TIF1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TIF1B_HUMAN
• UniProt AC: Q13263
• Protein Name: Transcription intermediary factor 1-beta
• Gene Name: TRIM28
• Organism: Homo sapiens (Human).
• Sequence Length: 835
• Subcellular Localization: Nucleus . Associated with centromeric heterochromatin during cell differentiation through CBX1..
• Protein Description: Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteosomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg). [PubMed: 23543754 Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells]
• Protein Sequence: MAASAAAASAAAASAASGSPGPGEGSAGGEKRSTAPSAAASASASAAASSPAGGGAEALELLEHCGVCRERLRPEREPRLLPCLHSACSACLGPAAPAAANSSGDGGAAGDGTVVDCPVCKQQCFSKDIVENYFMRDSGSKAATDAQDANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRSTGPAKSRDGERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKSTKEVRSSIRQVSDVQKRVQVDVKMAILQIMKELNKRGRVLVNDAQKVTEGQQERLERQHWTMTKIQKHQEHILRFASWALESDNNTALLLSKKLIYFQLHRALKMIVDPVEPHGEMKFQWDLNAWTKSAEAFGKIVAERPGTNSTGPAPMAPPRAPGPLSKQGSGSSQPMEVQEGYGFGSGDDPYSSAEPHVSGVKRSRSGEGEVSGLMRKVPRVSLERLDLDLTADSQPPVFKVFPGSTTEDYNLIVIERGAAAAATGQPGTAPAGTPGAPPLAGMAIVKEEETEAAIGAPPTATEGPETKPVLMALAEGPGAEGPRLASPSGSTSSGLEVVAPEGTSAPGGGPGTLDDSATICRVCQKPGDLVMCNQCEFCFHLDCHLPALQDVPGEEWSCSLCHVLPDLKEEDGSLSLDGADSTGVVAKLSPANQRKCERVLLALFCHEPCRPLHQLATDSTFSLDQPGGTLDLTLIRARLQEKLSPPYSSPQEFAQDVGRMFKQFNKLTEDKADVQSIIGLQRFFETRMNEAFGDTKFSAVLVEPPPMSLPGAGLSSQELSGGPGDGP

