MTA1_MOUSE - dbPTM
MTA1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTA1_MOUSE
UniProt AC Q8K4B0
Protein Name Metastasis-associated protein MTA1
Gene Name Mta1
Organism Mus musculus (Mouse).
Sequence Length 715
Subcellular Localization Nucleus. Nucleus envelope . Cytoplasm. Cytoplasm, cytoskeleton. Associated with microtubules. Primarily localized in the cytoplasm in embryonic tissues. Localization at the nuclear envelope is TPR-dependent.
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. With Tfcp2l1, promotes establishment and maintenance of pluripotency in embryonic stem cells (ESCs) and inhibits endoderm differentiation. [PubMed: 28982712]
Protein Sequence MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTANGNVEAKVVCFYRRRDISSSLIALADKHATLSVCYRAGPGADTGEEGEVEEEVENPEMVDLPEKLKHQLRHRELFLSRQLESLPATHIRGKCSVTLLNETESLKSYLEREDFFFYSLVYDPQQKTLLADKGEIRVGNRYQADITDLLKEGEEDGRDQSKLETKVWEAHNPLVDKQIDQFLVVARSVGTFARALDCSSSVRQPSLHMSAAAASRDITLFHAMDTLHKNIYDISKAISALVPQGGPVLCRDEMEEWSASEANLFEEALEKYGKDFTDIQQDFLPWKSLTSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPNYNKPNPNQISASSVKATVVNGTGTPGQSPGAGRACESCYTTQSYQWYSWGPPNMQCRLCASCWTYWKKYGGLKMPTRLDGERPGPNRNNMSPHGIPARSSGSPKFAMKTRQAFYLHTTKLTRIARRLCREILRPWHAARHPYMPINSAAIKAECTARLPEASQSPLVLKQVVRKPLEAVLRYLETHPRPPKPDPVKSSSSVLSSLTPAKSAPVINNGSPTILGKRSYEQHNGVDGNMKKRLLMPSRGLANHGQTRHMGPSRNLLLNGKSYPTKVRLIRGGSLPPVKRRRMNWIDAPDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPLRPPPPAPVNDEPIVIED
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
32UbiquitinationRRIEELNKTANGNVE
HHHHHHHHHCCCCEE		62.73-
52PhosphorylationFYRRRDISSSLIALA
EEECCCCCHHHHHHH		20.4022817900
53PhosphorylationYRRRDISSSLIALAD
EECCCCCHHHHHHHH		29.5128066266
54PhosphorylationRRRDISSSLIALADK
ECCCCCHHHHHHHHH		19.6028418008
120PhosphorylationQLESLPATHIRGKCS
HHHHCCCCCCCCCEE		18.8525338131
237PhosphorylationSSSVRQPSLHMSAAA
CCCCCCCCHHHHHHH		23.6727566939
241PhosphorylationRQPSLHMSAAAASRD
CCCCHHHHHHHHHCC		12.1926026062
266PhosphorylationHKNIYDISKAISALV
HHCHHHHHHHHHHHC		17.0925521595
270PhosphorylationYDISKAISALVPQGG
HHHHHHHHHHCCCCC		22.0222705319
355PhosphorylationESKLKQVYIPNYNKP
HHHHCEEECCCCCCC		14.25-
361UbiquitinationVYIPNYNKPNPNQIS
EECCCCCCCCCCCCC		35.4922790023
375PhosphorylationSASSVKATVVNGTGT
CCCCCEEEEECCCCC		21.1925777480
380PhosphorylationKATVVNGTGTPGQSP
EEEEECCCCCCCCCC		32.4526745281
382PhosphorylationTVVNGTGTPGQSPGA
EEECCCCCCCCCCCC		24.8825521595
386PhosphorylationGTGTPGQSPGAGRAC
CCCCCCCCCCCCCCC		31.0825521595
449PhosphorylationGPNRNNMSPHGIPAR
CCCCCCCCCCCCCCC		18.8327087446
457PhosphorylationPHGIPARSSGSPKFA
CCCCCCCCCCCCCCH		40.9521183079
458PhosphorylationHGIPARSSGSPKFAM
CCCCCCCCCCCCCHH		37.4221183079
460PhosphorylationIPARSSGSPKFAMKT
CCCCCCCCCCCHHHH		27.1922942356
520PhosphorylationTARLPEASQSPLVLK
HHCCCHHHCCCCHHH		29.5426824392
522PhosphorylationRLPEASQSPLVLKQV
CCCHHHCCCCHHHHH		20.0825521595
527UbiquitinationSQSPLVLKQVVRKPL
