NOTC2_HUMAN - dbPTM
NOTC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOTC2_HUMAN
UniProt AC Q04721
Protein Name Neurogenic locus notch homolog protein 2
Gene Name NOTCH2 {ECO:0000312|HGNC:HGNC:7882}
Organism Homo sapiens (Human).
Sequence Length 2471
Subcellular Localization Notch 2 extracellular truncation: Cell membrane
Single-pass type I membrane protein .
Notch 2 intracellular domain: Nucleus . Cytoplasm . Following proteolytical processing NICD is translocated to the nucleus. Retained at the cytoplasm by TCIM (Pu
Protein Description Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs (By similarity). Involved in bone remodeling and homeostasis. In collaboration with RELA/p65 enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation. [PubMed: 29149593 Positively regulates self-renewal of liver cancer cells]
Protein Sequence MPALRPALLWALLALWLCCAAPAHALQCRDGYEPCVNEGMCVTYHNGTGYCKCPEGFLGEYCQHRDPCEKNRCQNGGTCVAQAMLGKATCRCASGFTGEDCQYSTSHPCFVSRPCLNGGTCHMLSRDTYECTCQVGFTGKECQWTDACLSHPCANGSTCTTVANQFSCKCLTGFTGQKCETDVNECDIPGHCQHGGTCLNLPGSYQCQCPQGFTGQYCDSLYVPCAPSPCVNGGTCRQTGDFTFECNCLPGFEGSTCERNIDDCPNHRCQNGGVCVDGVNTYNCRCPPQWTGQFCTEDVDECLLQPNACQNGGTCANRNGGYGCVCVNGWSGDDCSENIDDCAFASCTPGSTCIDRVASFSCMCPEGKAGLLCHLDDACISNPCHKGALCDTNPLNGQYICTCPQGYKGADCTEDVDECAMANSNPCEHAGKCVNTDGAFHCECLKGYAGPRCEMDINECHSDPCQNDATCLDKIGGFTCLCMPGFKGVHCELEINECQSNPCVNNGQCVDKVNRFQCLCPPGFTGPVCQIDIDDCSSTPCLNGAKCIDHPNGYECQCATGFTGVLCEENIDNCDPDPCHHGQCQDGIDSYTCICNPGYMGAICSDQIDECYSSPCLNDGRCIDLVNGYQCNCQPGTSGVNCEINFDDCASNPCIHGICMDGINRYSCVCSPGFTGQRCNIDIDECASNPCRKGATCINGVNGFRCICPEGPHHPSCYSQVNECLSNPCIHGNCTGGLSGYKCLCDAGWVGINCEVDKNECLSNPCQNGGTCDNLVNGYRCTCKKGFKGYNCQVNIDECASNPCLNQGTCFDDISGYTCHCVLPYTGKNCQTVLAPCSPNPCENAAVCKESPNFESYTCLCAPGWQGQRCTIDIDECISKPCMNHGLCHNTQGSYMCECPPGFSGMDCEEDIDDCLANPCQNGGSCMDGVNTFSCLCLPGFTGDKCQTDMNECLSEPCKNGGTCSDYVNSYTCKCQAGFDGVHCENNINECTESSCFNGGTCVDGINSFSCLCPVGFTGSFCLHEINECSSHPCLNEGTCVDGLGTYRCSCPLGYTGKNCQTLVNLCSRSPCKNKGTCVQKKAESQCLCPSGWAGAYCDVPNVSCDIAASRRGVLVEHLCQHSGVCINAGNTHYCQCPLGYTGSYCEEQLDECASNPCQHGATCSDFIGGYRCECVPGYQGVNCEYEVDECQNQPCQNGGTCIDLVNHFKCSCPPGTRGLLCEENIDDCARGPHCLNGGQCMDRIGGYSCRCLPGFAGERCEGDINECLSNPCSSEGSLDCIQLTNDYLCVCRSAFTGRHCETFVDVCPQMPCLNGGTCAVASNMPDGFICRCPPGFSGARCQSSCGQVKCRKGEQCVHTASGPRCFCPSPRDCESGCASSPCQHGGSCHPQRQPPYYSCQCAPPFSGSRCELYTAPPSTPPATCLSQYCADKARDGVCDEACNSHACQWDGGDCSLTMENPWANCSSPLPCWDYINNQCDELCNTVECLFDNFECQGNSKTCKYDKYCADHFKDNHCDQGCNSEECGWDGLDCAADQPENLAEGTLVIVVLMPPEQLLQDARSFLRALGTLLHTNLRIKRDSQGELMVYPYYGEKSAAMKKQRMTRRSLPGEQEQEVAGSKVFLEIDNRQCVQDSDHCFKNTDAAAALLASHAIQGTLSYPLVSVVSESLTPERTQLLYLLAVAVVIILFIILLGVIMAKRKRKHGSLWLPEGFTLRRDASNHKRREPVGQDAVGLKNLSVQVSEANLIGTGTSEHWVDDEGPQPKKVKAEDEALLSEEDDPIDRRPWTQQHLEAADIRRTPSLALTPPQAEQEVDVLDVNVRGPDGCTPLMLASLRGGSSDLSDEDEDAEDSSANIITDLVYQGASLQAQTDRTGEMALHLAARYSRADAAKRLLDAGADANAQDNMGRCPLHAAVAADAQGVFQILIRNRVTDLDARMNDGTTPLILAARLAVEGMVAELINCQADVNAVDDHGKSALHWAAAVNNVEATLLLLKNGANRDMQDNKEETPLFLAAREGSYEAAKILLDHFANRDITDHMDRLPRDVARDRMHHDIVRLLDEYNVTPSPPGTVLTSALSPVICGPNRSFLSLKHTPMGKKSRRPSAKSTMPTSLPNLAKEAKDAKGSRRKKSLSEKVQLSESSVTLSPVDSLESPHTYVSDTTSSPMITSPGILQASPNPMLATAAPPAPVHAQHALSFSNLHEMQPLAHGASTVLPSVSQLLSHHHIVSPGSGSAGSLSRLHPVPVPADWMNRMEVNETQYNEMFGMVLAPAEGTHPGIAPQSRPPEGKHITTPREPLPPIVTFQLIPKGSIAQPAGAPQPQSTCPPAVAGPLPTMYQIPEMARLPSVAFPTAMMPQQDGQVAQTILPAYHPFPASVGKYPTPPSQHSYASSNAAERTPSHSGHLQGEHPYLTPSPESPDQWSSSSPHSASDWSDVTTSPTPGGAGGGQRGPGTHMSEPPHNNMQVYA
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
46N-linked_GlycosylationGMCVTYHNGTGYCKC
CEEEEEECCCCEEEC		39.03UniProtKB CARBOHYD
155N-linked_GlycosylationCLSHPCANGSTCTTV
HHCCCCCCCCHHHHH		52.22UniProtKB CARBOHYD
161O-linked_GlycosylationANGSTCTTVANQFSC
CCCCHHHHHHHHHCC		21.55OGP
175O-linked_GlycosylationCKCLTGFTGQKCETD
CCCCCCCCCCCCCCC		39.7928657654
359PhosphorylationTCIDRVASFSCMCPE
CHHHHHHEEEEECCC		18.1623401153
436PhosphorylationHAGKCVNTDGAFHCE
CCCCCCCCCCCEECC		18.5320058876
613O-linked_GlycosylationDQIDECYSSPCLNDG
HCCCHHHCCCCCCCC		39.19UniProtKB CARBOHYD
675O-linked_GlycosylationCVCSPGFTGQRCNID
CEECCCCCCCCCCCC		38.0228657654
733N-linked_GlycosylationSNPCIHGNCTGGLSG
CCCCCCCCCCCCCCC		13.15UniProtKB CARBOHYD
838O-linked_GlycosylationQTVLAPCSPNPCENA
CEEEEECCCCCCCCC		27.01OGP
942O-linked_GlycosylationCLCLPGFTGDKCQTD
CEECCCCCCCCCCCC		50.8428657654
948PhosphorylationFTGDKCQTDMNECLS
CCCCCCCCCHHHHHC		46.8430576142
955PhosphorylationTDMNECLSEPCKNGG
CCHHHHHCCCCCCCC		51.6730576142
967PhosphorylationNGGTCSDYVNSYTCK
CCCCHHHHHHCEECE		5.8030576142
1102N-linked_GlycosylationGAYCDVPNVSCDIAA
CCCCCCCCCCCCCHH		37.88UniProtKB CARBOHYD
1248PhosphorylationCMDRIGGYSCRCLPG
CHHHCCCEECCCCCC		10.2122210691
1249PhosphorylationMDRIGGYSCRCLPGF
HHHCCCEECCCCCCC		9.8122210691
1380PhosphorylationDCESGCASSPCQHGG
CCCCCCCCCCCCCCC		38.6030576142
1381PhosphorylationCESGCASSPCQHGGS
CCCCCCCCCCCCCCC		15.9230576142
1388PhosphorylationSPCQHGGSCHPQRQP
CCCCCCCCCCCCCCC		17.5330576142