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	Acetylation	------MAASAAAAS ------CHHHHHHHH	15.32	20068231
4	Phosphorylation	----MAASAAAASAA ----CHHHHHHHHHH	14.65	25867546
9	Phosphorylation	AASAAAASAAAASAA HHHHHHHHHHHHHHH	17.45	23401153
14	Phosphorylation	AASAAAASAASGSPG HHHHHHHHHHCCCCC	21.46	29255136
17	Phosphorylation	AAAASAASGSPGPGE HHHHHHHCCCCCCCC	39.25	29255136
19	Phosphorylation	AASAASGSPGPGEGS HHHHHCCCCCCCCCC	24.96	29255136
26	Phosphorylation	SPGPGEGSAGGEKRS CCCCCCCCCCCCCCC	21.31	29255136
31	Sumoylation	EGSAGGEKRSTAPSA CCCCCCCCCCCCCCH	55.73	-
31	2-Hydroxyisobutyrylation	EGSAGGEKRSTAPSA CCCCCCCCCCCCCCH	55.73	-
31	Acetylation	EGSAGGEKRSTAPSA CCCCCCCCCCCCCCH	55.73	23749302
31	Sumoylation	EGSAGGEKRSTAPSA CCCCCCCCCCCCCCH	55.73	28112733
31	Ubiquitination	EGSAGGEKRSTAPSA CCCCCCCCCCCCCCH	55.73	24816145
33	Phosphorylation	SAGGEKRSTAPSAAA CCCCCCCCCCCCHHH	39.73	23927012
34	Phosphorylation	AGGEKRSTAPSAAAS CCCCCCCCCCCHHHH	46.77	23927012
37	Phosphorylation	EKRSTAPSAAASASA CCCCCCCCHHHHHHH	28.24	23927012
41	Phosphorylation	TAPSAAASASASAAA CCCCHHHHHHHHHHH	20.31	30278072
43	Phosphorylation	PSAAASASASAAASS CCHHHHHHHHHHHCC	21.91	23927012
45	Phosphorylation	AAASASASAAASSPA HHHHHHHHHHHCCCC	18.88	30278072
49	Phosphorylation	ASASAAASSPAGGGA HHHHHHHCCCCCCHH	31.93	29255136
50	Phosphorylation	SASAAASSPAGGGAE HHHHHHCCCCCCHHH	17.65	29255136
68	Glutathionylation	LLEHCGVCRERLRPE HHHHCCCCHHHHCCC	1.96	22555962
102	Phosphorylation	AAPAAANSSGDGGAA CCCHHHHCCCCCCCC	30.85	23401153
103	Phosphorylation	APAAANSSGDGGAAG CCHHHHCCCCCCCCC	40.48	28464451
121	Acetylation	VVDCPVCKQQCFSKD EEECHHHCCCCCCCH	43.57	26051181
127	Acetylation	CKQQCFSKDIVENYF HCCCCCCCHHHHHHC	31.08	26051181
127	Sumoylation	CKQQCFSKDIVENYF HCCCCCCCHHHHHHC	31.08	28112733
127	Ubiquitination	CKQQCFSKDIVENYF HCCCCCCCHHHHHHC	31.08	22817900
127 (in isoform 1)	Ubiquitination	-	31.08	21890473
131 (in isoform 2)	Ubiquitination	-	46.69	21890473
133	Phosphorylation	SKDIVENYFMRDSGS CCHHHHHHCCCCCCC	5.80	20873877
138	Phosphorylation	ENYFMRDSGSKAATD HHHCCCCCCCCCCCC	34.30	25159151
140	Phosphorylation	YFMRDSGSKAATDAQ HCCCCCCCCCCCCHH	24.07	22199227
156 (in isoform 2)	Ubiquitination	-	4.03	21890473
163	Phosphorylation	CEDNAPATSYCVECS CCCCCCCCEEEEECC	21.12	28348404
164	Phosphorylation	EDNAPATSYCVECSE CCCCCCCEEEEECCC	20.74	28348404
170	Phosphorylation	TSYCVECSEPLCETC CEEEEECCCCHHHHH	28.83	28348404
179 (in isoform 2)	Ubiquitination	-	42.45	21890473
184 (in isoform 2)	Ubiquitination	-	4.46	21890473
188	Sumoylation	HQRVKYTKDHTVRST HHHHCCCCCCCCEEC	44.41	-
188	2-Hydroxyisobutyrylation	HQRVKYTKDHTVRST HHHHCCCCCCCCEEC	44.41	-
188	Acetylation	HQRVKYTKDHTVRST HHHHCCCCCCCCEEC	44.41	23749302
188	Sumoylation	HQRVKYTKDHTVRST HHHHCCCCCCCCEEC	44.41	-
188	Ubiquitination	HQRVKYTKDHTVRST HHHHCCCCCCCCEEC	44.41	33845483
190 (in isoform 2)	Ubiquitination	-	28.02	21890473
193 (in isoform 2)	Ubiquitination	-	29.65	21890473
199	Sumoylation	VRSTGPAKSRDGERT CEECCCCCCCCCCEE	49.51	-
199	Sumoylation	VRSTGPAKSRDGERT CEECCCCCCCCCCEE	49.51	28112733
206	Phosphorylation	KSRDGERTVYCNVHK CCCCCCEEEEEEEEC	16.12	27080861
207 (in isoform 2)	Ubiquitination	-	6.85	21890473
208	Phosphorylation	RDGERTVYCNVHKHE CCCCEEEEEEEECCC	4.25	27080861
213	Acetylation	TVYCNVHKHEPLVLF EEEEEEECCCCEEEE	45.43	25953088
213	Ubiquitination	TVYCNVHKHEPLVLF EEEEEEECCCCEEEE	45.43	21906983
213 (in isoform 1)	Ubiquitination	-	45.43	21890473
214 (in isoform 2)	Ubiquitination	-	27.33	21890473
222 (in isoform 2)	Ubiquitination	-	47.25	21890473
223	Phosphorylation	PLVLFCESCDTLTCR CEEEEECCCCCEEEC	20.62	27080861
224	Glutathionylation	LVLFCESCDTLTCRD EEEEECCCCCEEECC	1.85	22555962
226	Phosphorylation	LFCESCDTLTCRDCQ EEECCCCCEEECCCC	28.44	27080861
228	Phosphorylation	CESCDTLTCRDCQLN ECCCCCEEECCCCCC	13.95	27080861
237 (in isoform 2)	Ubiquitination	-	34.70	21890473
238	2-Hydroxyisobutyrylation	DCQLNAHKDHQYQFL CCCCCCCCCHHHHHH	55.27	-
238	Acetylation	DCQLNAHKDHQYQFL CCCCCCCCCHHHHHH	55.27	25953088
238	Ubiquitination	DCQLNAHKDHQYQFL CCCCCCCCCHHHHHH	55.27	21906983
238 (in isoform 1)	Ubiquitination	-	55.27	21890473
242	Nitration	NAHKDHQYQFLEDAV CCCCCHHHHHHHHHH	9.60	-
242	Phosphorylation	NAHKDHQYQFLEDAV CCCCCHHHHHHHHHH	9.60	28152594
254	Sumoylation	DAVRNQRKLLASLVK HHHHHHHHHHHHHHH	37.78	-
254	Malonylation	DAVRNQRKLLASLVK HHHHHHHHHHHHHHH	37.78	26320211
254	Neddylation	DAVRNQRKLLASLVK HHHHHHHHHHHHHHH	37.78	32015554
