MTA3_HUMAN - dbPTM
MTA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTA3_HUMAN
UniProt AC Q9BTC8
Protein Name Metastasis-associated protein MTA3
Gene Name MTA3
Organism Homo sapiens (Human).
Sequence Length 594
Subcellular Localization Nucleus .
Protein Description Plays a role in maintenance of the normal epithelial architecture through the repression of SNAI1 transcription in a histone deacetylase-dependent manner, and thus the regulation of E-cadherin levels. Contributes to transcriptional repression by BCL6..
Protein Sequence MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTASGNVEAKVVCFYRRRDISNTLIMLADKHAKEIEEESETTVEADLTDKQKHQLKHRELFLSRQYESLPATHIRGKCSVALLNETESVLSYLDKEDTFFYSLVYDPSLKTLLADKGEIRVGPRYQADIPEMLLEGESDEREQSKLEVKVWDPNSPLTDRQIDQFLVVARAVGTFARALDCSSSVRQPSLHMSAAAASRDITLFHAMDTLYRHSYDLSSAISVLVPLGGPVLCRDEMEEWSASEASLFEEALEKYGKDFNDIRQDFLPWKSLTSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPTYSKPNPNQISTSNGKPGAVNGAVGTTFQPQNPLLGRACESCYATQSHQWYSWGPPNMQCRLCAICWLYWKKYGGLKMPTQSEEEKLSPSPTTEDPRVRSHVSRQAMQGMPVRNTGSPKSAVKTRQAFFLHTTYFTKFARQVCKNTLRLRQAARRPFVAINYAAIRAEYADRHAELSGSPLKSKSTRKPLACIIGYLEIHPAKKPNVIRSTPSLQTPTTKRMLTTPNHTSLSILGKRNYSHHNGLDELTCCVSD
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
11PhosphorylationNMYRVGDYVYFENSS
CCEEECCEEEEECCC
7.3622817900
13PhosphorylationYRVGDYVYFENSSSN
EEECCEEEEECCCCC
10.03-
16PhosphorylationGDYVYFENSSSNPYL
CCEEEEECCCCCCHH
36.97-
17PhosphorylationDYVYFENSSSNPYLI
CEEEEECCCCCCHHH
28.13-
32AcetylationRRIEELNKTASGNVE
HHHHHHHCCCCCCCE
59.0826051181
32 (in isoform 2)Ubiquitination-59.08-
33PhosphorylationRIEELNKTASGNVEA
HHHHHHCCCCCCCEE
25.61-
35PhosphorylationEELNKTASGNVEAKV
HHHHCCCCCCCEEEE
35.8128348404
41AcetylationASGNVEAKVVCFYRR
CCCCCEEEEEEEEEE
22.9926051181
46PhosphorylationEAKVVCFYRRRDISN
EEEEEEEEEECCCHH
9.70-
52PhosphorylationFYRRRDISNTLIMLA
EEEECCCHHHHHHHH
28.2220068231
54PhosphorylationRRRDISNTLIMLADK
EECCCHHHHHHHHHH
15.7520068231
57SulfoxidationDISNTLIMLADKHAK
CCHHHHHHHHHHHHH
2.5821406390
61 (in isoform 2)Ubiquitination-39.5921890473
61 (in isoform 1)Ubiquitination-39.5921890473
61UbiquitinationTLIMLADKHAKEIEE
HHHHHHHHHHHHHHH
39.5921890473
72PhosphorylationEIEEESETTVEADLT
HHHHHCCCEEEECCC
45.48-
73PhosphorylationIEEESETTVEADLTD
HHHHCCCEEEECCCH
16.58-
91UbiquitinationHQLKHRELFLSRQYE
HHHHHHHHHHHHCHH
5.44-
129PhosphorylationSYLDKEDTFFYSLVY
HHCCCCCCCEEEEEE
19.4128787133
130PhosphorylationYLDKEDTFFYSLVYD
HCCCCCCCEEEEEEC
9.29-
133PhosphorylationKEDTFFYSLVYDPSL
CCCCCEEEEEECCCH
13.2528787133