1397PhosphorylationHPQRQPPYYSCQCAP
CCCCCCCCCCCCCCC		18.0724043423
1398PhosphorylationPQRQPPYYSCQCAPP
CCCCCCCCCCCCCCC		14.5624043423
1399PhosphorylationQRQPPYYSCQCAPPF
CCCCCCCCCCCCCCC		7.5924043423
1407PhosphorylationCQCAPPFSGSRCELY
CCCCCCCCCCCEEEE		41.4524043423
1409PhosphorylationCAPPFSGSRCELYTA
CCCCCCCCCEEEEEC		32.3424043423
1415O-linked_GlycosylationGSRCELYTAPPSTPP
CCCEEEEECCCCCCC		45.36OGP
1419O-linked_GlycosylationELYTAPPSTPPATCL
EEEECCCCCCCCCHH		53.11OGP
1419PhosphorylationELYTAPPSTPPATCL
EEEECCCCCCCCCHH		53.1130576142
1420O-linked_GlycosylationLYTAPPSTPPATCLS
EEECCCCCCCCCHHH		38.78OGP
1424O-linked_GlycosylationPPSTPPATCLSQYCA
CCCCCCCCHHHHHHH		21.54OGP
1424PhosphorylationPPSTPPATCLSQYCA
CCCCCCCCHHHHHHH		21.5430576142
1427PhosphorylationTPPATCLSQYCADKA
CCCCCHHHHHHHHHH		22.6530576142
1465N-linked_GlycosylationTMENPWANCSSPLPC
EECCCCCCCCCCCCH		23.49UniProtKB CARBOHYD
1564PhosphorylationQLLQDARSFLRALGT
HHHHHHHHHHHHHHH		30.2824945436
1580AcetylationLHTNLRIKRDSQGEL
HHHCCEEEECCCCCE		43.667662391
1596AcetylationVYPYYGEKSAAMKKQ
EEECCCCCHHHHHHH		40.827662403
1602UbiquitinationEKSAAMKKQRMTRRS
CCHHHHHHHHHCCCC		30.01-
1622UbiquitinationEQEVAGSKVFLEIDN
HHHHHCCEEEEEECC		35.77-
1660PhosphorylationHAIQGTLSYPLVSVV
HHHHCCCCCCCEEHH		25.2530576142
1668PhosphorylationYPLVSVVSESLTPER
CCCEEHHCCCCCHHH		21.2230576142
1670PhosphorylationLVSVVSESLTPERTQ
CEEHHCCCCCHHHHH		30.0030576142
1705UbiquitinationIMAKRKRKHGSLWLP
HHHHHHHHCCCCCCC		56.1821890473
1708PhosphorylationKRKRKHGSLWLPEGF
HHHHHCCCCCCCCCC		18.9825159151
1716PhosphorylationLWLPEGFTLRRDASN
CCCCCCCCCCCCCCC		30.1625159151
1722PhosphorylationFTLRRDASNHKRREP
CCCCCCCCCCCCCCC		43.7029514088
1738UbiquitinationGQDAVGLKNLSVQVS
CCCCCCCCCEEEEEE		50.33-
1745PhosphorylationKNLSVQVSEANLIGT
CCEEEEEEEEEEECC		17.5628857561
1767AcetylationDDEGPQPKKVKAEDE
CCCCCCCCCCCHHHH		66.0226051181
1770UbiquitinationGPQPKKVKAEDEALL
CCCCCCCCHHHHHHH		55.74-
1778PhosphorylationAEDEALLSEEDDPID
HHHHHHHCCCCCCCC		39.5329255136
1790PhosphorylationPIDRRPWTQQHLEAA
CCCCCCCHHHHHHHH		22.4920068231
1802PhosphorylationEAADIRRTPSLALTP
HHHHHCCCCCCCCCC		13.8429255136
1804PhosphorylationADIRRTPSLALTPPQ
HHHCCCCCCCCCCCC		26.1729255136
1808PhosphorylationRTPSLALTPPQAEQE
CCCCCCCCCCCHHCE		27.5829255136
1830PhosphorylationVRGPDGCTPLMLASL
CCCCCCCCHHHHHHH		25.6129255136
1836PhosphorylationCTPLMLASLRGGSSD
CCHHHHHHHCCCCCC		18.0328857561
1841PhosphorylationLASLRGGSSDLSDED
