MTG16_HUMAN - dbPTM
MTG16_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTG16_HUMAN
UniProt AC O75081
Protein Name Protein CBFA2T3
Gene Name CBFA2T3
Organism Homo sapiens (Human).
Sequence Length 653
Subcellular Localization Isoform 1: Nucleus, nucleolus. The RUNX1-CBFA2T3 fusion protein localizes to the nucleoplasm.
Isoform 2: Nucleus, nucleoplasm . Golgi apparatus membrane .
Protein Description Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes. [PubMed: 12559562]
Protein Sequence MPASRLRDRAASSASGSTCGSMSQTHPVLESGLLASAGCSAPRGPRKGGPAPVDRKAKASAMPDSPAEVKTQPRSTPPSMPPPPPAASQGATRPPSFTPHTHREDGPATLPHGRFHGCLKWSMVCLLMNGSSHSPTAINGAPCTPNGFSNGPATSSTASLSTQHLPPACGARQLSKLKRFLTTLQQFGSDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQTPAQYLAQHEQLLLDASASSPIDSSELLLEVNENGKRRTPDRTKENGSDRDPLHPEHLSKRPCTLNPAQRYSPSNGPPQPTPPPHYRLEDIAMAHHFRDAYRHPDPRELRERHRPLVVPGSRQEEVIDHKLTEREWAEEWKHLNNLLNCIMDMVEKTRRSLTVLRRCQEADREELNHWARRYSDAEDTKKGPAPAAARPRSSSAGPEGPQLDVPREFLPRTLTGYVPEDIWRKAEEAVNEVKRQAMSELQKAVSDAERKAHELITTERAKMERALAEAKRQASEDALTVINQQEDSSESCWNCGRKASETCSGCNAARYCGSFCQHRDWEKHHHVCGQSLQGPTAVVADPVPGPPEAAHSLGPSLPVGAASPSEAGSAGPSRPGSPSPPGPLDTVPR
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
12PhosphorylationRLRDRAASSASGSTC
HHHHHHHHCCCCCCC		26.0030576142
15PhosphorylationDRAASSASGSTCGSM
HHHHHCCCCCCCCCC		34.91-
25PhosphorylationTCGSMSQTHPVLESG
CCCCCCCCCCHHHHC		22.3530576142
36PhosphorylationLESGLLASAGCSAPR
HHHCHHHHCCCCCCC		25.7630576142
40PhosphorylationLLASAGCSAPRGPRK
HHHHCCCCCCCCCCC		40.1526434552
47MethylationSAPRGPRKGGPAPVD
CCCCCCCCCCCCCCC		71.94-
65PhosphorylationKASAMPDSPAEVKTQ
HHHCCCCCCHHHCCC		21.8223401153
70UbiquitinationPDSPAEVKTQPRSTP
CCCCHHHCCCCCCCC		32.71-
75PhosphorylationEVKTQPRSTPPSMPP
HHCCCCCCCCCCCCC		52.5323401153
76PhosphorylationVKTQPRSTPPSMPPP
HCCCCCCCCCCCCCC		40.2623186163
79PhosphorylationQPRSTPPSMPPPPPA
CCCCCCCCCCCCCCC		45.1623186163
88PhosphorylationPPPPPAASQGATRPP
CCCCCCCCCCCCCCC		31.1123186163
244PhosphorylationKANLPLLQRELLHCA
HCCCHHHHHHHHHHH		44.4732142685
300UbiquitinationRRTPDRTKENGSDRD
CCCCCCCCCCCCCCC		50.50-
320PhosphorylationHLSKRPCTLNPAQRY
HHCCCCCCCCHHHCC		32.0526552605
327PhosphorylationTLNPAQRYSPSNGPP
CCCHHHCCCCCCCCC		16.9228450419
328PhosphorylationLNPAQRYSPSNGPPQ
CCHHHCCCCCCCCCC		24.8423401153
330PhosphorylationPAQRYSPSNGPPQPT
HHHCCCCCCCCCCCC		48.7728464451
337PhosphorylationSNGPPQPTPPPHYRL
CCCCCCCCCCCCCCH		43.0823401153
342PhosphorylationQPTPPPHYRLEDIAM
CCCCCCCCCHHHHHH		23.7530108239
429UbiquitinationRCQEADREELNHWAR
HHHHHCHHHHHHHHH		68.3429967540
439PhosphorylationNHWARRYSDAEDTKK
HHHHHHHCCHHHHCC		28.6524719451
444PhosphorylationRYSDAEDTKKGPAPA
HHCCHHHHCCCCCCC		26.5926074081
449UbiquitinationEDTKKGPAPAAARPR