161MethylationPRYQADIPEMLLEGE
CCCCCCCCHHHHCCC
22.84-
186PhosphorylationVKVWDPNSPLTDRQI
EEEECCCCCCCHHHH
27.03-
213PhosphorylationFARALDCSSSVRQPS
HHHHHCCCCCCCCCC
25.8923879269
214PhosphorylationARALDCSSSVRQPSL
HHHHCCCCCCCCCCH
38.9023879269
215PhosphorylationRALDCSSSVRQPSLH
HHHCCCCCCCCCCHH
12.6723879269
217MethylationLDCSSSVRQPSLHMS
HCCCCCCCCCCHHHH
44.64-
220PhosphorylationSSSVRQPSLHMSAAA
CCCCCCCCHHHHHHH
23.6721406692
224PhosphorylationRQPSLHMSAAAASRD
CCCCHHHHHHHHHCC
12.1921406692
229PhosphorylationHMSAAAASRDITLFH
HHHHHHHHCCHHHHH
26.2621406692
232UbiquitinationAAAASRDITLFHAMD
HHHHHCCHHHHHHHH
3.33-
233PhosphorylationAAASRDITLFHAMDT
HHHHCCHHHHHHHHH
27.8825867546
240PhosphorylationTLFHAMDTLYRHSYD
HHHHHHHHHHHHCCC
16.7725867546
242PhosphorylationFHAMDTLYRHSYDLS
HHHHHHHHHHCCCHH
14.3625867546
267UbiquitinationGPVLCRDEMEEWSAS
CCEECCHHHHHCCHH
29.19-
272PhosphorylationRDEMEEWSASEASLF
CHHHHHCCHHHHHHH
25.7929759185
302PhosphorylationQDFLPWKSLTSIIEY
HHCCCHHHHHHHHHH
32.7724043423
304PhosphorylationFLPWKSLTSIIEYYY
CCCHHHHHHHHHHHH
25.6024043423
305PhosphorylationLPWKSLTSIIEYYYM
CCHHHHHHHHHHHHH
27.1924043423
309PhosphorylationSLTSIIEYYYMWKTT
HHHHHHHHHHHHHHH
6.8924043423
310PhosphorylationLTSIIEYYYMWKTTD
HHHHHHHHHHHHHHH
3.6624043423
311PhosphorylationTSIIEYYYMWKTTDR
HHHHHHHHHHHHHHH
8.8024043423
356AcetylationQISTSNGKPGAVNGA
CCCCCCCCCCCCCCC
44.5226051181
365PhosphorylationGAVNGAVGTTFQPQN
CCCCCCCCCCCCCCC
20.64-
369UbiquitinationGAVGTTFQPQNPLLG
CCCCCCCCCCCCCCC
36.26-
371PhosphorylationVGTTFQPQNPLLGRA
CCCCCCCCCCCCCHH
54.0820068231
373PhosphorylationTTFQPQNPLLGRACE
CCCCCCCCCCCHHCC
24.5818452278
375PhosphorylationFQPQNPLLGRACESC
CCCCCCCCCHHCCCC
4.62-
376PhosphorylationQPQNPLLGRACESCY
CCCCCCCCHHCCCCC
23.8720068231
398PhosphorylationYSWGPPNMQCRLCAI
CCCCCCCHHHHHHHH
4.99-
400PhosphorylationWGPPNMQCRLCAICW
CCCCCHHHHHHHHHH
2.20-
413PhosphorylationCWLYWKKYGGLKMPT
HHHHHHHHCCCCCCC
16.8229083192
420PhosphorylationYGGLKMPTQSEEEKL
HCCCCCCCCCCCCCC
41.0329255136
422PhosphorylationGLKMPTQSEEEKLSP
CCCCCCCCCCCCCCC
49.8329255136
426AcetylationPTQSEEEKLSPSPTT
CCCCCCCCCCCCCCC
58.5026051181
426 (in isoform 2)Ubiquitination-58.50-
428PhosphorylationQSEEEKLSPSPTTED
CCCCCCCCCCCCCCC
34.1129255136
430PhosphorylationEEEKLSPSPTTEDPR
CCCCCCCCCCCCCHH
31.3530266825
432PhosphorylationEKLSPSPTTEDPRVR
CCCCCCCCCCCHHHH
47.3430266825
433PhosphorylationKLSPSPTTEDPRVRS
CCCCCCCCCCHHHHH
41.6030266825
455PhosphorylationQGMPVRNTGSPKSAV
CCCCCCCCCCCHHHH
28.5922199227
457PhosphorylationMPVRNTGSPKSAVKT
CCCCCCCCCHHHHHH
27.4122199227
