JARD2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: JARD2_HUMAN
• UniProt AC: Q92833
• Protein Name: Protein Jumonji
• Gene Name: JARID2
• Organism: Homo sapiens (Human).
• Sequence Length: 1246
• Subcellular Localization: Nucleus . Colocalizes with the PRC2 complex on chromatin.
• Protein Description: Regulator of histone methyltransferase complexes that plays an essential role in embryonic development, including heart and liver development, neural tube fusion process and hematopoiesis. Acts by modulating histone methyltransferase activity and promoting the recruitment of histone methyltransferase complexes to their target genes. Binds DNA and mediates the recruitment of the PRC2 complex to target genes in embryonic stem cells. Does not have histone demethylase activity but regulates activity of various histone methyltransferase complexes. In embryonic stem cells, it associates with the PRC2 complex and inhibits trimethylation of 'Lys-27' of histone H3 (H3K27me3) by the PRC2 complex, thereby playing a key role in differentiation of embryonic stem cells and normal development. In cardiac cells, it is required to repress expression of cyclin-D1 (CCND1) by activating methylation of 'Lys-9' of histone H3 (H3K9me) by the GLP1/EHMT1 and G9a/EHMT2 histone methyltransferases. Also acts as a transcriptional repressor of ANF via its interaction with GATA4 and NKX2-5. Participates in the negative regulation of cell proliferation signaling..
• Protein Sequence: MSKERPKRNIIQKKYDDSDGIPWSEERVVRKVLYLSLKEFKNSQKRQHAEGIAGSLKTVNGLLGNDQSKGLGPASEQSENEKDDASQVSSTSNDVSSSDFEEGPSRKRPRLQAQRKFAQSQPNSPSTTPVKIVEPLLPPPATQISDLSKRKPKTEDFLTFLCLRGSPALPNSMVYFGSSQDEEEVEEEDDETEDVKTATNNASSSCQSTPRKGKTHKHVHNGHVFNGSSRSTREKEPVQKHKSKEATPAKEKHSDHRADSRREQASANHPAAAPSTGSSAKGLAATHHHPPLHRSAQDLRKQVSKVNGVTRMSSLGAGVTSAKKMREVRPSPSKTVKYTATVTKGAVTYTKAKRELVKDTKPNHHKPSSAVNHTISGKTESSNAKTRKQVLSLGGASKSTGPAVNGLKVSGRLNPKSCTKEVGGRQLREGLQLREGLRNSKRRLEEAHQAEKPQSPPKKMKGAAGPAEGPGKKAPAERGLLNGHVKKEVPERSLERNRPKRATAGKSTPGRQAHGKADSASCENRSTSQPESVHKPQDSGKAEKGGGKAGWAAMDEIPVLRPSAKEFHDPLIYIESVRAQVEKFGMCRVIPPPDWRPECKLNDEMRFVTQIQHIHKLGRRWGPNVQRLACIKKHLKSQGITMDELPLIGGCELDLACFFRLINEMGGMQQVTDLKKWNKLADMLRIPRTAQDRLAKLQEAYCQYLLSYDSLSPEEHRRLEKEVLMEKEILEKRKGPLEGHTENDHHKFHPLPRFEPKNGLIHGVAPRNGFRSKLKEVGQAQLKTGRRRLFAQEKEVVKEEEEDKGVLNDFHKCIYKGRSVSLTTFYRTARNIMSMCFSKEPAPAEIEQEYWRLVEEKDCHVAVHCGKVDTNTHGSGFPVGKSEPFSRHGWNLTVLPNNTGSILRHLGAVPGVTIPWLNIGMVFSTSCWSRDQNHLPYIDYLHTGADCIWYCIPAEEENKLEDVVHTLLQANGTPGLQMLESNVMISPEVLCKEGIKVHRTVQQSGQFVVCFPGSFVSKVCCGYSVSETVHFATTQWTSMGFETAKEMKRRHIAKPFSMEKLLYQIAQAEAKKENGPTLSTISALLDELRDTELRQRRQLFEAGLHSSARYGSHDGSSTVADGKKKPRKWLQLETSERRCQICQHLCYLSMVVQENENVVFCLECALRHVEKQKSCRGLKLMYRYDEEQIISLVNQICGKVSGKNGSIENCLSKPTPKRGPRKRATVDVPPSRLSASSSSKSASSSS

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
15	Phosphorylation	RNIIQKKYDDSDGIP CCCCCCCCCCCCCCC	31.83	27259358
18	Phosphorylation	IQKKYDDSDGIPWSE CCCCCCCCCCCCCCH	34.53	27259358
34	Phosphorylation	RVVRKVLYLSLKEFK HHHHHHHHHHHHHHH	9.38	23025827
36	Phosphorylation	VRKVLYLSLKEFKNS HHHHHHHHHHHHHCH	24.68	23025827
38	Ubiquitination	KVLYLSLKEFKNSQK HHHHHHHHHHHCHHH	58.70	30230243
75	Phosphorylation	SKGLGPASEQSENEK CCCCCCCCCCCCCCC	39.02	25159151
78	Phosphorylation	LGPASEQSENEKDDA CCCCCCCCCCCCCCH	38.03	25849741
86	Phosphorylation	ENEKDDASQVSSTSN CCCCCCHHHCCCCCC	37.80	19664994
89	Phosphorylation	KDDASQVSSTSNDVS CCCHHHCCCCCCCCC	21.91	-
90	Phosphorylation	DDASQVSSTSNDVSS CCHHHCCCCCCCCCH	36.68	28348404
91	Phosphorylation	DASQVSSTSNDVSSS CHHHCCCCCCCCCHH	24.84	28348404
96	Phosphorylation	SSTSNDVSSSDFEEG CCCCCCCCHHHCCCC	27.30	21406692
97	Phosphorylation	STSNDVSSSDFEEGP CCCCCCCHHHCCCCC	33.50	21406692
98	Phosphorylation	TSNDVSSSDFEEGPS CCCCCCHHHCCCCCC	38.52	21406692
105	Phosphorylation	SDFEEGPSRKRPRLQ HHCCCCCCCCCHHHH	62.38	21406692
116	"N6,N6-dimethyllysine"	PRLQAQRKFAQSQPN HHHHHHHHHHHCCCC	32.73	-
116	Methylation	PRLQAQRKFAQSQPN HHHHHHHHHHHCCCC	32.73	-
120	Phosphorylation	AQRKFAQSQPNSPST HHHHHHHCCCCCCCC	44.14	28450419
124	Phosphorylation	FAQSQPNSPSTTPVK HHHCCCCCCCCCCCE	27.23	19664995
126	Phosphorylation	QSQPNSPSTTPVKIV HCCCCCCCCCCCEEE	44.74	28450419
127	Phosphorylation	SQPNSPSTTPVKIVE CCCCCCCCCCCEEEE	38.20	28450419
128	Phosphorylation	QPNSPSTTPVKIVEP CCCCCCCCCCEEEEC	30.35	28450419
197	Phosphorylation	DETEDVKTATNNASS CCCCHHHHHCCCCCC	38.26	25262027
199	Phosphorylation	TEDVKTATNNASSSC CCHHHHHCCCCCCCC	33.95	25262027
203	Phosphorylation	KTATNNASSSCQSTP HHHCCCCCCCCCCCC	25.55	28450419
204	Phosphorylation	TATNNASSSCQSTPR HHCCCCCCCCCCCCC	32.49	28450419
205	Phosphorylation	ATNNASSSCQSTPRK HCCCCCCCCCCCCCC	17.43	25849741
206	Acetylation	TNNASSSCQSTPRKG CCCCCCCCCCCCCCC	3.91	19608861
