SMCE1_HUMAN - dbPTM
SMCE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMCE1_HUMAN
UniProt AC Q969G3
Protein Name SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
Gene Name SMARCE1
Organism Homo sapiens (Human).
Sequence Length 411
Subcellular Localization Nucleus .
Protein Description Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Required for the coactivation of estrogen responsive promoters by SWI/SNF complexes and the SRC/p160 family of histone acetyltransferases (HATs). Also specifically interacts with the CoREST corepressor resulting in repression of neuronal specific gene promoters in non-neuronal cells..
Protein Sequence MSKRPSYAPPPTPAPATQMPSTPGFVGYNPYSHLAYNNYRLGGNPGTNSRVTASSGITIPKPPKPPDKPLMPYMRYSRKVWDQVKASNPDLKLWEIGKIIGGMWRDLTDEEKQEYLNEYEAEKIEYNESMKAYHNSPAYLAYINAKSRAEAALEEESRQRQSRMEKGEPYMSIQPAEDPDDYDDGFSMKHTATARFQRNHRLISEILSESVVPDVRSVVTTARMQVLKRQVQSLMVHQRKLEAELLQIEERHQEKKRKFLESTDSFNNELKRLCGLKVEVDMEKIAAEIAQAEEQARKRQEEREKEAAEQAERSQSSIVPEEEQAANKGEEKKDDENIPMETEETHLEETTESQQNGEEGTSTPEDKESGQEGVDSMAEEGTSDSNTGSESNSATVEEPPTDPIPEDEKKE
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
2Phosphorylation------MSKRPSYAP
------CCCCCCCCC		37.0521406692
3Trimethylation-----MSKRPSYAPP
-----CCCCCCCCCC		68.01-
3Acetylation-----MSKRPSYAPP
-----CCCCCCCCCC		68.0123749302
3Methylation-----MSKRPSYAPP
-----CCCCCCCCCC		68.0123644510
3Sumoylation-----MSKRPSYAPP
-----CCCCCCCCCC		68.0128112733
4Methylation----MSKRPSYAPPP
----CCCCCCCCCCC		20.3524129315
6Phosphorylation--MSKRPSYAPPPTP
--CCCCCCCCCCCCC		37.6521406692
7Phosphorylation-MSKRPSYAPPPTPA
-CCCCCCCCCCCCCC		26.3021406692
12PhosphorylationPSYAPPPTPAPATQM
CCCCCCCCCCCCCCC		37.5421406692
17PhosphorylationPPTPAPATQMPSTPG
CCCCCCCCCCCCCCC		25.0921406692
21PhosphorylationAPATQMPSTPGFVGY
CCCCCCCCCCCCCCC		41.7221406692
22PhosphorylationPATQMPSTPGFVGYN
CCCCCCCCCCCCCCC		22.8928655764
28PhosphorylationSTPGFVGYNPYSHLA
CCCCCCCCCCCCCEE		13.9921406692
31PhosphorylationGFVGYNPYSHLAYNN
CCCCCCCCCCEEECC		12.7017360941
32PhosphorylationFVGYNPYSHLAYNNY
CCCCCCCCCEEECCC		17.1821406692
36PhosphorylationNPYSHLAYNNYRLGG
CCCCCEEECCCCCCC		15.4221406692
39PhosphorylationSHLAYNNYRLGGNPG
CCEEECCCCCCCCCC		11.9921406692
40MethylationHLAYNNYRLGGNPGT
CEEECCCCCCCCCCC		29.0424129315
47PhosphorylationRLGGNPGTNSRVTAS
CCCCCCCCCCCEEEC		31.1427251275
52PhosphorylationPGTNSRVTASSGITI
CCCCCCEEECCCCCC		21.5120068231
54PhosphorylationTNSRVTASSGITIPK
CCCCEEECCCCCCCC		21.5220068231
55PhosphorylationNSRVTASSGITIPKP
CCCEEECCCCCCCCC		31.5820068231
57UbiquitinationRVTASSGITIPKPPK
CEEECCCCCCCCCCC		3.2221890473
58PhosphorylationVTASSGITIPKPPKP
EEECCCCCCCCCCCC		34.4520068231
73PhosphorylationPDKPLMPYMRYSRKV
CCCCCCCCCHHCHHH		4.73-
85UbiquitinationRKVWDQVKASNPDLK
HHHHHHHHHHCCCCH		40.23-
92UbiquitinationKASNPDLKLWEIGKI
