dbPTM

ZN326_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZN326_HUMAN
UniProt AC	Q5BKZ1
Protein Name	DBIRD complex subunit ZNF326
Gene Name	ZNF326
Organism	Homo sapiens (Human).
Sequence Length	582
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. May play a role in neuronal differentiation and is able to bind DNA and activate expression in vitro..
Protein Sequence	MDFEDDYTHSACRNTYQGFNGMDRDYGPGSYGGMDRDYGHGSYGGQRSMDSYLNQSYGMDNHSGGGGGSRFGPYESYDSRSSLGGRDLYRSGYGFNEPEQSRFGGSYGGRFESSYRNSLDSFGGRNQGGSSWEAPYSRSKLRPGFMEDRGRENYSSYSSFSSPHMKPAPVGSRGRGTPAYPESTFGSRNYDAFGGPSTGRGRGRGHMGDFGSIHRPGIVVDYQNKSTNVTVAAARGIKRKMMQPFNKPSGTFIKKPKLAKPMEKISLSKSPTKTDPKNEEEEKRRIEARREKQRRRREKNSEKYGDGYRMAFTCSFCKFRTFEEKDIELHLESSSHQETLDHIQKQTKFDKVVMEFLHECMVNKFKKTSIRKQQTNNQTEVVKIIEKDVMEGVTVDDHMMKVETVHCSACSVYIPALHSSVQQHLKSPDHIKGKQAYKEQIKRESVLTATSILNNPIVKARYERFVKGENPFEIQDHSQDQQIEGDEEDEEKIDEPIEEEEDEDEEEEAEEVGEVEEVEEVEEVREGGIEGEGNIQGVGEGGEVGVVGEVEGVGEVEEVEELEEETAKEEPADFPVEQPEEN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDFEDDYT -------CCCCHHCC	13.87	-
7	Phosphorylation	-MDFEDDYTHSACRN -CCCCHHCCCHHHCC	20.76	27642862
8	Phosphorylation	MDFEDDYTHSACRNT CCCCHHCCCHHHCCC	19.15	26552605
10	Phosphorylation	FEDDYTHSACRNTYQ CCHHCCCHHHCCCCC	22.67	25159151
16	Phosphorylation	HSACRNTYQGFNGMD CHHHCCCCCCCCCCC	15.36	27642862
30	Phosphorylation	DRDYGPGSYGGMDRD CCCCCCCCCCCCCCC	24.60	28555341
38	Phosphorylation	YGGMDRDYGHGSYGG CCCCCCCCCCCCCCC	16.35	28555341
41 (in isoform 3)	Acetylation	-	20.42	-
42	Phosphorylation	DRDYGHGSYGGQRSM CCCCCCCCCCCCHHH	18.22	28555341
48	Phosphorylation	GSYGGQRSMDSYLNQ CCCCCCHHHHHHHHH	21.03	28348404
51	Phosphorylation	GGQRSMDSYLNQSYG CCCHHHHHHHHHHCC	23.91	28450419
52	Phosphorylation	GQRSMDSYLNQSYGM CCHHHHHHHHHHCCC	12.86	28450419
56	Phosphorylation	MDSYLNQSYGMDNHS HHHHHHHHCCCCCCC	23.68	23401153
57	Phosphorylation	DSYLNQSYGMDNHSG HHHHHHHCCCCCCCC	13.50	28555341
63	Phosphorylation	SYGMDNHSGGGGGSR HCCCCCCCCCCCCCC	45.44	21712546
64 (in isoform 3)	Phosphorylation	-	31.08	-
66 (in isoform 3)	Phosphorylation	-	40.59	-
68 (in isoform 3)	Phosphorylation	-	20.94	-
69	Phosphorylation	HSGGGGGSRFGPYES CCCCCCCCCCCCCCC	27.93	29978859
74	Phosphorylation	GGSRFGPYESYDSRS CCCCCCCCCCCCCCC	20.20	28796482
76	Phosphorylation	SRFGPYESYDSRSSL CCCCCCCCCCCCCCC	28.53	29083192