208	Phosphorylation	NASSSCQSTPRKGKT CCCCCCCCCCCCCCC	44.71	28450419
209	Phosphorylation	ASSSCQSTPRKGKTH CCCCCCCCCCCCCCC	10.96	19664995
212	Acetylation	SCQSTPRKGKTHKHV CCCCCCCCCCCCCCC	67.00	69433
231	Phosphorylation	VFNGSSRSTREKEPV CCCCCCCCCCCCCCC	33.49	22617229
232	Phosphorylation	FNGSSRSTREKEPVQ CCCCCCCCCCCCCCH	41.56	22617229
244	Acetylation	PVQKHKSKEATPAKE CCHHCCCCCCCCCHH	57.05	7664583
247	Phosphorylation	KHKSKEATPAKEKHS HCCCCCCCCCHHHCC	25.52	23532336
250	Acetylation	SKEATPAKEKHSDHR CCCCCCCHHHCCCHH	69.38	7664593
276	Phosphorylation	HPAAAPSTGSSAKGL CCCCCCCCCCCHHCH	39.77	25627689
278	Phosphorylation	AAAPSTGSSAKGLAA CCCCCCCCCHHCHHH	27.49	25627689
279	Phosphorylation	AAPSTGSSAKGLAAT CCCCCCCCHHCHHHH	35.03	25627689
310	Phosphorylation	VSKVNGVTRMSSLGA HHHHCCCCHHHHCCC	23.27	20860994
314	Phosphorylation	NGVTRMSSLGAGVTS CCCCHHHHCCCCCCC	22.83	24247654
320	Phosphorylation	SSLGAGVTSAKKMRE HHCCCCCCCHHHHCC	23.27	28122231
321	Phosphorylation	SLGAGVTSAKKMREV HCCCCCCCHHHHCCC	35.37	28122231
323	Acetylation	GAGVTSAKKMREVRP CCCCCCHHHHCCCCC	47.04	25953088
324	Ubiquitination	AGVTSAKKMREVRPS CCCCCHHHHCCCCCC	42.79	-
331	Phosphorylation	KMREVRPSPSKTVKY HHCCCCCCCCCCEEE	31.10	23401153
333	Phosphorylation	REVRPSPSKTVKYTA CCCCCCCCCCEEEEE	45.34	30266825
335	Phosphorylation	VRPSPSKTVKYTATV CCCCCCCCEEEEEEE	26.94	21712546
338	Phosphorylation	SPSKTVKYTATVTKG CCCCCEEEEEEEECC	9.40	22817900
339	Phosphorylation	PSKTVKYTATVTKGA CCCCEEEEEEEECCC	15.33	21712546
349	Phosphorylation	VTKGAVTYTKAKREL EECCCEEEHHHHHHH	10.31	-
378	Acetylation	VNHTISGKTESSNAK CCCCCCCCCCCCCCH	42.18	19608861
393	Ubiquitination	TRKQVLSLGGASKST HHHHHHHCCCCCCCC	6.84	29967540
417	Phosphorylation	SGRLNPKSCTKEVGG ECCCCCCCCCCCCCC	28.42	26330541
419	Phosphorylation	RLNPKSCTKEVGGRQ CCCCCCCCCCCCCCH	37.01	26330541
455	Phosphorylation	HQAEKPQSPPKKMKG HHCCCCCCCCCCCCC	52.26	23401153
459	Acetylation	KPQSPPKKMKGAAGP CCCCCCCCCCCCCCC	52.17	18604547
461	Acetylation	QSPPKKMKGAAGPAE CCCCCCCCCCCCCCC	55.03	18604555
472	Acetylation	GPAEGPGKKAPAERG CCCCCCCCCCCHHHC	49.23	25953088
473	Acetylation	PAEGPGKKAPAERGL CCCCCCCCCCHHHCC	66.57	7304103
493	Phosphorylation	KKEVPERSLERNRPK CCCCCHHHHHHCCCC	32.68	24719451
503	Ubiquitination	RNRPKRATAGKSTPG HCCCCCCCCCCCCCC	39.72	29967540
521	Phosphorylation	HGKADSASCENRSTS CCCCCCCCCCCCCCC	26.39	20860994
524	Ubiquitination	ADSASCENRSTSQPE CCCCCCCCCCCCCCC	47.75	29967540
