• Protein Name: CUGBP Elav-like family member 2
• Gene Name: CELF2
• Organism: Homo sapiens (Human).
• Sequence Length: 508
• Subcellular Localization: Nucleus. Cytoplasm. Accumulates in the cytoplasm after ionizing radiation (By similarity). Colocalizes with APOBEC1 and A1CF. RNA-binding activity is detected in both nuclear and cytoplasmic compartments..
• Protein Description: RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of TNNT2 in embryonic, but not adult, skeletal muscle. Activates TNNT2 exon 5 inclusion by antagonizing the repressive effect of PTB. Acts as both an activator and repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs. Promotes inclusion of exonS 21 and exclusion of exon 5 of the NMDA receptor R1 pre-mRNA. Involved in the apoB RNA editing activity. Increases COX2 mRNA stability and inhibits COX2 mRNA translation in epithelial cells after radiation injury (By similarity). Modulates the cellular apoptosis program by regulating COX2-mediated prostaglandin E2 (PGE2) expression (By similarity). Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK. Binds to the muscle-specific splicing enhancer (MSE) intronic sites flanking the TNNT2 alternative exon 5. Binds preferentially to UG-rich sequences, in particular UG repeat and UGUU motifs. Binds to apoB mRNA, specifically to AU-rich sequences located immediatly upstream of the edited cytidine. Binds AU-rich sequences in the 3'-UTR of COX2 mRNA (By similarity). Binds to an intronic RNA element responsible for the silencing of exon 21 splicing (By similarity). Binds to (CUG)n repeats (By similarity). May be a specific regulator of miRNA biogenesis. Binds to primary microRNA pri-MIR140 and, with CELF1, negatively regulates the processing to mature miRNA. [PubMed: 28431233]
• Protein Sequence: MRCPKSAVTMRNEELLLSNGTANKMNGALDHSDQPDPDAIKMFVGQIPRSWSEKELKELFEPYGAVYQINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNIKTLPGMHHPIQMKPADSEKSNAVEDRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFSTRAMAQNAIKAMHQSQTMEGCSSPIVVKFADTQKDKEQRRLQQQLAQQMQQLNTATWGNLTGLGGLTPQYLALLQQATSSSNLGAFSGIQQMAGMNALQLQNLATLAAAAAAAQTSATSTNANPLSTTSSALGALTSPVAASTPNSTAGAAMNSLTSLGTLQGLAGATVGLNNINALAGMAALNGGLGATGLTNGTAGTMDALTQAYSGIQQYAAAALPTLYSQSLLQQQSAAGSQKEGPEGANLFIYHLPQEFGDQDILQMFMPFGNVISAKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQAMNGFQIGMKRLKVQLKRSKNDSKPY

