dbPTM

ZBT7A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZBT7A_MOUSE
UniProt AC	O88939
Protein Name	Zinc finger and BTB domain-containing protein 7A
Gene Name	Zbtb7a
Organism	Mus musculus (Mouse).
Sequence Length	569
Subcellular Localization	Nucleus .
Protein Description	Plays a key role in the instruction of early lymphoid progenitors to develop into B lineage by repressing T-cell instructive Notch signals. Specifically represses the transcription of the CDKN2A gene. Efficiently abrogates E2F1-dependent CDKN2A transactivation/de-repression. Binds to the consensus sequence 5'-[GA][CA]GACCCCCCCCC-3'..
Protein Sequence	MAGGVDGPIGIPFPDHSSDILSGLNEQRTQGLLCDVVILVEGREFPTHRSVLAACSQYFKKLFTSGAVVDQQNVYEIDFVSAEALTALMDFAYTATLTVSTANVGDILSAARLLEIPAVSHVCADLLERQILAADDVGDASQPDGAGPTDQRNLLRAKEYLEFFRSNPMNSLPPTAFPWSGFGAPDDDLDATKEAVAAAVAAVAAGDCNGLDFYGPGPPADRPPAGDGDEGDSTPGLWPERDEDAPPGGLFPPPTAPPATTQNGHYGRAGAGTGEEEAAALSEAAPEPGDSPGFLSGAAEGEDGDAADVDGLAASTLLQQMMSSVGRAGDSDEESRTDDKGVMDYYLKYFSGAHEGDVYPAWSQKGEKKIRAKAFQKCPICEKVIQGAGKLPRHIRTHTGEKPYECNICKVRFTRQDKLKVHMRKHTGEKPYLCQQCGAAFAHNYDLKNHMRVHTGLRPYQCDSCCKTFVRSDHLHRHLKKDGCNGVPSRRGRKPRVRGVPPDVPAGAGAPPGLPDAPRNGQEKHFKDEEEDEEEASPDGSGRLNVAGSGGDDGAGGPAVATAEGNFAT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
141	Phosphorylation	ADDVGDASQPDGAGP CCCCCCCCCCCCCCC	47.16	25159016
149	Phosphorylation	QPDGAGPTDQRNLLR CCCCCCCCHHHHHHH	43.79	30635358
158	Ubiquitination	QRNLLRAKEYLEFFR HHHHHHHHHHHHHHH	40.22	-
273	Phosphorylation	YGRAGAGTGEEEAAA CCCCCCCCCHHHHHH	40.67	23649490
282	Phosphorylation	EEEAAALSEAAPEPG HHHHHHHHHHCCCCC	22.06	23649490
291	Phosphorylation	AAPEPGDSPGFLSGA HCCCCCCCCCCCCCC	32.60	25338131
296	Phosphorylation	GDSPGFLSGAAEGED CCCCCCCCCCCCCCC	24.91	23649490
315	Phosphorylation	DVDGLAASTLLQQMM CCCHHHHHHHHHHHH	17.61	23649490
331	Phosphorylation	SVGRAGDSDEESRTD HHCCCCCCCCHHCCC	46.10	25521595
335	Phosphorylation	AGDSDEESRTDDKGV CCCCCCHHCCCCCCH	38.13	25521595
337	Phosphorylation	DSDEESRTDDKGVMD CCCCHHCCCCCCHHH	58.80	25521595
345	Phosphorylation	DDKGVMDYYLKYFSG CCCCHHHHHHHHHCC	7.81	25777480
346	Phosphorylation	DKGVMDYYLKYFSGA CCCHHHHHHHHHCCC	7.77	25777480
390	Ubiquitination	KVIQGAGKLPRHIRT HHHCCCCCCCCCCCC	55.58	27667366
399	Phosphorylation	PRHIRTHTGEKPYEC CCCCCCCCCCCCEEC	46.56	25266776
427	Phosphorylation	KVHMRKHTGEKPYLC HHEEECCCCCCCCHH	50.50	21183079
432	Phosphorylation	KHTGEKPYLCQQCGA CCCCCCCCHHHHCCC	31.04	22817900
469	Ubiquitination	CDSCCKTFVRSDHLH CCHHHHHHHCHHHHH	2.35	27667366
489	Phosphorylation	DGCNGVPSRRGRKPR HCCCCCCCCCCCCCC	32.00	18779572
537	Phosphorylation	EEDEEEASPDGSGRL HHCHHHHCCCCCCCE	27.14	25521595
541	Phosphorylation	EEASPDGSGRLNVAG HHHCCCCCCCEEECC	28.28	25619855
549	Phosphorylation	GRLNVAGSGGDDGAG CCEEECCCCCCCCCC	29.84	30635358

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 ZBT7A_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZBT7A_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 ZBT7A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZBT7B_HUMAN	ZBTB7B	physical	11691585
CO4A_HUMAN	C4A	physical	26496610
CX6B1_HUMAN	COX6B1	physical	26496610
BAG6_HUMAN	BAG6	physical	26496610
CYH1_HUMAN	CYTH1	physical	26496610
FND3A_HUMAN	FNDC3A	physical	26496610
RBM26_HUMAN	RBM26	physical	26496610

Drug and Disease Associations

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

Regulatory Network of ZBT7A_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, AND MASSSPECTROMETRY.	19367708 [Abstract]
"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-331 AND SER-335, ANDMASS SPECTROMETRY.	17242355 [Abstract]
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells."; Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; J. Proteome Res. 6:3174-3186(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331 AND THR-337, ANDMASS SPECTROMETRY.	17622165 [Abstract]