ZBT37_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZBT37_HUMAN
• UniProt AC: Q5TC79
• Protein Name: Zinc finger and BTB domain-containing protein 37
• Gene Name: ZBTB37
• Organism: Homo sapiens (Human).
• Sequence Length: 503
• Subcellular Localization: Nucleus .
• Protein Description: May be involved in transcriptional regulation..
• Protein Sequence: MEKGGNIQLEIPDFSNSVLSHLNQLRMQGRLCDIVVNVQGQAFRAHKVVLAASSPYFRDHMSLNEMSTVSISVIKNPTVFEQLLSFCYTGRICLQLADIISYLTAASFLQMQHIIDKCTQILEGIHFKINVAEVEAELSQTRTKHQERPPESHRVTPNLNRSLSPRHNTPKGNRRGQVSAVLDIRELSPPEESTSPQIIEPSSDVESREPILRINRAGQWYVETGVADRGGRSDDEVRVLGAVHIKTENLEEWLGPENQPSGEDGSSAEEVTAMVIDTTGHGSVGQENYTLGSSGAKVARPTSSEVDRFSPSGSVVPLTERHRARSESPGRMDEPKQPSSQVEESAMMGVSGYVEYLREQEVSERWFRYNPRLTCIYCAKSFNQKGSLDRHMRLHMGITPFVCRMCGKKYTRKDQLEYHIRKHTGNKPFHCHVCGKSFPFQAILNQHFRKNHPGCIPLEGPHSISPETTVTSRGQAEEESPSQEETVAPGEAVQGSVSTTGPD

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
67	Phosphorylation	HMSLNEMSTVSISVI CCCCCCCCEEEEEEE	21.34	-
68	Phosphorylation	MSLNEMSTVSISVIK CCCCCCCEEEEEEEC	19.57	-
152	Phosphorylation	HQERPPESHRVTPNL CCCCCCCHHCCCCCC	23.51	27251275
156	Phosphorylation	PPESHRVTPNLNRSL CCCHHCCCCCCCCCC	13.35	27251275
162	Phosphorylation	VTPNLNRSLSPRHNT CCCCCCCCCCCCCCC	31.93	23927012
164	Phosphorylation	PNLNRSLSPRHNTPK CCCCCCCCCCCCCCC	22.57	30278072
188	Phosphorylation	VLDIRELSPPEESTS EEEHHHCCCCCCCCC	33.39	26657352
193	Phosphorylation	ELSPPEESTSPQIIE HCCCCCCCCCCCCCC	32.30	27732954
194	Phosphorylation	LSPPEESTSPQIIEP CCCCCCCCCCCCCCC	47.94	26657352
195	Phosphorylation	SPPEESTSPQIIEPS CCCCCCCCCCCCCCC	24.88	27732954
233	Phosphorylation	VADRGGRSDDEVRVL CCCCCCCCHHHCEEE	53.33	24275748
302	Phosphorylation	GAKVARPTSSEVDRF CCEEECCCCCCCCCC	39.05	28857561
303	Phosphorylation	AKVARPTSSEVDRFS CEEECCCCCCCCCCC	27.47	28857561
304	Phosphorylation	KVARPTSSEVDRFSP EEECCCCCCCCCCCC	44.08	28857561
310	Phosphorylation	SSEVDRFSPSGSVVP CCCCCCCCCCCCEEE	21.03	29255136
312	Phosphorylation	EVDRFSPSGSVVPLT CCCCCCCCCCEEECC	42.37	29255136
314	Phosphorylation	DRFSPSGSVVPLTER CCCCCCCCEEECCHH	25.03	29255136
319	Phosphorylation	SGSVVPLTERHRARS CCCEEECCHHHHHHC	25.55	23312004
326	Phosphorylation	TERHRARSESPGRMD CHHHHHHCCCCCCCC	41.25	26657352
326	O-linked_Glycosylation	TERHRARSESPGRMD CHHHHHHCCCCCCCC	41.25	30379171
328	Phosphorylation	RHRARSESPGRMDEP HHHHHCCCCCCCCCC	33.62	26657352
363	Phosphorylation	YLREQEVSERWFRYN HHHHCHHHHHHHHHC	22.23	22210691
385	Ubiquitination	CAKSFNQKGSLDRHM ECCCCCCCCCHHHHH	52.12	-
387	Phosphorylation	KSFNQKGSLDRHMRL CCCCCCCCHHHHHHH	33.85	24719451
413	Ubiquitination	CGKKYTRKDQLEYHI CCCCCCCHHHHHHHH	41.86	-
463	Phosphorylation	IPLEGPHSISPETTV EECCCCCCCCCCCCC	28.09	30108239
465	Phosphorylation	LEGPHSISPETTVTS CCCCCCCCCCCCCCC	21.50	25849741
468	Phosphorylation	PHSISPETTVTSRGQ CCCCCCCCCCCCCCC	29.92	30108239
469	Phosphorylation	HSISPETTVTSRGQA CCCCCCCCCCCCCCC	21.81	30108239
471	Phosphorylation	ISPETTVTSRGQAEE CCCCCCCCCCCCCCC	15.60	30108239
472	Phosphorylation	SPETTVTSRGQAEEE CCCCCCCCCCCCCCC	30.03	30108239
480	Phosphorylation	RGQAEEESPSQEETV CCCCCCCCCCCCCCC	32.88	28348404
482	Phosphorylation	QAEEESPSQEETVAP CCCCCCCCCCCCCCC	60.55	28348404

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

Oops, there are no upstream regulatory protein records of ZBT37_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ZBT37_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ZBT37_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of ZBT37_HUMAN !!

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.