MYSM1_HUMAN - dbPTM
MYSM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYSM1_HUMAN
UniProt AC Q5VVJ2
Protein Name Histone H2A deubiquitinase MYSM1
Gene Name MYSM1
Organism Homo sapiens (Human).
Sequence Length 828
Subcellular Localization Nucleus .
Protein Description Metalloprotease that specifically deubiquitinates monoubiquitinated histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Preferentially deubiquitinates monoubiquitinated H2A in hyperacetylated nucleosomes. Deubiquitination of histone H2A leads to facilitate the phosphorylation and dissociation of histone H1 from the nucleosome. Acts as a coactivator by participating in the initiation and elongation steps of androgen receptor (AR)-induced gene activation..
Protein Sequence MAAEEADVDIEGDVVAAAGAQPGSGENTASVLQKDHYLDSSWRTENGLIPWTLDNTISEENRAVIEKMLLEEEYYLSKKSQPEKVWLDQKEDDKKYMKSLQKTAKIMVHSPTKPASYSVKWTIEEKELFEQGLAKFGRRWTKISKLIGSRTVLQVKSYARQYFKNKVKCGLDKETPNQKTGHNLQVKNEDKGTKAWTPSCLRGRADPNLNAVKIEKLSDDEEVDITDEVDELSSQTPQKNSSSDLLLDFPNSKMHETNQGEFITSDSQEALFSKSSRGCLQNEKQDETLSSSEITLWTEKQSNGDKKSIELNDQKFNELIKNCNKHDGRGIIVDARQLPSPEPCEIQKNLNDNEMLFHSCQMVEESHEEEELKPPEQEIEIDRNIIQEEEKQAIPEFFEGRQAKTPERYLKIRNYILDQWEICKPKYLNKTSVRPGLKNCGDVNCIGRIHTYLELIGAINFGCEQAVYNRPQTVDKVRIRDRKDAVEAYQLAQRLQSMRTRRRRVRDPWGNWCDAKDLEGQTFEHLSAEELAKRREEEKGRPVKSLKVPRPTKSSFDPFQLIPCNFFSEEKQEPFQVKVASEALLIMDLHAHVSMAEVIGLLGGRYSEVDKVVEVCAAEPCNSLSTGLQCEMDPVSQTQASETLAVRGFSVIGWYHSHPAFDPNPSLRDIDTQAKYQSYFSRGGAKFIGMIVSPYNRNNPLPYSQITCLVISEEISPDGSYRLPYKFEVQQMLEEPQWGLVFEKTRWIIEKYRLSHSSVPMDKIFRRDSDLTCLQKLLECMRKTLSKVTNCFMAEEFLTEIENLFLSNYKSNQENGVTEENCTKELLM
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
11UbiquitinationEEADVDIEGDVVAAA
CCCCCCCCCCEEEEC		44.8922817900
12UbiquitinationEADVDIEGDVVAAAG
CCCCCCCCCEEEECC		33.0922817900
17UbiquitinationIEGDVVAAAGAQPGS
CCCCEEEECCCCCCC		8.5321890473
23UbiquitinationAAAGAQPGSGENTAS
EECCCCCCCCCCHHH		35.8822817900
27UbiquitinationAQPGSGENTASVLQK
CCCCCCCCHHHHHHH		44.4622817900
28UbiquitinationQPGSGENTASVLQKD
CCCCCCCHHHHHHHC		18.9222817900
31UbiquitinationSGENTASVLQKDHYL
CCCCHHHHHHHCCCC		6.4322817900
31 (in isoform 2)Ubiquitination-6.4321890473
35UbiquitinationTASVLQKDHYLDSSW
HHHHHHHCCCCCCCC		23.7827667366
40PhosphorylationQKDHYLDSSWRTENG
HHCCCCCCCCCCCCC		29.2530108239
41PhosphorylationKDHYLDSSWRTENGL
HCCCCCCCCCCCCCC		21.9030108239
44PhosphorylationYLDSSWRTENGLIPW
CCCCCCCCCCCCCCC		27.7822468782
