dbPTM

KCD12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCD12_HUMAN
UniProt AC	Q96CX2
Protein Name	BTB/POZ domain-containing protein KCTD12
Gene Name	KCTD12
Organism	Homo sapiens (Human).
Sequence Length	325
Subcellular Localization	Cell junction, synapse, presynaptic cell membrane. Cell junction, synapse, postsynaptic cell membrane.
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 (By similarity)..
Protein Sequence	MALADSTRGLPNGGGGGGGSGSSSSSAEPPLFPDIVELNVGGQVYVTRRCTVVSVPDSLLWRMFTQQQPQELARDSKGRFFLDRDGFLFRYILDYLRDLQLVLPDYFPERSRLQREAEYFELPELVRRLGAPQQPGPGPPPSRRGVHKEGSLGDELLPLGYSEPEQQEGASAGAPSPTLELASRSPSGGAAGPLLTPSQSLDGSRRSGYITIGYRGSYTIGRDAQADAKFRRVARITVCGKTSLAKEVFGDTLNESRDPDRPPERYTSRYYLKFNFLEQAFDKLSESGFHMVACSSTGTCAFASSTDQSEDKIWTSYTEYVFCRE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MALADSTRG ------CCCCCCCCC	16.09	22814378
6	Phosphorylation	--MALADSTRGLPNG --CCCCCCCCCCCCC	17.88	24719451
7	Phosphorylation	-MALADSTRGLPNGG -CCCCCCCCCCCCCC	29.33	29255136
63	Sulfoxidation	PDSLLWRMFTQQQPQ CHHHHHHHHHCCCHH	2.63	21406390
91	Phosphorylation	RDGFLFRYILDYLRD CCCHHHHHHHHHHHH	9.86	-
119	Phosphorylation	RLQREAEYFELPELV HHHHHHHHHCHHHHH	14.92	24927040
142	Phosphorylation	PGPGPPPSRRGVHKE CCCCCCCCCCCCCCC	40.14	23312004
151	Phosphorylation	RGVHKEGSLGDELLP CCCCCCCCCCCCEEC	30.21	28355574
161	Phosphorylation	DELLPLGYSEPEQQE CCEECCCCCCHHHCC	19.97	22167270
162	Phosphorylation	ELLPLGYSEPEQQEG CEECCCCCCHHHCCC	44.89	22167270
171	Phosphorylation	PEQQEGASAGAPSPT HHHCCCCCCCCCCCC	37.78	22167270
176	Phosphorylation	GASAGAPSPTLELAS CCCCCCCCCCEEHHH	29.95	22167270
178	Phosphorylation	SAGAPSPTLELASRS CCCCCCCCEEHHHCC	36.88	22167270
183	Phosphorylation	SPTLELASRSPSGGA CCCEEHHHCCCCCCC	46.01	22167270
185	Phosphorylation	TLELASRSPSGGAAG CEEHHHCCCCCCCCC	22.41	29255136
187	Phosphorylation	ELASRSPSGGAAGPL EHHHCCCCCCCCCCC	51.62	29255136
196	Phosphorylation	GAAGPLLTPSQSLDG CCCCCCCCCCCCCCC	28.69	29255136
198	Phosphorylation	AGPLLTPSQSLDGSR CCCCCCCCCCCCCCC	27.45	29255136
200	Phosphorylation	PLLTPSQSLDGSRRS CCCCCCCCCCCCCCC	32.53	29255136
204	Phosphorylation	PSQSLDGSRRSGYIT CCCCCCCCCCCCEEE	24.96	29255136
207	Phosphorylation	SLDGSRRSGYITIGY CCCCCCCCCEEEEEE	34.53	28857561
209	Phosphorylation	DGSRRSGYITIGYRG CCCCCCCEEEEEECC	8.99	27134283
211	Phosphorylation	SRRSGYITIGYRGSY CCCCCEEEEEECCEE	10.40	-
217	Phosphorylation	ITIGYRGSYTIGRDA EEEEECCEEEECCHH	15.31	26657352
218	Phosphorylation	TIGYRGSYTIGRDAQ EEEECCEEEECCHHH	12.75	23403867
219	Phosphorylation	IGYRGSYTIGRDAQA EEECCEEEECCHHHC	20.74	23403867
229	Ubiquitination	RDAQADAKFRRVARI CHHHCCCHHEEEEEE	39.69	22053931
229	Acetylation	RDAQADAKFRRVARI CHHHCCCHHEEEEEE	39.69	22424773
242	Phosphorylation	RITVCGKTSLAKEVF EEEECCCHHHHHHHH	17.79	20068231
243	Phosphorylation	ITVCGKTSLAKEVFG EEECCCHHHHHHHHC	29.80	20068231
246	Ubiquitination	CGKTSLAKEVFGDTL CCCHHHHHHHHCCCC	60.75	-
252	Phosphorylation	AKEVFGDTLNESRDP HHHHHCCCCCCCCCC	31.68	23403867
256	Phosphorylation	FGDTLNESRDPDRPP HCCCCCCCCCCCCCC	40.69	21712546
257	Methylation	GDTLNESRDPDRPPE CCCCCCCCCCCCCCC	53.99	115480857

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
200	S	Phosphorylation	Kinase	AURKA	O14965	GPS
243	S	Phosphorylation	Kinase	AURKA	O14965	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KCD12_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 KCD12_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GABPA_HUMAN	GABPA	physical	22863883
IMA5_HUMAN	KPNA1	physical	22863883
NUCL_HUMAN	NCL	physical	22863883
GABR2_HUMAN	GABBR2	physical	23996491
KCD12_HUMAN	KCTD12	physical	23996491

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 KCD12_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-171; SER-176; SER-185;SER-187; THR-196; SER-198 AND SER-200, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-185, AND MASSSPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND SER-198, ANDMASS SPECTROMETRY.	17525332 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185; SER-187; THR-196;SER-198; SER-200 AND SER-204, AND MASS SPECTROMETRY.	17287340 [Abstract]