dbPTM

CHD3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CHD3_HUMAN
UniProt AC	Q12873
Protein Name	Chromodomain-helicase-DNA-binding protein 3
Gene Name	CHD3
Organism	Homo sapiens (Human).
Sequence Length	2000
Subcellular Localization	Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Associates with centrosomes in interphase and mitosis.
Protein Description	Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity..
Protein Sequence	MKAADTVILWARSKNDQLRISFPPGLCWGDRMPDKDDIRLLPSALGVKKRKRGPKKQKENKPGKPRKRKKRDSEEEFGSERDEYREKSESGGSEYGTGPGRKRRRKHREKKEKKTKRRKKGEGDGGQKQVEQKSSATLLLTWGLEDVEHVFSEEDYHTLTNYKAFSQFMRPLIAKKNPKIPMSKMMTILGAKWREFSANNPFKGSAAAVAAAAAAAAAAVAEQVSAAVSSATPIAPSGPPALPPPPAADIQPPPIRRAKTKEGKGPGHKRRSKSPRVPDGRKKLRGKKMAPLKIKLGLLGGKRKKGGSYVFQSDEGPEPEAEESDLDSGSVHSASGRPDGPVRTKKLKRGRPGRKKKKVLGCPAVAGEEEVDGYETDHQDYCEVCQQGGEIILCDTCPRAYHLVCLDPELDRAPEGKWSCPHCEKEGVQWEAKEEEEEYEEEGEEEGEKEEEDDHMEYCRVCKDGGELLCCDACISSYHIHCLNPPLPDIPNGEWLCPRCTCPVLKGRVQKILHWRWGEPPVAVPAPQQADGNPDVPPPRPLQGRSEREFFVKWVGLSYWHCSWAKELQLEIFHLVMYRNYQRKNDMDEPPPLDYGSGEDDGKSDKRKVKDPHYAEMEEKYYRFGIKPEWMTVHRIINHSVDKKGNYHYLVKWRDLPYDQSTWEEDEMNIPEYEEHKQSYWRHRELIMGEDPAQPRKYKKKKKELQGDGPPSSPTNDPTVKYETQPRFITATGGTLHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPKFYVVTYTGDKDSRAIIRENEFSFEDNAIKGGKKAFKMKREAQVKFHVLLTSYELITIDQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRRLKADVFKNMPAKTELIVRVELSPMQKKYYKYILTRNFEALNSRGGGNQVSLLNIMMDLKKCCNHPYLFPVAAMESPKLPSGAYEGGALIKSSGKLMLLQKMLRKLKEQGHRVLIFSQMTKMLDLLEDFLDYEGYKYERIDGGITGALRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIFDSDWNPHNDIQAFSRAHRIGQANKVMIYRFVTRASVEERITQVAKRKMMLTHLVVRPGLGSKAGSMSKQELDDILKFGTEELFKDENEGENKEEDSSVIHYDNEAIARLLDRNQDATEDTDVQNMNEYLSSFKVAQYVVREEDKIEEIEREIIKQEENVDPDYWEKLLRHHYEQQQEDLARNLGKGKRVRKQVNYNDAAQEDQDNQSEYSVGSEEEDEDFDERPEGRRQSKRQLRNEKDKPLPPLLARVGGNIEVLGFNTRQRKAFLNAVMRWGMPPQDAFTTQWLVRDLRGKTEKEFKAYVSLFMRHLCEPGADGSETFADGVPREGLSRQQVLTRIGVMSLVKKKVQEFEHINGRWSMPELMPDPSADSKRSSRASSPTKTSPTTPEASATNSPCTSKPATPAPSEKGEGIRTPLEKEEAENQEEKPEKNSRIGEKMETEADAPSPAPSLGERLEPRKIPLEDEVPGVPGEMEPEPGYRGDREKSATESTPGERGEEKPLDGQEHRERPEGETGDLGKREDVKGDRELRPGPRDEPRSNGRREEKTEKPRFMFNIADGGFTELHTLWQNEERAAISSGKLNEIWHRRHDYWLLAGIVLHGYARWQDIQNDAQFAIINEPFKTEANKGNFLEMKNKFLARRFKLLEQALVIEEQLRRAAYLNLSQEPAHPAMALHARFAEAECLAESHQHLSKESLAGNKPANAVLHKVLNQLEELLSDMKADVTRLPATLSRIPPIAARLQMSERSILSRLASKGTEPHPTPAYPPGPYATPPGYGAAFSAAPVGALAAAGANYSQMPAGSFITAATNGPPVLVKKEKEMVGALVSDGLDRKEPRAGEVICIDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MKAADTVIL ------CCCCCEEEE	64.68	25953088
43	Phosphorylation	DDIRLLPSALGVKKR HHCCCCHHHHCCCCC	35.77	28509920
48	Acetylation	LPSALGVKKRKRGPK CHHHHCCCCCCCCCC	45.09	25953088
48	Ubiquitination	LPSALGVKKRKRGPK CHHHHCCCCCCCCCC	45.09	-
56	Methylation	KRKRGPKKQKENKPG CCCCCCCCCCCCCCC	70.50	-
58	Methylation	KRGPKKQKENKPGKP CCCCCCCCCCCCCCC	72.62	-
64	Methylation	QKENKPGKPRKRKKR CCCCCCCCCCCCCCC	50.61	-
66 (in isoform 3)	Phosphorylation	-	55.70	23927012
73	Phosphorylation	RKRKKRDSEEEFGSE CCCCCCCCHHHHCCC	51.44	23401153
73 (in isoform 2)	Phosphorylation	-	51.44	-
79	Phosphorylation	DSEEEFGSERDEYRE CCHHHHCCCHHHHHH	34.48	23401153
79 (in isoform 2)	Phosphorylation	-	34.48	-
84	Phosphorylation	FGSERDEYREKSESG HCCCHHHHHHHHHCC	28.50	20363803
84 (in isoform 2)	Phosphorylation	-	28.50	-
88	Phosphorylation	RDEYREKSESGGSEY HHHHHHHHHCCCCCC	32.04	25159151
90	Phosphorylation	EYREKSESGGSEYGT HHHHHHHCCCCCCCC	56.39	23927012
93	Phosphorylation	EKSESGGSEYGTGPG HHHHCCCCCCCCCCC	31.04	25159151
95	Phosphorylation	SESGGSEYGTGPGRK HHCCCCCCCCCCCHH	22.99	23663014
97	Phosphorylation	SGGSEYGTGPGRKRR CCCCCCCCCCCHHHH	39.02	28450419
175	Acetylation	FMRPLIAKKNPKIPM HHHHHHHCCCCCCCH	46.20	25953088
183	Phosphorylation	KNPKIPMSKMMTILG CCCCCCHHHHHHHHH	16.43	-
261	Acetylation	PIRRAKTKEGKGPGH CCCCCCCCCCCCCCC	64.86	55975877
264	Acetylation	RAKTKEGKGPGHKRR CCCCCCCCCCCCCCC	64.12	55975865
269	Acetylation	EGKGPGHKRRSKSPR CCCCCCCCCCCCCCC	56.26	55975857
272	Phosphorylation	GPGHKRRSKSPRVPD CCCCCCCCCCCCCCC	41.33	23403867
274	Phosphorylation	GHKRRSKSPRVPDGR CCCCCCCCCCCCCCC	21.13	23403867
302	Acetylation	KLGLLGGKRKKGGSY EEEECCCCCCCCCCE	60.28	25953088
302	Ubiquitination	KLGLLGGKRKKGGSY EEEECCCCCCCCCCE	60.28	-
308	Phosphorylation	GKRKKGGSYVFQSDE CCCCCCCCEEECCCC	27.13	26074081
309	Phosphorylation	KRKKGGSYVFQSDEG CCCCCCCEEECCCCC	14.46	26074081
