MTG8_HUMAN - dbPTM
MTG8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTG8_HUMAN
UniProt AC Q06455
Protein Name Protein CBFA2T1
Gene Name RUNX1T1
Organism Homo sapiens (Human).
Sequence Length 604
Subcellular Localization Nucleus . Colocalizes with ATN1 in discrete nuclear dots.
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 MISVKRNTWRALSLVIGDCRKKGNFEYCQDRTEKHSTMPDSPVDVKTQSRLTPPTMPPPPTTQGAPRTSSFTPTTLTNGTSHSPTALNGAPSPPNGFSNGPSSSSSSSLANQQLPPACGARQLSKLKRFLTTLQQFGNDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQNPAQYLAQHEQLLLDASTTSPVDSSELLLDVNENGKRRTPDRTKENGFDREPLHSEHPSKRPCTISPGQRYSPNNGLSYQPNGLPHPTPPPPQHYRLDDMAIAHHYRDSYRHPSHRDLRDRNRPMGLHGTRQEEMIDHRLTDREWAEEWKHLDHLLNCIMDMVEKTRRSLTVLRRCQEADREELNYWIRRYSDAEDLKKGGGSSSSHSRQQSPVNPDPVALDAHREFLHRPASGYVPEEIWKKAEEAVNEVKRQAMTELQKAVSEAERKAHDMITTERAKMERTVAEAKRQAAEDALAVINQQEDSSESCWNCGRKASETCSGCNTARYCGSFCQHKDWEKHHHICGQTLQAQQQGDTPAVSSSVTPNSGAGSPMDTPPAATPRSTTPGTPSTIETTPR
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
3Phosphorylation-----MISVKRNTWR
-----CCCCCCCHHH
21.9324719451
36PhosphorylationQDRTEKHSTMPDSPV
CCCCCCCCCCCCCCC
37.1527251275
37PhosphorylationDRTEKHSTMPDSPVD
CCCCCCCCCCCCCCC
32.2323403867
41PhosphorylationKHSTMPDSPVDVKTQ
CCCCCCCCCCCCCCC
22.4328674151
47PhosphorylationDSPVDVKTQSRLTPP
CCCCCCCCCCCCCCC
31.4627732954
49PhosphorylationPVDVKTQSRLTPPTM
CCCCCCCCCCCCCCC
34.1927732954
52PhosphorylationVKTQSRLTPPTMPPP
CCCCCCCCCCCCCCC
26.5527732954
55PhosphorylationQSRLTPPTMPPPPTT
CCCCCCCCCCCCCCC
43.4427732954
61PhosphorylationPTMPPPPTTQGAPRT
CCCCCCCCCCCCCCC
37.2124905233
62PhosphorylationTMPPPPTTQGAPRTS
CCCCCCCCCCCCCCC
30.6824905233
68PhosphorylationTTQGAPRTSSFTPTT
CCCCCCCCCCCCCCC
27.8824905233
69PhosphorylationTQGAPRTSSFTPTTL
CCCCCCCCCCCCCCC
25.4124905233
70PhosphorylationQGAPRTSSFTPTTLT
CCCCCCCCCCCCCCC
32.3124905233
72PhosphorylationAPRTSSFTPTTLTNG
CCCCCCCCCCCCCCC
22.9824905233
74PhosphorylationRTSSFTPTTLTNGTS
CCCCCCCCCCCCCCC
31.2324905233
75PhosphorylationTSSFTPTTLTNGTSH
CCCCCCCCCCCCCCC
32.5624905233
77PhosphorylationSFTPTTLTNGTSHSP
CCCCCCCCCCCCCCC
29.5224905233
80PhosphorylationPTTLTNGTSHSPTAL
CCCCCCCCCCCCCCC
25.9024905233
81PhosphorylationTTLTNGTSHSPTALN
CCCCCCCCCCCCCCC
24.3024905233
83PhosphorylationLTNGTSHSPTALNGA
CCCCCCCCCCCCCCC
24.5824905233
85PhosphorylationNGTSHSPTALNGAPS
CCCCCCCCCCCCCCC
46.9524905233
100PhosphorylationPPNGFSNGPSSSSSS
CCCCCCCCCCCCCHH
23.4427251275
106PhosphorylationNGPSSSSSSSLANQQ
CCCCCCCHHHHHHCC
26.3724719451
269PhosphorylationHPSKRPCTISPGQRY
CCCCCCCEECCCCCC
27.4627732954
271PhosphorylationSKRPCTISPGQRYSP
CCCCCEECCCCCCCC
12.5727732954
276PhosphorylationTISPGQRYSPNNGLS
EECCCCCCCCCCCCC
22.1629449344
277PhosphorylationISPGQRYSPNNGLSY
ECCCCCCCCCCCCCC
24.2822496350
283PhosphorylationYSPNNGLSYQPNGLP
CCCCCCCCCCCCCCC