HCCCCHHHHHHHHHH		33.3022790023
527AcetylationSQSPLVLKQVVRKPL
HCCCCHHHHHHHHHH		33.3022826441
543PhosphorylationAVLRYLETHPRPPKP
HHHHHHHHCCCCCCC		34.2922871156
555PhosphorylationPKPDPVKSSSSVLSS
CCCCCCCCCHHHHHH		35.3722802335
556PhosphorylationKPDPVKSSSSVLSSL
CCCCCCCCHHHHHHC		22.4022802335
557PhosphorylationPDPVKSSSSVLSSLT
CCCCCCCHHHHHHCC		31.4025619855
558PhosphorylationDPVKSSSSVLSSLTP
CCCCCCHHHHHHCCC		29.0825619855
561PhosphorylationKSSSSVLSSLTPAKS
CCCHHHHHHCCCCCC		22.5825619855
562PhosphorylationSSSSVLSSLTPAKSA
CCHHHHHHCCCCCCC		31.9125619855
564PhosphorylationSSVLSSLTPAKSAPV
HHHHHHCCCCCCCCC		24.1322942356
568PhosphorylationSSLTPAKSAPVINNG
HHCCCCCCCCCCCCC		39.6525619855
576PhosphorylationAPVINNGSPTILGKR
CCCCCCCCCCCCCCC		22.4625521595
578PhosphorylationVINNGSPTILGKRSY
CCCCCCCCCCCCCCH		30.4522942356
604DimethylationKRLLMPSRGLANHGQ
HCEECCCCCHHCCCC		37.97-
604MethylationKRLLMPSRGLANHGQ
HCEECCCCCHHCCCC		37.9712229023
626AcetylationRNLLLNGKSYPTKVR
CCEEECCCCCCCEEE		45.8266653
639PhosphorylationVRLIRGGSLPPVKRR
EEEEECCCCCCCCCC		40.2928833060
662PhosphorylationDDVFYMATEETRKIR
CCCEECCCHHHHHHH		20.1622871156
675PhosphorylationIRKLLSSSETKRAAR
HHHHHCCHHHHHHHC		46.0027841257
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTA1_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FYN_HUMANFYNphysical
11483358
HDAC2_MOUSEHdac2physical
18454139
MBD3_MOUSEMbd3physical
18454139
NANOG_MOUSENanogphysical
18454139
MTA2_MOUSEMta2physical
18454139
RBBP7_MOUSERbbp7physical
18454139
FOSB_MOUSEFosbphysical
21258411
TGM2_MOUSETgm2physical
21156794
TF65_MOUSERelaphysical
21156794
SH3G3_MOUSESh3gl3physical
15978591
CHD3_HUMANCHD3physical
26496610
CHD4_HUMANCHD4physical
26496610
KC1G2_HUMANCSNK1G2physical
26496610
ERCC6_HUMANERCC6physical
26496610
HDAC1_HUMANHDAC1physical
26496610
HDAC2_HUMANHDAC2physical
26496610
SYMC_HUMANMARSphysical
26496610
RBBP4_HUMANRBBP4physical
26496610
RBBP7_HUMANRBBP7physical
26496610
RL37A_HUMANRPL37Aphysical
26496610
TCF20_HUMANTCF20physical
26496610
TRPS1_HUMANTRPS1physical
26496610
AF10_HUMANMLLT10physical
26496610
CDKA1_HUMANCDK2AP1physical
26496610
MBD2_HUMANMBD2physical
26496610
DDX21_HUMANDDX21physical
26496610
PHF14_HUMANPHF14physical
26496610
NPA1P_HUMANURB1physical
26496610
HM20A_HUMANHMG20Aphysical
26496610
PUR6_HUMANPAICSphysical
26496610
RAI1_HUMANRAI1physical
26496610
PKCB1_HUMANZMYND8physical
26496610
BABA1_HUMANBABAM1physical
26496610
HERC5_HUMANHERC5physical
26496610
ZN639_HUMANZNF639physical
26496610
MBD3_HUMANMBD3physical
26496610
P66A_HUMANGATAD2Aphysical
26496610
SALL4_HUMANSALL4physical
26496610
P66B_HUMANGATAD2Bphysical
26496610
MTA3_HUMANMTA3physical
26496610
ZN687_HUMANZNF687physical
26496610
ZBTB2_HUMANZBTB2physical
26496610
PWP2A_HUMANPWWP2Aphysical
26496610
MTA2_HUMANMTA2physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MTA1_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory