dbPTM

CPEB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CPEB1_HUMAN
UniProt AC	Q9BZB8
Protein Name	Cytoplasmic polyadenylation element-binding protein 1
Gene Name	CPEB1
Organism	Homo sapiens (Human).
Sequence Length	566
Subcellular Localization	Cytoplasm . Nucleus . Cytoplasm, P-body. Cytoplasmic granule. Cell junction, synapse. Membrane. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cell projection, dendrite. Continuously shuttling between nucleus and cytoplasm
Protein Description	Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism. [PubMed: 24990967 In absence of phosphorylation and in association with TACC3 is also involved as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation (By similarity Involved in the transport of CPE-containing mRNA to dendrites; those mRNAs may be transported to dendrites in a translationally dormant form and translationally activated at synapses (By similarity Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation (By similarity Induces the assembly of stress granules in the absence of stress. Required for cell cycle progression, specifically for prophase entry]
Protein Sequence	MALSLEEEAGRIKDCWDNQEAPALSTCSNANIFRRINAILDNSLDFSRVCTTPINRGIHDHLPDFQDSEETVTSRMLFPTSAQESSRGLPDANDLCLGLQSLSLTGWDRPWSTQDSDSSAQSSTHSVLSMLHNPLGNVLGKPPLSFLPLDPLGSDLVDKFPAPSVRGSRLDTRPILDSRSSSPSDSDTSGFSSGSDHLSDLISSLRISPPLPFLSLSGGGPRDPLKMGVGSRMDQEQAALAAVTPSPTSASKRWPGASVWPSWDLLEAPKDPFSIEREARLHRQAAAVNEATCTWSGQLPPRNYKNPIYSCKVFLGGVPWDITEAGLVNTFRVFGSLSVEWPGKDGKHPRCPPKGNMPKGYVYLVFELEKSVRSLLQACSHDPLSPDGLSEYYFKMSSRRMRCKEVQVIPWVLADSNFVRSPSQRLDPSRTVFVGALHGMLNAEALAAILNDLFGGVVYAGIDTDKHKYPIGSGRVTFNNQRSYLKAVSAAFVEIKTTKFTKKVQIDPYLEDSLCHICSSQPGPFFCRDQVCFKYFCRSCWHWRHSMEGLRHHSPLMRNQKNRDSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MALSLEEEAGR ----CCCCHHHHHCC	24.97	23612710
43	Phosphorylation	INAILDNSLDFSRVC HHHHHCCCCCHHHHC	29.05	19690332
52	Phosphorylation	DFSRVCTTPINRGIH CHHHHCCCCCCCCHH	19.62	21712546
80	Phosphorylation	TSRMLFPTSAQESSR HHHEECCCCHHHHHC	29.38	24719451
172	Phosphorylation	VRGSRLDTRPILDSR CCCCCCCCCCCCCCC	42.83	-
178	Phosphorylation	DTRPILDSRSSSPSD CCCCCCCCCCCCCCC	30.53	25850435
180	Phosphorylation	RPILDSRSSSPSDSD CCCCCCCCCCCCCCC	38.84	27732954
181	Phosphorylation	PILDSRSSSPSDSDT CCCCCCCCCCCCCCC	45.20	27732954
182	Phosphorylation	ILDSRSSSPSDSDTS CCCCCCCCCCCCCCC	29.66	27732954
184	Phosphorylation	DSRSSSPSDSDTSGF CCCCCCCCCCCCCCC	52.25	18669648
186	Phosphorylation	RSSSPSDSDTSGFSS CCCCCCCCCCCCCCC	47.31	27732954
188	Phosphorylation	SSPSDSDTSGFSSGS CCCCCCCCCCCCCCC	34.40	28111955
203	Phosphorylation	DHLSDLISSLRISPP HHHHHHHHHCCCCCC	30.53	24719451
204	Phosphorylation	HLSDLISSLRISPPL HHHHHHHHCCCCCCC	18.05	25954137
208	Phosphorylation	LISSLRISPPLPFLS HHHHCCCCCCCCCEE	17.65	29255136
231	Phosphorylation	PLKMGVGSRMDQEQA CCCCCCCCCCCHHHH	23.25	28674151
305	Ubiquitination	QLPPRNYKNPIYSCK CCCCCCCCCCCEEEE	60.85	-
347	Acetylation	EWPGKDGKHPRCPPK ECCCCCCCCCCCCCC	61.64	7925751
374	Phosphorylation	ELEKSVRSLLQACSH EHHHHHHHHHHHHCC	31.13	23879269
380	Phosphorylation	RSLLQACSHDPLSPD HHHHHHHCCCCCCCC	33.66	23879269
390	Phosphorylation	PLSPDGLSEYYFKMS CCCCCCHHHHHHHHH	29.14	23879269
501	Phosphorylation	EIKTTKFTKKVQIDP EEEECCCEEEEECCC	31.35	29496963

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
172	T	Phosphorylation	Kinase	AURKA	O14965	Uniprot
172	T	Phosphorylation	Kinase	CAMK2A	Q9UQM7	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:24658274

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
172	T	Phosphorylation	15731006
Phosphorylation and dephosphorylation on Thr-172 regulates cytoplasmic polyadenylation and translation of CPE-containing mRNAs.
172	T	Phosphorylation	15731006
Phosphorylation on Thr-172 by AURKA and CAMK2A activates CPEB1.
172	T	Phosphorylation	15731006
Phosphorylation on Thr-172 may be promoted by APLP1.

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 CPEB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CPEB1_HUMAN	CPEB1	physical	22456264
A4_HUMAN	APP	physical	21832049
MOT2_HUMAN	SLC16A7	physical	21988832
SYMPK_HUMAN	SYMPK	physical	28514442
MAP12_HUMAN	METAP1D	physical	28514442
GBP5_HUMAN	GBP5	physical	28514442
APBA3_HUMAN	APBA3	physical	28514442
CSTFT_HUMAN	CSTF2T	physical	28514442
GAN_HUMAN	GAN	physical	28514442
NMD3_HUMAN	NMD3	physical	28514442
CSTF2_HUMAN	CSTF2	physical	28514442

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 CPEB1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASSSPECTROMETRY.	19690332 [Abstract]

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