526	Phosphorylation	SASCENRSTSQPESV CCCCCCCCCCCCCCC	43.95	21406692
527	Phosphorylation	ASCENRSTSQPESVH CCCCCCCCCCCCCCC	28.30	21406692
528	Phosphorylation	SCENRSTSQPESVHK CCCCCCCCCCCCCCC	45.01	21406692
532	Phosphorylation	RSTSQPESVHKPQDS CCCCCCCCCCCCCCC	35.88	21406692
539	Phosphorylation	SVHKPQDSGKAEKGG CCCCCCCCCCCCCCC	36.63	21406692
548	Ubiquitination	KAEKGGGKAGWAAMD CCCCCCCHHCCHHHH	47.18	-
549	Ubiquitination	AEKGGGKAGWAAMDE CCCCCCHHCCHHHHC	23.26	29967540
555	Ubiquitination	KAGWAAMDEIPVLRP HHCCHHHHCCCCCCC	46.04	29967540
565	Ubiquitination	PVLRPSAKEFHDPLI CCCCCCCHHHCCCEE	66.31	29967540
575	Ubiquitination	HDPLIYIESVRAQVE CCCEEEHHHHHHHHH	26.64	29967540
583	Ubiquitination	SVRAQVEKFGMCRVI HHHHHHHHHCCCEEC	48.65	-
603	Ubiquitination	RPECKLNDEMRFVTQ CCCCCCCHHHHHHHH	62.60	29967540
611	Ubiquitination	EMRFVTQIQHIHKLG HHHHHHHHHHHHHHH	2.05	29967540
616	Ubiquitination	TQIQHIHKLGRRWGP HHHHHHHHHHHHCCC	52.62	-
640	Ubiquitination	KHLKSQGITMDELPL HHHHHCCCCHHCCCC	1.93	29967540
672	Phosphorylation	MGGMQQVTDLKKWNK HCCCHHHCCHHHHHH	31.14	24043423
675	Ubiquitination	MQQVTDLKKWNKLAD CHHHCCHHHHHHHHH	59.56	29967540
679	Ubiquitination	TDLKKWNKLADMLRI CCHHHHHHHHHHHHC	43.89	-
685	Ubiquitination	NKLADMLRIPRTAQD HHHHHHHHCCCHHHH	30.17	29967540
696	Ubiquitination	TAQDRLAKLQEAYCQ HHHHHHHHHHHHHHH	56.12	29967540
721	Ubiquitination	EEHRRLEKEVLMEKE HHHHHHHHHHHHHHH	58.68	29967540
727	Ubiquitination	EKEVLMEKEILEKRK HHHHHHHHHHHHHCC	35.77	29967540
747	Ubiquitination	HTENDHHKFHPLPRF CCCCCCCCCCCCCCC	41.78	29967540
757	Ubiquitination	PLPRFEPKNGLIHGV CCCCCCCCCCCCCCC	57.35	-
775	Ubiquitination	NGFRSKLKEVGQAQL CCHHHHHHHHHHHHH	54.83	29967540
783	Ubiquitination	EVGQAQLKTGRRRLF HHHHHHHHHHHHHHH	36.53	29967540
812	Ubiquitination	GVLNDFHKCIYKGRS CCCCHHHHHHHCCCC	23.48	29967540
815	Phosphorylation	NDFHKCIYKGRSVSL CHHHHHHHCCCCCCH	19.50	-
819	Phosphorylation	KCIYKGRSVSLTTFY HHHHCCCCCCHHHHH	25.40	-
821	Phosphorylation	IYKGRSVSLTTFYRT HHCCCCCCHHHHHHH	22.65	30576142
826	Phosphorylation	SVSLTTFYRTARNIM CCCHHHHHHHHHHHH	12.64	30576142
834	Phosphorylation	RTARNIMSMCFSKEP HHHHHHHHHHCCCCC	14.49	-
838	Phosphorylation	NIMSMCFSKEPAPAE HHHHHHCCCCCCCHH	31.05	24719451
839	Ubiquitination	IMSMCFSKEPAPAEI HHHHHCCCCCCCHHH	47.68	-
857	Ubiquitination	YWRLVEEKDCHVAVH HHHHHHHHCCEEEEE	52.75	29967540
