MTF2_HUMAN - dbPTM
MTF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTF2_HUMAN
UniProt AC Q9Y483
Protein Name Metal-response element-binding transcription factor 2
Gene Name MTF2
Organism Homo sapiens (Human).
Sequence Length 593
Subcellular Localization Nucleus.
Protein Description Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex, leading to enhance PRC2 H3K27me3 methylation activity. Regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation. Promotes recruitment of the PRC2 complex to the inactive X chromosome in differentiating XX ES cells and PRC2 recruitment to target genes in undifferentiated ES cells. Required to repress Hox genes by enhancing H3K27me3 methylation of the PRC2 complex. In some conditions may act as an inhibitor of PRC2 activity: able to activate the CDKN2A gene and promote cellular senescence by suppressing the catalytic activity of the PRC2 complex locally. Binds to the metal-regulating-element (MRE) of MT1A gene promoter (By similarity)..
Protein Sequence MRDSTGAGNSLVHKRSPLRRNQKTPTSLTKLSLQDGHKAKKPACKFEEGQDVLARWSDGLFYLGTIKKINILKQSCFIIFEDSSKSWVLWKDIQTGATGSGEMVCTICQEEYSEAPNEMVICDKCGQGYHQLCHTPHIDSSVIDSDEKWLCRQCVFATTTKRGGALKKGPNAKALQVMKQTLPYSVADLEWDAGHKTNVQQCYCYCGGPGDWYLKMLQCCKCKQWFHEACVQCLQKPMLFGDRFYTFICSVCSSGPEYLKRLPLQWVDIAHLCLYNLSVIHKKKYFDSELELMTYINENWDRLHPGELADTPKSERYEHVLEALNDYKTMFMSGKEIKKKKHLFGLRIRVPPVPPNVAFKAEKEPEGTSHEFKIKGRKASKPISDSREVSNGIEKKGKKKSVGRPPGPYTRKMIQKTAEPLLDKESISENPTLDLPCSIGRTEGTAHSSNTSDVDFTGASSAKETTSSSISRHYGLSDSRKRTRTGRSWPAAIPHLRRRRGRLPRRALQTQNSEIVKDDEGKEDYQFDELNTEILNNLADQELQLNHLKNSITSYFGAAGRIACGEKYRVLARRVTLDGKVQYLVEWEGATAS
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
4Phosphorylation----MRDSTGAGNSL
----CCCCCCCCCCC		20.5530576142
5Phosphorylation---MRDSTGAGNSLV
---CCCCCCCCCCCC		35.0328555341
10PhosphorylationDSTGAGNSLVHKRSP
CCCCCCCCCCCCCCC		30.7425159151
16PhosphorylationNSLVHKRSPLRRNQK
CCCCCCCCCCCCCCC		32.8424719451
24PhosphorylationPLRRNQKTPTSLTKL
CCCCCCCCCCCCCCC		23.2622199227
26PhosphorylationRRNQKTPTSLTKLSL
CCCCCCCCCCCCCCC		41.4222199227
27PhosphorylationRNQKTPTSLTKLSLQ
CCCCCCCCCCCCCCC		34.9322199227
29PhosphorylationQKTPTSLTKLSLQDG
CCCCCCCCCCCCCCC		29.70-
30AcetylationKTPTSLTKLSLQDGH
CCCCCCCCCCCCCCC		41.1825953088
30MethylationKTPTSLTKLSLQDGH
CCCCCCCCCCCCCCC		41.18115973347
45MethylationKAKKPACKFEEGQDV
CCCCCCCCCCCCCCH		58.90115973353
161UbiquitinationCVFATTTKRGGALKK
HHEEECCCCCCCCCC		47.13-
161UbiquitinationCVFATTTKRGGALKK
HHEEECCCCCCCCCC		47.13-
161AcetylationCVFATTTKRGGALKK
HHEEECCCCCCCCCC		47.1325953088
179UbiquitinationAKALQVMKQTLPYSV
HHHHHHHHHHCCCCE		41.07-
245PhosphorylationMLFGDRFYTFICSVC
HHHCCCHHHHHHHHH		11.13-
285PhosphorylationSVIHKKKYFDSELEL
HHHCCHHCCCCHHHH		22.8426552605
288PhosphorylationHKKKYFDSELELMTY
CCHHCCCCHHHHHHH		33.8926552605
294PhosphorylationDSELELMTYINENWD
CCHHHHHHHHHCCCH		33.6026552605
295PhosphorylationSELELMTYINENWDR
CHHHHHHHHHCCCHH		6.4426552605
313UbiquitinationGELADTPKSERYEHV
CCCCCCCCHHHHHHH		68.02-
313UbiquitinationGELADTPKSERYEHV
CCCCCCCCHHHHHHH		68.02-
327PhosphorylationVLEALNDYKTMFMSG