HHHCCCCCCCCCCCC		18.2917203973
457PhosphorylationPAAARPRSSSAGPEG
CCCCCCCCCCCCCCC		31.1823401153
458PhosphorylationAAARPRSSSAGPEGP
CCCCCCCCCCCCCCC		26.0330278072
459PhosphorylationAARPRSSSAGPEGPQ
CCCCCCCCCCCCCCC		38.1923401153
477PhosphorylationPREFLPRTLTGYVPE
CHHHCCCHHCCCCCH		27.08-
479PhosphorylationEFLPRTLTGYVPEDI
HHCCCHHCCCCCHHH		26.3423186163
489UbiquitinationVPEDIWRKAEEAVNE
CCHHHHHHHHHHHHH		45.19-
498UbiquitinationEEAVNEVKRQAMSEL
HHHHHHHHHHHHHHH		32.39-
510UbiquitinationSELQKAVSDAERKAH
HHHHHHHHHHHHHHH		35.6417203973
515UbiquitinationAVSDAERKAHELITT
HHHHHHHHHHHHHHH		45.6729967540
521PhosphorylationRKAHELITTERAKME
HHHHHHHHHHHHHHH		34.92-
535UbiquitinationERALAEAKRQASEDA
HHHHHHHHHHHCHHH		36.2317203973
539PhosphorylationAEAKRQASEDALTVI
HHHHHHHCHHHHHHH		27.8924275569
578PhosphorylationNAARYCGSFCQHRDW
CHHHHCCCHHHCCCH		21.20-
627PhosphorylationSLPVGAASPSEAGSA
CCCCCCCCHHHCCCC		28.5526074081
629PhosphorylationPVGAASPSEAGSAGP
CCCCCCHHHCCCCCC		37.2726074081
633PhosphorylationASPSEAGSAGPSRPG
CCHHHCCCCCCCCCC		36.7826074081
637PhosphorylationEAGSAGPSRPGSPSP
HCCCCCCCCCCCCCC		50.6326074081
641PhosphorylationAGPSRPGSPSPPGPL
CCCCCCCCCCCCCCC		25.5326074081
643PhosphorylationPSRPGSPSPPGPLDT
CCCCCCCCCCCCCCC		45.4826074081
650PhosphorylationSPPGPLDTVPR----
CCCCCCCCCCC----		39.8411823486
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 MTG16_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTG16_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 MTG16_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTG8_HUMANRUNX1T1physical
14703694
MTG8R_HUMANCBFA2T2physical
12242670
HDAC1_HUMANHDAC1physical
12242670
HDAC3_HUMANHDAC3physical
12242670
TAL1_HUMANTAL1physical
16407974
TFE2_HUMANTCF3physical
16407974
LDB1_HUMANLDB1physical
16407974
KAP2_HUMANPRKAR2Aphysical
11823486
SIN3B_HUMANSIN3Bphysical
18586123
NCOR1_HUMANNCOR1physical
18586123
ZBT47_HUMANZBTB47physical
20116376
MATN2_HUMANMATN2physical
21988832
GMEB2_HUMANGMEB2physical
21988832
SC24A_HUMANSEC24Aphysical
21988832
ZBTB4_HUMANZBTB4physical
23251453
ZBT38_HUMANZBTB38physical
23251453
KAISO_HUMANZBTB33physical
23251453
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 MTG16_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 THR-337 AND SER-459, ANDMASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"The proteomic reactor facilitates the analysis of affinity-purifiedproteins by mass spectrometry: application for identifyingubiquitinated proteins in human cells.";
Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,Haines D.S., Figeys D.;
J. Proteome Res. 6:298-305(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-535, AND MASSSPECTROMETRY.

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