ZN670_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZN670_HUMAN
• UniProt AC: Q9BS34
• Protein Name: Zinc finger protein 670
• Gene Name: ZNF670
• Organism: Homo sapiens (Human).
• Sequence Length: 389
• Subcellular Localization: Nucleus .
• Protein Description: May be involved in transcriptional regulation..
• Protein Sequence: MDSVSFEDVAVAFTQEEWALLDPSQKNLYRDVMQEIFRNLASVGNKSEDQNIQDDFKNPGRNLSSHVVERLFEIKEGSQYGETFSQDSNLNLNKKVSTGVKPCECSVCGKVFICHSALHRHILSHIGNKLFECEECPEKLYHCKQCGKAFISLTSVDRHMVTHTSNGPYKGPVYEKPFDFPSVFQMPQSTYTGEKTYKCKHCDKAFNYSSYLREHERTHTGEKPYACKKCGKSFTFSSSLRQHERSHTGEKPYECKECGKAFSRSTYLGIHERTHTGEKPYECIKCGKAFRCSRVLRVHERTHSGEKPYECKQCGKAFKYSSNLCEHERTHTGVKPYGCKECGKSFTSSSALRSHERTHTGEKPYECKKCGKAFSCSSSLRKHERAYMW

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
57	Ubiquitination	QNIQDDFKNPGRNLS CCCCHHCCCCCCCHH	70.04	29967540
64	Phosphorylation	KNPGRNLSSHVVERL CCCCCCHHHHHHHHH	23.19	25159151
65	Phosphorylation	NPGRNLSSHVVERLF CCCCCHHHHHHHHHH	24.38	23836654
93	Ubiquitination	QDSNLNLNKKVSTGV CCCCCCCCCCCCCCC	40.82	29967540
94	Ubiquitination	DSNLNLNKKVSTGVK CCCCCCCCCCCCCCC	58.69	29967540
162	Phosphorylation	SVDRHMVTHTSNGPY EEECCCEEECCCCCC	16.32	-
165	Phosphorylation	RHMVTHTSNGPYKGP CCCEEECCCCCCCCC	31.98	-
169	Phosphorylation	THTSNGPYKGPVYEK EECCCCCCCCCCCCC	29.94	-
204	Methylation	YKCKHCDKAFNYSSY EECCCCCCCCCHHHH	61.34	23644510
209	Phosphorylation	CDKAFNYSSYLREHE CCCCCCHHHHHHHHC	17.38	28555341
218	Phosphorylation	YLREHERTHTGEKPY HHHHHCCCCCCCCCC	22.32	-
220	Phosphorylation	REHERTHTGEKPYAC HHHCCCCCCCCCCCC	46.56	-
223	Ubiquitination	ERTHTGEKPYACKKC CCCCCCCCCCCCCCC	44.68	-
232	Sumoylation	YACKKCGKSFTFSSS CCCCCCCCEEEECHH	52.44	-
238	Phosphorylation	GKSFTFSSSLRQHER CCEEEECHHHHHHHH	29.24	28555341
253	Phosphorylation	SHTGEKPYECKECGK HCCCCCCCCHHHHHC	45.05	-
256	Sumoylation	GEKPYECKECGKAFS CCCCCCHHHHHCCCC	44.06	-
256	Sumoylation	GEKPYECKECGKAFS CCCCCCHHHHHCCCC	44.06	-
265	Phosphorylation	CGKAFSRSTYLGIHE HHCCCCCCCEEEEEC	21.87	26699800
266	Phosphorylation	GKAFSRSTYLGIHER HCCCCCCCEEEEECC	22.96	26699800
274	Phosphorylation	YLGIHERTHTGEKPY EEEEECCCCCCCCCE	22.32	-
276	Phosphorylation	GIHERTHTGEKPYEC EEECCCCCCCCCEEE	46.56	28152594
281	Phosphorylation	THTGEKPYECIKCGK CCCCCCCEEEEECCC	34.20	28152594
302	Phosphorylation	VLRVHERTHSGEKPY EEEEECCCCCCCCCE	19.87	27794612
304	Phosphorylation	RVHERTHSGEKPYEC EEECCCCCCCCCEEE	48.29	27251275
312	Sumoylation	GEKPYECKQCGKAFK CCCCEEECCCCCEEE	36.36	-
312	Sumoylation	GEKPYECKQCGKAFK CCCCEEECCCCCEEE	36.36	-
337	Phosphorylation	THTGVKPYGCKECGK CCCCCCCCCCCCCCC	29.45	22468782
345	Phosphorylation	GCKECGKSFTSSSAL CCCCCCCCCCCHHHH	21.02	-
347	Phosphorylation	KECGKSFTSSSALRS CCCCCCCCCHHHHHH	34.49	-
349	Phosphorylation	CGKSFTSSSALRSHE CCCCCCCHHHHHHCC	19.30	-
358	Phosphorylation	ALRSHERTHTGEKPY HHHHCCCCCCCCCCC	22.32	29396449
360	Phosphorylation	RSHERTHTGEKPYEC HHCCCCCCCCCCCCC	46.56	29496963
362	Ubiquitination	HERTHTGEKPYECKK CCCCCCCCCCCCCCC	52.60	22505724
363	Ubiquitination	ERTHTGEKPYECKKC CCCCCCCCCCCCCCC	55.00	22505724
369	Ubiquitination	EKPYECKKCGKAFSC CCCCCCCCCCCEEEC	60.93	-
379	Phosphorylation	KAFSCSSSLRKHERA CEEECCHHHHHHHHH	18.85	25627689

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

Oops, there are no upstream regulatory protein records of ZN670_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ZN670_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 ZN670_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MDFI_HUMAN	MDFI	physical	19060904
SUV91_HUMAN	SUV39H1	physical	23455924
KR107_HUMAN	KRTAP10-7	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-281, AND MASSSPECTROMETRY.
PubMed: 15592455