46UbiquitinationDSSWRTENGLIPWTL
CCCCCCCCCCCCCCC		50.3821890473
56PhosphorylationIPWTLDNTISEENRA
CCCCCCCCCCHHHHH		26.0822468782
56UbiquitinationIPWTLDNTISEENRA
CCCCCCCCCCHHHHH		26.0827667366
58PhosphorylationWTLDNTISEENRAVI
CCCCCCCCHHHHHHH		36.5022468782
67UbiquitinationENRAVIEKMLLEEEY
HHHHHHHHHHHHHHH		24.5922817900
67 (in isoform 1)Ubiquitination-24.5921890473
68UbiquitinationNRAVIEKMLLEEEYY
HHHHHHHHHHHHHHH		3.1521890473
74PhosphorylationKMLLEEEYYLSKKSQ
HHHHHHHHHHCCCCC		17.0025072903
75PhosphorylationMLLEEEYYLSKKSQP
HHHHHHHHHCCCCCC		14.0525072903
77PhosphorylationLEEEYYLSKKSQPEK
HHHHHHHCCCCCCCC		23.1625072903
78UbiquitinationEEEYYLSKKSQPEKV
HHHHHHCCCCCCCCE		54.5721906983
78 (in isoform 1)Ubiquitination-54.5721890473
79UbiquitinationEEYYLSKKSQPEKVW
HHHHHCCCCCCCCEE		51.4522817900
81 (in isoform 3)Ubiquitination-60.0821890473
84UbiquitinationSKKSQPEKVWLDQKE
CCCCCCCCEECCCHH		45.4527667366
84 (in isoform 1)Ubiquitination-45.4521890473
90UbiquitinationEKVWLDQKEDDKKYM
CCEECCCHHHHHHHH		63.8827667366
90 (in isoform 1)Ubiquitination-63.8821890473
94UbiquitinationLDQKEDDKKYMKSLQ
CCCHHHHHHHHHHHH		59.1122817900
95UbiquitinationDQKEDDKKYMKSLQK
CCHHHHHHHHHHHHH		58.5322817900
96PhosphorylationQKEDDKKYMKSLQKT
CHHHHHHHHHHHHHH		18.6027134283
98UbiquitinationEDDKKYMKSLQKTAK
HHHHHHHHHHHHHHE		44.9527667366
99PhosphorylationDDKKYMKSLQKTAKI
HHHHHHHHHHHHHEE		21.3630576142
102UbiquitinationKYMKSLQKTAKIMVH
HHHHHHHHHHEEEEC		56.6027667366
105UbiquitinationKSLQKTAKIMVHSPT
HHHHHHHEEEECCCC		36.2429967540
110PhosphorylationTAKIMVHSPTKPASY
HHEEEECCCCCCCCE		23.8929255136
112PhosphorylationKIMVHSPTKPASYSV
EEEECCCCCCCCEEE		53.3129255136
112UbiquitinationKIMVHSPTKPASYSV
EEEECCCCCCCCEEE		53.3127667366
116PhosphorylationHSPTKPASYSVKWTI
CCCCCCCCEEEEEEE		26.8529255136
117PhosphorylationSPTKPASYSVKWTIE
CCCCCCCEEEEEEEC		21.4228450419
118PhosphorylationPTKPASYSVKWTIEE
CCCCCCEEEEEEECH		18.0929255136
126UbiquitinationVKWTIEEKELFEQGL
EEEEECHHHHHHHHH		47.1029967540
135UbiquitinationLFEQGLAKFGRRWTK
HHHHHHHHHHHHHHH		54.0923000965
135 (in isoform 1)Ubiquitination-54.0921890473
145UbiquitinationRRWTKISKLIGSRTV
HHHHHHHHHHCCCCH		47.8227667366
149PhosphorylationKISKLIGSRTVLQVK
HHHHHHCCCCHHHHH		20.1321406692
162PhosphorylationVKSYARQYFKNKVKC
HHHHHHHHHHCCCCC		15.8025367160
173UbiquitinationKVKCGLDKETPNQKT
CCCCCCCCCCCCCCC		69.4127667366
175PhosphorylationKCGLDKETPNQKTGH
