MTA1_HUMAN - dbPTM
MTA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTA1_HUMAN
UniProt AC Q13330
Protein Name Metastasis-associated protein MTA1
Gene Name MTA1
Organism Homo sapiens (Human).
Sequence Length 715
Subcellular Localization Isoform Short: Cytoplasm.
Isoform Long: Nucleus. Nucleus envelope. Cytoplasm. Cytoplasm, cytoskeleton. Associated with microtubules. 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. Involved in the epigenetic regulation of ESR1 expression in breast cancer in a TFAP2C, IFI16 and HDAC4/5/6-dependent manner. 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. Isoform Short binds to ESR1 and sequesters it in the cytoplasm and enhances its non-genomic responses. With TFCP2L1, promotes establishment and maintenance of pluripotency in embryonic stem cells (ESCs) and inhibits endoderm differentiation (By similarity)..
Protein Sequence MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTANGNVEAKVVCFYRRRDISSTLIALADKHATLSVCYKAGPGADNGEEGEIEEEMENPEMVDLPEKLKHQLRHRELFLSRQLESLPATHIRGKCSVTLLNETESLKSYLEREDFFFYSLVYDPQQKTLLADKGEIRVGNRYQADITDLLKEGEEDGRDQSRLETQVWEAHNPLTDKQIDQFLVVARSVGTFARALDCSSSVRQPSLHMSAAAASRDITLFHAMDTLHKNIYDISKAISALVPQGGPVLCRDEMEEWSASEANLFEEALEKYGKDFTDIQQDFLPWKSLTSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPNYNKPNPNQISVNNVKAGVVNGTGAPGQSPGAGRACESCYTTQSYQWYSWGPPNMQCRLCASCWTYWKKYGGLKMPTRLDGERPGPNRSNMSPHGLPARSSGSPKFAMKTRQAFYLHTTKLTRIARRLCREILRPWHAARHPYLPINSAAIKAECTARLPEASQSPLVLKQAVRKPLEAVLRYLETHPRPPKPDPVKSVSSVLSSLTPAKVAPVINNGSPTILGKRSYEQHNGVDGNMKKRLLMPSRGLANHGQARHMGPSRNLLLNGKSYPTKVRLIRGGSLPPVKRRRMNWIDAPDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPPRPPPPAPVNDEPIVIED
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-
32UbiquitinationRRIEELNKTANGNVE
HHHHHHHHHCCCCEE		62.7321906983
32 (in isoform 1)Ubiquitination-62.7321890473
32 (in isoform 2)Ubiquitination-62.7321890473
41AcetylationANGNVEAKVVCFYRR
CCCCEEEEEEEEEEC		22.9926051181
52PhosphorylationFYRRRDISSTLIALA
EEECCCCHHHHHHHH		22.8930108239
53PhosphorylationYRRRDISSTLIALAD
EECCCCHHHHHHHHH		27.8030108239
54PhosphorylationRRRDISSTLIALADK
ECCCCHHHHHHHHHH		18.5230108239
61 (in isoform 3)Ubiquitination-29.54-
83 (in isoform 3)Ubiquitination-13.69-
98UbiquitinationEMVDLPEKLKHQLRH
HHCCCCHHHHHHHHH		61.98-
125UbiquitinationPATHIRGKCSVTLLN
CCCCCCCCEEEEEEC		17.31-
149PhosphorylationEREDFFFYSLVYDPQ
HHCCCEEEEEEECHH		8.9230631047
150PhosphorylationREDFFFYSLVYDPQQ
HCCCEEEEEEECHHC		13.2530631047
164UbiquitinationQKTLLADKGEIRVGN
CCEEEECCCCCCCCC		53.49-
1642-HydroxyisobutyrylationQKTLLADKGEIRVGN
CCEEEECCCCCCCCC		53.49-
182UbiquitinationADITDLLKEGEEDGR
CCHHHHHHHCCCCCC		71.60PubMed
191UbiquitinationGEEDGRDQSRLETQV
CCCCCCCHHHHHHHH		29.1421890473
208UbiquitinationAHNPLTDKQIDQFLV
HCCCCCHHHHHHHHH		43.8721890473
208 (in isoform 1)Ubiquitination-43.8721890473
208 (in isoform 2)Ubiquitination-43.8721890473
230PhosphorylationFARALDCSSSVRQPS
HHHHHCCCCCCCCCC		25.8923879269
231PhosphorylationARALDCSSSVRQPSL
HHHHCCCCCCCCCCH		38.9023879269
232PhosphorylationRALDCSSSVRQPSLH
