JARD2_MOUSE - dbPTM
JARD2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JARD2_MOUSE
UniProt AC Q62315
Protein Name Protein Jumonji
Gene Name Jarid2
Organism Mus musculus (Mouse).
Sequence Length 1234
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 MSKERPKRNIIQKKYDDSDGIPWSEERVVRKVLYLSLKEFKNAQKRQHGEGLAGSLKAVNGLLGNAQAKALGPASEQSENEKDDASQVSSTSNDVSSSDFEEGPSRKRPRLQAQRKFAQSQPNSPSTTPVKIVEPLLPPPATQISDLSKRKPKTEDFLTFLCLRGSPALPNSMVYFGSSQDEEDVEEEDDETEDVKATTNNASSSCQSTPRKGKTHKHVHNGHVFNGSSRSAREKEPAHKHRSKEATPGKEKHSEPRADSRREQASGAQPTAASAAASSAKGLAANHQPPPSHRSAQDLRKQVSKVNGVTRMSSLGAGTNSAKKIREVRPSPSKTVKYTATVTKGTVTYTKAKRELVKETKPNHHKPSSAVNHTISGKTESSNAKTRKQVLSLGGASKSTGPAASGLKASSRLNPKSCTKEVGGRQLREGLRNSKRRLEEAQQVDKPQSPPKKMKGVAGNAEAPGKKASAASGEKSLLNGHVKKEVPERSLERNRPKRAAAGKNMLGKQAHGKTEGTPCENRSTSQPESSHKPHDPQGKPEKGSGKSGWAAMDEIPVLRPSAKEFHDPLIYIESVRAQVEKYGMCRVIPPPDWRPECKLNDEMRFVTQIQHIHKLGRRWGPNVQRLACIKKHLRSQGITMDELPLIGGCELDLACFFRLINEMGGMQQVTDLKKWNKLADMLRIPKTAQDRLAKLQEAYCQYLLSYDSLSPEEHRRLEKEVLMEKEILEKRKGPLEGHTESDHHKFHSLPRFEPKNGLVHGVTPRNGFRSKLKEVGRAPLKTGRRRLFAQEKEVVKEEEEDKGVLNDFHKCIYKGRSVSLTTFYRTARNIMNMCFSKEPAPAEIEQEYWRLVEEKDCHVAVHCGKVDTNTHGSGFPVGKSEPFSRHGWNLTVLPNNTGSILRHLGAVPGVTIPWLNIGMVFSTSCWSRDQNHLPYIDYLHTGADCIWYCIPAEEENKLEDVVHTLLQGNGTPGLQMLESNVMISPEVLCKKGIKVHRTVQQSGQFVVCFPGSFVSKVCCGYNVSETVHFATTQWTSMGFETAKEMKRRHIAKPFSMEKLLYQIAQAEAKKENGPTLSTISALLDELRDTELRQRRLLFEAGLHSSARYGSHDGNSTVADGKKKPRKWLQLETSERRCQICQHLCYLSMVVQENENVVFCLECALRHVEKQKSCRGLKLMYRYDEEQIISLVNQICGKVSGKHGGIENCLNKPTPKRGPRKRATVDVPPSRLPSS
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 Orthologous
Protein Cluster
78PhosphorylationLGPASEQSENEKDDA
HCCCCCCCCCCCCCH		38.0327841257
89PhosphorylationKDDASQVSSTSNDVS
CCCHHHCCCCCCCCC		21.9123375375
90PhosphorylationDDASQVSSTSNDVSS
CCHHHCCCCCCCCCH		36.6823375375
91PhosphorylationDASQVSSTSNDVSSS
CHHHCCCCCCCCCHH		24.8423375375
92PhosphorylationASQVSSTSNDVSSSD
HHHCCCCCCCCCHHH		32.7425293948
96PhosphorylationSSTSNDVSSSDFEEG
CCCCCCCCHHHCCCC		27.3025293948
203PhosphorylationKATTNNASSSCQSTP
HHHCCCCCCCCCCCC		25.5522871156
204PhosphorylationATTNNASSSCQSTPR
HHCCCCCCCCCCCCC		32.4922871156
208PhosphorylationNASSSCQSTPRKGKT
CCCCCCCCCCCCCCC		44.7130482847
209PhosphorylationASSSCQSTPRKGKTH
CCCCCCCCCCCCCCC		10.9622006019
295PhosphorylationQPPPSHRSAQDLRKQ
CCCCCCCCHHHHHHH		25.5128285833
