dbPTM

BTBDA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BTBDA_HUMAN
UniProt AC	Q9BSF8
Protein Name	BTB/POZ domain-containing protein 10
Gene Name	BTBD10
Organism	Homo sapiens (Human).
Sequence Length	475
Subcellular Localization	Nucleus . Cytoplasm . Colocalizes with KCTD20 in filamentous structures.
Protein Description	Plays a major role as an activator of AKT family members by inhibiting PPP2CA-mediated dephosphorylation, thereby keeping AKTs activated. Plays a role in preventing motor neuronal death and accelerating the growth of pancreatic beta cells..
Protein Sequence	MAGRPHPYDGNSSDPENWDRKLHSRPRKLYKHSSTSSRIAKGGVDHTKMSLHGASGGHERSRDRRRSSDRSRDSSHERTESQLTPCIRNVTSPTRQHHVEREKDHSSSRPSSPRPQKASPNGSISSAGNSSRNSSQSSSDGSCKTAGEMVFVYENAKEGARNIRTSERVTLIVDNTRFVVDPSIFTAQPNTMLGRMFGSGREHNFTRPNEKGEYEVAEGIGSTVFRAILDYYKTGIIRCPDGISIPELREACDYLCISFEYSTIKCRDLSALMHELSNDGARRQFEFYLEEMILPLMVASAQSGERECHIVVLTDDDVVDWDEEYPPQMGEEYSQIIYSTKLYRFFKYIENRDVAKSVLKERGLKKIRLGIEGYPTYKEKVKKRPGGRPEVIYNYVQRPFIRMSWEKEEGKSRHVDFQCVKSKSITNLAAAAADIPQDQLVVMHPTPQVDELDILPIHPPSGNSDLDPDAQNPML

