CELF1_HUMAN - dbPTM
CELF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CELF1_HUMAN
UniProt AC Q92879
Protein Name CUGBP Elav-like family member 1
Gene Name CELF1
Organism Homo sapiens (Human).
Sequence Length 486
Subcellular Localization Nucleus . Cytoplasm . 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 cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. 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. Activates SM exon 5 inclusion by antagonizing the repressive effect of PTB. Promotes exclusion of exon 11 of the INSR pre-mRNA. Inhibits, together with HNRNPH1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Increases translation and controls the choice of translation initiation codon of CEBPB mRNA. Increases mRNA translation of CEBPB in aging liver (By similarity). Increases translation of CDKN1A mRNA by antagonizing the repressive effect of CALR3. Mediates rapid cytoplasmic mRNA deadenylation. Recruits the deadenylase PARN to the poly(A) tail of EDEN-containing mRNAs to promote their deadenylation. Required for completion of spermatogenesis (By similarity). Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK and to Bruno response elements (BREs). Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA. Binds to AU-rich sequences (AREs or EDEN-like) localized in the 3'-UTR of JUN and FOS mRNAs. Binds to the IR RNA. Binds to the 5'-region of CDKN1A and CEBPB mRNAs. Binds with the 5'-region of CEBPB mRNA in aging liver. May be a specific regulator of miRNA biogenesis. Binds to primary microRNA pri-MIR140 and, with CELF2, negatively regulates the processing to mature miRNA. [PubMed: 28431233]
Protein Sequence MNGTLDHPDQPDLDAIKMFVGQVPRTWSEKDLRELFEQYGAVYEINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNMKVLPGMHHPIQMKPADSEKNNAVEDRKLFIGMISKKCTENDIRVMFSSFGQIEECRILRGPDGLSRGCAFVTFTTRAMAQTAIKAMHQAQTMEGCSSPMVVKFADTQKDKEQKRMAQQLQQQMQQISAASVWGNLAGLNTLGPQYLALYLQLLQQTASSGNLNTLSSLHPMGGLNAMQLQNLAALAAAASAAQNTPSGTNALTTSSSPLSVLTSSGSSPSSSSSNSVNPIASLGALQTLAGATAGLNVGSLAGMAALNGGLGSSGLSNGTGSTMEALTQAYSGIQQYAAAALPTLYNQNLLTQQSIGAAGSQKEGPEGANLFIYHLPQEFGDQDLLQMFMPFGNVVSAKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQSMNGFQIGMKRLKVQLKRSKNDSKPY
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 Orthologous
Protein Cluster
1Acetylation-------MNGTLDHP
-------CCCCCCCC		10.6119413330
4Phosphorylation----MNGTLDHPDQP
----CCCCCCCCCCC		24.8223186163
18 (in isoform 4)Phosphorylation-2.4125159151
21 (in isoform 4)Phosphorylation-16.1125159151
22 (in isoform 4)Phosphorylation-36.4225159151
25MethylationMFVGQVPRTWSEKDL
HHCCCCCCCCCHHHH		50.39-
25 (in isoform 4)Phosphorylation-50.3925159151
26PhosphorylationFVGQVPRTWSEKDLR
HCCCCCCCCCHHHHH		27.5430266825
28PhosphorylationGQVPRTWSEKDLREL
CCCCCCCCHHHHHHH		33.8723401153
30UbiquitinationVPRTWSEKDLRELFE
CCCCCCHHHHHHHHH		57.45-
30AcetylationVPRTWSEKDLRELFE
CCCCCCHHHHHHHHH		57.4526051181
31 (in isoform 4)Phosphorylation-47.0825159151
