ZMY11_HUMAN - dbPTM
ZMY11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZMY11_HUMAN
UniProt AC Q15326
Protein Name Zinc finger MYND domain-containing protein 11 {ECO:0000305}
Gene Name ZMYND11 {ECO:0000312|HGNC:HGNC:16966}
Organism Homo sapiens (Human).
Sequence Length 602
Subcellular Localization Nucleus . Chromosome . Associates with chromatin and mitotic chromosomes.
Protein Description Chromatin reader that specifically recognizes and binds histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and regulates RNA polymerase II elongation. Does not bind other histone H3 subtypes (H3.1 or H3.2) (By similarity). Colocalizes with highly expressed genes and functions as a transcription corepressor by modulating RNA polymerase II at the elongation stage. Binds non-specifically to dsDNA. [PubMed: 24675531 Acts as a tumor-suppressor by repressing a transcriptional program essential for tumor cell growth.; (Microbial infection) Inhibits Epstein-Barr virus EBNA2-mediated transcriptional activation and host cell proliferation, through direct interaction.]
Protein Sequence MARLTKRRQADTKAIQHLWAAIEIIRNQKQIANIDRITKYMSRVHGMHPKETTRQLSLAVKDGLIVETLTVGCKGSKAGIEQEGYWLPGDEIDWETENHDWYCFECHLPGEVLICDLCFRVYHSKCLSDEFRLRDSSSPWQCPVCRSIKKKNTNKQEMGTYLRFIVSRMKERAIDLNKKGKDNKHPMYRRLVHSAVDVPTIQEKVNEGKYRSYEEFKADAQLLLHNTVIFYGADSEQADIARMLYKDTCHELDELQLCKNCFYLSNARPDNWFCYPCIPNHELVWAKMKGFGFWPAKVMQKEDNQVDVRFFGHHHQRAWIPSENIQDITVNIHRLHVKRSMGWKKACDELELHQRFLREGRFWKSKNEDRGEEEAESSISSTSNEQLKVTQEPRAKKGRRNQSVEPKKEEPEPETEAVSSSQEIPTMPQPIEKVSVSTQTKKLSASSPRMLHRSTQTTNDGVCQSMCHDKYTKIFNDFKDRMKSDHKRETERVVREALEKLRSEMEEEKRQAVNKAVANMQGEMDRKCKQVKEKCKEEFVEEIKKLATQHKQLISQTKKKQWCYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR
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
29UbiquitinationIEIIRNQKQIANIDR
HHHHHCHHHHCCHHH		2.01-
52PhosphorylationHGMHPKETTRQLSLA
CCCCCHHHHHHHHHH		9.9323898821
57PhosphorylationKETTRQLSLAVKDGL
HHHHHHHHHHHCCCE		40.8423312004
77UbiquitinationTVGCKGSKAGIEQEG
EECCCCCCCCCCCCC		2.29-
125UbiquitinationCFRVYHSKCLSDEFR
HHHHHHHHHCCCCCC		1.91-
137PhosphorylationEFRLRDSSSPWQCPV
CCCCCCCCCCCCCCC		40.0025627689
138PhosphorylationFRLRDSSSPWQCPVC
CCCCCCCCCCCCCCH		70.9225159151
160PhosphorylationTNKQEMGTYLRFIVS
CCHHHHHHHHHHHHH		34.8320049867
161PhosphorylationNKQEMGTYLRFIVSR
CHHHHHHHHHHHHHH		4.0020049867
167PhosphorylationTYLRFIVSRMKERAI
HHHHHHHHHHHHHCH		61.1120049867
200PhosphorylationHSAVDVPTIQEKVNE
HHHCCCHHHHHHHHC		2.69-
209UbiquitinationQEKVNEGKYRSYEEF
HHHHHCCCCCCHHHH		3.17-
217SumoylationYRSYEEFKADAQLLL
CCCHHHHHHHHHHHH		7.59-
246UbiquitinationDIARMLYKDTCHELD
HHHHHHHHHHHHHHC		8.45-
289AcetylationELVWAKMKGFGFWPA
CEEEEHHCCCCCCCC		18.7826051181
297UbiquitinationGFGFWPAKVMQKEDN
CCCCCCCEEEEECCC		6.97-
301UbiquitinationWPAKVMQKEDNQVDV
CCCEEEEECCCEEEE		9.60-
345UbiquitinationKRSMGWKKACDELEL
HHHHCHHHHHHHHHH		57.99-
366SumoylationEGRFWKSKNEDRGEE
HCCCCCCCCCCCCHH		51.3628112733
366AcetylationEGRFWKSKNEDRGEE
HCCCCCCCCCCCCHH		51.3626051181
377PhosphorylationRGEEEAESSISSTSN
CCHHHHHHHHCCCCC		17.5719691289
378PhosphorylationGEEEAESSISSTSNE
CHHHHHHHHCCCCCH		4.6719691289
380PhosphorylationEEAESSISSTSNEQL
HHHHHHHCCCCCHHC		29.4619691289
381PhosphorylationEAESSISSTSNEQLK