254	Sumoylation	DAVRNQRKLLASLVK HHHHHHHHHHHHHHH	37.78	28112733
254	Ubiquitination	DAVRNQRKLLASLVK HHHHHHHHHHHHHHH	37.78	27667366
255 (in isoform 2)	Ubiquitination	-	5.42	21890473
258	Phosphorylation	NQRKLLASLVKRLGD HHHHHHHHHHHHHCH	33.39	23911959
258 (in isoform 2)	Ubiquitination	-	33.39	21890473
261	Sumoylation	KLLASLVKRLGDKHA HHHHHHHHHHCHHHH	47.39	-
261	2-Hydroxyisobutyrylation	KLLASLVKRLGDKHA HHHHHHHHHHCHHHH	47.39	-
261	Acetylation	KLLASLVKRLGDKHA HHHHHHHHHHCHHHH	47.39	25953088
261	Malonylation	KLLASLVKRLGDKHA HHHHHHHHHHCHHHH	47.39	26320211
261	Sumoylation	KLLASLVKRLGDKHA HHHHHHHHHHCHHHH	47.39	28112733
261	Ubiquitination	KLLASLVKRLGDKHA HHHHHHHHHHCHHHH	47.39	27667366
261 (in isoform 1)	Ubiquitination	-	47.39	21890473
266	Acetylation	LVKRLGDKHATLQKS HHHHHCHHHHHHHHH	33.08	23749302
266	Ubiquitination	LVKRLGDKHATLQKS HHHHHCHHHHHHHHH	33.08	21906983
266 (in isoform 1)	Ubiquitination	-	33.08	21890473
272	Acetylation	DKHATLQKSTKEVRS HHHHHHHHHHHHHHH	64.30	25953088
272	Sumoylation	DKHATLQKSTKEVRS HHHHHHHHHHHHHHH	64.30	28112733
272	Ubiquitination	DKHATLQKSTKEVRS HHHHHHHHHHHHHHH	64.30	27667366
272 (in isoform 1)	Ubiquitination	-	64.30	21890473
275	Ubiquitination	ATLQKSTKEVRSSIR HHHHHHHHHHHHHHH	62.39	21906983
275 (in isoform 1)	Ubiquitination	-	62.39	21890473
280	Phosphorylation	STKEVRSSIRQVSDV HHHHHHHHHHHHHHH	15.95	27251275
282	Methylation	KEVRSSIRQVSDVQK HHHHHHHHHHHHHHH	32.56	115918461
283 (in isoform 2)	Ubiquitination	-	37.08	21890473
284 (in isoform 2)	Ubiquitination	-	3.66	21890473
285	Phosphorylation	RSSIRQVSDVQKRVQ HHHHHHHHHHHHHHH	24.59	24719451
289	Acetylation	RQVSDVQKRVQVDVK HHHHHHHHHHHHHHH	55.15	23749302
289	Ubiquitination	RQVSDVQKRVQVDVK HHHHHHHHHHHHHHH	55.15	21906983
289 (in isoform 1)	Ubiquitination	-	55.15	21890473
295 (in isoform 2)	Ubiquitination	-	4.86	21890473
296	Ubiquitination	KRVQVDVKMAILQIM HHHHHHHHHHHHHHH	20.39	21906983
296 (in isoform 1)	Ubiquitination	-	20.39	21890473
304	Acetylation	MAILQIMKELNKRGR HHHHHHHHHHHHCCC	61.76	19608861
304	Neddylation	MAILQIMKELNKRGR HHHHHHHHHHHHCCC	61.76	32015554
304	Sumoylation	MAILQIMKELNKRGR HHHHHHHHHHHHCCC	61.76	28112733
304	Ubiquitination	MAILQIMKELNKRGR HHHHHHHHHHHHCCC	61.76	23000965
304 (in isoform 1)	Ubiquitination	-	61.76	21890473
308	Ubiquitination	QIMKELNKRGRVLVN HHHHHHHHCCCEEEC	69.70	23000965
308 (in isoform 2)	Ubiquitination	-	69.70	21890473
318 (in isoform 2)	Ubiquitination	-	43.55	21890473
319	Sumoylation	VLVNDAQKVTEGQQE EEECCHHHCCHHHHH	53.50	-
319	Acetylation	VLVNDAQKVTEGQQE EEECCHHHCCHHHHH	53.50	25953088
319	Malonylation	VLVNDAQKVTEGQQE EEECCHHHCCHHHHH	53.50	26320211
319	Sumoylation	VLVNDAQKVTEGQQE EEECCHHHCCHHHHH	53.50	28112733
319	Ubiquitination	VLVNDAQKVTEGQQE EEECCHHHCCHHHHH	53.50	27667366
319 (in isoform 1)	Ubiquitination	-	53.50	21890473
321	Phosphorylation	VNDAQKVTEGQQERL ECCHHHCCHHHHHHH	41.24	27174698
325 (in isoform 2)	Ubiquitination	-	48.94	21890473
337	Sumoylation	RQHWTMTKIQKHQEH HHHCHHHHHHHHHHH	32.11	-
337	Acetylation	RQHWTMTKIQKHQEH HHHCHHHHHHHHHHH	32.11	25953088
337	Sumoylation	RQHWTMTKIQKHQEH HHHCHHHHHHHHHHH	32.11	-
337	Ubiquitination	RQHWTMTKIQKHQEH HHHCHHHHHHHHHHH	32.11	22817900
337 (in isoform 1)	Ubiquitination	-	32.11	21890473
340	Acetylation	WTMTKIQKHQEHILR CHHHHHHHHHHHHHH	51.21	19608861
340	Ubiquitination	WTMTKIQKHQEHILR CHHHHHHHHHHHHHH	51.21	22817900
340 (in isoform 1)	Ubiquitination	-	51.21	21890473
352 (in isoform 2)	Ubiquitination	-	10.04	21890473
355	Phosphorylation	FASWALESDNNTALL HHHHHHHCCCCHHHH	46.63	21712546
365	Acetylation	NTALLLSKKLIYFQL CHHHHHHHHHHHHHH	52.12	25953088
365	Ubiquitination	NTALLLSKKLIYFQL CHHHHHHHHHHHHHH	52.12	23000965
365 (in isoform 1)	Ubiquitination	-	52.12	21890473
366	Sumoylation	TALLLSKKLIYFQLH HHHHHHHHHHHHHHH	36.42	-
366	Acetylation	TALLLSKKLIYFQLH HHHHHHHHHHHHHHH	36.42	26051181
366	Sumoylation	TALLLSKKLIYFQLH HHHHHHHHHHHHHHH	36.42	25218447
366	Ubiquitination	TALLLSKKLIYFQLH HHHHHHHHHHHHHHH	36.42	23000965
366 (in isoform 1)	Ubiquitination	-	36.42	21890473
369	Phosphorylation	LLSKKLIYFQLHRAL HHHHHHHHHHHHHHH	8.84	28152594
377	Sumoylation	FQLHRALKMIVDPVE HHHHHHHHHHHCCCC	26.12	-
377	Acetylation	FQLHRALKMIVDPVE HHHHHHHHHHHCCCC	26.12	19608861
377	Malonylation	FQLHRALKMIVDPVE HHHHHHHHHHHCCCC	26.12	26320211
377	Sumoylation	FQLHRALKMIVDPVE HHHHHHHHHHHCCCC	26.12	19608861
377	Ubiquitination	FQLHRALKMIVDPVE HHHHHHHHHHHCCCC	26.12	23000965