52PhosphorylationINVLRDRSQNPPQSK
EEEEECCCCCCCCCC		38.30-
53 (in isoform 4)Phosphorylation-68.3024719451
55 (in isoform 4)Phosphorylation-22.2224719451
59 (in isoform 1)Ubiquitination-51.2021890473
59 (in isoform 2)Ubiquitination-51.2021890473
59 (in isoform 3)Ubiquitination-51.2021890473
59UbiquitinationSQNPPQSKGCCFVTF
CCCCCCCCCEEEEEE		51.2021906983
61S-nitrosylationNPPQSKGCCFVTFYT
CCCCCCCEEEEEEEC		1.5519483679
61S-nitrosocysteineNPPQSKGCCFVTFYT
CCCCCCCEEEEEEEC		1.55-
62S-nitrosylationPPQSKGCCFVTFYTR
CCCCCCEEEEEEECH		4.1319483679
62S-nitrosocysteinePPQSKGCCFVTFYTR
CCCCCCEEEEEEECH		4.13-
70 (in isoform 1)Ubiquitination-30.1621890473
70 (in isoform 2)Ubiquitination-30.1621890473
70 (in isoform 3)Ubiquitination-30.1621890473
70UbiquitinationFVTFYTRKAALEAQN
EEEEECHHHHHHHHH		30.1621906983
82SulfoxidationAQNALHNMKVLPGMH
HHHHHHCCCCCCCCC		1.9021406390
83UbiquitinationQNALHNMKVLPGMHH
HHHHHCCCCCCCCCC		46.03-
86 (in isoform 4)Ubiquitination-40.8421890473
95UbiquitinationMHHPIQMKPADSEKN
CCCCCCCCCCCHHCC		22.22-
97 (in isoform 4)Ubiquitination-27.6921890473
101UbiquitinationMKPADSEKNNAVEDR
CCCCCHHCCCHHHHH		60.50-
109SumoylationNNAVEDRKLFIGMIS
CCHHHHHHHHHHHHC		61.13-
109SumoylationNNAVEDRKLFIGMIS
CCHHHHHHHHHHHHC		61.1328112733
117AcetylationLFIGMISKKCTENDI
HHHHHHCCCCCHHHH		40.7325953088
118 (in isoform 1)Ubiquitination-39.3321890473
118UbiquitinationFIGMISKKCTENDIR
HHHHHCCCCCHHHHH		39.3322053931
120 (in isoform 3)Phosphorylation-46.86-
120 (in isoform 2)Phosphorylation-46.86-
120PhosphorylationGMISKKCTENDIRVM
HHHCCCCCHHHHHHH		46.8620068231
129PhosphorylationNDIRVMFSSFGQIEE
HHHHHHHHHCCCEEE		13.4820068231
130PhosphorylationDIRVMFSSFGQIEEC
HHHHHHHHCCCEEEE		23.3320068231
137GlutathionylationSFGQIEECRILRGPD
HCCCEEEEEECCCCC		1.8122555962
141MethylationIEECRILRGPDGLSR
EEEEEECCCCCCCCC		52.83-
157PhosphorylationCAFVTFTTRAMAQTA
CEEEEEHHHHHHHHH		16.5524667141
166UbiquitinationAMAQTAIKAMHQAQT
HHHHHHHHHHHHHHH		36.87-
173PhosphorylationKAMHQAQTMEGCSSP
HHHHHHHHCCCCCCC		21.8720068231
177GlutathionylationQAQTMEGCSSPMVVK
HHHHCCCCCCCEEEE		2.0122555962
178 (in isoform 2)Phosphorylation-48.62-
178 (in isoform 3)Phosphorylation-48.62-
178PhosphorylationAQTMEGCSSPMVVKF
HHHCCCCCCCEEEEE		48.6225159151
179PhosphorylationQTMEGCSSPMVVKFA
HHCCCCCCCEEEEEC		22.5325159151
184UbiquitinationCSSPMVVKFADTQKD
CCCCEEEEECCCHHH		24.35-
184AcetylationCSSPMVVKFADTQKD
CCCCEEEEECCCHHH		24.3526051181
190UbiquitinationVKFADTQKDKEQKRM
EEECCCHHHHHHHHH		73.24-
192 (in isoform 4)Ubiquitination-69.91-
204 (in isoform 4)Phosphorylation-20.7724719451
205 (in isoform 4)Phosphorylation-2.4827251275
241PhosphorylationLLQQTASSGNLNTLS
HHHHHHHCCCCCCHH		29.27-
279O-linked_GlycosylationSAAQNTPSGTNALTT
HHHHCCCCCCCCCCC		57.1023301498
281O-linked_GlycosylationAQNTPSGTNALTTSS
HHCCCCCCCCCCCCC		22.9623301498
295PhosphorylationSSPLSVLTSSGSSPS
CCCCEEEECCCCCCC		20.7726074081
295O-linked_GlycosylationSSPLSVLTSSGSSPS
CCCCEEEECCCCCCC		20.7723301498