77	Phosphorylation	RFGPYESYDSRSSLG CCCCCCCCCCCCCCC	13.14	29083192
79	Phosphorylation	GPYESYDSRSSLGGR CCCCCCCCCCCCCCH	26.32	30576142
81	Phosphorylation	YESYDSRSSLGGRDL CCCCCCCCCCCCHHH	33.59	23917254
82	Phosphorylation	ESYDSRSSLGGRDLY CCCCCCCCCCCHHHH	29.89	30576142
91	Phosphorylation	GGRDLYRSGYGFNEP CCHHHHHCCCCCCCH	23.86	28152594
93	Phosphorylation	RDLYRSGYGFNEPEQ HHHHHCCCCCCCHHH	21.57	20090780
95 (in isoform 3)	Phosphorylation	-	7.63	-
98 (in isoform 3)	Phosphorylation	-	46.13	-
101	Phosphorylation	GFNEPEQSRFGGSYG CCCCHHHCCCCCCCC	28.10	28555341
106	Phosphorylation	EQSRFGGSYGGRFES HHCCCCCCCCCCCCH	22.45	30108239
107 (in isoform 3)	Phosphorylation	-	27.20	-
107	Phosphorylation	QSRFGGSYGGRFESS HCCCCCCCCCCCCHH	27.20	23186163
109 (in isoform 3)	Phosphorylation	-	23.91	-
110	Methylation	FGGSYGGRFESSYRN CCCCCCCCCCHHCCC	28.00	115920465
113	Phosphorylation	SYGGRFESSYRNSLD CCCCCCCHHCCCCCH	29.92	30108239
114	Phosphorylation	YGGRFESSYRNSLDS CCCCCCHHCCCCCHH	22.40	30108239
115	Phosphorylation	GGRFESSYRNSLDSF CCCCCHHCCCCCHHC	24.08	30108239
118	Phosphorylation	FESSYRNSLDSFGGR CCHHCCCCCHHCCCC	25.26	25159151
121	Phosphorylation	SYRNSLDSFGGRNQG HCCCCCHHCCCCCCC	30.96	23911959
125	Methylation	SLDSFGGRNQGGSSW CCHHCCCCCCCCCCC	32.45	115386837
130	Phosphorylation	GGRNQGGSSWEAPYS CCCCCCCCCCCCCCC	38.82	21945579
131	Phosphorylation	GRNQGGSSWEAPYSR CCCCCCCCCCCCCCH	32.01	21945579
136	Phosphorylation	GSSWEAPYSRSKLRP CCCCCCCCCHHHCCC	24.62	21945579
137	Phosphorylation	SSWEAPYSRSKLRPG CCCCCCCCHHHCCCC	29.08	21945579
138	Methylation	SWEAPYSRSKLRPGF CCCCCCCHHHCCCCC	31.78	115386845
140	Sumoylation	EAPYSRSKLRPGFME CCCCCHHHCCCCCCC	47.61	-
140	Ubiquitination	EAPYSRSKLRPGFME CCCCCHHHCCCCCCC	47.61	-
140	Sumoylation	EAPYSRSKLRPGFME CCCCCHHHCCCCCCC	47.61	28112733
140	Acetylation	EAPYSRSKLRPGFME CCCCCHHHCCCCCCC	47.61	25953088
142	Methylation	PYSRSKLRPGFMEDR CCCHHHCCCCCCCCC	32.79	115920469
149	Methylation	RPGFMEDRGRENYSS CCCCCCCCCCCCCCC	32.53	54560843
154	Phosphorylation	EDRGRENYSSYSSFS CCCCCCCCCCCCCCC	8.34	21945579
155	Phosphorylation	DRGRENYSSYSSFSS CCCCCCCCCCCCCCC	34.09	21945579
156	Phosphorylation	RGRENYSSYSSFSSP CCCCCCCCCCCCCCC	20.76	21945579
157	Phosphorylation	GRENYSSYSSFSSPH CCCCCCCCCCCCCCC	11.46	21945579
158	Phosphorylation	RENYSSYSSFSSPHM CCCCCCCCCCCCCCC	27.19	23401153
