ZN326_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZN326_MOUSE
• UniProt AC: O88291
• Protein Name: DBIRD complex subunit ZNF326
• Gene Name: Znf326
• Organism: Mus musculus (Mouse).
• Sequence Length: 580
• Subcellular Localization: Nucleus matrix .
• Protein Description: Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions (By similarity). May also play a role in neuronal differentiation. Able to bind DNA and activate expression in vitro..
• Protein Sequence: MDFEDDYVHSTCRGAYQDFNGMDRDYGPGSYGGLDRDYGHGSYGGQRSMDSYLNQSYGMDNHSGGGGGSRFGPYESYDSRSSLGGRDLYRSGYGFNEPEQTRFGGSYGGRFESSYRNSLDSFGGRNQGGSSWEAPYSRSKLRPGFMEDRGRENYSSYSSFSSPHMKPAPVGSRGRGTPAYPESTFGSRSYDAFGGPSTGRGRGRGHMGDFGSFHRPGIIVDYQNKPANVTIATARGIKRKMMQIFIKPGGAFIKKPKLAKPMDKMNLSKSPTKTDPKNEEEEKRRIEARREKQRRRREKNSEKYGDGYRMAFTCSFCKFRTFEEKDIELHLESSSHQETLDHIQKQTKFDKVVMEFLHECMVNKFKKASIRKQQTLNHPEAYKIIEKDIMEGVTADDHMMKVETVHCSACSVYIPALHSSVQLHLKSPDHSKGKQAYKEQIKRESVLTATSILNNPIVKARYERFVKGENPFEIQDHPQDQQIEGDEEDEEKIDEPIEEEEEEEEEEEEEGEEAGSVEEEGDVEGEEGTAEAAAAGEADAVGEAEGAGEAEEAEEEEEEEGTQEFAAQACATEQCEHRQM

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
30	Phosphorylation	DRDYGPGSYGGLDRD CCCCCCCCCCCCCCC	24.60	28066266
42	Phosphorylation	DRDYGHGSYGGQRSM CCCCCCCCCCCCHHH	18.22	27841257
48	Phosphorylation	GSYGGQRSMDSYLNQ CCCCCCHHHHHHHHH	21.03	22817900
56	Phosphorylation	MDSYLNQSYGMDNHS HHHHHHHHCCCCCCC	23.68	25338131
63	Phosphorylation	SYGMDNHSGGGGGSR HCCCCCCCCCCCCCC	45.44	27841257
69	Phosphorylation	HSGGGGGSRFGPYES CCCCCCCCCCCCCCC	27.93	-
76	Phosphorylation	SRFGPYESYDSRSSL CCCCCCCCCCCCCCC	28.53	22871156
77	Phosphorylation	RFGPYESYDSRSSLG CCCCCCCCCCCCCCC	13.14	22871156
79	Phosphorylation	GPYESYDSRSSLGGR CCCCCCCCCCCCCCH	26.32	22871156
81	Phosphorylation	YESYDSRSSLGGRDL CCCCCCCCCCCCHHH	33.59	25338131
82	Phosphorylation	ESYDSRSSLGGRDLY CCCCCCCCCCCHHHH	29.89	29514104
91	Phosphorylation	GGRDLYRSGYGFNEP CCHHHHHCCCCCCCC	23.86	24719451
106	Phosphorylation	EQTRFGGSYGGRFES CCCCCCCCCCCCCCH	22.45	28066266
107	Phosphorylation	QTRFGGSYGGRFESS CCCCCCCCCCCCCHH	27.20	28066266
114	Phosphorylation	YGGRFESSYRNSLDS CCCCCCHHHCCCCHH	22.40	-
118	Phosphorylation	FESSYRNSLDSFGGR CCHHHCCCCHHCCCC	25.26	26370283
121	Phosphorylation	SYRNSLDSFGGRNQG HHCCCCHHCCCCCCC	30.96	26370283
130	Phosphorylation	GGRNQGGSSWEAPYS CCCCCCCCCCCCCCC	38.82	28066266
131	Phosphorylation	GRNQGGSSWEAPYSR CCCCCCCCCCCCCCH	32.01	28066266
136	Phosphorylation	GSSWEAPYSRSKLRP CCCCCCCCCHHHCCC	24.62	28066266
137	Phosphorylation	SSWEAPYSRSKLRPG CCCCCCCCHHHCCCC	29.08	28066266
149	Methylation	RPGFMEDRGRENYSS CCCCCCCCCCCCCCC	32.53	54560845
155	Phosphorylation	DRGRENYSSYSSFSS CCCCCCCCCCCCCCC	34.09	29472430
156	Phosphorylation	RGRENYSSYSSFSSP CCCCCCCCCCCCCCC	20.76	29472430
157	Phosphorylation	GRENYSSYSSFSSPH CCCCCCCCCCCCCCC	11.46	29472430
158	Phosphorylation	RENYSSYSSFSSPHM CCCCCCCCCCCCCCC	27.19	29472430
159	Phosphorylation	ENYSSYSSFSSPHMK CCCCCCCCCCCCCCC	22.40	29472430
161	Phosphorylation	YSSYSSFSSPHMKPA CCCCCCCCCCCCCCC	44.93	26643407
162	Phosphorylation	SSYSSFSSPHMKPAP CCCCCCCCCCCCCCC	19.47	26643407
173	Methylation	KPAPVGSRGRGTPAY CCCCCCCCCCCCCCC	32.66	24391489
189	Phosphorylation	ESTFGSRSYDAFGGP CCCCCCCCCCCCCCC	29.12	22817900
190	Phosphorylation	STFGSRSYDAFGGPS CCCCCCCCCCCCCCC	15.35	22817900
212	Phosphorylation	GHMGDFGSFHRPGII CCCCCCCCCCCCCEE	20.20	-
235	Methylation	NVTIATARGIKRKMM CEEEEECHHHHHHHH	42.91	24129315
247	Acetylation	KMMQIFIKPGGAFIK HHHHEEECCCCCCCC	27.19	-
268	Phosphorylation	PMDKMNLSKSPTKTD CCCCCCCCCCCCCCC	26.53	23984901
270	Phosphorylation	DKMNLSKSPTKTDPK CCCCCCCCCCCCCCC	34.13	26824392
272	Phosphorylation	MNLSKSPTKTDPKNE CCCCCCCCCCCCCCH	54.38	23684622
274	Phosphorylation	LSKSPTKTDPKNEEE CCCCCCCCCCCCHHH	61.07	25619855
450	Phosphorylation	RESVLTATSILNNPI HHHCHHHHHHHCCHH	15.86	20139300
459	Ubiquitination	ILNNPIVKARYERFV HHCCHHHHHHHHHHH	28.06	22790023

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

Oops, there are no upstream regulatory protein records of ZN326_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ZN326_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ZN326_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ZN326_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND TYR-190, ANDMASS SPECTROMETRY.
PubMed: 19367708