CCCCCCCCCCCCCCC		33.0225159151
179UbiquitinationDKETPNQKTGHNLQV
CCCCCCCCCCCCCEE		64.2127667366
187SumoylationTGHNLQVKNEDKGTK
CCCCCEEECCCCCCC		41.48-
187SumoylationTGHNLQVKNEDKGTK
CCCCCEEECCCCCCC		41.4828112733
195UbiquitinationNEDKGTKAWTPSCLR
CCCCCCCCCCHHHHC		18.4022817900
197PhosphorylationDKGTKAWTPSCLRGR
CCCCCCCCHHHHCCC		15.3523312004
199PhosphorylationGTKAWTPSCLRGRAD
CCCCCCHHHHCCCCC		20.5723312004
217UbiquitinationNAVKIEKLSDDEEVD
CCEEEEECCCCCCCC		4.3822817900
218PhosphorylationAVKIEKLSDDEEVDI
CEEEEECCCCCCCCC		54.8325159151
226PhosphorylationDDEEVDITDEVDELS
CCCCCCCHHHHHHHH		22.9530266825
233PhosphorylationTDEVDELSSQTPQKN
HHHHHHHHHCCCCCC		20.5323403867
234PhosphorylationDEVDELSSQTPQKNS
HHHHHHHHCCCCCCC		51.1817525332
236PhosphorylationVDELSSQTPQKNSSS
HHHHHHCCCCCCCCC		29.6319690332
241PhosphorylationSQTPQKNSSSDLLLD
HCCCCCCCCCCEEEE		37.9526074081
242PhosphorylationQTPQKNSSSDLLLDF
CCCCCCCCCCEEEEC		36.9525850435
243PhosphorylationTPQKNSSSDLLLDFP
CCCCCCCCCEEEECC		31.9026074081
264PhosphorylationTNQGEFITSDSQEAL
CCCCCEECCCCHHHH		31.6329255136
265PhosphorylationNQGEFITSDSQEALF
CCCCEECCCCHHHHH		30.3729255136
267PhosphorylationGEFITSDSQEALFSK
CCEECCCCHHHHHCC		29.6817525332
273PhosphorylationDSQEALFSKSSRGCL
CCHHHHHCCCCCCCC		32.2630108239
280UbiquitinationSKSSRGCLQNEKQDE
CCCCCCCCCCHHCCC		7.3522817900
280 (in isoform 2)Ubiquitination-7.3521890473
284UbiquitinationRGCLQNEKQDETLSS
CCCCCCHHCCCCCCH		71.2722817900
284 (in isoform 1)Ubiquitination-71.2721890473
290PhosphorylationEKQDETLSSSEITLW
HHCCCCCCHHEEEEE		38.9623403867
291PhosphorylationKQDETLSSSEITLWT
HCCCCCCHHEEEEEE		34.7923403867
292PhosphorylationQDETLSSSEITLWTE
CCCCCCHHEEEEEEE		29.6423403867
295PhosphorylationTLSSSEITLWTEKQS
CCCHHEEEEEEEECC		16.5223403867
300UbiquitinationEITLWTEKQSNGDKK
EEEEEEEECCCCCCC		52.2129967540
315UbiquitinationSIELNDQKFNELIKN
CEECCHHHHHHHHHH		53.6829967540
321UbiquitinationQKFNELIKNCNKHDG
HHHHHHHHHCCCCCC		68.9829967540
337UbiquitinationGIIVDARQLPSPEPC
CEEEECCCCCCCCCC		60.4927667366
340PhosphorylationVDARQLPSPEPCEIQ
EECCCCCCCCCCCCC		50.9529255136
359UbiquitinationDNEMLFHSCQMVEES
CCCHHHHHHHHHHHH		9.9427667366
391UbiquitinationNIIQEEEKQAIPEFF
HHCHHHHHHHCHHHH		48.5929967540
405PhosphorylationFEGRQAKTPERYLKI
HCCCCCCCHHHHHHH		33.14-
409PhosphorylationQAKTPERYLKIRNYI
CCCCHHHHHHHHHHH		15.64-
411AcetylationKTPERYLKIRNYILD
CCHHHHHHHHHHHHH		30.5911792101
422UbiquitinationYILDQWEICKPKYLN
