CPEB4_HUMAN - dbPTM
CPEB4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPEB4_HUMAN
UniProt AC Q17RY0
Protein Name Cytoplasmic polyadenylation element-binding protein 4
Gene Name CPEB4
Organism Homo sapiens (Human).
Sequence Length 729
Subcellular Localization Cytoplasm . Cell projection, dendrite . Cell projection, dendritic spine . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . Cell projection, axon . Cell projection, growth cone . Endoplasmic reticulum . Cytoplasm, perinuclear reg
Protein Description Sequence-specific RNA-binding protein that binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. [PubMed: 24990967 RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism]
Protein Sequence MGDYGFGVLVQSNTGNKSAFPVRFHPHLQPPHHHQNATPSPAAFINNNTAANGSSAGSAWLFPAPATHNIQDEILGSEKAKSQQQEQQDPLEKQQLSPSPGQEAGILPETEKAKSEENQGDNSSENGNGKEKIRIESPVLTGFDYQEATGLGTSTQPLTSSASSLTGFSNWSAAIAPSSSTIINEDASFFHQGGVPAASANNGALLFQNFPHHVSPGFGGSFSPQIGPLSQHHPHHPHFQHHHSQHQQQRRSPASPHPPPFTHRNAAFNQLPHLANNLNKPPSPWSSYQSPSPTPSSSWSPGGGGYGGWGGSQGRDHRRGLNGGITPLNSISPLKKNFASNHIQLQKYARPSSAFAPKSWMEDSLNRADNIFPFPDRPRTFDMHSLESSLIDIMRAENDTIKGRLNYSYPGSDSSLLINARTYGRRRGQSSLFPMEDGFLDDGRGDQPLHSGLGSPHCFSHQNGERVERYSRKVFVGGLPPDIDEDEITASFRRFGPLIVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACIEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGEIDKRVEVKPYVLDDQLCDECQGARCGGKFAPFFCANVTCLQYYCEYCWAAIHSRAGREFHKPLVKEGGDRPRHISFRWN
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
18PhosphorylationQSNTGNKSAFPVRFH
ECCCCCCCCCEEEEC		38.8620068231
23MethylationNKSAFPVRFHPHLQP
CCCCCEEEECCCCCC		25.13-
77PhosphorylationIQDEILGSEKAKSQQ
HHHHHHCCHHHHHHH		32.26-
97PhosphorylationPLEKQQLSPSPGQEA
HHHHCCCCCCCCHHC		20.9929255136
99PhosphorylationEKQQLSPSPGQEAGI
HHCCCCCCCCHHCCC		37.9829255136
110PhosphorylationEAGILPETEKAKSEE
HCCCCCHHHHHHCCC		40.6322199227
115PhosphorylationPETEKAKSEENQGDN
CHHHHHHCCCCCCCC		55.8128102081
123PhosphorylationEENQGDNSSENGNGK
CCCCCCCCCCCCCCC		43.7128102081
124PhosphorylationENQGDNSSENGNGKE
CCCCCCCCCCCCCCC		41.1428985074
137PhosphorylationKEKIRIESPVLTGFD
CCCEEEECCEECCCC		20.2422468782
251MethylationSQHQQQRRSPASPHP
HHHHHHHCCCCCCCC		42.53-
252PhosphorylationQHQQQRRSPASPHPP
HHHHHHCCCCCCCCC		27.3229255136
255PhosphorylationQQRRSPASPHPPPFT
HHHCCCCCCCCCCCC		27.4229255136
262PhosphorylationSPHPPPFTHRNAAFN
CCCCCCCCCCCHHHH		26.2123312004
288PhosphorylationPPSPWSSYQSPSPTP
CCCCCHHCCCCCCCC		13.9030576142
294PhosphorylationSYQSPSPTPSSSWSP
HCCCCCCCCCCCCCC		39.8930576142
306PhosphorylationWSPGGGGYGGWGGSQ
CCCCCCCCCCCCCCC		18.7530576142
326PhosphorylationRGLNGGITPLNSISP
CCCCCCCCCCCCCCH		25.6226055452
330PhosphorylationGGITPLNSISPLKKN
CCCCCCCCCCHHHHH		31.9322167270
332PhosphorylationITPLNSISPLKKNFA
CCCCCCCCHHHHHCC		24.8122167270
336UbiquitinationNSISPLKKNFASNHI
CCCCHHHHHCCCCCC		66.05-
340PhosphorylationPLKKNFASNHIQLQK
HHHHHCCCCCCEEHH		25.4625159151
347UbiquitinationSNHIQLQKYARPSSA
CCCCEEHHHCCCCCC		49.85-
348PhosphorylationNHIQLQKYARPSSAF
CCCEEHHHCCCCCCC		8.5526074081
352PhosphorylationLQKYARPSSAFAPKS
EHHHCCCCCCCCCHH		28.8426074081
353PhosphorylationQKYARPSSAFAPKSW
HHHCCCCCCCCCHHH		30.0426074081
359PhosphorylationSSAFAPKSWMEDSLN
CCCCCCHHHHHHHHH		30.5126074081
364PhosphorylationPKSWMEDSLNRADNI
CHHHHHHHHHCCCCC		17.7826074081
380PhosphorylationPFPDRPRTFDMHSLE
CCCCCCCCCCHHHHH		27.0318452278
385PhosphorylationPRTFDMHSLESSLID
CCCCCHHHHHHHHHH		27.4828348404
388PhosphorylationFDMHSLESSLIDIMR
CCHHHHHHHHHHHHH		35.4228348404
389PhosphorylationDMHSLESSLIDIMRA
CHHHHHHHHHHHHHH		21.7028348404
430PhosphorylationYGRRRGQSSLFPMED
CCCCCCCCCCCCCCC		31.6522210691
431PhosphorylationGRRRGQSSLFPMEDG
CCCCCCCCCCCCCCC		26.5822210691
451PhosphorylationRGDQPLHSGLGSPHC
CCCCCCCCCCCCCCC		43.3125850435
455PhosphorylationPLHSGLGSPHCFSHQ
CCCCCCCCCCCCCCC		19.2625850435
460PhosphorylationLGSPHCFSHQNGERV
CCCCCCCCCCCCCCE		29.5625850435
505AcetylationLIVDWPHKAESKSYF
EEEECCCCCCCCCCC		50.177935075
509AcetylationWPHKAESKSYFPPKG
CCCCCCCCCCCCCCC		40.457935085
511PhosphorylationHKAESKSYFPPKGYA
CCCCCCCCCCCCCEE		24.68-
554UbiquitinationSSPTIKDKPVQIRPW
ECCCCCCCCCEECCC		41.93-
604PhosphorylationAMIMDRLYGGVCYAG
HHHHHHHHCCCCCCC		16.84-
609PhosphorylationRLYGGVCYAGIDTDP
HHHCCCCCCCCCCCC		12.88-
614PhosphorylationVCYAGIDTDPELKYP
CCCCCCCCCCCCCCC		52.08-
620PhosphorylationDTDPELKYPKGAGRV
CCCCCCCCCCCCCCE		23.85-
635PhosphorylationAFSNQQSYIAAISAR
EECCCHHHHHHHHHH		7.11-
725PhosphorylationGDRPRHISFRWN---
CCCCCCCCEECC---		11.57-
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 CPEB4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPEB4_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 CPEB4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NDST1_HUMANNDST1physical
22939629
UBE3C_HUMANUBE3Cphysical
22939629
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 CPEB4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-252; SER-255;THR-326 AND SER-332, AND MASS SPECTROMETRY.

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