dbPTM

KCD12_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCD12_MOUSE
UniProt AC	Q6WVG3
Protein Name	BTB/POZ domain-containing protein KCTD12
Gene Name	Kctd12
Organism	Mus musculus (Mouse).
Sequence Length	327
Subcellular Localization	Cell junction, synapse, presynaptic cell membrane . Cell junction, synapse, postsynaptic cell membrane . Colocalizes with GABRB1.
Protein Description	Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization..
Protein Sequence	MALADSARGLPNGGGGGGGSGSSSSSAEPPLFPDIVELNVGGQVYVTRRCTVVSVPDSLLWRMFTQQQPQELARDSKGRFFLDRDGFFFRYILDYLRDLQLVLPDYFPERSRLQREAEYFELPELVRRLGAPQQPGPGPPPPHSRRGVHKEGSLGDELLPLGYAEPEPQEGASAGAPSPTLELASRSPSGGAAGPLLTPSQSLDGSRRSGYITIGYRGSYTIGRDAQADAKFRRVARITVCGKTSLAKEVFGDTLNESRDPDRPPERYTSRYYLKFNFLEQAFDKLSESGFHMVACSSTGTCAFASSTDQSEDKIWTSYTEYVFCRE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MALADSARG ------CCCCCCCCC	16.09	-
119	Phosphorylation	RLQREAEYFELPELV HHHHHHHHHCHHHHH	14.92	17242355
144	Phosphorylation	PGPPPPHSRRGVHKE CCCCCCCCCCCCCCC	29.46	21183079
153	Phosphorylation	RGVHKEGSLGDELLP CCCCCCCCCCCCEEC	30.21	24925903
163	Phosphorylation	DELLPLGYAEPEPQE CCEECCCCCCCCCCC	18.57	25159016
173	Phosphorylation	PEPQEGASAGAPSPT CCCCCCCCCCCCCCC	37.78	24925903
178	Phosphorylation	GASAGAPSPTLELAS CCCCCCCCCCEEEHH	29.95	25521595
180	Phosphorylation	SAGAPSPTLELASRS CCCCCCCCEEEHHCC	36.88	25521595
185	Phosphorylation	SPTLELASRSPSGGA CCCEEEHHCCCCCCC	46.01	25159016
187	Phosphorylation	TLELASRSPSGGAAG CEEEHHCCCCCCCCC	22.41	25521595
189	Phosphorylation	ELASRSPSGGAAGPL EEHHCCCCCCCCCCC	51.62	25521595
198	Phosphorylation	GAAGPLLTPSQSLDG CCCCCCCCCCCCCCC	28.69	25521595
200	Phosphorylation	AGPLLTPSQSLDGSR CCCCCCCCCCCCCCC	27.45	25521595
202	Phosphorylation	PLLTPSQSLDGSRRS CCCCCCCCCCCCCCC	32.53	25521595
206	Phosphorylation	PSQSLDGSRRSGYIT CCCCCCCCCCCCEEE	24.96	24925903
219	Phosphorylation	ITIGYRGSYTIGRDA EEEEECCEEEECCHH	15.31	30635358
220	Phosphorylation	TIGYRGSYTIGRDAQ EEEECCEEEECCHHH	12.75	30635358
221	Phosphorylation	IGYRGSYTIGRDAQA EEECCEEEECCHHHC	20.74	30635358
231	Acetylation	RDAQADAKFRRVARI CHHHCCCHHEEEEEE	39.69	22902405
254	Phosphorylation	AKEVFGDTLNESRDP HHHHHCCCCCCCCCC	31.68	29176673
258	Phosphorylation	FGDTLNESRDPDRPP HCCCCCCCCCCCCCC	40.69	29176673

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 KCD12_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KCD12_MOUSE !!

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 KCD12_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of KCD12_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KCD12_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-189 ANDTHR-198, AND MASS SPECTROMETRY.	17242355 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND THR-198, ANDMASS SPECTROMETRY.	17114649 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND MASSSPECTROMETRY.	15345747 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-119, AND MASSSPECTROMETRY.	18034455 [Abstract]