HHHCCCCHHHHHHHH		59.9621890473
92UbiquitinationKASNPDLKLWEIGKI
HHHCCCCHHHHHHHH		59.9621890473
92SumoylationKASNPDLKLWEIGKI
HHHCCCCHHHHHHHH		59.96-
92AcetylationKASNPDLKLWEIGKI
HHHCCCCHHHHHHHH		59.9625953088
92SumoylationKASNPDLKLWEIGKI
HHHCCCCHHHHHHHH		59.9625114211
92UbiquitinationKASNPDLKLWEIGKI
HHHCCCCHHHHHHHH		59.9621890473
92 (in isoform 1)Ubiquitination-59.9621890473
92 (in isoform 2)Ubiquitination-59.9621890473
98UbiquitinationLKLWEIGKIIGGMWR
CHHHHHHHHHHHHHH		36.49-
112AcetylationRDLTDEEKQEYLNEY
HCCCHHHHHHHHHHH		46.5126051181
112UbiquitinationRDLTDEEKQEYLNEY
HCCCHHHHHHHHHHH		46.51-
115PhosphorylationTDEEKQEYLNEYEAE
CHHHHHHHHHHHHHH		16.60-
123AcetylationLNEYEAEKIEYNESM
HHHHHHHHCCCCHHH		48.1326051181
129PhosphorylationEKIEYNESMKAYHNS
HHCCCCHHHHHHCCC		23.1922817901
131UbiquitinationIEYNESMKAYHNSPA
CCCCHHHHHHCCCHH		55.8821890473
131UbiquitinationIEYNESMKAYHNSPA
CCCCHHHHHHCCCHH		55.8821890473
131UbiquitinationIEYNESMKAYHNSPA
CCCCHHHHHHCCCHH		55.8821890473
131SumoylationIEYNESMKAYHNSPA
CCCCHHHHHHCCCHH		55.8828112733
131UbiquitinationIEYNESMKAYHNSPA
CCCCHHHHHHCCCHH		55.8821890473
131 (in isoform 1)Ubiquitination-55.8821890473
131 (in isoform 2)Ubiquitination-55.8821890473
133PhosphorylationYNESMKAYHNSPAYL
CCHHHHHHCCCHHHH		8.9429759185
136PhosphorylationSMKAYHNSPAYLAYI
HHHHHCCCHHHHHHH		9.5225159151
139PhosphorylationAYHNSPAYLAYINAK
HHCCCHHHHHHHCHH		8.6828152594
142PhosphorylationNSPAYLAYINAKSRA
CCHHHHHHHCHHHHH		7.6628152594
146UbiquitinationYLAYINAKSRAEAAL
HHHHHCHHHHHHHHH		35.6721890473
146UbiquitinationYLAYINAKSRAEAAL
HHHHHCHHHHHHHHH		35.6721890473
146AcetylationYLAYINAKSRAEAAL
HHHHHCHHHHHHHHH		35.6725953088
146MalonylationYLAYINAKSRAEAAL
HHHHHCHHHHHHHHH		35.6726320211
146SumoylationYLAYINAKSRAEAAL
HHHHHCHHHHHHHHH		35.6728112733
146UbiquitinationYLAYINAKSRAEAAL
HHHHHCHHHHHHHHH		35.6721890473
146 (in isoform 1)Ubiquitination-35.6721890473
146 (in isoform 2)Ubiquitination-35.6721890473
157PhosphorylationEAALEEESRQRQSRM
HHHHHHHHHHHHHHH		36.6720068231
162PhosphorylationEESRQRQSRMEKGEP
HHHHHHHHHHHCCCC		35.4726657352
166SumoylationQRQSRMEKGEPYMSI
HHHHHHHCCCCCCCC		60.2728112733
166UbiquitinationQRQSRMEKGEPYMSI
HHHHHHHCCCCCCCC		60.27-
166 (in isoform 2)Ubiquitination-60.27-
170UbiquitinationRMEKGEPYMSIQPAE
HHHCCCCCCCCCCCC		10.1321890473
170PhosphorylationRMEKGEPYMSIQPAE
HHHCCCCCCCCCCCC		10.1317360941
172PhosphorylationEKGEPYMSIQPAEDP
HCCCCCCCCCCCCCC		16.5428555341
182PhosphorylationPAEDPDDYDDGFSMK
CCCCCCCCCCCCCCC		24.2618767875
187PhosphorylationDDYDDGFSMKHTATA
CCCCCCCCCCHHHHH		32.2424719451
189UbiquitinationYDDGFSMKHTATARF
CCCCCCCCHHHHHHH		36.28-
189 (in isoform 2)Ubiquitination-36.28-
191PhosphorylationDGFSMKHTATARFQR
CCCCCCHHHHHHHHH		21.86-
193PhosphorylationFSMKHTATARFQRNH
CCCCHHHHHHHHHHH		21.37-
201UbiquitinationARFQRNHRLISEILS