881	Ubiquitination	GSGFPVGKSEPFSRH CCCCCCCCCCCCCCC	52.45	-
882	Ubiquitination	SGFPVGKSEPFSRHG CCCCCCCCCCCCCCC	44.57	29967540
1054	Ubiquitination	MKRRHIAKPFSMEKL HHHHHCCCCCCHHHH	46.09	29967540
1072	Ubiquitination	IAQAEAKKENGPTLS HHHHHHHHHHCCCHH	64.56	-
1091	Phosphorylation	LLDELRDTELRQRRQ HHHHHHHHHHHHHHH	30.41	24719451
1106	Phosphorylation	LFEAGLHSSARYGSH HHHHCCCCCCCCCCC	30.64	24719451
1107	Phosphorylation	FEAGLHSSARYGSHD HHHCCCCCCCCCCCC	13.15	24719451
1112	Phosphorylation	HSSARYGSHDGSSTV CCCCCCCCCCCCCCC	14.96	22210691
1117	Phosphorylation	YGSHDGSSTVADGKK CCCCCCCCCCCCCCC	32.22	22210691
1118	Phosphorylation	GSHDGSSTVADGKKK CCCCCCCCCCCCCCC	22.78	22210691
1124	Ubiquitination	STVADGKKKPRKWLQ CCCCCCCCCCCCHHH	73.81	-
1174	Phosphorylation	RHVEKQKSCRGLKLM HHHHHHHCCCCCCEE	13.42	24719451
1179	Ubiquitination	QKSCRGLKLMYRYDE HHCCCCCCEEEECCH	33.75	-
1191	Phosphorylation	YDEEQIISLVNQICG CCHHHHHHHHHHHHC	28.08	27174698
1199	Ubiquitination	LVNQICGKVSGKNGS HHHHHHCCCCCCCCC	28.90	-
1201	Phosphorylation	NQICGKVSGKNGSIE HHHHCCCCCCCCCHH	47.76	27174698
1203	Ubiquitination	ICGKVSGKNGSIENC HHCCCCCCCCCHHHH	51.10	-
1213	Acetylation	SIENCLSKPTPKRGP CHHHHHCCCCCCCCC	39.71	26051181
1213	Ubiquitination	SIENCLSKPTPKRGP CHHHHHCCCCCCCCC	39.71	-
1215	Phosphorylation	ENCLSKPTPKRGPRK HHHHCCCCCCCCCCC	45.22	28122231
1225	Phosphorylation	RGPRKRATVDVPPSR CCCCCCCEECCCHHH	22.67	-

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

Oops, there are no upstream regulatory protein records of JARD2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of JARD2_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 JARD2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EHMT2_HUMAN	EHMT2	physical	19010785
EHMT1_HUMAN	EHMT1	physical	19010785
EZH2_HUMAN	EZH2	physical	20123894
SUZ12_HUMAN	SUZ12	physical	20123894
SETB1_HUMAN	SETDB1	physical	22110129
NKX25_HUMAN	NKX2-5	physical	15542826
GATA4_HUMAN	GATA4	physical	15542826
EZH2_HUMAN	EZH2	physical	20075857
SUZ12_HUMAN	SUZ12	physical	20075857
EZH1_HUMAN	EZH1	physical	20075857
EED_HUMAN	EED	physical	20075857
AEBP2_HUMAN	AEBP2	physical	20075857
RBBP4_HUMAN	RBBP4	physical	20075857
RBBP7_HUMAN	RBBP7	physical	20075857
HDAC2_HUMAN	HDAC2	physical	20075857

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

"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-378, AND MASS SPECTROMETRY.
PubMed: 19608861