377 (in isoform 1)	Ubiquitination	-	26.12	21890473
387 (in isoform 2)	Ubiquitination	-	47.62	21890473
390	Sumoylation	VEPHGEMKFQWDLNA CCCCCCEEEEEEHHH	30.06	-
390	Ubiquitination	VEPHGEMKFQWDLNA CCCCCCEEEEEEHHH	30.06	21906983
390 (in isoform 1)	Ubiquitination	-	30.06	21890473
400	Ubiquitination	WDLNAWTKSAEAFGK EEHHHHHHHHHHHHH	36.65	21963094
400 (in isoform 1)	Ubiquitination	-	36.65	21890473
401	Phosphorylation	DLNAWTKSAEAFGKI EHHHHHHHHHHHHHH	24.78	27251275
407	Acetylation	KSAEAFGKIVAERPG HHHHHHHHHEEECCC	27.79	25953088
407	Malonylation	KSAEAFGKIVAERPG HHHHHHHHHEEECCC	27.79	30639696
407	Sumoylation	KSAEAFGKIVAERPG HHHHHHHHHEEECCC	27.79	28112733
407	Ubiquitination	KSAEAFGKIVAERPG HHHHHHHHHEEECCC	27.79	21963094
407 (in isoform 1)	Ubiquitination	-	27.79	21890473
415	O-linked_Glycosylation	IVAERPGTNSTGPAP HEEECCCCCCCCCCC	28.78	23301498
415	Phosphorylation	IVAERPGTNSTGPAP HEEECCCCCCCCCCC	28.78	30108239
417	Phosphorylation	AERPGTNSTGPAPMA EECCCCCCCCCCCCC	34.28	25159151
418	Phosphorylation	ERPGTNSTGPAPMAP ECCCCCCCCCCCCCC	49.61	30108239
423	Sulfoxidation	NSTGPAPMAPPRAPG CCCCCCCCCCCCCCC	10.71	21406390
425 (in isoform 2)	Ubiquitination	-	16.80	21890473
427	Methylation	PAPMAPPRAPGPLSK CCCCCCCCCCCCCCC	52.97	115368019
433	Phosphorylation	PRAPGPLSKQGSGSS CCCCCCCCCCCCCCC	26.51	26074081
434	Sumoylation	RAPGPLSKQGSGSSQ CCCCCCCCCCCCCCC	67.38	-
434	Sumoylation	RAPGPLSKQGSGSSQ CCCCCCCCCCCCCCC	67.38	28112733
434	Ubiquitination	RAPGPLSKQGSGSSQ CCCCCCCCCCCCCCC	67.38	21963094
434 (in isoform 1)	Ubiquitination	-	67.38	21890473
437	Phosphorylation	GPLSKQGSGSSQPME CCCCCCCCCCCCCCE	32.76	25159151
439	Phosphorylation	LSKQGSGSSQPMEVQ CCCCCCCCCCCCEEE	27.74	21945579
440	Phosphorylation	SKQGSGSSQPMEVQE CCCCCCCCCCCEEEC	41.66	25159151
449	Phosphorylation	PMEVQEGYGFGSGDD CCEEECCCCCCCCCC	14.45	21945579
453	Phosphorylation	QEGYGFGSGDDPYSS ECCCCCCCCCCCCCC	36.47	21945579
458	Phosphorylation	FGSGDDPYSSAEPHV CCCCCCCCCCCCCCC	23.42	21945579
459	Phosphorylation	GSGDDPYSSAEPHVS CCCCCCCCCCCCCCC	28.58	21945579
460	Phosphorylation	SGDDPYSSAEPHVSG CCCCCCCCCCCCCCC	30.70	21945579
466	Phosphorylation	SSAEPHVSGVKRSRS CCCCCCCCCCCCCCC	34.53	21945579
469	Sumoylation	EPHVSGVKRSRSGEG CCCCCCCCCCCCCCC	48.45	-
469	Acetylation	EPHVSGVKRSRSGEG CCCCCCCCCCCCCCC	48.45	25953088
469	Sumoylation	EPHVSGVKRSRSGEG CCCCCCCCCCCCCCC	48.45	25114211
469	Ubiquitination	EPHVSGVKRSRSGEG CCCCCCCCCCCCCCC	48.45	21963094
469 (in isoform 1)	Ubiquitination	-	48.45	21890473
470	Citrullination	PHVSGVKRSRSGEGE CCCCCCCCCCCCCCC	34.59	-
470	Citrullination	PHVSGVKRSRSGEGE CCCCCCCCCCCCCCC	34.59	-
471	Phosphorylation	HVSGVKRSRSGEGEV CCCCCCCCCCCCCCC	25.69	29255136
472	Citrullination	VSGVKRSRSGEGEVS CCCCCCCCCCCCCCC	53.35	-
472	Citrullination	VSGVKRSRSGEGEVS CCCCCCCCCCCCCCC	53.35	-
473	Phosphorylation	SGVKRSRSGEGEVSG CCCCCCCCCCCCCCH	42.30	19664994
479	Phosphorylation	RSGEGEVSGLMRKVP CCCCCCCCHHHCCCC	23.16	20201521
482	Sulfoxidation	EGEVSGLMRKVPRVS CCCCCHHHCCCCCEE	4.43	21406390
489	Phosphorylation	MRKVPRVSLERLDLD HCCCCCEEHHHCCCC	26.28	25159151
493 (in isoform 2)	Ubiquitination	-	5.83	21890473
498	Phosphorylation	ERLDLDLTADSQPPV HHCCCCCCCCCCCCE	28.25	30266825
501	Phosphorylation	DLDLTADSQPPVFKV CCCCCCCCCCCEEEE	41.97	19664994
507	Sumoylation	DSQPPVFKVFPGSTT CCCCCEEEECCCCCC	43.11	28112733
507	Ubiquitination	DSQPPVFKVFPGSTT CCCCCEEEECCCCCC	43.11	21906983
507 (in isoform 1)	Ubiquitination	-	43.11	21890473
512	Phosphorylation	VFKVFPGSTTEDYNL EEEECCCCCCCCCCE	32.18	29978859
513	Phosphorylation	FKVFPGSTTEDYNLI EEECCCCCCCCCCEE	39.87	29978859
514	Phosphorylation	KVFPGSTTEDYNLIV EECCCCCCCCCCEEE	28.67	29978859
517	Nitration	PGSTTEDYNLIVIER CCCCCCCCCEEEEEC	12.97	-
517	Phosphorylation	PGSTTEDYNLIVIER CCCCCCCCCEEEEEC	12.97	25159151
531	Phosphorylation	RGAAAAATGQPGTAP CCHHHHHCCCCCCCC	31.46	29255136
536	Phosphorylation	AATGQPGTAPAGTPG HHCCCCCCCCCCCCC	35.83	30266825
541	Phosphorylation	PGTAPAGTPGAPPLA CCCCCCCCCCCCCCC	22.21	29255136
550	Sulfoxidation	GAPPLAGMAIVKEEE CCCCCCCEEEEEHHH	1.59	28183972
554	Sumoylation	LAGMAIVKEEETEAA CCCEEEEEHHHHHHH	53.98	-
554	Sumoylation	LAGMAIVKEEETEAA CCCEEEEEHHHHHHH	53.98	17079232
558	Phosphorylation	AIVKEEETEAAIGAP EEEEHHHHHHHCCCC	33.92	28464451
567	Phosphorylation	AAIGAPPTATEGPET HHCCCCCCCCCCCCC	45.19	24173317
569	Phosphorylation	IGAPPTATEGPETKP CCCCCCCCCCCCCCC	43.91	26074081
574	Phosphorylation	TATEGPETKPVLMAL CCCCCCCCCCEEHHH	43.72	26074081