HHHHHHHHHHHHHHC		36.9521890473
204PhosphorylationQRNHRLISEILSESV
HHHHHHHHHHHCCCC		24.1528857561
208PhosphorylationRLISEILSESVVPDV
HHHHHHHCCCCCCCH		33.2228270605
210PhosphorylationISEILSESVVPDVRS
HHHHHCCCCCCCHHH		25.6628270605
214UbiquitinationLSESVVPDVRSVVTT
HCCCCCCCHHHHHHH		36.5321890473
228MethylationTARMQVLKRQVQSLM
HHHHHHHHHHHHHHH		41.76115980931
240AcetylationSLMVHQRKLEAELLQ
HHHHHHHHHHHHHHH		44.0726051181
240UbiquitinationSLMVHQRKLEAELLQ
HHHHHHHHHHHHHHH		44.0721906983
240 (in isoform 1)Ubiquitination-44.0721890473
240 (in isoform 2)Ubiquitination-44.0721890473
258UbiquitinationRHQEKKRKFLESTDS
HHHHHHHHHHHCCHH		64.2821890473
258UbiquitinationRHQEKKRKFLESTDS
HHHHHHHHHHHCCHH		64.2821890473
258UbiquitinationRHQEKKRKFLESTDS
HHHHHHHHHHHCCHH		64.2821890473
258AcetylationRHQEKKRKFLESTDS
HHHHHHHHHHHCCHH		64.2825953088
258UbiquitinationRHQEKKRKFLESTDS
HHHHHHHHHHHCCHH		64.2821890473
258 (in isoform 1)Ubiquitination-64.2821890473
258 (in isoform 2)Ubiquitination-64.2821890473
262PhosphorylationKKRKFLESTDSFNNE
HHHHHHHCCHHHHHH		39.3930108239
263PhosphorylationKRKFLESTDSFNNEL
HHHHHHCCHHHHHHH		26.7019690332
265PhosphorylationKFLESTDSFNNELKR
HHHHCCHHHHHHHHH		29.9325159151
271UbiquitinationDSFNNELKRLCGLKV
HHHHHHHHHHHCCCE		36.8321890473
271UbiquitinationDSFNNELKRLCGLKV
HHHHHHHHHHHCCCE		36.8321890473
2712-HydroxyisobutyrylationDSFNNELKRLCGLKV
HHHHHHHHHHHCCCE		36.83-
271AcetylationDSFNNELKRLCGLKV
HHHHHHHHHHHCCCE		36.8325953088
271UbiquitinationDSFNNELKRLCGLKV
HHHHHHHHHHHCCCE		36.8321890473
271 (in isoform 1)Ubiquitination-36.8321890473
271 (in isoform 2)Ubiquitination-36.8321890473
277SumoylationLKRLCGLKVEVDMEK
HHHHHCCCEEECHHH		22.95-
277AcetylationLKRLCGLKVEVDMEK
HHHHHCCCEEECHHH		22.9526051181
277SumoylationLKRLCGLKVEVDMEK
HHHHHCCCEEECHHH		22.9528112733
277UbiquitinationLKRLCGLKVEVDMEK
HHHHHCCCEEECHHH		22.95-
284UbiquitinationKVEVDMEKIAAEIAQ
CEEECHHHHHHHHHH		30.892190698
284 (in isoform 1)Ubiquitination-30.8921890473
284 (in isoform 2)Ubiquitination-30.8921890473
314PhosphorylationAAEQAERSQSSIVPE
HHHHHHHHHHCCCCH		26.3929255136
316PhosphorylationEQAERSQSSIVPEEE
HHHHHHHHCCCCHHH		24.2329255136
317PhosphorylationQAERSQSSIVPEEEQ
HHHHHHHCCCCHHHH		21.7025159151
328AcetylationEEEQAANKGEEKKDD
HHHHHHHCCCCCCCC		64.0723236377
328UbiquitinationEEEQAANKGEEKKDD
HHHHHHHCCCCCCCC		64.07-
342PhosphorylationDENIPMETEETHLEE
CCCCCCCCCCHHHHH		32.6320873877
345PhosphorylationIPMETEETHLEETTE
CCCCCCCHHHHHHCH		26.0623663014
350PhosphorylationEETHLEETTESQQNG
CCHHHHHHCHHHHCC		26.8723663014
351PhosphorylationETHLEETTESQQNGE
CHHHHHHCHHHHCCC		36.6023663014
353PhosphorylationHLEETTESQQNGEEG
HHHHHCHHHHCCCCC		34.6728348404
361PhosphorylationQQNGEEGTSTPEDKE
HHCCCCCCCCHHHHH		32.4823663014
362PhosphorylationQNGEEGTSTPEDKES
HCCCCCCCCHHHHHC		53.4723663014
363PhosphorylationNGEEGTSTPEDKESG