24.1029449344
284PhosphorylationSPNNGLSYQPNGLPH
CCCCCCCCCCCCCCC
32.7929449344
315PhosphorylationAHHYRDSYRHPSHRD
HHHHHHHCCCCCHHH
19.7518083107
336PhosphorylationPMGLHGTRQEEMIDH
CCCCCCCCHHHHHHH
46.6427251275
380PhosphorylationRSLTVLRRCQEADRE
HHHHHHHHHHHHCHH
23.47-
390 (in isoform 2)Phosphorylation-33.11-
408PhosphorylationDLKKGGGSSSSHSRQ
HHHCCCCCCCCCCCC
30.2621406692
409PhosphorylationLKKGGGSSSSHSRQQ
HHCCCCCCCCCCCCC
38.8521406692
410PhosphorylationKKGGGSSSSHSRQQS
HCCCCCCCCCCCCCC
33.4921406692
411PhosphorylationKGGGSSSSHSRQQSP
CCCCCCCCCCCCCCC
27.6821406692
413PhosphorylationGGSSSSHSRQQSPVN
CCCCCCCCCCCCCCC
33.4625954137
417PhosphorylationSSHSRQQSPVNPDPV
CCCCCCCCCCCCCCH
23.6017572682
438PhosphorylationEFLHRPASGYVPEEI
HHHHCCCCCCCCHHH
33.0827732954
448UbiquitinationVPEEIWKKAEEAVNE
CCHHHHHHHHHHHHH
46.14-
457UbiquitinationEEAVNEVKRQAMTEL
HHHHHHHHHHHHHHH
32.39-
462PhosphorylationEVKRQAMTELQKAVS
HHHHHHHHHHHHHHH
36.2423917254
476PhosphorylationSEAERKAHDMITTER
HHHHHHHHHHHHHHH
28.3624719451
553PhosphorylationKHHHICGQTLQAQQQ
HHHCCCHHHHHHHHC
34.33-
554PhosphorylationHHHICGQTLQAQQQG
HHCCCHHHHHHHHCC
13.2119664995
555PhosphorylationHHICGQTLQAQQQGD
HCCCHHHHHHHHCCC
2.82-
558PhosphorylationCGQTLQAQQQGDTPA
CHHHHHHHHCCCCCC
24.14-
563 (in isoform 2)Phosphorylation-21.70-
564 (in isoform 2)Phosphorylation-35.09-
565 (in isoform 2)Phosphorylation-18.86-
567PhosphorylationQGDTPAVSSSVTPNS
CCCCCCCCCCCCCCC
20.9929449344
568 (in isoform 2)Phosphorylation-23.41-
568PhosphorylationGDTPAVSSSVTPNSG
CCCCCCCCCCCCCCC
23.4129449344
569PhosphorylationDTPAVSSSVTPNSGA
CCCCCCCCCCCCCCC
23.6229449344
571PhosphorylationPAVSSSVTPNSGAGS
CCCCCCCCCCCCCCC
20.7829449344
574PhosphorylationSSSVTPNSGAGSPMD
CCCCCCCCCCCCCCC
31.0929449344
578PhosphorylationTPNSGAGSPMDTPPA
CCCCCCCCCCCCCCC
19.2729449344
582PhosphorylationGAGSPMDTPPAATPR
CCCCCCCCCCCCCCC
25.5629449344
590PhosphorylationPPAATPRSTTPGTPS
CCCCCCCCCCCCCCC
37.5223911959
591PhosphorylationPAATPRSTTPGTPST
CCCCCCCCCCCCCCC
37.9928674151
592PhosphorylationAATPRSTTPGTPSTI
CCCCCCCCCCCCCCC
22.4428674151
595PhosphorylationPRSTTPGTPSTIETT
CCCCCCCCCCCCCCC
18.4428674151
597PhosphorylationSTTPGTPSTIETTPR
CCCCCCCCCCCCCCC
41.6823403867
598PhosphorylationTTPGTPSTIETTPR-
CCCCCCCCCCCCCC-
24.8423403867
601PhosphorylationGTPSTIETTPR----
CCCCCCCCCCC----
37.9423403867
602PhosphorylationTPSTIETTPR-----
CCCCCCCCCC-----
12.3223403867
650Phosphorylation-----------------------------------------------------
-----------------------------------------------------
27251275
651Phosphorylation------------------------------------------------------
------------------------------------------------------
24719451
654Phosphorylation---------------------------------------------------------
---------------------------------------------------------
