ZN235_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZN235_HUMAN
• UniProt AC: Q14590
• Protein Name: Zinc finger protein 235
• Gene Name: ZNF235
• Organism: Homo sapiens (Human).
• Sequence Length: 738
• Subcellular Localization: Nucleus .
• Protein Description: May be involved in transcriptional regulation..
• Protein Sequence: MTKFQEAVTFKDVAVAFTEEELGLLDSAQRKLYRDVMLENFRNLVSVGHQSFKPDMISQLEREEKLWMKELQTQRGKHSGDRNQNEMATLHKAGLRCFSLGELSCWQIKRHIASKLARSQDSMINIEGKSSQFPKHHDSPCQVGAGESIQASVDDNCLVNHIGDHSSIIENQEFPTGKVPNSWSKIYLNETQNYQRSCKQTQMKNKLCIFAPYVDIFSCISHHHDDNIVHKRDKVHSNSDCGKDTLKVSPLTQRSIHTGQKTYQGNECEEAFNDSSSLELHKQVHLGKKSPACSTHEKDTSYSSGIPVQQSVRTGKKRYWCHECGKGFSQSSNLQTHQRVHTGEKPYTCHECGKSFNQSSHLYAHLPIHTGEKPYRCDSCGKGFSRSTDLNIHCRVHTGEKPYKCEVCGKGFTQRSHLQAHERIHTGEKPYKCGDCGKRFSCSSNLHTHQRVHTEEKPYKCDECGKCFSLSFNLHSHQRVHTGEKPYKCEECGKGFSSASSFQSHQRVHTGEKPFRCNVCGKGFSQSSYFQAHQRVHTGEKPYKCEVCGKRFNWSLNLHNHQRVHTGEKPYKCEECGKGFSQASNLQAHQSVHTGEKPFKCDACQKRFSQASHLQAHQRVHTGEKPYKCDTCGKAFSQRSNLQVHQIIHTGEKPFKCEECGKEFSWSAGLSAHQRVHTGEKPYTCQQCGKGFSQASHFHTHQRVHTGERPYICDVCCKGFSQRSHLIYHQRVHTGGNL