HHHHHHHCCCCCCCC		3.1423000965
422 (in isoform 2)Ubiquitination-3.1421890473
426UbiquitinationQWEICKPKYLNKTSV
HHHCCCCCCCCCCCC		48.1127667366
444UbiquitinationLKNCGDVNCIGRIHT
CCCCCCCCHHHHHHH		19.2122817900
466UbiquitinationINFGCEQAVYNRPQT
HHHCCCHHHHCCCCC		5.4022817900
533UbiquitinationLSAEELAKRREEEKG
CCHHHHHHHHHHHCC		65.6922817900
533 (in isoform 1)Ubiquitination-65.6921890473
545PhosphorylationEKGRPVKSLKVPRPT
HCCCCCCCCCCCCCC		33.3924719451
557UbiquitinationRPTKSSFDPFQLIPC
CCCCCCCCCCCEEEC		45.0823503661
586UbiquitinationVASEALLIMDLHAHV
EHHHHHHHHHHHHCH		1.7823000965
608UbiquitinationLLGGRYSEVDKVVEV
HHCCCHHHHCHHHHH		45.8923000965
675UbiquitinationRDIDTQAKYQSYFSR
HHCCHHHHHHHHHCC		33.7223000965
675 (in isoform 1)Ubiquitination-33.7221890473
693PhosphorylationKFIGMIVSPYNRNNP
CEEEEEECCCCCCCC		15.6728464451
721UbiquitinationEISPDGSYRLPYKFE
EECCCCCCCCCEEEE		23.0023503661
743UbiquitinationPQWGLVFEKTRWIIE
CCCEEEEHHHHHHHH		46.1423503661
757PhosphorylationEKYRLSHSSVPMDKI
HHHCCCCCCCCHHHH		29.6529759185
758PhosphorylationKYRLSHSSVPMDKIF
HHCCCCCCCCHHHHH		25.4729759185
784PhosphorylationLLECMRKTLSKVTNC
HHHHHHHHHHHHHCH		26.3728152594
786PhosphorylationECMRKTLSKVTNCFM
HHHHHHHHHHHCHHH		30.2528152594
809UbiquitinationENLFLSNYKSNQENG
HHHHHHCCCCCCCCC		16.6523503661
810UbiquitinationNLFLSNYKSNQENGV
HHHHHCCCCCCCCCC		47.3723503661
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 MYSM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYSM1_HUMAN !!
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 MYSM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H2A2C_HUMANHIST2H2ACphysical
17707232
MEP50_HUMANWDR77physical
17707232
HNRH1_HUMANHNRNPH1physical
17707232
TBB1_HUMANTUBB1physical
17707232
EF1A1_HUMANEEF1A1physical
17707232
STK38_HUMANSTK38physical
17707232
ANM5_HUMANPRMT5physical
17707232
UBC_HUMANUBCphysical
17707232
KAT2B_HUMANKAT2Bphysical
17707232
RBM10_HUMANRBM10physical
17707232
KIF11_HUMANKIF11physical
17707232
H2A2C_HUMANHIST2H2ACphysical
21245042
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 MYSM1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-218 AND THR-236, ANDMASS SPECTROMETRY.
"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-218, AND MASSSPECTROMETRY.
"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-218; SER-234 ANDSER-267, AND MASS SPECTROMETRY.

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