313	Phosphorylation	GGSYVFQSDEGPEPE CCCEEECCCCCCCCC	26.60	30576142
324	Phosphorylation	PEPEAEESDLDSGSV CCCCCCCCCCCCCCC	34.67	23401153
324 (in isoform 2)	Phosphorylation	-	34.67	-
328	Phosphorylation	AEESDLDSGSVHSAS CCCCCCCCCCCCCCC	40.02	22167270
330	Phosphorylation	ESDLDSGSVHSASGR CCCCCCCCCCCCCCC	22.17	22167270
333	Phosphorylation	LDSGSVHSASGRPDG CCCCCCCCCCCCCCC	23.21	21955146
335	Phosphorylation	SGSVHSASGRPDGPV CCCCCCCCCCCCCCC	38.05	30576142
374	Phosphorylation	GEEEVDGYETDHQDY CCCCCCCCCCCCHHH	15.93	27251275
376	Phosphorylation	EEVDGYETDHQDYCE CCCCCCCCCCHHHHH	30.23	30576142
381	Phosphorylation	YETDHQDYCEVCQQG CCCCCHHHHHHHHCC	5.50	25849741
506	Ubiquitination	RCTCPVLKGRVQKIL CCCCHHHCCCHHHHH	44.92	-
578	Phosphorylation	EIFHLVMYRNYQRKN HHHHHHHHHCCCCCC	6.55	20068231
595	Phosphorylation	DEPPPLDYGSGEDDG CCCCCCCCCCCCCCC	22.37	23927012
597	Phosphorylation	PPPLDYGSGEDDGKS CCCCCCCCCCCCCCC	32.55	22167270
597 (in isoform 2)	Phosphorylation	-	32.55	-
604	Phosphorylation	SGEDDGKSDKRKVKD CCCCCCCCCCCCCCC	54.62	23403867
620	Ubiquitination	HYAEMEEKYYRFGIK CHHHHHHHHHHCCCC	33.99	-
627	Sumoylation	KYYRFGIKPEWMTVH HHHHCCCCCCHHHHH	36.95	-
627	Sumoylation	KYYRFGIKPEWMTVH HHHHCCCCCCHHHHH	36.95	28112733
640	Phosphorylation	VHRIINHSVDKKGNY HHHHHCCCCCCCCCE	27.76	-
644	Ubiquitination	INHSVDKKGNYHYLV HCCCCCCCCCEEEEE	48.18	-
652	Ubiquitination	GNYHYLVKWRDLPYD CCEEEEEEECCCCCC	33.64	-
712	Phosphorylation	LQGDGPPSSPTNDPT HCCCCCCCCCCCCCC	52.67	29255136
712 (in isoform 2)	Phosphorylation	-	52.67	-
713	Phosphorylation	QGDGPPSSPTNDPTV CCCCCCCCCCCCCCC	41.33	29255136
713 (in isoform 2)	Phosphorylation	-	41.33	-
715	Phosphorylation	DGPPSSPTNDPTVKY CCCCCCCCCCCCCCC	54.95	30266825
715 (in isoform 2)	Phosphorylation	-	54.95	-
719	Phosphorylation	SSPTNDPTVKYETQP CCCCCCCCCCCCCCC	32.28	22167270
721	Sumoylation	PTNDPTVKYETQPRF CCCCCCCCCCCCCEE	39.59	25114211
721	Ubiquitination	PTNDPTVKYETQPRF CCCCCCCCCCCCCEE	39.59	-
722	Phosphorylation	TNDPTVKYETQPRFI CCCCCCCCCCCCEEE	21.63	24732914
724	Phosphorylation	DPTVKYETQPRFITA CCCCCCCCCCEEEEE	40.56	24732914
739	Phosphorylation	TGGTLHMYQLEGLNW CCCEEEEEEECCCCC	10.13	-
777	Phosphorylation	QTIVFLYSLYKEGHT HHHHHHHHHHHCCCC	27.63	24719451
820	Acetylation	VVTYTGDKDSRAIIR EEEEECCCCCCEEEE	59.97	26051181
820	Ubiquitination	VVTYTGDKDSRAIIR EEEEECCCCCCEEEE	59.97	-
832	Phosphorylation	IIRENEFSFEDNAIK EEECCCCCCCCCCCC	22.88	20873877
839	Ubiquitination	SFEDNAIKGGKKAFK CCCCCCCCCCHHHHH	60.23	-
860	Phosphorylation	VKFHVLLTSYELITI HHHEEEECEEEEEEE	25.71	20068231
860 (in isoform 2)	Phosphorylation	-	25.71	-
861	Phosphorylation	KFHVLLTSYELITID HHEEEECEEEEEEEC	19.31	23403867
861 (in isoform 2)	Phosphorylation	-	19.31	-
862	Phosphorylation	FHVLLTSYELITIDQ HEEEECEEEEEEECH	14.98	23403867
866	Phosphorylation	LTSYELITIDQAALG ECEEEEEEECHHHHH	31.00	23403867
866 (in isoform 2)	Phosphorylation	-	31.00	-
874	Phosphorylation	IDQAALGSIRWACLV ECHHHHHCCHHHHHH	15.16	20068231
874 (in isoform 2)	Phosphorylation	-	15.16	-
894	Acetylation	RLKNNQSKFFRVLNG HHHCCCCHHHHHHCC	38.46	19608861
894	Ubiquitination	RLKNNQSKFFRVLNG HHHCCCCHHHHHHCC	38.46	-
954	Ubiquitination	ISKEDQIKKLHDLLG CCHHHHHHHHHHHHC	43.58	-
969	Acetylation	PHMLRRLKADVFKNM HHHHHHHHCHHHCCC	40.50	27452117
969	Ubiquitination	PHMLRRLKADVFKNM HHHHHHHHCHHHCCC	40.50	-
974	Ubiquitination	RLKADVFKNMPAKTE HHHCHHHCCCCCCEE	52.78	-
979	Ubiquitination	VFKNMPAKTELIVRV HHCCCCCCEEEEEEE	36.34	-
989	Phosphorylation	LIVRVELSPMQKKYY EEEEEEECHHHHHHH	12.57	24719451
991	Sulfoxidation	VRVELSPMQKKYYKY EEEEECHHHHHHHHH	9.07	21406390
993	Acetylation	VELSPMQKKYYKYIL EEECHHHHHHHHHHH	36.17	25953088
997	Acetylation	PMQKKYYKYILTRNF HHHHHHHHHHHHHCH	23.79	19608861
997	Ubiquitination	PMQKKYYKYILTRNF HHHHHHHHHHHHHCH	23.79	-
997 (in isoform 1)	Ubiquitination	-	23.79	21890473
997 (in isoform 2)	Ubiquitination	-	23.79	21890473
998	Phosphorylation	MQKKYYKYILTRNFE HHHHHHHHHHHHCHH	5.76	-
1001	Phosphorylation	KYYKYILTRNFEALN HHHHHHHHHCHHHHH	17.63	-
1044	Ubiquitination	VAAMESPKLPSGAYE HHHCCCCCCCCCCCC	80.47	-
1047	Phosphorylation	MESPKLPSGAYEGGA CCCCCCCCCCCCCCE	46.63	24719451
1050	Phosphorylation	PKLPSGAYEGGALIK CCCCCCCCCCCEEEH	20.73	24719451
1057	Ubiquitination	YEGGALIKSSGKLML CCCCEEEHHCHHHHH	39.14	-
1059	Phosphorylation	GGALIKSSGKLMLLQ CCEEEHHCHHHHHHH	34.64	24719451
1067	Ubiquitination	GKLMLLQKMLRKLKE HHHHHHHHHHHHHHH	39.61	-
1083	Phosphorylation	GHRVLIFSQMTKMLD CCCEEEEHHHHHHHH	16.43	24719451