575	Sumoylation	ATEGPETKPVLMALA CCCCCCCCCEEHHHH	31.31	-
575	Acetylation	ATEGPETKPVLMALA CCCCCCCCCEEHHHH	31.31	23954790
575	Sumoylation	ATEGPETKPVLMALA CCCCCCCCCEEHHHH	31.31	25218447
575	Ubiquitination	ATEGPETKPVLMALA CCCCCCCCCEEHHHH	31.31	21906983
575 (in isoform 1)	Ubiquitination	-	31.31	21890473
594	Phosphorylation	AEGPRLASPSGSTSS CCCCCCCCCCCCCCC	24.96	20201521
596	Phosphorylation	GPRLASPSGSTSSGL CCCCCCCCCCCCCCE	42.77	23927012
598	Phosphorylation	RLASPSGSTSSGLEV CCCCCCCCCCCCEEE	29.47	23927012
599	Phosphorylation	LASPSGSTSSGLEVV CCCCCCCCCCCEEEE	30.36	23927012
600	Phosphorylation	ASPSGSTSSGLEVVA CCCCCCCCCCEEEEC	24.89	25159151
601	Phosphorylation	SPSGSTSSGLEVVAP CCCCCCCCCEEEECC	47.70	23927012
611	Phosphorylation	EVVAPEGTSAPGGGP EEECCCCCCCCCCCC	21.76	30278072
612	Phosphorylation	VVAPEGTSAPGGGPG EECCCCCCCCCCCCC	43.24	30278072
613 (in isoform 2)	Ubiquitination	-	13.44	-
620	Phosphorylation	APGGGPGTLDDSATI CCCCCCCCCCCCCHH	30.10	30278072
624	Phosphorylation	GPGTLDDSATICRVC CCCCCCCCCHHHHHC	27.29	30278072
626	Phosphorylation	GTLDDSATICRVCQK CCCCCCCHHHHHCCC	25.26	30278072
668 (in isoform 2)	Ubiquitination	-	2.48	21890473
676	Sumoylation	CHVLPDLKEEDGSLS HHCCCCCCCCCCCEE	67.45	-
676	Sumoylation	CHVLPDLKEEDGSLS HHCCCCCCCCCCCEE	67.45	18488044
681	Phosphorylation	DLKEEDGSLSLDGAD CCCCCCCCEECCCCC	27.40	30266825
683	Phosphorylation	KEEDGSLSLDGADST CCCCCCEECCCCCCC	26.55	29255136
688 (in isoform 2)	Ubiquitination	-	52.87	21890473
689	Phosphorylation	LSLDGADSTGVVAKL EECCCCCCCCCEEEC	26.91	23927012
690	Phosphorylation	SLDGADSTGVVAKLS ECCCCCCCCCEEECC	34.25	30108239
692 (in isoform 2)	Ubiquitination	-	3.71	21890473
695	Ubiquitination	DSTGVVAKLSPANQR CCCCCEEECCHHHHH	37.58	32015554
697	Phosphorylation	TGVVAKLSPANQRKC CCCEEECCHHHHHHH	22.66	23401153
697 (in isoform 2)	Ubiquitination	-	22.66	21890473
750	Sumoylation	IRARLQEKLSPPYSS HHHHHHHHCCCCCCC	41.10	-
750	Acetylation	IRARLQEKLSPPYSS HHHHHHHHCCCCCCC	41.10	26051181
750	Neddylation	IRARLQEKLSPPYSS HHHHHHHHCCCCCCC	41.10	32015554
750	Sumoylation	IRARLQEKLSPPYSS HHHHHHHHCCCCCCC	41.10	18082607
750	Ubiquitination	IRARLQEKLSPPYSS HHHHHHHHCCCCCCC	41.10	23000965
750 (in isoform 1)	Ubiquitination	-	41.10	21890473
752	Phosphorylation	ARLQEKLSPPYSSPQ HHHHHHCCCCCCCHH	34.59	29255136
755	Phosphorylation	QEKLSPPYSSPQEFA HHHCCCCCCCHHHHH	25.76	29255136
756	Phosphorylation	EKLSPPYSSPQEFAQ HHCCCCCCCHHHHHH	41.12	29255136
757	Phosphorylation	KLSPPYSSPQEFAQD HCCCCCCCHHHHHHH	25.43	29255136
770	Sumoylation	QDVGRMFKQFNKLTE HHHHHHHHHHHHHCC	44.64	-
770	Acetylation	QDVGRMFKQFNKLTE HHHHHHHHHHHHHCC	44.64	19608861
770	Malonylation	QDVGRMFKQFNKLTE HHHHHHHHHHHHHCC	44.64	26320211
770	Sumoylation	QDVGRMFKQFNKLTE HHHHHHHHHHHHHCC	44.64	28112733
770	Ubiquitination	QDVGRMFKQFNKLTE HHHHHHHHHHHHHCC	44.64	27667366
770 (in isoform 1)	Ubiquitination	-	44.64	21890473
774	Sumoylation	RMFKQFNKLTEDKAD HHHHHHHHHCCCHHH	59.06	-
774	Acetylation	RMFKQFNKLTEDKAD HHHHHHHHHCCCHHH	59.06	19608861
774	Sumoylation	RMFKQFNKLTEDKAD HHHHHHHHHCCCHHH	59.06	28112733
774	Ubiquitination	RMFKQFNKLTEDKAD HHHHHHHHHCCCHHH	59.06	27667366
774 (in isoform 1)	Ubiquitination	-	59.06	21890473
779	Sumoylation	FNKLTEDKADVQSII HHHHCCCHHHHHHHH	40.01	-
779	2-Hydroxyisobutyrylation	FNKLTEDKADVQSII HHHHCCCHHHHHHHH	40.01	-
779	Acetylation	FNKLTEDKADVQSII HHHHCCCHHHHHHHH	40.01	25953088
779	Neddylation	FNKLTEDKADVQSII HHHHCCCHHHHHHHH	40.01	32015554
779	Sumoylation	FNKLTEDKADVQSII HHHHCCCHHHHHHHH	40.01	25114211
779	Ubiquitination	FNKLTEDKADVQSII HHHHCCCHHHHHHHH	40.01	27667366
779 (in isoform 1)	Ubiquitination	-	40.01	21890473
784	Phosphorylation	EDKADVQSIIGLQRF CCHHHHHHHHHHHHH	18.93	27499020
790	Methylation	QSIIGLQRFFETRMN HHHHHHHHHHHHHHH	43.17	115918465
796	Sulfoxidation	QRFFETRMNEAFGDT HHHHHHHHHHHHCCC	7.49	28183972
803	Phosphorylation	MNEAFGDTKFSAVLV HHHHHCCCCEEEEEE	34.08	20068231
804	Sumoylation	NEAFGDTKFSAVLVE HHHHCCCCEEEEEEC	41.90	-
804	Sumoylation	NEAFGDTKFSAVLVE HHHHCCCCEEEEEEC	41.90	17079232
804	Ubiquitination	NEAFGDTKFSAVLVE HHHHCCCCEEEEEEC	41.90	24816145
806	Phosphorylation	AFGDTKFSAVLVEPP HHCCCCEEEEEECCC	21.01	20873877
816	Phosphorylation	LVEPPPMSLPGAGLS EECCCCCCCCCCCCC	36.87	28176443
823	Phosphorylation	SLPGAGLSSQELSGG CCCCCCCCCCCCCCC	29.11	30278072
824	Phosphorylation	LPGAGLSSQELSGGP CCCCCCCCCCCCCCC	32.49	25159151
828	Phosphorylation	GLSSQELSGGPGDGP CCCCCCCCCCCCCCC	40.74	30278072