CCCCCCCCHHHHHCC		30.4528348404
376PhosphorylationSGQEGVDSMAEEGTS
CCCCCHHHHHHCCCC		19.9330576142
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
-KUbiquitinationE3 ubiquitin ligaseTRIP12Q14669
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMCE1_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 SMCE1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ESR2_HUMANESR2physical
12145209
ESR1_HUMANESR1physical
12145209
SMCA4_HUMANSMARCA4physical
9845365
SMRC2_HUMANSMARCC2physical
9845365
SMRC1_HUMANSMARCC1physical
9845365
SNF5_HUMANSMARCB1physical
9845365
ACTB_HUMANACTBphysical
9845365
ACL6A_HUMANACTL6Aphysical
9845365
ARI1A_HUMANARID1Aphysical
16940996
SMCA4_HUMANSMARCA4physical
16940996
SMRC2_HUMANSMARCC2physical
16940996
SMRC1_HUMANSMARCC1physical
16940996
SMRC2_HUMANSMARCC2physical
19164553
PB1_HUMANPBRM1physical
19650111
ARI1A_HUMANARID1Aphysical
19650111
SMRC2_HUMANSMARCC2physical
19650111
SMRC1_HUMANSMARCC1physical
19650111
SNF5_HUMANSMARCB1physical
18809673
SMRC1_HUMANSMARCC1physical
18809673
SMCA4_HUMANSMARCA4physical
18809673
ARI1A_HUMANARID1Aphysical
18809673
ARID2_HUMANARID2physical
18809673
BRD7_HUMANBRD7physical
18809673
SMRD1_HUMANSMARCD1physical
18809673
REQU_HUMANDPF2physical
18809673
ACL6A_HUMANACTL6Aphysical
18809673
ACTB_HUMANACTBphysical
18809673
BCL7C_HUMANBCL7Cphysical
18809673
ESR1_HUMANESR1physical
16538531
NCOA1_HUMANNCOA1physical
16538531
SMRC1_HUMANSMARCC1physical
16199878
SMRC2_HUMANSMARCC2physical
16199878
SMRD1_HUMANSMARCD1physical
16199878
SNF5_HUMANSMARCB1physical
16199878
SMCA4_HUMANSMARCA4physical
12192000
RCOR1_HUMANRCOR1physical
12192000
REST_HUMANRESTphysical
12192000
HDAC1_HUMANHDAC1physical
12192000
HDAC2_HUMANHDAC2physical
12192000
ANDR_HUMANARphysical
15743818
IKZF1_HUMANIKZF1physical
11003653
SMCA4_HUMANSMARCA4physical
11003653
CHD4_HUMANCHD4physical
11003653
SMRC1_HUMANSMARCC1physical
20829358
TRIPC_HUMANTRIP12physical
20829358
ARID2_HUMANARID2physical
15985610
ACL6A_HUMANACTL6Aphysical
20305087
ARI1A_HUMANARID1Aphysical
20305087
ARI1B_HUMANARID1Bphysical
20305087
ARID2_HUMANARID2physical
20305087
BRD7_HUMANBRD7physical
20305087
REQU_HUMANDPF2physical
20305087
PHF10_HUMANPHF10physical
20305087
SMCA2_HUMANSMARCA2physical
20305087
SMCA4_HUMANSMARCA4physical
20305087
SNF5_HUMANSMARCB1physical
20305087
SMRC1_HUMANSMARCC1physical
20305087
SMRC2_HUMANSMARCC2physical
20305087
SMRD1_HUMANSMARCD1physical
20305087
SMRD2_HUMANSMARCD2physical
20305087
SMRD3_HUMANSMARCD3physical
20305087
SMRC1_HUMANSMARCC1physical
22939629
SMRD1_HUMANSMARCD1physical
22939629
SMRC2_HUMANSMARCC2physical
22939629
SNF5_HUMANSMARCB1physical
22939629
SMRD2_HUMANSMARCD2physical
22939629
SMRD3_HUMANSMARCD3physical
22939629
TOP2B_HUMANTOP2Bphysical
22939629
STX11_HUMANSTX11physical
25416956
