dbPTM

KCD15_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCD15_HUMAN
UniProt AC	Q96SI1
Protein Name	BTB/POZ domain-containing protein KCTD15
Gene Name	KCTD15
Organism	Homo sapiens (Human).
Sequence Length	283
Subcellular Localization
Protein Description	During embryonic development, interferes with neural crest formation (By similarity). Inhibits AP2 transcriptional activity by interaction with its activation domain..
Protein Sequence	MPHRKERPSGSSLHTHGSTGTAEGGNMSRLSLTRSPVSPLAAQGIPLPAQLTKSNAPVHIDVGGHMYTSSLATLTKYPDSRISRLFNGTEPIVLDSLKQHYFIDRDGEIFRYVLSFLRTSKLLLPDDFKDFSLLYEEARYYQLQPMVRELERWQQEQEQRRRSRACDCLVVRVTPDLGERIALSGEKALIEEVFPETGDVMCNSVNAGWNQDPTHVIRFPLNGYCRLNSVQVLERLFQRGFSVAASCGGGVDSSQFSEYVLCREERRPQPTPTAVRIKQEPLD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	PHRKERPSGSSLHTH CCCCCCCCCCCCEEC	58.49	30576142
11	Phosphorylation	RKERPSGSSLHTHGS CCCCCCCCCCEECCC	33.78	-
12	Phosphorylation	KERPSGSSLHTHGST CCCCCCCCCEECCCC	27.91	30576142
15	Phosphorylation	PSGSSLHTHGSTGTA CCCCCCEECCCCCCC	32.97	30576142
18	Phosphorylation	SSLHTHGSTGTAEGG CCCEECCCCCCCCCC	18.96	30576142
19	Phosphorylation	SLHTHGSTGTAEGGN CCEECCCCCCCCCCC	43.05	28555341
21	Phosphorylation	HTHGSTGTAEGGNMS EECCCCCCCCCCCCC	22.94	30576142
28	Phosphorylation	TAEGGNMSRLSLTRS CCCCCCCCEEEEECC	33.79	-
31	Phosphorylation	GGNMSRLSLTRSPVS CCCCCEEEEECCCCC	26.95	25159151
33	Phosphorylation	NMSRLSLTRSPVSPL CCCEEEEECCCCCHH	26.23	25159151
35	Phosphorylation	SRLSLTRSPVSPLAA CEEEEECCCCCHHHH	25.15	29255136
38	Phosphorylation	SLTRSPVSPLAAQGI EEECCCCCHHHHCCC	19.99	29255136
52	Phosphorylation	IPLPAQLTKSNAPVH CCCCHHHCCCCCCEE	21.98	23403867
69	Phosphorylation	VGGHMYTSSLATLTK ECCEEEECCHHHHHC	13.08	-
70	Phosphorylation	GGHMYTSSLATLTKY CCEEEECCHHHHHCC	17.77	-
73	Phosphorylation	MYTSSLATLTKYPDS EEECCHHHHHCCCCC	40.01	-
112	Phosphorylation	RDGEIFRYVLSFLRT CCCHHHHHHHHHHHH	8.59	23532336
115	Phosphorylation	EIFRYVLSFLRTSKL HHHHHHHHHHHHCCC	16.52	23532336
132	Phosphorylation	PDDFKDFSLLYEEAR CCCCCCHHHHHHHHH	27.83	25072903
135	Phosphorylation	FKDFSLLYEEARYYQ CCCHHHHHHHHHHHH	19.60	25072903
140	Phosphorylation	LLYEEARYYQLQPMV HHHHHHHHHHHHHHH	11.56	25072903
141	Phosphorylation	LYEEARYYQLQPMVR HHHHHHHHHHHHHHH	9.37	25072903
163	Phosphorylation	EQEQRRRSRACDCLV HHHHHHHHHCCCEEE	23.55	23927012
204	Phosphorylation	TGDVMCNSVNAGWNQ CCCEECCCCCCCCCC	16.30	-
271	Phosphorylation	EERRPQPTPTAVRIK CCCCCCCCCCEEEEE	28.20	27732954
273	Phosphorylation	RRPQPTPTAVRIKQE CCCCCCCCEEEEECC	40.02	27732954
278	Sumoylation	TPTAVRIKQEPLD-- CCCEEEEECCCCC--	37.74	-
278	Sumoylation	TPTAVRIKQEPLD-- CCCEEEEECCCCC--	37.74	-

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 KCD15_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KCD15_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 KCD15_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WIPI1_HUMAN	WIPI1	physical	16169070
RENI_HUMAN	REN	physical	16169070
AP2A_HUMAN	TFAP2A	physical	23382213
KCTD1_HUMAN	KCTD1	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956

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 KCD15_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASSSPECTROMETRY.	19369195 [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-31; SER-35 AND SER-38,AND MASS SPECTROMETRY.	18669648 [Abstract]