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MAGRPHPYDGNSSDP CCCCCCCCCCCCCCC	33.19	30108239
12	Phosphorylation	PHPYDGNSSDPENWD CCCCCCCCCCCCHHH	41.47	25159151
13	Phosphorylation	HPYDGNSSDPENWDR CCCCCCCCCCCHHHH	62.27	23401153
35	Phosphorylation	KLYKHSSTSSRIAKG HHHCCCCCCCCHHCC	33.46	30576142
37	Phosphorylation	YKHSSTSSRIAKGGV HCCCCCCCCHHCCCC	28.00	30576142
50	Phosphorylation	GVDHTKMSLHGASGG CCCCCCCCCCCCCCC	20.83	26852163
55	Phosphorylation	KMSLHGASGGHERSR CCCCCCCCCCCHHHC	50.31	25627689
67	Phosphorylation	RSRDRRRSSDRSRDS HHCHHHHCCCCCCCC	34.48	-
71	Phosphorylation	RRRSSDRSRDSSHER HHHCCCCCCCCHHHC	45.49	27251275
74	Phosphorylation	SSDRSRDSSHERTES CCCCCCCCHHHCHHH	32.27	23403867
75	Phosphorylation	SDRSRDSSHERTESQ CCCCCCCHHHCHHHH	33.39	23927012
79	Phosphorylation	RDSSHERTESQLTPC CCCHHHCHHHHHCHH	36.68	23403867
81	Phosphorylation	SSHERTESQLTPCIR CHHHCHHHHHCHHHH	29.85	23403867
84	Phosphorylation	ERTESQLTPCIRNVT HCHHHHHCHHHHHCC	14.42	23403867
91	Phosphorylation	TPCIRNVTSPTRQHH CHHHHHCCCCCHHHH	32.32	30266825
92	Phosphorylation	PCIRNVTSPTRQHHV HHHHHCCCCCHHHHH	21.71	30266825
94	Phosphorylation	IRNVTSPTRQHHVER HHHCCCCCHHHHHHH	42.61	30266825
106	Phosphorylation	VEREKDHSSSRPSSP HHHCCCCCCCCCCCC	39.89	30576142
107	Phosphorylation	EREKDHSSSRPSSPR HHCCCCCCCCCCCCC	27.26	30576142
108	Phosphorylation	REKDHSSSRPSSPRP HCCCCCCCCCCCCCC	51.75	25159151
111	Phosphorylation	DHSSSRPSSPRPQKA CCCCCCCCCCCCCCC	52.44	25159151
112	Phosphorylation	HSSSRPSSPRPQKAS CCCCCCCCCCCCCCC	27.84	25159151
119	Phosphorylation	SPRPQKASPNGSISS CCCCCCCCCCCCCCC	26.40	22199227
123	Phosphorylation	QKASPNGSISSAGNS CCCCCCCCCCCCCCC	26.41	23090842
125	Phosphorylation	ASPNGSISSAGNSSR CCCCCCCCCCCCCCC	18.81	23090842
126	Phosphorylation	SPNGSISSAGNSSRN CCCCCCCCCCCCCCC	38.23	23090842
130	Phosphorylation	SISSAGNSSRNSSQS CCCCCCCCCCCCCCC	29.74	23090842
131	Phosphorylation	ISSAGNSSRNSSQSS CCCCCCCCCCCCCCC	39.21	23090842
134	Phosphorylation	AGNSSRNSSQSSSDG CCCCCCCCCCCCCCC	28.75	23090842
135	Phosphorylation	GNSSRNSSQSSSDGS CCCCCCCCCCCCCCC	37.32	23090842
137	Phosphorylation	SSRNSSQSSSDGSCK CCCCCCCCCCCCCCC	33.48	25627689
138	Phosphorylation	SRNSSQSSSDGSCKT CCCCCCCCCCCCCCC	25.47	25627689
139	Phosphorylation	RNSSQSSSDGSCKTA CCCCCCCCCCCCCCC	51.76	25627689
142	Phosphorylation	SQSSSDGSCKTAGEM CCCCCCCCCCCCCEE	19.89	23090842
153	Phosphorylation	AGEMVFVYENAKEGA CCEEEEEEECHHCHH	7.63	-
157	Ubiquitination	VFVYENAKEGARNIR EEEEECHHCHHHCCC	69.16	21906983
165	Ubiquitination	EGARNIRTSERVTLI CHHHCCCCCCCEEEE	31.01	-
183	Phosphorylation	TRFVVDPSIFTAQPN CEEEECHHHHCCCCC	26.35	22798277
186	Phosphorylation	VVDPSIFTAQPNTML EECHHHHCCCCCCHH	23.78	22798277
191	Phosphorylation	IFTAQPNTMLGRMFG HHCCCCCCHHHHCCC	22.06	22798277
211	Ubiquitination	NFTRPNEKGEYEVAE CCCCCCCCCCEEEEC	64.78	21906983
219	Ubiquitination	GEYEVAEGIGSTVFR CCEEEECCCCHHHHH	21.59	-
223	Phosphorylation	VAEGIGSTVFRAILD EECCCCHHHHHHHHH	20.60	24719451
233	Ubiquitination	RAILDYYKTGIIRCP HHHHHHHHHCCEECC	33.76	-
234	Phosphorylation	AILDYYKTGIIRCPD HHHHHHHHCCEECCC	19.93	26552605
241	Ubiquitination	TGIIRCPDGISIPEL HCCEECCCCCCHHHH	71.35	-
244	Phosphorylation	IRCPDGISIPELREA EECCCCCCHHHHHHH	37.31	24719451
254	Phosphorylation	ELREACDYLCISFEY HHHHHCCEEEEEEEC	11.89	26552605
258	Phosphorylation	ACDYLCISFEYSTIK HCCEEEEEEECEEEE	15.84	26552605
261	Phosphorylation	YLCISFEYSTIKCRD EEEEEEECEEEECCH	14.76	26552605
262	Phosphorylation	LCISFEYSTIKCRDL EEEEEECEEEECCHH	19.23	26552605
263	Phosphorylation	CISFEYSTIKCRDLS EEEEECEEEECCHHH	24.45	26552605
347	Ubiquitination	TKLYRFFKYIENRDV HHHHHHHHHHHCHHH	42.48	-
357	Phosphorylation	ENRDVAKSVLKERGL HCHHHHHHHHHHCCC	23.97	21406692
377	Phosphorylation	GIEGYPTYKEKVKKR ECCCCCCHHHHHCCC	16.79	17924679
407	Ubiquitination	FIRMSWEKEEGKSRH EEECEEECCCCCCCC	55.60	-
421	Ubiquitination	HVDFQCVKSKSITNL CCCEEEEECHHHHHH	60.85	-
422	Phosphorylation	VDFQCVKSKSITNLA CCEEEEECHHHHHHH	15.96	26074081
424	Phosphorylation	FQCVKSKSITNLAAA EEEEECHHHHHHHHH	41.56	26074081
426	Phosphorylation	CVKSKSITNLAAAAA EEECHHHHHHHHHHC	31.13	26074081
429	Ubiquitination	SKSITNLAAAAADIP CHHHHHHHHHHCCCC	9.34	-

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 BTBDA_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
DLG5_HUMAN	DLG5	physical	16169070
CUL3_HUMAN	CUL3	physical	21988832

Drug and Disease Associations

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

Regulatory Network of BTBDA_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-377, AND MASSSPECTROMETRY.	17924679 [Abstract]