HHHCCCCCCCCCCHH		12.6723879269
234MethylationLDCSSSVRQPSLHMS
HCCCCCCCCCCHHHH		44.64-
237PhosphorylationSSSVRQPSLHMSAAA
CCCCCCCCHHHHHHH		23.6721406692
241PhosphorylationRQPSLHMSAAAASRD
CCCCHHHHHHHHHCC		12.1921406692
243UbiquitinationPSLHMSAAAASRDIT
CCHHHHHHHHHCCHH		9.0321890473
246PhosphorylationHMSAAAASRDITLFH
HHHHHHHHCCHHHHH		26.2621406692
260UbiquitinationHAMDTLHKNIYDISK
HHHHHHHHCHHHHHH		48.42-
260 (in isoform 1)Ubiquitination-48.4221890473
260 (in isoform 2)Ubiquitination-48.4221890473
305UbiquitinationEALEKYGKDFTDIQQ
HHHHHHCCCCHHHHH		46.72-
319PhosphorylationQDFLPWKSLTSIIEY
HHCCCHHHHHHHHHH		32.7724043423
321PhosphorylationFLPWKSLTSIIEYYY
CCCHHHHHHHHHHHH		25.6024043423
322PhosphorylationLPWKSLTSIIEYYYM
CCHHHHHHHHHHHHH		27.1924043423
326PhosphorylationSLTSIIEYYYMWKTT
HHHHHHHHHHHHHHH		6.8924043423
327PhosphorylationLTSIIEYYYMWKTTD
HHHHHHHHHHHHHHH		3.6624043423
328PhosphorylationTSIIEYYYMWKTTDR
HHHHHHHHHHHHHHH		8.8024043423
340UbiquitinationTDRYVQQKRLKAAEA
HHHHHHHHHHHHHHH		42.48-
344UbiquitinationVQQKRLKAAEAESKL
HHHHHHHHHHHHHHH		18.3521890473
355PhosphorylationESKLKQVYIPNYNKP
HHHHCEEECCCCCCC		14.2528152594
359PhosphorylationKQVYIPNYNKPNPNQ
CEEECCCCCCCCCCC		21.1428152594
361UbiquitinationVYIPNYNKPNPNQIS
EECCCCCCCCCCCEE		35.4921890473
361 (in isoform 1)Ubiquitination-35.4921890473
361 (in isoform 2)Ubiquitination-35.4921890473
368PhosphorylationKPNPNQISVNNVKAG
CCCCCCEEECCEEEE		14.7228152594
380PhosphorylationKAGVVNGTGAPGQSP
EEEEECCCCCCCCCC		25.6029255136
386PhosphorylationGTGAPGQSPGAGRAC
CCCCCCCCCCCCCCC		31.0829255136
395PhosphorylationGAGRACESCYTTQSY
CCCCCCCCCEECCCE		16.5924043423
397PhosphorylationGRACESCYTTQSYQW
CCCCCCCEECCCEEE		23.3124043423
398PhosphorylationRACESCYTTQSYQWY
CCCCCCEECCCEEEE		23.7630576142
399PhosphorylationACESCYTTQSYQWYS
CCCCCEECCCEEEEE		6.7724043423
401PhosphorylationESCYTTQSYQWYSWG
CCCEECCCEEEEECC		19.7324043423
402PhosphorylationSCYTTQSYQWYSWGP
CCEECCCEEEEECCC		8.0124043423
405PhosphorylationTTQSYQWYSWGPPNM
ECCCEEEEECCCCCC		4.4930576142
406PhosphorylationTQSYQWYSWGPPNMQ
CCCEEEEECCCCCCC		23.6924043423
419PhosphorylationMQCRLCASCWTYWKK
CCCCCHHHHHHHHHH		14.8030576142
427PhosphorylationCWTYWKKYGGLKMPT
HHHHHHHHCCCCCCC		16.82-
434PhosphorylationYGGLKMPTRLDGERP
HCCCCCCCCCCCCCC		40.1222210691
446PhosphorylationERPGPNRSNMSPHGL
CCCCCCCCCCCCCCC		43.4522167270
449PhosphorylationGPNRSNMSPHGLPAR
CCCCCCCCCCCCCCC		20.2822167270
457PhosphorylationPHGLPARSSGSPKFA
CCCCCCCCCCCCCCH		40.9522199227
458PhosphorylationHGLPARSSGSPKFAM
CCCCCCCCCCCCCHH		37.4222199227
460PhosphorylationLPARSSGSPKFAMKT
CCCCCCCCCCCHHHH		27.1925159151
462UbiquitinationARSSGSPKFAMKTRQ
CCCCCCCCCHHHHHH		47.67-
467PhosphorylationSPKFAMKTRQAFYLH
CCCCHHHHHHHHHHH		18.2222817900
509SumoylationPINSAAIKAECTARL
CCCHHHHHHHHHHCC		33.15-
509SumoylationPINSAAIKAECTARL
CCCHHHHHHHHHHCC		33.1528112733
509MalonylationPINSAAIKAECTARL
CCCHHHHHHHHHHCC		33.1526320211
509AcetylationPINSAAIKAECTARL
CCCHHHHHHHHHHCC		33.1525953088
510UbiquitinationINSAAIKAECTARLP
CCHHHHHHHHHHCCC		15.8121890473
