ZN740_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZN740_HUMAN
• UniProt AC: Q8NDX6
• Protein Name: Zinc finger protein 740
• Gene Name: ZNF740
• Organism: Homo sapiens (Human).
• Sequence Length: 193
• Subcellular Localization: Nucleus .
• Protein Description: May be involved in transcriptional regulation..
• Protein Sequence: MAQASLLACEGLAGVSLVPTAASKKMMLSQIASKQAENGERAGSPDVLRCSSQGHRKDSDKSRSRKDDDSLSEASHSKKTVKKVVVVEQNGSFQVKIPKNFVCEHCFGAFRSSYHLKRHILIHTGEKPFECDICDMRFIQKYHLERHKRVHSGEKPYQCERCHQCFSRTDRLLRHKRMCQGCQSKTSDGQFSL

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
5	Phosphorylation	---MAQASLLACEGL ---CCHHHHHHHCCC	16.31	22210691
16	Phosphorylation	CEGLAGVSLVPTAAS HCCCCCCCCCCCHHC	23.80	24043423
20	Phosphorylation	AGVSLVPTAASKKMM CCCCCCCCHHCHHHH	27.63	24043423
23	Phosphorylation	SLVPTAASKKMMLSQ CCCCCHHCHHHHHHH	30.28	24043423
24	Acetylation	LVPTAASKKMMLSQI CCCCHHCHHHHHHHH	39.71	25953088
25	Acetylation	VPTAASKKMMLSQIA CCCHHCHHHHHHHHH	27.35	26051181
34	Acetylation	MLSQIASKQAENGER HHHHHHHHHHHCCCC	44.50	25953088
34	Sumoylation	MLSQIASKQAENGER HHHHHHHHHHHCCCC	44.50	28112733
34	Sumoylation	MLSQIASKQAENGER HHHHHHHHHHHCCCC	44.50	-
44	Phosphorylation	ENGERAGSPDVLRCS HCCCCCCCCCCCHHC	19.55	29255136
51	Phosphorylation	SPDVLRCSSQGHRKD CCCCCHHCCCCCCCC	21.18	26074081
52	Phosphorylation	PDVLRCSSQGHRKDS CCCCHHCCCCCCCCC	43.75	26074081
64	Phosphorylation	KDSDKSRSRKDDDSL CCCCCCCCCCCCCCC	51.26	23312004
70	Phosphorylation	RSRKDDDSLSEASHS CCCCCCCCCHHHHHC	40.57	20873877
72	Phosphorylation	RKDDDSLSEASHSKK CCCCCCCHHHHHCCC	34.76	25849741
75	Phosphorylation	DDSLSEASHSKKTVK CCCCHHHHHCCCCCC	25.00	23312004
77	Phosphorylation	SLSEASHSKKTVKKV CCHHHHHCCCCCCEE	33.09	23312004
78	Acetylation	LSEASHSKKTVKKVV CHHHHHCCCCCCEEE	47.22	25953088
79	Acetylation	SEASHSKKTVKKVVV HHHHHCCCCCCEEEE	62.66	7693221
92	Phosphorylation	VVVEQNGSFQVKIPK EEEEECCEEEEEECC	21.76	28555341
96	Ubiquitination	QNGSFQVKIPKNFVC ECCEEEEEECCCEEE	42.37	21890473
99	Ubiquitination	SFQVKIPKNFVCEHC EEEEEECCCEEEHHH	67.50	23000965
112	Phosphorylation	HCFGAFRSSYHLKRH HHCCCHHHHHHHCCC	28.88	24719451
124	Phosphorylation	KRHILIHTGEKPFEC CCCEEEECCCCCCCC	39.79	28122231
142	Phosphorylation	DMRFIQKYHLERHKR CHHHHHHHHHHHHCC	8.68	18083107
152	Phosphorylation	ERHKRVHSGEKPYQC HHHCCCCCCCCCCCC	45.87	29496963
155	Acetylation	KRVHSGEKPYQCERC CCCCCCCCCCCCCCH	53.18	25825284
157	Phosphorylation	VHSGEKPYQCERCHQ CCCCCCCCCCCCHHH	36.54	27794612

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

Oops, there are no upstream regulatory protein records of ZN740_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ZN740_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 ZN740_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND MASSSPECTROMETRY.
PubMed: 18669648

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND MASSSPECTROMETRY.
PubMed: 18691976

"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND MASSSPECTROMETRY.
PubMed: 19007248

"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND MASSSPECTROMETRY.
PubMed: 16964243