MTA1_RAT - dbPTM
MTA1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTA1_RAT
UniProt AC Q62599
Protein Name Metastasis-associated protein MTA1
Gene Name Mta1
Organism Rattus norvegicus (Rat).
Sequence Length 703
Subcellular Localization Isoform 1: Nucleus. Nucleus envelope . Cytoplasm. Cytoplasm, cytoskeleton. Associated with microtubules. Localization at the nuclear envelope is TPR-dependent (By similarity)..
Isoform 2: Rough endoplasmic reticulum. Golgi apparatus. Cytoplasmic ves
Protein Description Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator. As a part of the histone-deacetylase multiprotein complex (NuRD), regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA. In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3, PAX5 and SUMO2, independent of the NuRD complex. Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3. Regulates p53-dependent and -independent DNA repair processes following genotoxic stress. Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair. Plays an important role in tumorigenesis, tumor invasion, and metastasis. Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light-dark (LD) cycles. Positively regulates the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1. Regulates deacetylation of ARNTL/BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1-mediated transcription repression (By similarity). Isoform 2 may be involved in the sorting of amylase during zymogen granule formation in the pancreas. With Tfcp2l1, promotes establishment and maintenance of pluripotency in embryonic stem cells (ESCs) and inhibits endoderm differentiation (By similarity)..
Protein Sequence MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTANGNVEAKVVCFYRRRDISSSLIALADKHATLSVCYRAGPGADTGEEGEVEEEVENPEMVDLPEKLKHQLRHRELFLSRQLESLPATHIRGKCSVTLLNETESLKSYLEREDFFFYSLVYDPQQKTLLADKGEIRVGNRYQADITDLLKDGEEDGRDQSKLETKVWEAHNPLVDKQIDQFLVVARSVGTFARALDCSSSVRQPSLHMSAAAASRDITLFHAMDTLHKNIYDISKAISALVPQGGPVLCRDEMEEWSASEANLFEEALEKYGKDFTDIQQDFLPWKSLTSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPNYNKPNPNQISVNSVKASVVNGTGTPGQSPGAGRACESCYTTQSYQWYSWGPPNMQCRLCASCWTYWKKYGGLKMPTRLDGERPGPNRNNMSPHGIPARSSGSPKFAMKTRQAFYLHTTKLTRIARRLCREILRPWHAARHPYMPINSAAIKAECTARLPEASQSPLVLKQVVRKPLEAVLRYLETHPRPPKPDPVKSSSSVLSSLTPAKSAPVINNGSPTILGKRSYEQHNGVDGLANHGQTRHMGPSRNLLLNGKSYPTKVRLIRGGSLPPVKRRRMNWIDAPDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPLRPPPPAPVNDEPIVIED
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
52PhosphorylationFYRRRDISSSLIALA
EEECCCCCHHHHHHH
20.4028432305
53PhosphorylationYRRRDISSSLIALAD
EECCCCCHHHHHHHH
29.5128432305
54PhosphorylationRRRDISSSLIALADK
ECCCCCHHHHHHHHH
19.6027097102
380PhosphorylationKASVVNGTGTPGQSP
EEEEECCCCCCCCCC
32.4523984901
382PhosphorylationSVVNGTGTPGQSPGA
EEECCCCCCCCCCCC
24.8828689409
386PhosphorylationGTGTPGQSPGAGRAC
CCCCCCCCCCCCCCC
31.0827097102
449PhosphorylationGPNRNNMSPHGIPAR
CCCCCCCCCCCCCCC
18.8323712012
520PhosphorylationTARLPEASQSPLVLK
HHCCCHHHCCCCHHH
29.5427097102
522PhosphorylationRLPEASQSPLVLKQV
CCCHHHCCCCHHHHH
20.0827097102
561PhosphorylationKSSSSVLSSLTPAKS
CCCHHHHHHCCCCCC
22.5828432305
562PhosphorylationSSSSVLSSLTPAKSA
CCHHHHHHCCCCCCC
31.9128432305
564PhosphorylationSSVLSSLTPAKSAPV
HHHHHHCCCCCCCCC
24.1327097102
576PhosphorylationAPVINNGSPTILGKR
CCCCCCCCCCCCCCC
22.4623712012
578PhosphorylationVINNGSPTILGKRSY
CCCCCCCCCCCCCCH
30.4527097102
583MethylationSPTILGKRSYEQHNG
CCCCCCCCCHHCCCC
42.5526494469
614AcetylationRNLLLNGKSYPTKVR
CCEEECCCCCCCEEE
45.82-
624MethylationPTKVRLIRGGSLPPV
CCEEEEEECCCCCCC
48.2726494463
627PhosphorylationVRLIRGGSLPPVKRR
EEEEECCCCCCCCCC
40.2925403869

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 MTA1_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTA1_RAT !!

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 MTA1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MTA1_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MTA1_RAT

loading...

Related Literatures of Post-Translational Modification

TOP