HHHHHHCCCCCHHCE		25.0725849741
382PhosphorylationAESSISSTSNEQLKV
HHHHHCCCCCHHCEE		55.3719691289
383PhosphorylationESSISSTSNEQLKVT
HHHHCCCCCHHCEEC		53.5427135362
403PhosphorylationKKGRRNQSVEPKKEE
HCCCCCCCCCCCCCC		5.7221712546
407SumoylationRNQSVEPKKEEPEPE
CCCCCCCCCCCCCCC		19.08-
407SumoylationRNQSVEPKKEEPEPE
CCCCCCCCCCCCCCC		19.0828112733
408AcetylationNQSVEPKKEEPEPET
CCCCCCCCCCCCCCC		24.1726051181
408SumoylationNQSVEPKKEEPEPET
CCCCCCCCCCCCCCC		24.1728112733
415PhosphorylationKEEPEPETEAVSSSQ
CCCCCCCCCCCCCCC		29.8628555341
419PhosphorylationEPETEAVSSSQEIPT
CCCCCCCCCCCCCCC		47.6430278072
420PhosphorylationPETEAVSSSQEIPTM
CCCCCCCCCCCCCCC		49.1330278072
421PhosphorylationETEAVSSSQEIPTMP
CCCCCCCCCCCCCCC		24.9517525332
426PhosphorylationSSSQEIPTMPQPIEK
CCCCCCCCCCCCCCE		0.6923663014
444PhosphorylationSTQTKKLSASSPRML
CCCCCCCCCCCCCCC		35.2930266825
446PhosphorylationQTKKLSASSPRMLHR
CCCCCCCCCCCCCCC		37.8630266825
447PhosphorylationTKKLSASSPRMLHRS
CCCCCCCCCCCCCCC		57.8530266825
470AcetylationCQSMCHDKYTKIFND
HHHHHCHHHHHHHHH		32.7326051181
470UbiquitinationCQSMCHDKYTKIFND
HHHHHCHHHHHHHHH		32.73-
483SumoylationNDFKDRMKSDHKRET
HHHHHHHHCHHHHHH		22.48-
500UbiquitinationVVREALEKLRSEMEE
HHHHHHHHHHHHHHH		7.94-
551UbiquitinationKKLATQHKQLISQTK
HHHHHHHHHHHHHHC		24.13-
555PhosphorylationTQHKQLISQTKKKQW
HHHHHHHHHHCCCCC		40.69-
572PhosphorylationNCEEEAMYHCCWNTS
CCCHHHHHHHHHCCC		30576142
580PhosphorylationHCCWNTSYCSIKCQQ
HHHHCCCCCEEEEHH		30576142
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 ZMY11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZMY11_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 ZMY11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAB1_HUMANTAB1physical
9663660
MYB_HUMANMYBphysical
11244510
SMCA2_HUMANSMARCA2physical
16565076
EZH2_HUMANEZH2physical
16565076
EZH1_HUMANEZH1physical
16565076
E2F6_HUMANE2F6physical
16565076
P53_HUMANTP53physical
17721438
EP400_HUMANEP400physical
17721438
PDLI7_HUMANPDLIM7physical
16382137
TRAF6_HUMANTRAF6physical
16382137
ZMY11_HUMANZMYND11physical
19766626
PIAS1_HUMANPIAS1physical
19766626
UBC9_HUMANUBE2Iphysical
19766626
TRAF3_HUMANTRAF3physical
20138174
TRADD_HUMANTRADDphysical
19379743
MAGC2_HUMANMAGEC2physical
24866244
H31T_HUMANHIST3H3physical
24675531
H31T_HUMANHIST3H3physical
25263594
PRP8_HUMANPRPF8physical
25263594
SRRM2_HUMANSRRM2physical
25263594
U520_HUMANSNRNP200physical
25263594
SRRM1_HUMANSRRM1physical
25263594
PININ_HUMANPNNphysical
25263594
SRSF4_HUMANSRSF4physical
25263594
SRSF1_HUMANSRSF1physical
25263594
PABP1_HUMANPABPC1physical
25263594
U5S1_HUMANEFTUD2physical
25263594
SAP18_HUMANSAP18physical
25263594
PPIG_HUMANPPIGphysical
25263594
MGN2_HUMANMAGOHBphysical
25263594
SRS10_HUMANSRSF10physical
25263594
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=A chromosomal aberration involving ZMYND11 is a cause of acute poorly differentiated myeloid leukemia. Translocation (10
17)(p15
q21) with MBTD1.
616083
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZMY11_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-381, 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-381, AND MASSSPECTROMETRY.

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