513PhosphorylationAAIKAECTARLPEAS
HHHHHHHHHCCCCHH		13.3026074081
520PhosphorylationTARLPEASQSPLVLK
HHCCCCHHCCCHHHH		29.5425159151
522PhosphorylationRLPEASQSPLVLKQA
CCCCHHCCCHHHHHH		20.0829255136
527UbiquitinationSQSPLVLKQAVRKPL
HCCCHHHHHHCHHHH		28.822189047
527 (in isoform 1)Ubiquitination-28.8221890473
532MethylationVLKQAVRKPLEAVLR
HHHHHCHHHHHHHHH		47.56-
532"N6,N6-dimethyllysine"VLKQAVRKPLEAVLR
HHHHHCHHHHHHHHH		47.56-
555O-linked_GlycosylationPKPDPVKSVSSVLSS
CCCCCCCCHHHHHHH		27.7128657654
555PhosphorylationPKPDPVKSVSSVLSS
CCCCCCCCHHHHHHH		27.7123403867
557PhosphorylationPDPVKSVSSVLSSLT
CCCCCCHHHHHHHCC		23.0928176443
558PhosphorylationDPVKSVSSVLSSLTP
CCCCCHHHHHHHCCH		25.5628176443
561PhosphorylationKSVSSVLSSLTPAKV
CCHHHHHHHCCHHHE		22.5830266825
562PhosphorylationSVSSVLSSLTPAKVA
CHHHHHHHCCHHHEE		31.9130266825
564PhosphorylationSSVLSSLTPAKVAPV
HHHHHHCCHHHEECE		24.1319664994
576PhosphorylationAPVINNGSPTILGKR
ECEECCCCCCCCCCC		22.4619664994
578PhosphorylationVINNGSPTILGKRSY
EECCCCCCCCCCCCH		30.4529255136
582MethylationGSPTILGKRSYEQHN
CCCCCCCCCCHHHHC		34.42115973315
582UbiquitinationGSPTILGKRSYEQHN
CCCCCCCCCCHHHHC		34.42-
582AcetylationGSPTILGKRSYEQHN
CCCCCCCCCCHHHHC		34.4225953088
584PhosphorylationPTILGKRSYEQHNGV
CCCCCCCCHHHHCCC		36.1925159151
604MethylationKRLLMPSRGLANHGQ
HHHCCCCCCCCCCCC		37.9712019133
618PhosphorylationQARHMGPSRNLLLNG
CCCCCCCCCCEEECC		28.2430387612
626AcetylationRNLLLNGKSYPTKVR
CCEEECCCCCCCEEE		45.8217671180
626UbiquitinationRNLLLNGKSYPTKVR
CCEEECCCCCCCEEE		45.82PubMed
636MethylationPTKVRLIRGGSLPPV
CCEEEEEECCCCCCC		48.2726494465
639PhosphorylationVRLIRGGSLPPVKRR
EEEEECCCCCCCCCC		40.2923401153
659PhosphorylationDAPDDVFYMATEETR
CCCCCCEECCCHHHH		5.9118083107
670UbiquitinationEETRKIRKLLSSSET
HHHHHHHHHHCCHHH		58.20-
673PhosphorylationRKIRKLLSSSETKRA
HHHHHHHCCHHHHHH		42.1027732954
674PhosphorylationKIRKLLSSSETKRAA
HHHHHHCCHHHHHHH		31.9627732954
675PhosphorylationIRKLLSSSETKRAAR
HHHHHCCHHHHHHHC		46.0030624053
677PhosphorylationKLLSSSETKRAARRP
HHHCCHHHHHHHCCC		27.9827732954
678UbiquitinationLLSSSETKRAARRPY
HHCCHHHHHHHCCCC		35.67-
685PhosphorylationKRAARRPYKPIALRQ
HHHHCCCCCCCCCCC		27.82-
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
522SPhosphorylationKinaseCDK2P24941
PSP
-KUbiquitinationE3 ubiquitin ligaseDET1Q7L5Y6
PMID:19805145
-KUbiquitinationE3 ubiquitin ligaseDET1#COP1Q7L5Y6#Q8NHY2
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseCOP1Q8NHY2
PMID:19805145
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTA1_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 MTA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHD4_HUMANCHD4physical
12920132
SIN3A_HUMANSIN3Aphysical
12920132
MTA2_HUMANMTA2physical
12920132
HDAC1_HUMANHDAC1physical
12920132
HDAC2_HUMANHDAC2physical
12920132
RBBP4_HUMANRBBP4physical
12920132
RBBP7_HUMANRBBP7physical
12920132
ESR1_HUMANESR1physical
12167865
MAT1_HUMANMNAT1physical
12527756
HDAC1_HUMANHDAC1physical
11146623
HDAC2_HUMANHDAC2physical
11146623
HIF1A_HUMANHIF1Aphysical
16511565
HDAC1_HUMANHDAC1physical
16511565