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
449	Y	Phosphorylation	Kinase	LYN	P07948	PSP
458	Y	Phosphorylation	Kinase	LYN	P07948	PSP
473	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
473	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
473	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
517	Y	Phosphorylation	Kinase	LYN	P07948	PSP
824	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
824	S	Phosphorylation	Kinase	ATR	Q13535	Uniprot
824	S	Phosphorylation	Kinase	DSDNA KINASE	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
554	K	Sumoylation	Lys-554, Lys-779 and Lys-804 are the major sites of sumoylation.	17079232
779	K	Sumoylation	Lys-554, Lys-779 and Lys-804 are the major sites of sumoylation.	17079232
804	K	Sumoylation	Lys-554, Lys-779 and Lys-804 are the major sites of sumoylation.	17079232
824	S	Phosphorylation	ATM-induced phosphorylation on Ser-824 represses sumoylation leading to the de-repression of expression of a subset of genes involved in cell cycle control and apoptosis in response to genotoxic stress.	17178852
824	S	Phosphorylation	In response to Dox-induced DNA damage, enhanced phosphorylation on Ser-824 prevents sumoylation and allows de-repression of CDKN1A/p21.	17178852
824	S	Phosphorylation	Represses and is repressed by Ser-824 phosphorylation.	17178852
824	S	Sumoylation	ATM-induced phosphorylation on Ser-824 represses sumoylation leading to the de-repression of expression of a subset of genes involved in cell cycle control and apoptosis in response to genotoxic stress.	17178852
824	S	Sumoylation	In response to Dox-induced DNA damage, enhanced phosphorylation on Ser-824 prevents sumoylation and allows de-repression of CDKN1A/p21.	17178852