27251275

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 MTG8_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTG8_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 MTG8_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABI3_HUMANABI3physical
16189514
CS057_HUMANC19orf57physical
16189514
NECA2_HUMANNECAB2physical
16189514
WBP11_HUMANWBP11physical
16189514
TAF9B_HUMANTAF9Bphysical
16189514
MTG8R_HUMANCBFA2T2physical
16189514
OTUD4_HUMANOTUD4physical
17353931
TR150_HUMANTHRAP3physical
17353931
MTG16_HUMANCBFA2T3physical
12242670
MTG8R_HUMANCBFA2T2physical
12242670
KAP2_HUMANPRKAR2Aphysical
11593431
NCOR2_HUMANNCOR2physical
11113190
MTG8_HUMANRUNX1T1physical
11113190
NCOR1_HUMANNCOR1physical
11113190
VDR_HUMANVDRphysical
12460926
SIN3A_HUMANSIN3Aphysical
11150306
ZBT16_HUMANZBTB16physical
10688654
GFI1_HUMANGFI1physical
12874834
ZBT16_HUMANZBTB16physical
11090081
NGN1_HUMANNEUROG1physical
20211142
TAL2_HUMANTAL2physical
20211142
PRD14_HUMANPRDM14physical
20211142
PHS2_HUMANPCBD2physical
20211142
MTG8R_HUMANCBFA2T2physical
15333839
HTF4_HUMANTCF12physical
15333839
TFE2_HUMANTCF3physical
15333839
NCOR1_HUMANNCOR1physical
15333839
HDAC3_HUMANHDAC3physical
15333839
SIN3A_HUMANSIN3Aphysical
15333839
HDAC1_HUMANHDAC1physical
15333839
NCOR2_HUMANNCOR2physical
9819405
NCOR1_HUMANNCOR1physical
9819405
HDAC1_HUMANHDAC1physical
9819405
HDAC1_HUMANHDAC1physical
17389244
DNMT1_HUMANDNMT1physical
15735013
ETS1_HUMANETS1physical
7774816
BCL6_HUMANBCL6physical
14551142
NCOR1_HUMANNCOR1physical
17572682
EPS8_HUMANEPS8physical
25416956
MEOX2_HUMANMEOX2physical
25416956
STX11_HUMANSTX11physical
25416956
ZMYM4_HUMANZMYM4physical
25416956
LPXN_HUMANLPXNphysical
25416956
HOME3_HUMANHOMER3physical
25416956
SPY2_HUMANSPRY2physical
25416956
TRIM1_HUMANMID2physical
25416956
GSE1_HUMANGSE1physical
25416956
ABI3_HUMANABI3physical
25416956
NECA2_HUMANNECAB2physical
25416956
PRD14_HUMANPRDM14physical
25416956
CS057_HUMANC19orf57physical
25416956
CPSF7_HUMANCPSF7physical
25416956
EFHC2_HUMANEFHC2physical
25416956
LZTS2_HUMANLZTS2physical
25416956
CR3L1_HUMANCREB3L1physical
25416956
SPERT_HUMANSPERTphysical
25416956
TRI42_HUMANTRIM42physical
25416956
IHO1_HUMANCCDC36physical
25416956
BRCA1_HUMANBRCA1physical
25184681
LPXN_HUMANLPXNphysical
21516116
HOME3_HUMANHOMER3physical
21516116
ZBT16_HUMANZBTB16physical
25241761
HDAC1_HUMANHDAC1physical
25241761

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=A chromosomal aberration involving RUNX1T1 is a cause of acute myeloid leukemia (AML-M2). Translocation t(8
21)(q22
q22) with RUNX1/AML1.
114500
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MTG8_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592 AND THR-595, ANDMASS SPECTROMETRY.

TOP