HIF1A_HUMANHIF1Aphysical
16969516
ESR1_HUMANESR1physical
16807247
EP300_HUMANEP300physical
16617102
LMO4_HUMANLMO4physical
16288053
HDAC2_HUMANHDAC2physical
12431981
CHD3_HUMANCHD3physical
12431981
BC11B_HUMANBCL11Bphysical
16091750
CENPR_HUMANITGB3BPphysical
15254226
KC1G2_HUMANCSNK1G2physical
15077195
RBBP7_HUMANRBBP7physical
18067919
RBBP4_HUMANRBBP4physical
18067919
HSF1_HUMANHSF1physical
17922035
HDAC1_HUMANHDAC1physical
17922035
CHD3_HUMANCHD3physical
17922035
P53_HUMANTP53physical
17914590
HDAC2_HUMANHDAC2physical
17671180
PARK7_HUMANPARK7physical
21368136
ATR_HUMANATRphysical
20427275
HDAC2_HUMANHDAC2physical
20651739
MDM2_HUMANMDM2physical
19837670
JUN_HUMANJUNphysical
21555589
BL1S1_HUMANBLOC1S1physical
12639951
UBC9_HUMANUBE2Iphysical
21965678
NR2C2_HUMANNR2C2physical
21670149
NR2C1_HUMANNR2C1physical
21670149
DNMT1_HUMANDNMT1physical
21670149
KDM1A_HUMANKDM1Aphysical
21670149
HDAC1_HUMANHDAC1physical
21670149
HDAC2_HUMANHDAC2physical
21670149
MTA2_HUMANMTA2physical
21670149
CHD4_HUMANCHD4physical
21670149
RBBP4_HUMANRBBP4physical
21670149
MBD3_HUMANMBD3physical
21670149
DPOD3_HUMANPOLD3physical
21670149
P66B_HUMANGATAD2Bphysical
22939629
HIC1_HUMANHIC1physical
23417673
NACC2_HUMANNACC2physical
22926524
DNMT1_HUMANDNMT1physical
23708667
IKZF1_HUMANIKZF1physical
25416956
LZTS2_HUMANLZTS2physical
25416956
K1C40_HUMANKRT40physical
25416956
KHDR2_HUMANKHDRBS2physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
RBBP4_HUMANRBBP4physical
26186194
RBBP7_HUMANRBBP7physical
26186194
TSH3_HUMANTSHZ3physical
26186194
Z512B_HUMANZNF512Bphysical
26186194
ZN521_HUMANZNF521physical
26186194
ZN423_HUMANZNF423physical
26186194
IMA3_HUMANKPNA4physical
26186194
IMA4_HUMANKPNA3physical
26186194
SIR1_HUMANSIRT1physical
26186194
BC11A_HUMANBCL11Aphysical
26186194
TRI33_HUMANTRIM33physical
26344197
RBBP7_HUMANRBBP7physical
28514442
ZN521_HUMANZNF521physical
28514442
ZN423_HUMANZNF423physical
28514442
BC11A_HUMANBCL11Aphysical
28514442
TSH3_HUMANTSHZ3physical
28514442
RBBP4_HUMANRBBP4physical
28514442
SIR1_HUMANSIRT1physical
28514442
Z512B_HUMANZNF512Bphysical
28514442
RBBP4_HUMANRBBP4physical
27098840
RBBP7_HUMANRBBP7physical
27098840
HDAC1_HUMANHDAC1physical
27098840
TRI25_HUMANTRIM25physical
28861931
UBE4A_HUMANUBE4Aphysical
28861931
UBE3C_HUMANUBE3Cphysical
28861931
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 MTA1_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 SER-386; SER-522; THR-564;SER-576 AND THR-578, AND MASS SPECTROMETRY.
"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 SER-386; SER-520; SER-522;THR-564; SER-576 AND THR-578, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-449; SER-522;THR-564 AND SER-576, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-522 ANDTHR-578, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND THR-564, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-564, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-467, AND MASSSPECTROMETRY.

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