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TIF1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SETB1_HUMAN	SETDB1	physical	11959841
TIF1B_HUMAN	TRIM28	physical	12684500
TIF1A_HUMAN	TRIM24	physical	12684500
SPG7_HUMAN	SPG7	physical	16169070
VIME_HUMAN	VIM	physical	16169070
CHD3_HUMAN	CHD3	physical	16169070
TIF1B_HUMAN	TRIM28	physical	10748030
TRI23_HUMAN	TRIM23	physical	11331580
CBX5_HUMAN	CBX5	physical	12154074
CBX5_HUMAN	CBX5	physical	10938122
HP1_DROME	Su(var)205	physical	10938122
TIF1B_HUMAN	TRIM28	physical	12096914
CEBPB_HUMAN	CEBPB	physical	9742105
GCR_HUMAN	NR3C1	physical	9742105
AIRE_HUMAN	AIRE	physical	20085707
HDA10_HUMAN	HDAC10	physical	20032463
PAX3_HUMAN	PAX3	physical	20032463
NR4A1_HUMAN	NR4A1	physical	19321449
NR4A3_HUMAN	NR4A3	physical	19321449
MDM2_HUMAN	MDM2	physical	16107876
SRTD1_HUMAN	SERTAD1	physical	17141982
SRTD2_HUMAN	SERTAD2	physical	17141982
CDCA4_HUMAN	CDCA4	physical	17141982
PARP1_HUMAN	PARP1	physical	18676401
PARP2_HUMAN	PARP2	physical	18676401
ZN224_HUMAN	ZNF224	physical	16150558
CBX5_HUMAN	CBX5	physical	15882967
STAT1_HUMAN	STAT1	physical	18381204
MYB_HUMAN	MYB	physical	14761981
SKI_HUMAN	SKI	physical	14761981
SIN3A_HUMAN	SIN3A	physical	14761981
E2F1_HUMAN	E2F1	physical	17704056
PP1A_HUMAN	PPP1CA	physical	20424263
PP1G_HUMAN	PPP1CC	physical	20424263
PP1B_HUMAN	PPP1CB	physical	20424263
H31_HUMAN	HIST1H3A	physical	20424263
PO5F1_HUMAN	POU5F1	physical	20508149
CBP_HUMAN	CREBBP	physical	20508149
SMRCD_HUMAN	SMARCAD1	physical	20508149
SMCA4_HUMAN	SMARCA4	physical	20508149
SMRC1_HUMAN	SMARCC1	physical	20508149
ZN274_HUMAN	ZNF274	physical	21170338
MAGA2_HUMAN	MAGEA2	physical	20864041
MAGC2_HUMAN	MAGEC2	physical	20864041
MAGE1_HUMAN	MAGEE1	physical	20864041
MAGB2_HUMAN	MAGEB2	physical	20864041
MAGA3_HUMAN	MAGEA3	physical	20864041
MAGA6_HUMAN	MAGEA6	physical	20864041
MAGD1_HUMAN	MAGED1	physical	20864041
UBC_HUMAN	UBC	physical	20864041
TIF1B_HUMAN	TRIM28	physical	20864041
P53_HUMAN	TP53	physical	20864041
CHD3_HUMAN	CHD3	physical	21642969
SMRCD_HUMAN	SMARCAD1	physical	21549307
UHRF1_HUMAN	UHRF1	physical	22055183
DNMT1_HUMAN	DNMT1	physical	22055183
DNM3A_HUMAN	DNMT3A	physical	22055183
DNM3B_HUMAN	DNMT3B	physical	22055183
CBX5_HUMAN	CBX5	physical	22496453
E2F1_HUMAN	E2F1	physical	22496453
P4R3B_HUMAN	SMEK2	physical	22491012
PP4C_HUMAN	PPP4C	physical	22491012
NR2C2_HUMAN	NR2C2	physical	21670149
NR2C1_HUMAN	NR2C1	physical	21670149
DNMT1_HUMAN	DNMT1	physical	21670149
IRF7_HUMAN	IRF7	physical	21940674
SETB1_HUMAN	SETDB1	physical	18082607
CHD3_HUMAN	CHD3	physical	18082607
FES_HUMAN	FES	physical	16792528
ERBB4_HUMAN	ERBB4	physical	20858735
MDM2_HUMAN	MDM2	physical	20858735
P53_HUMAN	TP53	physical	20858735
MDM2_HUMAN	MDM2	physical	17056014
ZNF10_HUMAN	ZNF10	physical	10653693
ZNF10_HUMAN	ZNF10	physical	10022127
TIF1B_HUMAN	TRIM28	physical	10653693
NF2L2_MOUSE	Nfe2l2	physical	21382013
UBE2H_HUMAN	UBE2H	physical	20864041
UBE2N_HUMAN	UBE2N	physical	20864041
UB2R1_HUMAN	CDC34	physical	20864041
UB2D1_HUMAN	UBE2D1	physical	20864041
UB2D2_HUMAN	UBE2D2	physical	20864041
UB2D3_HUMAN	UBE2D3	physical	20864041
UB2E1_HUMAN	UBE2E1	physical	20864041
UB2L3_HUMAN	UBE2L3	physical	20864041
UB2E2_HUMAN	UBE2E2	physical	20864041
UBE2C_HUMAN	UBE2C	physical	20864041
UBIP1_HUMAN	UBP1	physical	22939629
TTL12_HUMAN	TTLL12	physical	22939629
IRF1_HUMAN	IRF1	physical	23134341
Z354A_HUMAN	ZNF354A	physical	8986806
ZNF2_HUMAN	ZNF2	physical	8986806
E2F3_HUMAN	E2F3	physical	23060449
E2F4_HUMAN	E2F4	physical	23060449
STAT3_HUMAN	STAT3	physical	18037959
STAT1_HUMAN	STAT1	physical	18037959
STAT4_HUMAN	STAT4	physical	18037959
STAT6_HUMAN	STAT6	physical	18037959
ZN420_HUMAN	ZNF420	physical	21988832
BRCC3_HUMAN	BRCC3	physical	22863883
ENAH_HUMAN	ENAH	physical	22863883
HNRPR_HUMAN	HNRNPR	physical	22863883
LARP7_HUMAN	LARP7	physical	22863883
MTA2_HUMAN	MTA2	physical	22863883
TIF1B_HUMAN	TRIM28	physical	12438698
CBX5_HUMAN	CBX5	physical	23645696
H31T_HUMAN	HIST3H3	physical	23645696
TIF1B_HUMAN	TRIM28	physical	24018422
UBC9_HUMAN	UBE2I	physical	24018422
RNF4_HUMAN	RNF4	physical	24907272
ZN274_HUMAN	ZNF274	physical	25421577
ZKSC8_HUMAN	ZKSCAN8	physical	25421577
HCFC1_HUMAN	HCFC1	physical	26344197
JUPI1_HUMAN	HN1	physical	26344197
HYPK_HUMAN	HYPK	physical	26344197
1433S_HUMAN	SFN	physical	26344197
RRP1B_HUMAN	RRP1B	physical	25092915
SIR1_HUMAN	SIRT1	physical	25905708
CDN2A_HUMAN	CDKN2A	physical	26055329
ARF_HUMAN	CDKN2A	physical	26055329
NPM_HUMAN	NPM1	physical	26055329
UBC9_HUMAN	UBE2I	physical	26055329
IMA5_MOUSE	Kpna1	physical	25960296
IMA1_MOUSE	Kpna2	physical	25960296
IMA3_MOUSE	Kpna4	physical	25960296
CBX1_HUMAN	CBX1	physical	25960296
POGK_HUMAN	POGK	physical	28514442
ZNF30_HUMAN	ZNF30	physical	28514442
ZNF28_HUMAN	ZNF28	physical	28514442
ZN573_HUMAN	ZNF573	physical	28514442
ZN658_HUMAN	ZNF658	physical	28514442
ZN112_HUMAN	ZNF112	physical	28514442
ZN620_HUMAN	ZNF620	physical	28514442
ZN268_HUMAN	ZNF268	physical	28514442
ZN721_HUMAN	ZNF721	physical	28514442
ZN195_HUMAN	ZNF195	physical	28514442
ZN845_HUMAN	ZNF845	physical	28514442
CBX5_HUMAN	CBX5	physical	28514442
ZN624_HUMAN	ZNF624	physical	28514442
ZN616_HUMAN	ZNF616	physical	28514442
ZN273_HUMAN	ZNF273	physical	28514442
ZN320_HUMAN	ZNF320	physical	28514442
ZN732_HUMAN	ZNF732	physical	28514442
ZFP1_HUMAN	ZFP1	physical	28514442
ZN267_HUMAN	ZNF267	physical	28514442
ZN708_HUMAN	ZNF708	physical	28514442
ZN460_HUMAN	ZNF460	physical	28514442
ZN33A_HUMAN	ZNF33A	physical	28514442
ZN33B_HUMAN	ZNF33B	physical	28514442
ZN720_HUMAN	ZNF720	physical	28514442
Z354A_HUMAN	ZNF354A	physical	28514442
ZN701_HUMAN	ZNF701	physical	28514442
ZNF85_HUMAN	ZNF85	physical	28514442
ZNF77_HUMAN	ZNF77	physical	28514442
Z585B_HUMAN	ZNF585B	physical	28514442
ZN445_HUMAN	ZNF445	physical	28514442
ZN766_HUMAN	ZNF766	physical	28514442
CBX1_HUMAN	CBX1	physical	28514442
ZN432_HUMAN	ZNF432	physical	28514442
ZNF84_HUMAN	ZNF84	physical	28514442
P73_HUMAN	TP73	physical	25893286
RMP_HUMAN	URI1	physical	27780869
ATM_HUMAN	ATM	physical	28249048

