EMSY_MOUSE - dbPTM
EMSY_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EMSY_MOUSE
UniProt AC Q8BMB0
Protein Name BRCA2-interacting transcriptional repressor EMSY {ECO:0000250|UniProtKB:Q7Z589}
Gene Name Emsy {ECO:0000250|UniProtKB:Q7Z589}
Organism Mus musculus (Mouse).
Sequence Length 1264
Subcellular Localization Nucleus . Localizes to DNA damage markers in irradiated cells, suggesting that it participates in DNA repair process.
Protein Description Regulator which is able to repress transcription, possibly via its interaction with a multiprotein chromatin remodeling complex that modifies the chromatin. Its interaction with BRCA2 suggests that it may play a central role in the DNA repair function of BRCA2 (By similarity). As part of a H3-specific methyltransferase complex may mediate ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity)..
Protein Sequence MPVVWPTLLDLSRDECKRILRKLELEAYAGVISALRAQGDLTKEKKDLLGELSKVLSISTERHRAEVRRAVNDERLTTIAHKMNLSLYLGERPSYSMSGPNSSSEWSIEGRRLVPLMPRLVPQTAFTVTANAVANAAVQHNASLPVPAETASKDGVSCSDEDEKPRKRRRTNSSSSSPVVLKEVPKAVVPVSKTITVPVSGSPKMSNIMQSIANSLPPHMSPVKITFTKPSTQTTNTTTQKVIIVTTSPSSTFVPNILSKSHNYAAVTKLVPTSVIASTTQKPPVVITASQASLVTSSSNGNSSSTSSPISSTVAVTTVVSSTPSVVMSTVAQGVSTSAIKVASTRLPSPKSLVSGPTQILAQFPKQHQQSPKQQLQQVQQQTQQPVAQPSSVSQQQQPQQSALPPGIKPTIQIKQESGVKIITQQVQPSKILPKPVTATLPTSSNSPIMVVSSNGAIMTTKLVTTPTGTQATYTRPTVSPSLGRVATTPGAATYVKTTSGSIITVVPKSLATLGGKIISSNIVSGTTTKITTIPMTSKPNVIVVQKTTGKGTTIQGLPGKNVVTTLLNAGGEKTLQTVPAGAKPAIITATRPITKMIVTQPKGIGSAVQPAAKIIPTKIVYGQQGKTQVLIKPKPVTFQATVVSEQTRQLVTETLQQASRVADASNSSAQEGKEEPQGYTDSSSSSTESSQSSQDSQPVVHVIASRRQDWSEHEIAMETSPTIIYQDVSSESQSATSTIKALLELQQTTVKEKLESKPRQPTIDLSQMAVPIQMTQEKRHSPESPSIAVVESELVAEYITTVSHRSQPQQPSQPQRTLLQHVAQSQTATQTSVVVKSIPASSPGAITHIMQQALSSHTAFTKHSEELGTEEGEVEEMDTLDPQTGLFYRSALTQSQSTKQQKLSQPQLEQTQLQVKTLQCFQTKQKQTIHLQADQLQHKLTQMPQLSIRHQKLNPLQQEQAQPKPDAQHTQHTVVAKDRQLPTLMAQPPQTVVQVLAVKTTQQLPKLQQAPNQPKIYVQPQTPQSQMALPSSEKQPASQVEQPIITQGSSVTKITFEGRQPPTVTKITGGSSVPKLTSPVTSISPIQASEKTAVSDILQMSLMEAQIDTNVEHMVVDPPKKALATNVLTGEAGALPSTHVVVAGMTKCRESCSSPSAVGPPLTTRKIEAAGVPTTGQFMRIQNVGQKKAEESPTEIIIQAIPQYAIPCHSSSNVVVEPSGLLELNNFTSQQLDDDETAMEQDIDSSTEDGTEPSPSQSAVERS
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
33PhosphorylationEAYAGVISALRAQGD
HHHHHHHHHHHHCCC		20.8828285833
157PhosphorylationTASKDGVSCSDEDEK
CCCCCCCCCCCCCCC		17.2725159016
159PhosphorylationSKDGVSCSDEDEKPR
CCCCCCCCCCCCCCC		36.2125159016
171PhosphorylationKPRKRRRTNSSSSSP
CCCCCCCCCCCCCCC		37.3323527152
173PhosphorylationRKRRRTNSSSSSPVV