1086	Phosphorylation	VLIFSQMTKMLDLLE EEEEHHHHHHHHHHH	12.98	27251275
1103	Phosphorylation	LDYEGYKYERIDGGI HCCCCCCEEEECCCC	11.27	22817900
1205	Phosphorylation	AKRKMMLTHLVVRPG HHHHHHHHHHHHCCC	8.68	-
1219	Phosphorylation	GLGSKAGSMSKQELD CCCCCCCCCCHHHHH	25.41	-
1222	Acetylation	SKAGSMSKQELDDIL CCCCCCCHHHHHHHH	38.87	20167786
1222	Ubiquitination	SKAGSMSKQELDDIL CCCCCCCHHHHHHHH	38.87	-
1230	Ubiquitination	QELDDILKFGTEELF HHHHHHHHHCHHHHH	41.92	-
1238	Sumoylation	FGTEELFKDENEGEN HCHHHHHCCCCCCCC	76.41	-
1238	Sumoylation	FGTEELFKDENEGEN HCHHHHHCCCCCCCC	76.41	-
1238	Ubiquitination	FGTEELFKDENEGEN HCHHHHHCCCCCCCC	76.41	-
1246	Ubiquitination	DENEGENKEEDSSVI CCCCCCCCCCCCCCE	59.17	-
1251	Phosphorylation	ENKEEDSSVIHYDNE CCCCCCCCCEEECHH	37.10	25849741
1274	Phosphorylation	NQDATEDTDVQNMNE CCCCCCCCCCCHHHH	31.66	-
1282	Phosphorylation	DVQNMNEYLSSFKVA CCCHHHHHHHHHHHH	13.59	-
1284	Phosphorylation	QNMNEYLSSFKVAQY CHHHHHHHHHHHHHH	32.59	-
1285	Phosphorylation	NMNEYLSSFKVAQYV HHHHHHHHHHHHHHH	26.87	-
1287	Ubiquitination	NEYLSSFKVAQYVVR HHHHHHHHHHHHHHC	38.31	-
1298	Ubiquitination	YVVREEDKIEEIERE HHHCCHHHHHHHHHH	56.12	-
1308	Sumoylation	EIEREIIKQEENVDP HHHHHHHHCHHCCCH	58.27	-
1308	Sumoylation	EIEREIIKQEENVDP HHHHHHHHCHHCCCH	58.27	28112733
1308	Ubiquitination	EIEREIIKQEENVDP HHHHHHHHCHHCCCH	58.27	-
1317	Phosphorylation	EENVDPDYWEKLLRH HHCCCHHHHHHHHHH	22.36	-
1320	Ubiquitination	VDPDYWEKLLRHHYE CCHHHHHHHHHHHHH	38.38	-
1323	Methylation	DYWEKLLRHHYEQQQ HHHHHHHHHHHHHHH	25.60	-
1339	Ubiquitination	DLARNLGKGKRVRKQ HHHHHCCCCHHHHHH	65.51	-
1349	Phosphorylation	RVRKQVNYNDAAQED HHHHHCCCCCHHHHC	18.63	22115753
1361	Phosphorylation	QEDQDNQSEYSVGSE HHCCCCCCCCCCCCH	44.77	22115753
1361 (in isoform 2)	Phosphorylation	-	44.77	-
1363	Phosphorylation	DQDNQSEYSVGSEEE CCCCCCCCCCCCHHC	17.57	28450419
1364	Phosphorylation	QDNQSEYSVGSEEED CCCCCCCCCCCHHCC	18.89	22617229
1364 (in isoform 2)	Phosphorylation	-	18.89	-
1367	Phosphorylation	QSEYSVGSEEEDEDF CCCCCCCCHHCCCCC	39.41	22617229
1367 (in isoform 2)	Phosphorylation	-	39.41	-
1394	Sumoylation	QLRNEKDKPLPPLLA HHHHCCCCCCCHHHH	60.57	-
1394	Sumoylation	QLRNEKDKPLPPLLA HHHHCCCCCCCHHHH	60.57	-
1394	Ubiquitination	QLRNEKDKPLPPLLA HHHHCCCCCCCHHHH	60.57	-
1436	Phosphorylation	MPPQDAFTTQWLVRD CCHHHHHHHHHHHHH	21.57	29083192
1437	Phosphorylation	PPQDAFTTQWLVRDL CHHHHHHHHHHHHHH	15.99	29083192
1522	Phosphorylation	PELMPDPSADSKRSS CHHCCCCCCCCCCCC	52.68	26074081
1525	Phosphorylation	MPDPSADSKRSSRAS CCCCCCCCCCCCCCC	29.68	26074081
1528	O-linked_Glycosylation	PSADSKRSSRASSPT CCCCCCCCCCCCCCC	28.10	29351928
1528	Phosphorylation	PSADSKRSSRASSPT CCCCCCCCCCCCCCC	28.10	29514088
1529	Phosphorylation	SADSKRSSRASSPTK CCCCCCCCCCCCCCC	35.58	30576142
1532	Phosphorylation	SKRSSRASSPTKTSP CCCCCCCCCCCCCCC	35.42	29116813
1533	Phosphorylation	KRSSRASSPTKTSPT CCCCCCCCCCCCCCC	35.29	30576142
1535	Phosphorylation	SSRASSPTKTSPTTP CCCCCCCCCCCCCCC	49.23	29116813
1536	Ubiquitination	SRASSPTKTSPTTPE CCCCCCCCCCCCCCC	50.84	-
1536 (in isoform 1)	Ubiquitination	-	50.84	21890473
1536 (in isoform 2)	Ubiquitination	-	50.84	21890473
1537	Phosphorylation	RASSPTKTSPTTPEA CCCCCCCCCCCCCCC	42.28	30266825
1538	Phosphorylation	ASSPTKTSPTTPEAS CCCCCCCCCCCCCCC	23.08	30266825
1540	Phosphorylation	SPTKTSPTTPEASAT CCCCCCCCCCCCCCC	55.54	30266825
1541	Phosphorylation	PTKTSPTTPEASATN CCCCCCCCCCCCCCC	23.63	23401153
1545	Phosphorylation	SPTTPEASATNSPCT CCCCCCCCCCCCCCC	33.68	23401153
1547	Phosphorylation	TTPEASATNSPCTSK CCCCCCCCCCCCCCC	33.46	23401153
1549	Phosphorylation	PEASATNSPCTSKPA CCCCCCCCCCCCCCC	19.59	30266825
1549 (in isoform 2)	Phosphorylation	-	19.59	-
1552	Phosphorylation	SATNSPCTSKPATPA CCCCCCCCCCCCCCC	43.07	30266825
1553	Phosphorylation	ATNSPCTSKPATPAP CCCCCCCCCCCCCCC	43.27	30266825
1554	Acetylation	TNSPCTSKPATPAPS CCCCCCCCCCCCCCC	22.10	26051181
1554	Ubiquitination	TNSPCTSKPATPAPS CCCCCCCCCCCCCCC	22.10	-
1554 (in isoform 1)	Ubiquitination	-	22.10	21890473
1554 (in isoform 2)	Ubiquitination	-	22.10	21890473
1557	Phosphorylation	PCTSKPATPAPSEKG CCCCCCCCCCCCCCC	28.63	30266825
1561	Phosphorylation	KPATPAPSEKGEGIR CCCCCCCCCCCCCCC	54.79	23927012
1569	Phosphorylation	EKGEGIRTPLEKEEA CCCCCCCCCHHHHHH	30.24	23898821
1569 (in isoform 2)	Phosphorylation	-	30.24	-
1573	Acetylation	GIRTPLEKEEAENQE CCCCCHHHHHHHCHH	69.41	26051181
1587	Phosphorylation	EEKPEKNSRIGEKME HCCCCHHCCHHHHHH	36.02	22817900
1592	Acetylation	KNSRIGEKMETEADA HHCCHHHHHHCCCCC	36.50	26051181
1595	Phosphorylation	RIGEKMETEADAPSP CHHHHHHCCCCCCCC	32.73	23927012
1601	Phosphorylation	ETEADAPSPAPSLGE HCCCCCCCCCCCHHH	35.10	29255136
1601 (in isoform 2)	Phosphorylation	-	35.10	-
1605	Phosphorylation	DAPSPAPSLGERLEP CCCCCCCCHHHCCCC	51.63	29255136
1605 (in isoform 2)	Phosphorylation	-	51.63	-
1634	Phosphorylation	EMEPEPGYRGDREKS CCCCCCCCCCCCCCC	23.34	26552605
1641	Phosphorylation	YRGDREKSATESTPG CCCCCCCCCCCCCCC	35.35	29396449
1643	Phosphorylation	GDREKSATESTPGER CCCCCCCCCCCCCCC	37.24	29396449
1645	Phosphorylation	REKSATESTPGERGE CCCCCCCCCCCCCCC	35.23	29396449
1646	Phosphorylation	EKSATESTPGERGEE CCCCCCCCCCCCCCC	29.13	26055452
1674	Acetylation	GETGDLGKREDVKGD CCCCCCCCCCCCCCC	60.97	25953088
1759	Methylation	IVLHGYARWQDIQND HHHHCHHCHHHHCCC	24.09	-
1782	Ubiquitination	PFKTEANKGNFLEMK CCCCCCCCCCHHHHH	63.38	-
1815	Phosphorylation	EQLRRAAYLNLSQEP HHHHHHHHCCCCCCC	8.64	21406692
1819	Phosphorylation	RAAYLNLSQEPAHPA HHHHCCCCCCCCCHH	31.27	21406692
1842	Phosphorylation	EAECLAESHQHLSKE HHHHHHHHHHHHCHH	23.88	21406692
1847	Phosphorylation	AESHQHLSKESLAGN HHHHHHHCHHHHCCC	32.05	21406692
1848	Ubiquitination	ESHQHLSKESLAGNK HHHHHHCHHHHCCCC	58.65	-
1850	Phosphorylation	HQHLSKESLAGNKPA HHHHCHHHHCCCCCH	27.53	-
1855	Ubiquitination	KESLAGNKPANAVLH HHHHCCCCCHHHHHH	44.59	-
1873	Phosphorylation	NQLEELLSDMKADVT HHHHHHHHHCCCCHH	48.56	24719451
1876	Ubiquitination	EELLSDMKADVTRLP HHHHHHCCCCHHHCC	46.56	-
1880	Phosphorylation	SDMKADVTRLPATLS HHCCCCHHHCCHHHH	27.34	24719451
1899	Phosphorylation	IAARLQMSERSILSR HHHHHHCCHHHHHHH	19.52	24719451
1902	Phosphorylation	RLQMSERSILSRLAS HHHCCHHHHHHHHHH	24.67	24719451
1905	Phosphorylation	MSERSILSRLASKGT CCHHHHHHHHHHCCC	24.47	24719451
1982	Phosphorylation	EMVGALVSDGLDRKE HHHHHHHCCCCCCCC	27.15	29083192
1988	Sumoylation	VSDGLDRKEPRAGEV HCCCCCCCCCCCCCE	72.27	28112733

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 CHD3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1971	K	Sumoylation		27068747
Sumoylation at Lys-1971 results in dissociation from chromatin and suppression of transcriptional repression.

