ZBT17_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZBT17_MOUSE
• UniProt AC: Q60821
• Protein Name: Zinc finger and BTB domain-containing protein 17
• Gene Name: Zbtb17
• Organism: Mus musculus (Mouse).
• Sequence Length: 794
• Subcellular Localization: Nucleus.
• Protein Description: Transcription factor that can function as an activator or repressor depending on its binding partners, and by targeting negative regulators of cell cycle progression. Has been shown to bind to the promoters of adenovirus major late protein and cyclin D1 and activate transcription. Required for early embryonic development during gastrulation. Plays a critical role in early lymphocyte development, where it is essential to prevent apoptosis in lymphoid precursors, allowing them to survive in response to IL7 and undergo proper lineage commitment. Represses RB1 transcription; this repression can be blocked by interaction with ZBTB49 (By similarity)..
• Protein Sequence: MDFPQHSQRVLEQLNQQRQLGLLCDCTFVVDGVDFKAHKAVLAACSEYFKMLFVDQKDVVHLDISNAAGLGQVLEFMYTAKLSLSPENVDDVLAVASFLQMQDIVTACHTLKSLAEPSSTTGESADASAVEGGDKRAKDEKAAATMLSRLDQARGSSSTGPGRELKEERGGQAESASSGAEQTEKADAPREPPPVELKPDPTSSMAAAEAEALSESSEQEMEVEPASKGEDGQEEEGAGPATVKEEGMHLDNGEPPEENEESAGTDSGQELGMEGQNLRSGTYGDRTESKAYGSIIHKCEDCGKEFTHTGNFKRHIRIHTGEKPFSCRECSKAFSDPAACKAHEKTHSPLKPYGCEECGKSYRLISLLNLHKKRHSGEARYRCGDCGKLFTTSGNLKRHQLVHSGQKPYQCDYCGRSFSDPTSKMRHLETHDTDKEHKCPHCDKKFNQVGNLKAHLKIHIADGPLKCRECGKQFTTSGNLKRHLRIHSGEKPYVCTHCQRQFADPGALQRHVRIHTGEKPCQCVICGKAFTQASSLIAHVRQHTGEKPYVCERCGKRFVQSSQLANHIRHHDNIRPHKCSVCSKAFVNVGDLSKHIIIHTGEKPYLCDKCGRGFNRVDNLRSHVKTVHQGKAGIKILEPEEGGEVSVVTVDDMVTLATEALAATAVTQLTVVPVGAAVTADETEVLKAEISKAVKQVQEEDPNTHILYACDSCGDKFLDANSLAQHVRIHTAQALVMFQTDADFYQQYGPGSTWPAGQMLQAGELVFRPRDGTEGQPTLAESPPTAPDCLPPAE

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
178	Phosphorylation	GQAESASSGAEQTEK CCCCCCCCCHHHHHC	41.56	-
346	Phosphorylation	ACKAHEKTHSPLKPY HHHHCCCCCCCCCCC	25.30	26643407
348	Phosphorylation	KAHEKTHSPLKPYGC HHCCCCCCCCCCCCC	36.84	26643407
388	Ubiquitination	YRCGDCGKLFTTSGN EEECCCCCEEECCCC	46.92	22184250
472	Ubiquitination	LKCRECGKQFTTSGN EECCCCCCEEECCCC	54.63	22184250

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ZBT17_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
388	K	ubiquitylation	Undergoes 'Lys-48'-linked polyubiquitination at Lys-388 and Lys-472 and subsequent proteasomal degradation in a TRAF2-dependent manner and upon TNFA stimulation.	22184250
472	K	ubiquitylation	Undergoes 'Lys-48'-linked polyubiquitination at Lys-388 and Lys-472 and subsequent proteasomal degradation in a TRAF2-dependent manner and upon TNFA stimulation.	22184250

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ZBT17_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IRF8_MOUSE	Irf8	physical	12904288

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Ubiquitylation

"Site-specific ubiquitination is required for relieving thetranscription factor Miz1-mediated suppression on TNF-alpha-inducedJNK activation and inflammation.";
Liu J., Yan J., Jiang S., Wen J., Chen L., Zhao Y., Lin A.;
Proc. Natl. Acad. Sci. U.S.A. 109:191-196(2012).
Cited for: UBIQUITINATION AT LYS-388 AND LYS-472, AND INTERACTION WITH TRAF2.
PubMed: 22184250