CCCCCCCCCCCCCEE		30.8625521595
174PhosphorylationKRRRTNSSSSSPVVL
CCCCCCCCCCCCEEE		35.9925168779
175PhosphorylationRRRTNSSSSSPVVLK
CCCCCCCCCCCEEEC		34.3628833060
176PhosphorylationRRTNSSSSSPVVLKE
CCCCCCCCCCEEECC		40.3828833060
177PhosphorylationRTNSSSSSPVVLKEV
CCCCCCCCCEEECCC		24.5421082442
192PhosphorylationPKAVVPVSKTITVPV
CCCEEECCCEEEEEC		20.2922817900
192O-linked_GlycosylationPKAVVPVSKTITVPV
CCCEEECCCEEEEEC		20.2922517741
196PhosphorylationVPVSKTITVPVSGSP
EECCCEEEEECCCCH		24.8025777480
200O-linked_GlycosylationKTITVPVSGSPKMSN
CEEEEECCCCHHHHH		27.7322517741
200PhosphorylationKTITVPVSGSPKMSN
CEEEEECCCCHHHHH		27.7325266776
202PhosphorylationITVPVSGSPKMSNIM
EEEECCCCHHHHHHH		17.5326824392
221PhosphorylationNSLPPHMSPVKITFT
HCCCCCCCCEEEEEE		24.4126643407
228O-linked_GlycosylationSPVKITFTKPSTQTT
CCEEEEEECCCCCCC		33.1422517741
231O-linked_GlycosylationKITFTKPSTQTTNTT
EEEEECCCCCCCCCC		34.4022517741
232O-linked_GlycosylationITFTKPSTQTTNTTT
EEEECCCCCCCCCCE		38.1655411821
234O-linked_GlycosylationFTKPSTQTTNTTTQK
EECCCCCCCCCCEEE		23.3155411813
235O-linked_GlycosylationTKPSTQTTNTTTQKV
ECCCCCCCCCCEEEE		22.2822517741
246O-linked_GlycosylationTQKVIIVTTSPSSTF
EEEEEEEECCCCCCC		15.9122517741
246PhosphorylationTQKVIIVTTSPSSTF
EEEEEEEECCCCCCC		15.9125159016
247O-linked_GlycosylationQKVIIVTTSPSSTFV
EEEEEEECCCCCCCC		27.9622517741
247PhosphorylationQKVIIVTTSPSSTFV
EEEEEEECCCCCCCC		27.9625159016
248PhosphorylationKVIIVTTSPSSTFVP
EEEEEECCCCCCCCC		17.2625159016
250PhosphorylationIIVTTSPSSTFVPNI
EEEECCCCCCCCCCH		41.6025159016
251PhosphorylationIVTTSPSSTFVPNIL
EEECCCCCCCCCCHH		29.2825159016
252PhosphorylationVTTSPSSTFVPNILS
EECCCCCCCCCCHHH		32.7525159016
259PhosphorylationTFVPNILSKSHNYAA
CCCCCHHHCCCCEEE		28.4525159016
345PhosphorylationSAIKVASTRLPSPKS
HHHHHHCCCCCCCHH		26.8723140645
349PhosphorylationVASTRLPSPKSLVSG
HHCCCCCCCHHHCCC		49.9424453211
352PhosphorylationTRLPSPKSLVSGPTQ
CCCCCCHHHCCCCHH		37.0729899451
465O-linked_GlycosylationIMTTKLVTTPTGTQA
EEEEEEEECCCCCEE		37.1822517741
470O-linked_GlycosylationLVTTPTGTQATYTRP
EEECCCCCEEEEECC		19.9422517741
499O-linked_GlycosylationAATYVKTTSGSIITV
CCEEEEECCCCEEEE		25.9322517741
500O-linked_GlycosylationATYVKTTSGSIITVV
CEEEEECCCCEEEEE		35.4622517741
517AcetylationSLATLGGKIISSNIV
HHHHCCCEEEECCCC		34.7622826441
520O-linked_GlycosylationTLGGKIISSNIVSGT
HCCCEEEECCCCCCC		22.3222517741
521O-linked_GlycosylationLGGKIISSNIVSGTT
CCCEEEECCCCCCCC		21.8422517741
525O-linked_GlycosylationIISSNIVSGTTTKIT
EEECCCCCCCCEEEE		26.9955411837