159	Phosphorylation	ENYSSYSSFSSPHMK CCCCCCCCCCCCCCC	22.40	21945579
161	Phosphorylation	YSSYSSFSSPHMKPA CCCCCCCCCCCCCCC	44.93	21945579
162	Phosphorylation	SSYSSFSSPHMKPAP CCCCCCCCCCCCCCC	19.47	21945579
166	Methylation	SFSSPHMKPAPVGSR CCCCCCCCCCCCCCC	34.69	115920457
166	Acetylation	SFSSPHMKPAPVGSR CCCCCCCCCCCCCCC	34.69	26051181
172	Phosphorylation	MKPAPVGSRGRGTPA CCCCCCCCCCCCCCC	31.62	21945579
173	Dimethylation	KPAPVGSRGRGTPAY CCCCCCCCCCCCCCC	32.66	-
173	Methylation	KPAPVGSRGRGTPAY CCCCCCCCCCCCCCC	32.66	24129315
175	Dimethylation	APVGSRGRGTPAYPE CCCCCCCCCCCCCCC	44.71	-
175	Methylation	APVGSRGRGTPAYPE CCCCCCCCCCCCCCC	44.71	54560851
177 (in isoform 3)	Acetylation	-	11.91	-
188	Methylation	PESTFGSRNYDAFGG CCCCCCCCCCCCCCC	46.21	54560859
190	Phosphorylation	STFGSRNYDAFGGPS CCCCCCCCCCCCCCC	13.92	-
197	Phosphorylation	YDAFGGPSTGRGRGR CCCCCCCCCCCCCCC	46.93	22210691
198	Phosphorylation	DAFGGPSTGRGRGRG CCCCCCCCCCCCCCC	33.75	22210691
200	Dimethylation	FGGPSTGRGRGRGHM CCCCCCCCCCCCCCC	31.55	-
200	Methylation	FGGPSTGRGRGRGHM CCCCCCCCCCCCCCC	31.55	80701879
202	Dimethylation	GPSTGRGRGRGHMGD CCCCCCCCCCCCCCC	30.21	-
202	Methylation	GPSTGRGRGRGHMGD CCCCCCCCCCCCCCC	30.21	80701887
204	Dimethylation	STGRGRGRGHMGDFG CCCCCCCCCCCCCCC	30.40	-
204	Methylation	STGRGRGRGHMGDFG CCCCCCCCCCCCCCC	30.40	80701895
212	Phosphorylation	GHMGDFGSIHRPGIV CCCCCCCCCCCCEEE	18.40	29691806
215	Methylation	GDFGSIHRPGIVVDY CCCCCCCCCEEEEEE	29.48	115920473
221 (in isoform 3)	Phosphorylation	-	28.54	-
227	Phosphorylation	VDYQNKSTNVTVAAA EEECCCCCCCHHHHH	35.00	28555341
235	Dimethylation	NVTVAAARGIKRKMM CCHHHHHHCCHHHHC	42.51	-
235	Methylation	NVTVAAARGIKRKMM CCHHHHHHCCHHHHC	42.51	24129315
238	Methylation	VAAARGIKRKMMQPF HHHHHCCHHHHCCCC	49.11	24129315
238	"N6,N6-dimethyllysine"	VAAARGIKRKMMQPF HHHHHCCHHHHCCCC	49.11	-
239	Methylation	AAARGIKRKMMQPFN HHHHCCHHHHCCCCC	30.13	115386853
240	Acetylation	AARGIKRKMMQPFNK HHHCCHHHHCCCCCC	33.45	26051181
240	Sumoylation	AARGIKRKMMQPFNK HHHCCHHHHCCCCCC	33.45	28112733
247	Acetylation	KMMQPFNKPSGTFIK HHCCCCCCCCCCCCC	40.72	19608861
247	Sumoylation	KMMQPFNKPSGTFIK HHCCCCCCCCCCCCC	40.72	28112733
249	Phosphorylation	MQPFNKPSGTFIKKP CCCCCCCCCCCCCCC	52.66	23186163
251	Phosphorylation	PFNKPSGTFIKKPKL CCCCCCCCCCCCCCC	26.90	23917254
254	Sumoylation	KPSGTFIKKPKLAKP CCCCCCCCCCCCCCC	59.85	28112733