305AcetylationDLRKQVSKVNGVTRM
HHHHHHHHHCCCCHH		40.647713345
319PhosphorylationMSSLGAGTNSAKKIR
HHHCCCCCCCCHHHE		26.0128066266
321PhosphorylationSLGAGTNSAKKIREV
HCCCCCCCCHHHEEC		41.1028066266
331PhosphorylationKIREVRPSPSKTVKY
HHEECCCCCCCCEEE		31.1029895711
333PhosphorylationREVRPSPSKTVKYTA
EECCCCCCCCEEEEE		45.3428066266
378AcetylationVNHTISGKTESSNAK
CCCCCCCCCCCCCCH		42.18-
405PhosphorylationKSTGPAASGLKASSR
CCCCCCHHCCCCCCC		46.9228059163
410PhosphorylationAASGLKASSRLNPKS
CHHCCCCCCCCCCCC		17.88-
411PhosphorylationASGLKASSRLNPKSC
HHCCCCCCCCCCCCC		45.7228059163
449PhosphorylationQQVDKPQSPPKKMKG
HHCCCCCCCCCCCCC		52.2625159016
490PhosphorylationKKEVPERSLERNRPK
CCCCCHHHHHHCCCC		32.68-
523PhosphorylationGTPCENRSTSQPESS
CCCCCCCCCCCCCCC		43.9529895711
673UbiquitinationMQQVTDLKKWNKLAD
CHHHCCHHHHHHHHH		59.5622790023
813PhosphorylationNDFHKCIYKGRSVSL
CHHHHHHHCCCCCCH		19.50-
819PhosphorylationIYKGRSVSLTTFYRT
HHCCCCCCHHHHHHH		22.6528059163
824PhosphorylationSVSLTTFYRTARNIM
CCCHHHHHHHHHHHH		12.6428059163
1172PhosphorylationRHVEKQKSCRGLKLM
HHHHHHHCCCCCCEE		13.42-
1213PhosphorylationENCLNKPTPKRGPRK
HHHCCCCCCCCCCCC		42.9528066266
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 JARD2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of JARD2_MOUSE !!
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 JARD2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUZ12_MOUSESuz12physical
20064375
EZH2_MOUSEEzh2physical
20064375
AEBP2_MOUSEAebp2physical
20064375
EED_MOUSEEedphysical
20064375
EZH1_MOUSEEzh1physical
20064376
EZH2_MOUSEEzh2physical
20064376
EED_MOUSEEedphysical
20064376
SUZ12_MOUSESuz12physical
20064376
RBBP4_MOUSERbbp4physical
20064376
AEBP2_MOUSEAebp2physical
20064376
MTF2_MOUSEMtf2physical
20064376
STK38_MOUSEStk38physical
20064376
SETX_MOUSESetxphysical
20064376
TRI35_MOUSETrim35physical
20064376
ELL_MOUSEEllphysical
20064376
TR150_MOUSEThrap3physical
20064376
BCLF1_MOUSEBclaf1physical
20064376
ST38L_MOUSEStk38lphysical
20064376
ICE1_MOUSEIce1physical
20064376
RB_MOUSERb1physical
15870077
PRD14_MOUSEPrdm14physical
23333148
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of JARD2_MOUSE

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Related Literatures of Post-Translational Modification

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