HHHHHHHHHHHHCCC		13.7929759185
329PhosphorylationEALNDYKTMFMSGKE
HHHHHHHHHHCCCCH		14.9329759185
360SumoylationVPPNVAFKAEKEPEG
CCCCCEEEEECCCCC		45.9928112733
378MethylationEFKIKGRKASKPISD
CEEECCEECCCCCCC		66.73116254059
384PhosphorylationRKASKPISDSREVSN
EECCCCCCCCHHHHC		37.7529083192
386PhosphorylationASKPISDSREVSNGI
CCCCCCCCHHHHCCC		24.4529083192
390PhosphorylationISDSREVSNGIEKKG
CCCCHHHHCCCCCCC		25.2829083192
401PhosphorylationEKKGKKKSVGRPPGP
CCCCCCCCCCCCCCH		38.3928985074
410PhosphorylationGRPPGPYTRKMIQKT
CCCCCHHHHHHHHHH		27.2628509920
412MethylationPPGPYTRKMIQKTAE
CCCHHHHHHHHHHCH		32.33-
416MethylationYTRKMIQKTAEPLLD
HHHHHHHHHCHHHCC		38.48-
417PhosphorylationTRKMIQKTAEPLLDK
HHHHHHHHCHHHCCH		21.6322985185
424UbiquitinationTAEPLLDKESISENP
HCHHHCCHHHCCCCC		54.02-
426PhosphorylationEPLLDKESISENPTL
HHHCCHHHCCCCCCC		36.8430266825
428PhosphorylationLLDKESISENPTLDL
HCCHHHCCCCCCCCC		40.3730266825
432PhosphorylationESISENPTLDLPCSI
HHCCCCCCCCCCCEE		44.4830266825
438PhosphorylationPTLDLPCSIGRTEGT
CCCCCCCEECCCCCC		26.5825159151
442PhosphorylationLPCSIGRTEGTAHSS
CCCEECCCCCCCCCC		33.2923186163
445PhosphorylationSIGRTEGTAHSSNTS
EECCCCCCCCCCCCC		18.2430576142
448PhosphorylationRTEGTAHSSNTSDVD
CCCCCCCCCCCCCCC		23.8730576142
449PhosphorylationTEGTAHSSNTSDVDF
CCCCCCCCCCCCCCC		33.9730576142
451PhosphorylationGTAHSSNTSDVDFTG
CCCCCCCCCCCCCCC		28.4030576142
452PhosphorylationTAHSSNTSDVDFTGA
CCCCCCCCCCCCCCC		39.6328112733
457PhosphorylationNTSDVDFTGASSAKE
CCCCCCCCCCCCCCC		27.6323186163
460PhosphorylationDVDFTGASSAKETTS
CCCCCCCCCCCCCCC		31.9723186163
461PhosphorylationVDFTGASSAKETTSS
CCCCCCCCCCCCCCC		42.7123186163
463UbiquitinationFTGASSAKETTSSSI
CCCCCCCCCCCCCHH		58.50-
469PhosphorylationAKETTSSSISRHYGL
CCCCCCCHHHHHCCC		25.0930576142
474PhosphorylationSSSISRHYGLSDSRK
CCHHHHHCCCCCCCC		20.74-
477PhosphorylationISRHYGLSDSRKRTR
HHHHCCCCCCCCCCC		29.2230108239
479PhosphorylationRHYGLSDSRKRTRTG
HHCCCCCCCCCCCCC		36.0023401153
480MethylationHYGLSDSRKRTRTGR
HCCCCCCCCCCCCCC		37.15115483987
485PhosphorylationDSRKRTRTGRSWPAA
CCCCCCCCCCCCCHH		36.0124247654
488PhosphorylationKRTRTGRSWPAAIPH
CCCCCCCCCCHHHHH		38.4630576142
513PhosphorylationRALQTQNSEIVKDDE
HHHHHCCCCCCCCCC		20.9124247654
522SumoylationIVKDDEGKEDYQFDE
CCCCCCCCCCCCHHH		45.4228112733
522UbiquitinationIVKDDEGKEDYQFDE
CCCCCCCCCCCCHHH		45.42-
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 MTF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTF2_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 MTF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EZH2_HUMANEZH2physical
20123894
SUZ12_HUMANSUZ12physical
20123894
JARD2_HUMANJARID2physical
20123894
TMED9_HUMANTMED9physical
21988832
KDM1A_HUMANKDM1Aphysical
23455924
ANM6_HUMANPRMT6physical
23455924
SUV91_HUMANSUV39H1physical
23455924
SUV92_HUMANSUV39H2physical
23455924
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 MTF2_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 THR-24; SER-27 AND SER-488,AND MASS SPECTROMETRY.

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