296PhosphorylationSPLSVLTSSGSSPSS
CCCEEEECCCCCCCC		28.6526074081
297PhosphorylationPLSVLTSSGSSPSSS
CCEEEECCCCCCCCC		37.1426074081
299PhosphorylationSVLTSSGSSPSSSSS
EEEECCCCCCCCCCC		40.8126074081
300O-linked_GlycosylationVLTSSGSSPSSSSSN
EEECCCCCCCCCCCC		32.1223301498
300PhosphorylationVLTSSGSSPSSSSSN
EEECCCCCCCCCCCC		32.1226074081
302PhosphorylationTSSGSSPSSSSSNSV
ECCCCCCCCCCCCCC		44.8118570922
302O-linked_GlycosylationTSSGSSPSSSSSNSV
ECCCCCCCCCCCCCC		44.8123301498
303O-linked_GlycosylationSSGSSPSSSSSNSVN
CCCCCCCCCCCCCCC		37.3123301498
303PhosphorylationSSGSSPSSSSSNSVN
CCCCCCCCCCCCCCC		37.3126074081
304PhosphorylationSGSSPSSSSSNSVNP
CCCCCCCCCCCCCCC		41.9726074081
305PhosphorylationGSSPSSSSSNSVNPI
CCCCCCCCCCCCCCC		35.1726074081
305O-linked_GlycosylationGSSPSSSSSNSVNPI
CCCCCCCCCCCCCCC		35.1723301498
306PhosphorylationSSPSSSSSNSVNPIA
CCCCCCCCCCCCCCH		34.7626074081
432AcetylationGNVVSAKVFIDKQTN
CCEEEEEEEEECCCC		5.2019608861
432UbiquitinationGNVVSAKVFIDKQTN
CCEEEEEEEEECCCC		5.2019608861
432 (in isoform 2)Acetylation-5.20-
432 (in isoform 2)Ubiquitination-5.2021890473
433AcetylationNVVSAKVFIDKQTNL
CEEEEEEEEECCCCH		6.1919608861
433UbiquitinationNVVSAKVFIDKQTNL
CEEEEEEEEECCCCH		6.1919608861
433 (in isoform 3)Acetylation-6.19-
433 (in isoform 3)Ubiquitination-6.1921890473
435AcetylationVSAKVFIDKQTNLSK
EEEEEEEECCCCHHH		26.0819608861
435UbiquitinationVSAKVFIDKQTNLSK
EEEEEEEECCCCHHH		26.0819608861
436UbiquitinationSAKVFIDKQTNLSKC
EEEEEEECCCCHHHH		54.9619608861
436SumoylationSAKVFIDKQTNLSKC
EEEEEEECCCCHHHH		54.96-
436SumoylationSAKVFIDKQTNLSKC
EEEEEEECCCCHHHH		54.9619608861
436AcetylationSAKVFIDKQTNLSKC
EEEEEEECCCCHHHH		54.9624497403
436 (in isoform 1)Ubiquitination-54.9621890473
436UbiquitinationSAKVFIDKQTNLSKC
EEEEEEECCCCHHHH		54.9621890473
462UbiquitinationAQAAIQSMNGFQIGM
HHHHHHHCCCCCCCH		3.0519608861
462AcetylationAQAAIQSMNGFQIGM
HHHHHHHCCCCCCCH		3.0519608861
462 (in isoform 4)Ubiquitination-3.0521890473
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
28SPhosphorylationKinaseAKT1P31749
PSP
28SPhosphorylationKinasePKCAP17252
PSP
52SPhosphorylationKinasePKCAP17252
PSP
173TPhosphorylationKinasePKCAP17252
PSP
178SPhosphorylationKinasePKCAP17252
PSP
179SPhosphorylationKinasePKCAP17252
PSP
241SPhosphorylationKinasePKCAP17252
PSP
300SPhosphorylationKinasePKCAP17252
PSP
302SPhosphorylationKinaseCDK4P11802
PSP
302SPhosphorylationKinaseCDK6Q00534
PSP
302SPhosphorylationKinasePKCAP17252
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CELF1_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 CELF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CXCL7_HUMANPPBPphysical
16169070
TM1L1_HUMANTOM1L1physical
16169070
A4_HUMANAPPphysical
21832049
HNRPC_HUMANHNRNPCphysical
22365833
RALY_HUMANRALYphysical
22365833
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 CELF1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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