dbPTM

KCD16_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCD16_MOUSE
UniProt AC	Q5DTY9
Protein Name	BTB/POZ domain-containing protein KCTD16
Gene Name	Kctd16
Organism	Mus musculus (Mouse).
Sequence Length	427
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	MALSGNCSRYYPRDQGAAVPNSFPEVIELNVGGQVYFTRHSTLISIPHSLLWKMFSPKRDTANDLAKDSKGRFFIDRDGFLFRYILDYLRDRQVVLPDHFPERGRLKREAEYFQLPDLVKLLAPEDVKQSPDEFCHSDFEDASQGSDTRICPPSSLLPHDRKWGFITVGYRGSCTLGREGQADAKFRRVPRILVCGRISLAKEVFGETLNESRDPDRAPERYTSRFYLKFKHLERAFDMLSECGFHMVACNSSVTASFVNQYTEDKIWSSYTEYVFYREPSRWSSSHCDCCCKNGKGDKGESGTSCNDLSTSSCDSQSEASSPQETVICGPVTRQSNIQTLDRPIKKGPVQLIQQSEMRRKSDLLRTLTSGSRESNISSKKKAAKEKLSIEEELEKCIQDFLKIKIPDRFPERKHPWQSELLRKYHL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
58	Ubiquitination	LWKMFSPKRDTANDL HHHHHCCCCCCHHHH	62.80	27667366
112	Phosphorylation	RLKREAEYFQLPDLV CCHHHHHHHCCCHHH	12.04	22817900
130	Phosphorylation	APEDVKQSPDEFCHS CCHHHCCCCCCCCCC	28.71	25521595
137	Phosphorylation	SPDEFCHSDFEDASQ CCCCCCCCCCCCCCC	45.21	25521595
143	Phosphorylation	HSDFEDASQGSDTRI CCCCCCCCCCCCCEE	47.60	22324799
146	Phosphorylation	FEDASQGSDTRICPP CCCCCCCCCCEECCH	28.33	25521595
148	Phosphorylation	DASQGSDTRICPPSS CCCCCCCCEECCHHH	24.51	22324799
154	Phosphorylation	DTRICPPSSLLPHDR CCEECCHHHHCCCCC	20.82	29899451
155	Phosphorylation	TRICPPSSLLPHDRK CEECCHHHHCCCCCC	39.43	-
284	Phosphorylation	YREPSRWSSSHCDCC EECCCCCCCCCCCCC	22.35	20415495
285	Phosphorylation	REPSRWSSSHCDCCC ECCCCCCCCCCCCCC	19.69	22817900
286	Phosphorylation	EPSRWSSSHCDCCCK CCCCCCCCCCCCCCC	23.71	21930439
322	Phosphorylation	DSQSEASSPQETVIC CCCCCCCCCCCEEEE	37.34	-
336	Phosphorylation	CGPVTRQSNIQTLDR ECCCCCCCCCCCCCC	32.39	20415495
340	Phosphorylation	TRQSNIQTLDRPIKK CCCCCCCCCCCCCCC	27.16	25521595
356	Phosphorylation	PVQLIQQSEMRRKSD HHHHHCHHHHHHHHH	19.58	22324799
362	Phosphorylation	QSEMRRKSDLLRTLT HHHHHHHHHHHHHHH	31.51	29899451
367	Phosphorylation	RKSDLLRTLTSGSRE HHHHHHHHHHHCCCC	34.06	19060867
369	Phosphorylation	SDLLRTLTSGSRESN HHHHHHHHHCCCCCC	30.35	22324799
370	Phosphorylation	DLLRTLTSGSRESNI HHHHHHHHCCCCCCH	37.57	22324799
372	Phosphorylation	LRTLTSGSRESNISS HHHHHHCCCCCCHHH	32.42	25521595
375	Phosphorylation	LTSGSRESNISSKKK HHHCCCCCCHHHHHH	38.05	22324799
378	Phosphorylation	GSRESNISSKKKAAK CCCCCCHHHHHHHHH	40.11	25521595
379	Phosphorylation	SRESNISSKKKAAKE CCCCCHHHHHHHHHH	44.70	22324799
389	Phosphorylation	KAAKEKLSIEEELEK HHHHHCCCHHHHHHH	38.74	25521595

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 KCD16_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KCD16_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 KCD16_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of KCD16_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of KCD16_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND SER-389, ANDMASS SPECTROMETRY.	16452087 [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-112, AND MASSSPECTROMETRY.	18034455 [Abstract]