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
32	Phosphorylation	MNGALDHSDQPDPDA CCCCCCCCCCCCHHH	37.29	28450419
52	Phosphorylation	GQIPRSWSEKELKEL CCCCCCCCHHHHHHH	39.78	23401153
54	Ubiquitination	IPRSWSEKELKELFE CCCCCCHHHHHHHHH	63.93	-
57	Ubiquitination	SWSEKELKELFEPYG CCCHHHHHHHHHCCC	54.16	-
58 (in isoform 4)	Phosphorylation	-	71.91	25147952
59 (in isoform 2)	Ubiquitination	-	5.87	21890473
59 (in isoform 5)	Ubiquitination	-	5.87	21890473
63	Phosphorylation	LKELFEPYGAVYQIN HHHHHHCCCEEEEEE	15.54	-
67	Phosphorylation	FEPYGAVYQINVLRD HHCCCEEEEEEEECC	11.80	-
76	Phosphorylation	INVLRDRSQNPPQSK EEEECCCCCCCCCCC	38.30	-
78 (in isoform 3)	Ubiquitination	-	52.01	21890473
83 (in isoform 1)	Ubiquitination	-	51.20	21890473
83	Acetylation	SQNPPQSKGCCFVTF CCCCCCCCCEEEEEE	51.20	26051181
83	Ubiquitination	SQNPPQSKGCCFVTF CCCCCCCCCEEEEEE	51.20	21906983
90 (in isoform 4)	Ubiquitination	-	5.01	21890473
94	Ubiquitination	FVTFYTRKAALEAQN EEEEECHHHHHHHHH	30.16	-
107	Ubiquitination	QNALHNIKTLPGMHH HHHHHCCCCCCCCCC	49.69	-
141	Methylation	LFIGMVSKKCNENDI HHHHHHCCCCCCCCC	50.35	23644510
141	Acetylation	LFIGMVSKKCNENDI HHHHHHCCCCCCCCC	50.35	25953088
151	Sulfoxidation	NENDIRVMFSPFGQI CCCCCEEEEECCCCE	1.66	21406390
165	Methylation	IEECRILRGPDGLSR EEEEEECCCCCCCCC	52.83	-
182	Methylation	AFVTFSTRAMAQNAI EEEEEHHHHHHHHHH	22.59	-
185 (in isoform 4)	Ubiquitination	-	9.86	-
190	Ubiquitination	AMAQNAIKAMHQSQT HHHHHHHHHHHHHHC	36.93	-
195	Phosphorylation	AIKAMHQSQTMEGCS HHHHHHHHHCCCCCC	16.97	23312004
197	Phosphorylation	KAMHQSQTMEGCSSP HHHHHHHCCCCCCCC	23.57	23312004
202	Phosphorylation	SQTMEGCSSPIVVKF HHCCCCCCCCEEEEE	50.43	23312004
203	Phosphorylation	QTMEGCSSPIVVKFA HCCCCCCCCEEEEEC	23.79	23312004
214	Ubiquitination	VKFADTQKDKEQRRL EEECCCHHHHHHHHH	73.24	-
295	O-linked_Glycosylation	AAAAAAQTSATSTNA HHHHHHHHCCCCCCC	18.66	29485866
296	O-linked_Glycosylation	AAAAAQTSATSTNAN HHHHHHHCCCCCCCC	19.92	29485866
298	O-linked_Glycosylation	AAAQTSATSTNANPL HHHHHCCCCCCCCCC	35.53	29485866
316	Phosphorylation	SSALGALTSPVAAST HHHHHHHCCCCCCCC	30.37	26074081
317	Phosphorylation	SALGALTSPVAASTP HHHHHHCCCCCCCCC	20.44	26074081
438 (in isoform 5)	Ubiquitination	-	48.59	21890473
440 (in isoform 2)	Ubiquitination	-	3.98	21890473
458	Sumoylation	SAKVFIDKQTNLSKC EEEEEEECCCCHHHH	54.96	-
458	Acetylation	SAKVFIDKQTNLSKC EEEEEEECCCCHHHH	54.96	23954790
458 (in isoform 1)	Ubiquitination	-	54.96	21890473
458	Ubiquitination	SAKVFIDKQTNLSKC EEEEEEECCCCHHHH	54.96	-
458	Malonylation	SAKVFIDKQTNLSKC EEEEEEECCCCHHHH	54.96	26320211
458	2-Hydroxyisobutyrylation	SAKVFIDKQTNLSKC EEEEEEECCCCHHHH	54.96	-
458	Sumoylation	SAKVFIDKQTNLSKC EEEEEEECCCCHHHH	54.96	-
459 (in isoform 4)	Ubiquitination	-	31.69	21890473
471 (in isoform 3)	Ubiquitination	-	17.90	21890473
471 (in isoform 4)	Ubiquitination	-	17.90	21890473

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

Oops, there are no upstream regulatory protein records of CELF2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CELF2_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 CELF2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A1CF_HUMAN	A1CF	physical	11577082
APOB_RAT	Apob	physical	11577082
A4_HUMAN	APP	physical	21832049
PGH2_HUMAN	PTGS2	physical	17383427
ELAV1_HUMAN	ELAVL1	physical	17383427
TRAF3_HUMAN	TRAF3	physical	28031331

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-458, AND MASS SPECTROMETRY.
PubMed: 19608861