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 CHD3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PAIRB_HUMAN	SERBP1	physical	12505151
HABP4_HUMAN	HABP4	physical	12505151
HDAC1_HUMAN	HDAC1	physical	9804427
HDAC2_HUMAN	HDAC2	physical	9804427
P53_HUMAN	TP53	physical	10961991
P73_HUMAN	TP73	physical	10961991
SUMO1_HUMAN	SUMO1	physical	10961991
MIC60_HUMAN	IMMT	physical	16169070
BCL6_HUMAN	BCL6	physical	15454082
HDAC2_HUMAN	HDAC2	physical	17827154
HDAC1_HUMAN	HDAC1	physical	17827154
CSK21_HUMAN	CSNK2A1	physical	17827154
PCNT_HUMAN	PCNT	physical	17626165
MYB_HUMAN	MYB	physical	17344210
DDX5_HUMAN	DDX5	physical	20676135
HDAC1_HUMAN	HDAC1	physical	9885572
CHD4_HUMAN	CHD4	physical	9885572
CHD3_HUMAN	CHD3	physical	9885572
HDAC2_HUMAN	HDAC2	physical	9885572
RBBP4_HUMAN	RBBP4	physical	9885572
MTA1_HUMAN	MTA1	physical	9885572
TIF1B_HUMAN	TRIM28	physical	21642969
SUMO1_HUMAN	SUMO1	physical	21642969
TWST1_HUMAN	TWIST1	physical	22457607
HD_HUMAN	HTT	physical	15383276
GIT1_HUMAN	GIT1	physical	15383276
PR40A_HUMAN	PRPF40A	physical	15383276
SUMO2_HUMAN	SUMO2	physical	15383276
VIME_HUMAN	VIM	physical	15383276
CHD3_HUMAN	CHD3	physical	15383276
LRIF1_HUMAN	LRIF1	physical	15383276
PIAS4_HUMAN	PIAS4	physical	15383276
ZHX1_HUMAN	ZHX1	physical	15383276
NFL_HUMAN	NEFL	physical	15383276
TCRG1_HUMAN	TCERG1	physical	15383276
P53_HUMAN	TP53	physical	15383276
PTN_HUMAN	PTN	physical	15383276
IMB1_HUMAN	KPNB1	physical	15383276
TAL1_HUMAN	TAL1	physical	15383276
MIC60_HUMAN	IMMT	physical	15383276
IKZF1_HUMAN	IKZF1	physical	10204490
MTA2_HUMAN	MTA2	physical	22939629
MBD3_HUMAN	MBD3	physical	22939629
HDAC2_HUMAN	HDAC2	physical	22939629
HDAC1_HUMAN	HDAC1	physical	22939629
RBBP7_HUMAN	RBBP7	physical	22939629
CHD4_HUMAN	CHD4	physical	22939629
RBBP4_HUMAN	RBBP4	physical	22939629
P66A_HUMAN	GATAD2A	physical	22939629
SMRC2_HUMAN	SMARCC2	physical	22939629
HDAC3_HUMAN	HDAC3	physical	22939629
TIF1B_HUMAN	TRIM28	physical	24018422
SUMO2_HUMAN	SUMO2	physical	24018422
CD2B2_HUMAN	CD2BP2	physical	26344197
CPSF1_HUMAN	CPSF1	physical	26344197
MAP2_HUMAN	METAP2	physical	26344197
MTA1_HUMAN	MTA1	physical	26344197
MTA2_HUMAN	MTA2	physical	26344197
MTA3_HUMAN	MTA3	physical	26344197
H31_HUMAN	HIST1H3A	physical	25533843
H2B1B_HUMAN	HIST1H2BB	physical	25533843

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 CHD3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-713; SER-1601 ANDSER-1605, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-1549; SER-1601AND SER-1605, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-713; SER-1361; SER-1364;SER-1367; SER-1601 AND SER-1605, AND MASS 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-713 AND SER-1601, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASSSPECTROMETRY.	18187866 [Abstract]
"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-324; SER-713; SER-1601AND SER-1605, AND MASS SPECTROMETRY.	17081983 [Abstract]
"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-713 AND SER-1601, ANDMASS SPECTROMETRY.	15302935 [Abstract]

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