260	Sumoylation	IKKPKLAKPMEKISL CCCCCCCCCHHHCCC	56.16	-
260	Sumoylation	IKKPKLAKPMEKISL CCCCCCCCCHHHCCC	56.16	-
260	Ubiquitination	IKKPKLAKPMEKISL CCCCCCCCCHHHCCC	56.16	-
264	Sumoylation	KLAKPMEKISLSKSP CCCCCHHHCCCCCCC	31.20	-
264	Sumoylation	KLAKPMEKISLSKSP CCCCCHHHCCCCCCC	31.20	28112733
266	Phosphorylation	AKPMEKISLSKSPTK CCCHHHCCCCCCCCC	37.34	23927012
266	O-linked_Glycosylation	AKPMEKISLSKSPTK CCCHHHCCCCCCCCC	37.34	23301498
268	Phosphorylation	PMEKISLSKSPTKTD CHHHCCCCCCCCCCC	25.05	30266825
268	O-linked_Glycosylation	PMEKISLSKSPTKTD CHHHCCCCCCCCCCC	25.05	23301498
270	Phosphorylation	EKISLSKSPTKTDPK HHCCCCCCCCCCCCC	34.13	29255136
272	Phosphorylation	ISLSKSPTKTDPKNE CCCCCCCCCCCCCCH	54.38	29255136
272 (in isoform 3)	Phosphorylation	-	54.38	-
274	Phosphorylation	LSKSPTKTDPKNEEE CCCCCCCCCCCCHHH	61.07	22167270
277	Sumoylation	SPTKTDPKNEEEEKR CCCCCCCCCHHHHHH	78.70	-
277	Sumoylation	SPTKTDPKNEEEEKR CCCCCCCCCHHHHHH	78.70	-
294	Ubiquitination	EARREKQRRRREKNS HHHHHHHHHHHHHHH	45.18	21890473
294	Ubiquitination	EARREKQRRRREKNS HHHHHHHHHHHHHHH	45.18	21890473
301	Phosphorylation	RRRREKNSEKYGDGY HHHHHHHHHHHCCCH	46.67	20068231
303	Acetylation	RREKNSEKYGDGYRM HHHHHHHHHCCCHHH	55.12	25953088
304	Phosphorylation	REKNSEKYGDGYRMA HHHHHHHHCCCHHHE	19.19	20068231
308	Phosphorylation	SEKYGDGYRMAFTCS HHHHCCCHHHEEEEE	11.27	20068231
313	Phosphorylation	DGYRMAFTCSFCKFR CCHHHEEEEEECCEE	9.56	20068231
315	Phosphorylation	YRMAFTCSFCKFRTF HHHEEEEEECCEEEE	30.53	20068231
318	Acetylation	AFTCSFCKFRTFEEK EEEEEECCEEEECHH	35.55	25825284
325	Acetylation	KFRTFEEKDIELHLE CEEEECHHCEEEEEC	57.73	26051181
345	Ubiquitination	ETLDHIQKQTKFDKV HHHHHHHHHHHHHHH	60.37	-
351	Acetylation	QKQTKFDKVVMEFLH HHHHHHHHHHHHHHH	39.60	26051181
364	"N6,N6-dimethyllysine"	LHECMVNKFKKTSIR HHHHHHHHHHHHHHH	47.34	-
364	Methylation	LHECMVNKFKKTSIR HHHHHHHHHHHHHHH	47.34	116265663
364	Acetylation	LHECMVNKFKKTSIR HHHHHHHHHHHHHHH	47.34	25953088
369	Phosphorylation	VNKFKKTSIRKQQTN HHHHHHHHHHHCCCC	29.31	-
372	Sumoylation	FKKTSIRKQQTNNQT HHHHHHHHCCCCCCC	45.12	-
372	Sumoylation	FKKTSIRKQQTNNQT HHHHHHHHCCCCCCC	45.12	-
372	Ubiquitination	FKKTSIRKQQTNNQT HHHHHHHHCCCCCCC	45.12	-
379	Phosphorylation	KQQTNNQTEVVKIIE HCCCCCCCEEEEEEE	32.63	24114839
383	Acetylation	NNQTEVVKIIEKDVM CCCCEEEEEEEHHHH	43.04	19608861