529O-linked_GlycosylationNIVSGTTTKITTIPM
CCCCCCCEEEEEEEC		21.9337820525
584AcetylationQTVPAGAKPAIITAT
EECCCCCCCEEEEEC		33.7823236377
763PhosphorylationESKPRQPTIDLSQMA
HCCCCCCCCCHHHCC		20.84-
782PhosphorylationMTQEKRHSPESPSIA
CCCCCCCCCCCCCEE		34.1026745281
785PhosphorylationEKRHSPESPSIAVVE
CCCCCCCCCCEEEEC		27.6026745281
787PhosphorylationRHSPESPSIAVVESE
CCCCCCCCEEEECHH		32.2426745281
838PhosphorylationQTSVVVKSIPASSPG
CEEEEEEECCCCCCC		23.3823984901
842PhosphorylationVVKSIPASSPGAITH
EEEECCCCCCCHHHH		31.5423984901
843PhosphorylationVKSIPASSPGAITHI
EEECCCCCCCHHHHH		29.4723984901
848PhosphorylationASSPGAITHIMQQAL
CCCCCHHHHHHHHHH		12.5723984901
903AcetylationSQSTKQQKLSQPQLE
CHHHHHHHCCCHHHH		47.8419851033
948PhosphorylationLTQMPQLSIRHQKLN
HHHCCHHHHHHHCCC		16.6022942356
1033PhosphorylationSQMALPSSEKQPASQ
HHCCCCCCCCCCHHH		47.04-
1039PhosphorylationSSEKQPASQVEQPII
CCCCCCHHHCCCCEE		41.25-
1069O-linked_GlycosylationPPTVTKITGGSSVPK
CCCEEEECCCCCCCC		36.7322517741
1078PhosphorylationGSSVPKLTSPVTSIS
CCCCCCCCCCCCCCC		36.7928833060
1079PhosphorylationSSVPKLTSPVTSISP
CCCCCCCCCCCCCCC		28.0128833060
1082PhosphorylationPKLTSPVTSISPIQA
CCCCCCCCCCCCCCC		24.5928833060
1083PhosphorylationKLTSPVTSISPIQAS
CCCCCCCCCCCCCCC		22.6928833060
1085PhosphorylationTSPVTSISPIQASEK
CCCCCCCCCCCCCHH		18.7328833060
1090PhosphorylationSISPIQASEKTAVSD
CCCCCCCCHHHHHHH		24.2128833060
1152PhosphorylationGMTKCRESCSSPSAV
CCCCHHHHCCCCCCC		10.4325619855
1154PhosphorylationTKCRESCSSPSAVGP
CCHHHHCCCCCCCCC		55.3425619855
1155PhosphorylationKCRESCSSPSAVGPP
CHHHHCCCCCCCCCC		27.4825619855
1157PhosphorylationRESCSSPSAVGPPLT
HHHCCCCCCCCCCCC		37.2225619855
1164PhosphorylationSAVGPPLTTRKIEAA
CCCCCCCCCCCEEEC		30.2622705319
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 EMSY_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EMSY_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 EMSY_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of EMSY_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EMSY_MOUSE

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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"O-linked N-acetylglucosamine proteomics of postsynaptic densitypreparations using lectin weak affinity chromatography and massspectrometry.";
Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,Maltby D.A., Schoepfer R., Burlingame A.L.;
Mol. Cell. Proteomics 5:923-934(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASSSPECTROMETRY.

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