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

Acetylation

"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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-14; SER-17; SER-19; SER-26; SER-473; SER-594;SER-596; SER-600; SER-601; SER-683; SER-689 AND SER-757, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-266; LYS-304; LYS-340;LYS-377; LYS-770 AND LYS-774, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"SUMOylation of the transcriptional co-repressor KAP1 is regulated bythe serine and threonine phosphatase PP1.";
Li X., Lin H.H., Chen H., Xu X., Shih H.M., Ann D.K.;
Sci. Signal. 3:RA32-RA32(2010).
Cited for: PHOSPHORYLATION AT SER-824, SUMOYLATION, FUNCTION, INTERACTION WITHPPP1CA AND PPP1CB, AND MUTAGENESIS OF PHE-370; SER-440; SER-501 ANDSER-824.
PubMed: 20424263

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-489; SER-501;SER-594 AND SER-757, AND MASS SPECTROMETRY.
PubMed: 19690332

"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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-14; SER-17; SER-19; SER-26; SER-473; SER-594;SER-596; SER-600; SER-601; SER-683; SER-689 AND SER-757, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-50; SER-258; SER-471;SER-473; SER-489; SER-752 AND SER-757, AND MASS SPECTROMETRY.
PubMed: 18669648

"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, AND MASSSPECTROMETRY.
PubMed: 19367720

"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-49 AND SER-50,AND MASS SPECTROMETRY.
PubMed: 18220336

"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-19; SER-594 AND SER-596,AND MASS SPECTROMETRY.
PubMed: 19007248

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440; SER-501 ANDSER-824, AND MASS SPECTROMETRY.
PubMed: 17525332

"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 SER-466; SER-471; SER-473;SER-501; THR-541 AND SER-594, AND MASS SPECTROMETRY.
PubMed: 17287340

"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-50 AND SER-473, AND MASSSPECTROMETRY.
PubMed: 17924679

"Role for KAP1 serine 824 phosphorylation andsumoylation/desumoylation switch in regulating KAP1-mediatedtranscriptional repression.";
Li X., Lee Y.K., Jeng J.C., Yen Y., Schultz D.C., Shih H.M., Ann D.K.;
J. Biol. Chem. 282:36177-36189(2007).
Cited for: PHOSPHORYLATION AT SER-824, SUMOYLATION, FUNCTION, AND MUTAGENESIS OFLEU-306; LYS-554; LYS-779; LYS-804 AND SER-824.
PubMed: 17942393

"Chromatin relaxation in response to DNA double-strand breaks ismodulated by a novel ATM- and KAP-1 dependent pathway.";
Ziv Y., Bielopolski D., Galanty Y., Lukas C., Taya Y., Schultz D.C.,Lukas J., Bekker-Jensen S., Bartek J., Shiloh Y.;
Nat. Cell Biol. 8:870-876(2006).
Cited for: PHOSPHORYLATION AT SER-824, AND FUNCTION.
PubMed: 16862143

"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-473; THR-541 ANDSER-757, AND MASS SPECTROMETRY.
PubMed: 16964243

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-50; SER-473;SER-681 AND SER-683, AND MASS SPECTROMETRY.
PubMed: 17081983

"KAP1, a novel substrate for PIKK family members, colocalizes withnumerous damage response factors at DNA lesions.";
White D.E., Negorev D., Peng H., Ivanov A.V., Maul G.G.,Rauscher F.J. III;
Cancer Res. 66:11594-11599(2006).
Cited for: PHOSPHORYLATION AT SER-824, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed: 17178852

"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND MASSSPECTROMETRY.
PubMed: 16083285

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND MASSSPECTROMETRY.
PubMed: 15302935

Sumoylation

"Structural insights into human KAP1 PHD finger-bromodomain and itsrole in gene silencing.";
Zeng L., Yap K.L., Ivanov A.V., Wang X., Mujtaba S., Plotnikova O.,Rauscher F.J. III, Zhou M.M.;
Nat. Struct. Mol. Biol. 15:626-633(2008).
Cited for: STRUCTURE BY NMR OF 624-812 OF WILD TYPE AND IN COMPLEX WITH UBE2I,SUMOYLATION AT LYS-676; LYS-750; LYS-779 AND LYS-804, AND MUTAGENESISOF CYS-651; LEU-653; LEU-668 AND LEU-709.
PubMed: 18488044

"Doxorubicin down-regulates Kruppel-associated box domain-associatedprotein 1 sumoylation that relieves its transcription repression onp21WAF1/CIP1 in breast cancer MCF-7 cells.";
Lee Y.K., Thomas S.N., Yang A.J., Ann D.K.;
J. Biol. Chem. 282:1595-1606(2007).
Cited for: INTERACTION WITH ZNF350, SUMOYLATION AT LYS-554; LYS-779 AND LYS-804,FUNCTION, AND MUTAGENESIS OF LYS-554; LYS-575; LYS-676; LYS-779 ANDLYS-804.
PubMed: 17079232