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
2	Phosphorylation	------MTKFQEAVT ------CCHHHHCEE	40.33	29514088
9	Phosphorylation	TKFQEAVTFKDVAVA CHHHHCEEHHHHEEE	31.83	29514088
31	Sumoylation	LLDSAQRKLYRDVML CCHHHHHHHHHHHHH	37.48	-
31	Sumoylation	LLDSAQRKLYRDVML CCHHHHHHHHHHHHH	37.48	-
104	Phosphorylation	CFSLGELSCWQIKRH EEECCCCCHHHHHHH	14.70	-
131	Phosphorylation	INIEGKSSQFPKHHD EECCCCHHCCCCCCC	39.05	30631047
239	Phosphorylation	RDKVHSNSDCGKDTL CCCCCCCCCCCCCEE	36.97	-
245	Phosphorylation	NSDCGKDTLKVSPLT CCCCCCCEEEECCCC	31.78	23312004
249	Phosphorylation	GKDTLKVSPLTQRSI CCCEEEECCCCEEEE	16.77	23312004
255	Phosphorylation	VSPLTQRSIHTGQKT ECCCCEEEEECCCCE	14.65	-
342	Phosphorylation	QTHQRVHTGEKPYTC CCCCCEECCCCCEEH	44.15	-
370	Phosphorylation	YAHLPIHTGEKPYRC EEECCCCCCCCCEEC	47.99	29496963
373	Sumoylation	LPIHTGEKPYRCDSC CCCCCCCCCEECCCC	49.01	-
373	Ubiquitination	LPIHTGEKPYRCDSC CCCCCCCCCEECCCC	49.01	-
373	Sumoylation	LPIHTGEKPYRCDSC CCCCCCCCCEECCCC	49.01	-
387	Phosphorylation	CGKGFSRSTDLNIHC CCCCCCCCCCCEEEE	25.69	27794612
388	Phosphorylation	GKGFSRSTDLNIHCR CCCCCCCCCCEEEEE	43.31	27794612
398	Phosphorylation	NIHCRVHTGEKPYKC EEEEEEECCCCCEEE	44.15	29496963
401	Sumoylation	CRVHTGEKPYKCEVC EEEECCCCCEEEEEC	55.80	-
401	Ubiquitination	CRVHTGEKPYKCEVC EEEECCCCCEEEEEC	55.80	-
401	Sumoylation	CRVHTGEKPYKCEVC EEEECCCCCEEEEEC	55.80	-
403	Phosphorylation	VHTGEKPYKCEVCGK EECCCCCEEEEECCC	39.06	-
404	Sumoylation	HTGEKPYKCEVCGKG ECCCCCEEEEECCCC	32.23	-
404	Sumoylation	HTGEKPYKCEVCGKG ECCCCCEEEEECCCC	32.23	-
426	Phosphorylation	QAHERIHTGEKPYKC HHHCCCCCCCCCEEC	44.67	29496963
457	Sumoylation	QRVHTEEKPYKCDEC CCCCCCCCCEECCCC	47.63	-
457	Sumoylation	QRVHTEEKPYKCDEC CCCCCCCCCEECCCC	47.63	-
482	Phosphorylation	HSHQRVHTGEKPYKC CCCCCEECCCCCEEC	44.15	29496963
485	Sumoylation	QRVHTGEKPYKCEEC CCEECCCCCEECCCC	55.80	-
485	Sumoylation	QRVHTGEKPYKCEEC CCEECCCCCEECCCC	55.80	-
485	Ubiquitination	QRVHTGEKPYKCEEC CCEECCCCCEECCCC	55.80	-
487	Phosphorylation	VHTGEKPYKCEECGK EECCCCCEECCCCCC	39.06	-
488	Sumoylation	HTGEKPYKCEECGKG ECCCCCEECCCCCCC	43.63	-
488	Ubiquitination	HTGEKPYKCEECGKG ECCCCCEECCCCCCC	43.63	-
488	Sumoylation	HTGEKPYKCEECGKG ECCCCCEECCCCCCC	43.63	-
510	Phosphorylation	QSHQRVHTGEKPFRC HCCCCCCCCCCCEEC	44.15	-
538	Phosphorylation	QAHQRVHTGEKPYKC HHHCCCCCCCCCEEE	44.15	29496963
541	Ubiquitination	QRVHTGEKPYKCEVC CCCCCCCCCEEEEEC	55.80	-
541	Sumoylation	QRVHTGEKPYKCEVC CCCCCCCCCEEEEEC	55.80	-
541	Sumoylation	QRVHTGEKPYKCEVC CCCCCCCCCEEEEEC	55.80	-
543	Phosphorylation	VHTGEKPYKCEVCGK CCCCCCCEEEEECCC	39.06	-
544	Sumoylation	HTGEKPYKCEVCGKR CCCCCCEEEEECCCE	32.23	-
544	Sumoylation	HTGEKPYKCEVCGKR CCCCCCEEEEECCCE	32.23	-
566	Phosphorylation	HNHQRVHTGEKPYKC CCCCCCCCCCCCEEC	44.15	29496963
569	Sumoylation	QRVHTGEKPYKCEEC CCCCCCCCCEECCCC	55.80	-
569	Sumoylation	QRVHTGEKPYKCEEC CCCCCCCCCEECCCC	55.80	-
569	Ubiquitination	QRVHTGEKPYKCEEC CCCCCCCCCEECCCC	55.80	-
571	Phosphorylation	VHTGEKPYKCEECGK CCCCCCCEECCCCCC	39.06	-
572	Sumoylation	HTGEKPYKCEECGKG CCCCCCEECCCCCCC	43.63	-
572	Ubiquitination	HTGEKPYKCEECGKG CCCCCCEECCCCCCC	43.63	-
572	Sumoylation	HTGEKPYKCEECGKG CCCCCCEECCCCCCC	43.63	-
594	Phosphorylation	QAHQSVHTGEKPFKC HHHCCCCCCCCCCCC	44.90	23898821
622	Phosphorylation	QAHQRVHTGEKPYKC HHHCCHHCCCCCCCC	44.15	29496963
625	Sumoylation	QRVHTGEKPYKCDTC CCHHCCCCCCCCCCC	55.80	-
625	Ubiquitination	QRVHTGEKPYKCDTC CCHHCCCCCCCCCCC	55.80	-
625	Sumoylation	QRVHTGEKPYKCDTC CCHHCCCCCCCCCCC	55.80	-
631	Phosphorylation	EKPYKCDTCGKAFSQ CCCCCCCCCCHHHHH	32.40	-
650	Phosphorylation	QVHQIIHTGEKPFKC EEEEEEECCCCCEEC	36.31	18669648
656	Sumoylation	HTGEKPFKCEECGKE ECCCCCEECCCCCCE	49.62	-
656	Sumoylation	HTGEKPFKCEECGKE ECCCCCEECCCCCCE	49.62	-
678	Phosphorylation	SAHQRVHTGEKPYTC CCCCCCCCCCCCEEC	44.15	-
706	Phosphorylation	HTHQRVHTGERPYIC CCCCCCCCCCCCEEC	37.57	-

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

Oops, there are no upstream regulatory protein records of ZN235_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ZN235_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 ZN235_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of ZN235_HUMAN !!

Drug and Disease Associations

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