460PhosphorylationRNTGSPKSAVKTRQA
CCCCCCHHHHHHHHH
41.50-
462PhosphorylationTGSPKSAVKTRQAFF
CCCCHHHHHHHHHHH
9.3232645325
464PhosphorylationSPKSAVKTRQAFFLH
CCHHHHHHHHHHHHH
22.7822210691
496PhosphorylationLRQAARRPFVAINYA
HHHHHHCCEEEEEHH
23.63-
502 (in isoform 2)Phosphorylation-7.41-
508PhosphorylationNYAAIRAEYADRHAE
EHHHHHHHHHHHHHH
31.26-
510 (in isoform 2)Ubiquitination-10.00-
517PhosphorylationADRHAELSGSPLKSK
HHHHHHHCCCCCCCC
28.8230266825
519PhosphorylationRHAELSGSPLKSKST
HHHHHCCCCCCCCCC
24.5523401153
523PhosphorylationLSGSPLKSKSTRKPL
HCCCCCCCCCCCCCC
39.2523312004
536PhosphorylationPLACIIGYLEIHPAK
CCEEEEEEEEECCCC
7.25-
553PhosphorylationNVIRSTPSLQTPTTK
CCCCCCCCCCCCCCC
32.9529396449
556PhosphorylationRSTPSLQTPTTKRML
CCCCCCCCCCCCCCC
28.0928674419
558PhosphorylationTPSLQTPTTKRMLTT
CCCCCCCCCCCCCCC
48.6229396449
559PhosphorylationPSLQTPTTKRMLTTP
CCCCCCCCCCCCCCC
20.1829396449
565PhosphorylationTTKRMLTTPNHTSLS
CCCCCCCCCCCCCCC
20.38-
589PhosphorylationHNGLDELTCCVSD--
CCCCCEEEEEECC--
11.2123663014
593PhosphorylationDELTCCVSD------
CEEEEEECC------
24.5623663014

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 MTA3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTA3_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 MTA3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHD3_HUMANCHD3physical
12705869
MBD3_HUMANMBD3physical
12705869
HDAC1_HUMANHDAC1physical
12705869
HDAC2_HUMANHDAC2physical
12705869
BCL6_HUMANBCL6physical
15454082
CHD4_HUMANCHD4physical
22075476
HDAC1_HUMANHDAC1physical
22075476
MTA2_HUMANMTA2physical
21258344
RBBP7_HUMANRBBP7physical
21258344
RBBP4_HUMANRBBP4physical
21258344
CDKA1_HUMANCDK2AP1physical
21258344
P66B_HUMANGATAD2Bphysical
21258344
P66A_HUMANGATAD2Aphysical
21258344
MBD2_HUMANMBD2physical
21258344
HDAC2_HUMANHDAC2physical
21258344
HDAC1_HUMANHDAC1physical
21258344
CHD4_HUMANCHD4physical
21258344
HM20B_HUMANHMG20Bphysical
21258344
HM20A_HUMANHMG20Aphysical
21258344
GSE1_HUMANGSE1physical
21258344
RCOR3_HUMANRCOR3physical
21258344
RCOR1_HUMANRCOR1physical
21258344
ROA2_HUMANHNRNPA2B1physical
22863883
P66A_HUMANGATAD2Aphysical
26344197
P66B_HUMANGATAD2Bphysical
26344197
MBD2_HUMANMBD2physical
26344197
MBD3_HUMANMBD3physical
26344197
MTA1_HUMANMTA1physical
26344197
MTA2_HUMANMTA2physical
26344197

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 MTA3_HUMAN

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Related Literatures of Post-Translational Modification

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