383	Ubiquitination	NNQTEVVKIIEKDVM CCCCEEEEEEEHHHH	43.04	21890473
383 (in isoform 1)	Ubiquitination	-	43.04	21890473
387	Acetylation	EVVKIIEKDVMEGVT EEEEEEEHHHHCCCC	45.26	25825284
394	Phosphorylation	KDVMEGVTVDDHMMK HHHHCCCCCCCCEEE	29.13	20860994
401	Sumoylation	TVDDHMMKVETVHCS CCCCCEEEEEEEECC	29.37	28112733
413	Phosphorylation	HCSACSVYIPALHSS ECCHHHHHHHHHHHH	5.72	28122231
419	Phosphorylation	VYIPALHSSVQQHLK HHHHHHHHHHHHHHC	32.81	28122231
420	Phosphorylation	YIPALHSSVQQHLKS HHHHHHHHHHHHHCC	17.13	28122231
426	Ubiquitination	SSVQQHLKSPDHIKG HHHHHHHCCCCHHCC	58.79	-
427	Phosphorylation	SVQQHLKSPDHIKGK HHHHHHCCCCHHCCH	41.75	30576142
438	Sumoylation	IKGKQAYKEQIKRES HCCHHHHHHHHHHHH	46.27	-
438	Sumoylation	IKGKQAYKEQIKRES HCCHHHHHHHHHHHH	46.27	-
442	Sumoylation	QAYKEQIKRESVLTA HHHHHHHHHHHCHHH	50.21	-
445	Phosphorylation	KEQIKRESVLTATSI HHHHHHHHCHHHHHH	26.85	27067055
450	Phosphorylation	RESVLTATSILNNPI HHHCHHHHHHHCCHH	15.86	-
451	Phosphorylation	ESVLTATSILNNPIV HHCHHHHHHHCCHHH	23.71	-
459	Sumoylation	ILNNPIVKARYERFV HHCCHHHHHHHHHHH	28.06	-
459	Sumoylation	ILNNPIVKARYERFV HHCCHHHHHHHHHHH	28.06	28112733
459	Ubiquitination	ILNNPIVKARYERFV HHCCHHHHHHHHHHH	28.06	-
467	Sumoylation	ARYERFVKGENPFEI HHHHHHHCCCCCCCC	58.77	-
467	Sumoylation	ARYERFVKGENPFEI HHHHHHHCCCCCCCC	58.77	28112733
467	Ubiquitination	ARYERFVKGENPFEI HHHHHHHCCCCCCCC	58.77	-
478	Phosphorylation	PFEIQDHSQDQQIEG CCCCCCCCCCCCCCC	43.68	25159151

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of ZN326_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZN326_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of ZN326_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BRNP1_HUMAN	BRINP1	physical	22446626
ROA1_HUMAN	HNRNPA1	physical	22446626
RPB1_HUMAN	POLR2A	physical	22446626

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.

Regulatory Network of ZN326_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-247, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-137 AND SER-270, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"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-270, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270 AND THR-274, ANDMASS SPECTROMETRY.	17924679 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-274, AND MASSSPECTROMETRY.	17287340 [Abstract]