CPEB3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CPEB3_HUMAN
• UniProt AC: Q8NE35
• Protein Name: Cytoplasmic polyadenylation element-binding protein 3
• Gene Name: CPEB3
• Organism: Homo sapiens (Human).
• Sequence Length: 698
• Subcellular Localization: Cytoplasm . Nucleus . Cell junction, synapse . Cell projection, dendrite . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . Predominantly cytoplasmic in unstimulated neurons but translocates to the nucleus following neuronal
• Protein Description: Sequence-specific RNA-binding protein which acts as a translational repressor in the basal unstimulated state but, following neuronal stimulation, acts as a translational activator (By similarity). In contrast to CPEB1, does not bind to the cytoplasmic polyadenylation element (CPE), a uridine-rich sequence element within the mRNA 3'-UTR, but binds to a U-rich loop within a stem-loop structure (By similarity). Required for the consolidation and maintenance of hippocampal-based long term memory (By similarity). In the basal state, binds to the mRNA 3'-UTR of the glutamate receptors GRIA2/GLUR2 mRNA and negatively regulates their translation (By similarity). Also represses the translation of DLG4, GRIN1, GRIN2A and GRIN2B (By similarity). When activated, acts as a translational activator of GRIA1 and GRIA2 (By similarity). In the basal state, suppresses SUMO2 translation but activates it following neuronal stimulation (By similarity). Binds to the 3'-UTR of TRPV1 mRNA and represses TRPV1 translation which is required to maintain normal thermoception (By similarity). Binds actin mRNA, leading to actin translational repression in the basal state and to translational activation following neuronal stimulation (By similarity). Negatively regulates target mRNA levels by binding to TOB1 which recruits CNOT7/CAF1 to a ternary complex and this leads to target mRNA deadenylation and decay. [PubMed: 21336257 In addition to its role in translation, binds to and inhibits the transcriptional activation activity of STAT5B without affecting its dimerization or DNA-binding activity. This, in turn, represses transcription of the STAT5B target gene EGFR which has been shown to play a role in enhancing learning and memory performance]
• Protein Sequence: MQDDLLMDKSKTQPQPQQQQRQQQQPQPESSVSEAPSTPLSSETPKPEENSAVPALSPAAAPPAPNGPDKMQMESPLLPGLSFHQPPQQPPPPQEPAAPGASLSPSFGSTWSTGTTNAVEDSFFQGITPVNGTMLFQNFPHHVNPVFGGTFSPQIGLAQTQHHQQPPPPAPAPQPAQPAQPPQAQPPQQRRSPASPSQAPYAQRSAAAAYGHQPIMTSKPSSSSAVAAAAAAAAASSASSSWNTHQSVNAAWSAPSNPWGGLQAGRDPRRAVGVGVGVGVGVPSPLNPISPLKKPFSSNVIAPPKFPRAAPLTSKSWMEDNAFRTDNGNNLLPFQDRSRPYDTFNLHSLENSLMDMIRTDHEPLKGKHYPPSGPPMSFADIMWRNHFAGRMGINFHHPGTDNIMALNNAFLDDSHGDQALSSGLSSPTRCQNGERVERYSRKVFVGGLPPDIDEDEITASFRRFGPLVVDWPHKAESKSYFPPKGYAFLLFQEESSVQALIDACLEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHNDIDKRVEVKPYVLDDQMCDECQGTRCGGKFAPFFCANVTCLQYYCEYCWASIHSRAGREFHKPLVKEGGDRPRHVPFRWS

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
9	Acetylation	QDDLLMDKSKTQPQP CCCCCCCCCCCCCCH	39.63	8242865
11	Acetylation	DLLMDKSKTQPQPQQ CCCCCCCCCCCCHHH	57.85	8242877
192	Phosphorylation	QPPQQRRSPASPSQA CCCCCCCCCCCHHHC	27.32	26055452
192 (in isoform 2)	Phosphorylation	-	27.32	18669648
195 (in isoform 2)	Phosphorylation	-	28.59	18669648
195	Phosphorylation	QQRRSPASPSQAPYA CCCCCCCCHHHCHHH	28.59	26055452
197	Phosphorylation	RRSPASPSQAPYAQR CCCCCCHHHCHHHHH	36.16	23663014
201	Phosphorylation	ASPSQAPYAQRSAAA CCHHHCHHHHHHHHH	20.55	23663014
210	Phosphorylation	QRSAAAAYGHQPIMT HHHHHHHHCCCCCCC	15.48	23663014
284	Phosphorylation	GVGVGVPSPLNPISP CCCCCCCCCCCCCCC	39.34	-
290	Phosphorylation	PSPLNPISPLKKPFS CCCCCCCCCCCCCCC	25.99	27050516
308	Asymmetric dimethylarginine	IAPPKFPRAAPLTSK CCCCCCCCCCCCCCC	46.65	-
308	Methylation	IAPPKFPRAAPLTSK CCCCCCCCCCCCCCC	46.65	-
348	Phosphorylation	YDTFNLHSLENSLMD CCCCCHHHHHHHHHH	40.31	20068231
400 (in isoform 2)	Phosphorylation	-	30.26	24719451
407 (in isoform 2)	Phosphorylation	-	28.39	23663014
408 (in isoform 2)	Phosphorylation	-	32.68	23663014
411 (in isoform 2)	Phosphorylation	-	7.12	23663014
412 (in isoform 2)	Phosphorylation	-	49.24	23663014
414 (in isoform 2)	Phosphorylation	-	29.09	23663014
422	Phosphorylation	HGDQALSSGLSSPTR CHHHHHHCCCCCCCC	44.60	18669648
425	Phosphorylation	QALSSGLSSPTRCQN HHHHCCCCCCCCCCC	37.48	29116813
426	Phosphorylation	ALSSGLSSPTRCQNG HHHCCCCCCCCCCCC	35.02	23663014
428	Phosphorylation	SSGLSSPTRCQNGER HCCCCCCCCCCCCCC	46.13	24275569
480	Phosphorylation	HKAESKSYFPPKGYA CCCCCCCCCCCCCEE	24.68	-
510	Acetylation	ACLEEDGKLYLCVSS HHHHHCCCEEEEEEC	46.40	10735637
521	Acetylation	CVSSPTIKDKPVQIR EEECCCCCCCCCEEC	63.28	10735641
523	Ubiquitination	SSPTIKDKPVQIRPW ECCCCCCCCCEECCC	41.93	-
523	Acetylation	SSPTIKDKPVQIRPW ECCCCCCCCCEECCC	41.93	10735629
573	Phosphorylation	AMIMDRLYGGVCYAG HHHHHHHHCCCCCCC	16.84	-
578	Phosphorylation	RLYGGVCYAGIDTDP HHHCCCCCCCCCCCC	12.88	-
583	Phosphorylation	VCYAGIDTDPELKYP CCCCCCCCCCCCCCC	52.08	-
589	Phosphorylation	DTDPELKYPKGAGRV CCCCCCCCCCCCCCE	23.85	-
604	Phosphorylation	AFSNQQSYIAAISAR EECCCHHHHHHHHHH	7.11	-

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

Oops, there are no upstream regulatory protein records of CPEB3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CPEB3_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 CPEB3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAN2_RAT	Capn2	physical	22711986

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

Phosphorylation

"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-192, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-192 AND SER-195, ANDMASS SPECTROMETRY.
PubMed: 18669648