CIP4_HUMANTRIP10physical
25416956
JKIP2_HUMANJAKMIP2physical
25416956
SPAG5_HUMANSPAG5physical
25416956
RBP1_HUMANRALBP1physical
25416956
EXOC7_HUMANEXOC7physical
25416956
MTUS2_HUMANMTUS2physical
25416956
NUP62_HUMANNUP62physical
25416956
TFP11_HUMANTFIP11physical
25416956
MED4_HUMANMED4physical
25416956
AMOL2_HUMANAMOTL2physical
25416956
TRI54_HUMANTRIM54physical
25416956
RINT1_HUMANRINT1physical
25416956
CC136_HUMANCCDC136physical
25416956
CEP63_HUMANCEP63physical
25416956
CEP70_HUMANCEP70physical
25416956
USBP1_HUMANUSHBP1physical
25416956
ING5_HUMANING5physical
25416956
SYCE1_HUMANSYCE1physical
25416956
MR1L1_HUMANMRFAP1L1physical
25416956
K1C40_HUMANKRT40physical
25416956
MIPO1_HUMANMIPOL1physical
25416956
TXLNA_HUMANTXLNAphysical
25416956
CC172_HUMANCCDC172physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
ARI1B_HUMANARID1Bphysical
26186194
ARI1A_HUMANARID1Aphysical
26186194
PHF10_HUMANPHF10physical
26186194
SMRC2_HUMANSMARCC2physical
26186194
SMRC1_HUMANSMARCC1physical
26186194
SMRD3_HUMANSMARCD3physical
26186194
SMRD2_HUMANSMARCD2physical
26186194
SMRD1_HUMANSMARCD1physical
26186194
SMCA4_HUMANSMARCA4physical
26186194
SMCA2_HUMANSMARCA2physical
26186194
ARID2_HUMANARID2physical
26186194
PB1_HUMANPBRM1physical
26186194
SNF5_HUMANSMARCB1physical
26186194
DPF1_HUMANDPF1physical
26186194
BRD7_HUMANBRD7physical
26186194
BCL7B_HUMANBCL7Bphysical
26186194
SSXT_HUMANSS18physical
26186194
CREST_HUMANSS18L1physical
26186194
ARI1A_HUMANARID1Aphysical
26344197
BCL7C_HUMANBCL7Cphysical
26344197
REQU_HUMANDPF2physical
26344197
SMCA2_HUMANSMARCA2physical
26344197
SMCA4_HUMANSMARCA4physical
26344197
SNF5_HUMANSMARCB1physical
26344197
SMRD2_HUMANSMARCD2physical
26344197
SMRD3_HUMANSMARCD3physical
26344197
SSXT_HUMANSS18physical
26344197
ESR1_HUMANESR1physical
17363140
NCOA1_HUMANNCOA1physical
17363140
RARB_HUMANRARBphysical
17363140
CEP63_HUMANCEP63physical
21516116
SMRC2_HUMANSMARCC2physical
28514442
SMRD1_HUMANSMARCD1physical
28514442
BRD7_HUMANBRD7physical
28514442
ARID2_HUMANARID2physical
28514442
PB1_HUMANPBRM1physical
28514442
ARI1B_HUMANARID1Bphysical
28514442
SMRD3_HUMANSMARCD3physical
28514442
BCL7B_HUMANBCL7Bphysical
28514442
DPF1_HUMANDPF1physical
28514442
PHF10_HUMANPHF10physical
28514442
SMCA2_HUMANSMARCA2physical
28514442
SSXT_HUMANSS18physical
28514442
SMRD2_HUMANSMARCD2physical
28514442
SNF5_HUMANSMARCB1physical
28514442
SMRC1_HUMANSMARCC1physical
28514442
SMCA4_HUMANSMARCA4physical
28514442
ARI1A_HUMANARID1Aphysical
28514442
CREST_HUMANSS18L1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607174Meningioma (MNGMA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMCE1_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-265, AND MASSSPECTROMETRY.

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