HHHHCCCCCCCCCCC		24.4130278072
1842PhosphorylationASLRGGSSDLSDEDE
HHHCCCCCCCCCCCC		45.9330278072
1845PhosphorylationRGGSSDLSDEDEDAE
CCCCCCCCCCCCCCC		43.9030278072
1854PhosphorylationEDEDAEDSSANIITD
CCCCCCCCCCHHHHH		23.9020873877
1855PhosphorylationDEDAEDSSANIITDL
CCCCCCCCCHHHHHH		37.3428176443
1860PhosphorylationDSSANIITDLVYQGA
CCCCHHHHHHHHCCC		21.3420068231
1864PhosphorylationNIITDLVYQGASLQA
HHHHHHHHCCCCCEE		14.4520068231
1868PhosphorylationDLVYQGASLQAQTDR
HHHHCCCCCEECCCC		28.0420068231
1873PhosphorylationGASLQAQTDRTGEMA
CCCCEECCCCHHHHH		30.3920068231
2009MalonylationNRDMQDNKEETPLFL
CCCCCCCCCCCCHHH		66.2826320211
2022PhosphorylationFLAAREGSYEAAKIL
HHHHHCCCHHHHHHH		18.2920068231
2023PhosphorylationLAAREGSYEAAKILL
HHHHCCCHHHHHHHH		22.0520068231
2039PhosphorylationHFANRDITDHMDRLP
HHCCCCCHHHHHHCC		24.9224719451
2065PhosphorylationIVRLLDEYNVTPSPP
HHHHHHHCCCCCCCC		18.0129255136
2068PhosphorylationLLDEYNVTPSPPGTV
HHHHCCCCCCCCCCE		17.8929255136
2070PhosphorylationDEYNVTPSPPGTVLT
HHCCCCCCCCCCEEE		34.0729255136
2074PhosphorylationVTPSPPGTVLTSALS
CCCCCCCCEEECCCC		20.3729255136
2077PhosphorylationSPPGTVLTSALSPVI
CCCCCEEECCCCCEE		13.9729255136
2078PhosphorylationPPGTVLTSALSPVIC
CCCCEEECCCCCEEE		24.0529255136
2081PhosphorylationTVLTSALSPVICGPN
CEEECCCCCEEECCC		19.4829255136
2090PhosphorylationVICGPNRSFLSLKHT
EEECCCCCCCCCCCC		36.8621815630
2093PhosphorylationGPNRSFLSLKHTPMG
CCCCCCCCCCCCCCC		33.1026055452
2095AcetylationNRSFLSLKHTPMGKK
CCCCCCCCCCCCCCC		41.9026051181
2097PhosphorylationSFLSLKHTPMGKKSR
CCCCCCCCCCCCCCC		17.2426055452
2101UbiquitinationLKHTPMGKKSRRPSA
CCCCCCCCCCCCCCC		41.13-
2102UbiquitinationKHTPMGKKSRRPSAK
CCCCCCCCCCCCCCC		43.39-
2107PhosphorylationGKKSRRPSAKSTMPT
CCCCCCCCCCCCCCC		46.6622210691
2110PhosphorylationSRRPSAKSTMPTSLP
CCCCCCCCCCCCCHH		29.6530576142
2111PhosphorylationRRPSAKSTMPTSLPN
CCCCCCCCCCCCHHH		26.8529396449
2114PhosphorylationSAKSTMPTSLPNLAK
CCCCCCCCCHHHHHH		31.8827794612
2115PhosphorylationAKSTMPTSLPNLAKE
CCCCCCCCHHHHHHH		35.6423401153
2121AcetylationTSLPNLAKEAKDAKG
CCHHHHHHHHHHHCC		62.4626051181
2121UbiquitinationTSLPNLAKEAKDAKG
CCHHHHHHHHHHHCC		62.46-
2129PhosphorylationEAKDAKGSRRKKSLS
HHHHHCCCHHCCCHH		28.36-
2134PhosphorylationKGSRRKKSLSEKVQL
CCCHHCCCHHHCEEC		39.9126699800
2136PhosphorylationSRRKKSLSEKVQLSE
CHHCCCHHHCEECCC		42.3226699800
2264PhosphorylationMEVNETQYNEMFGMV
CCCCHHHHHHHHCEE		22.1027642862
2292AcetylationQSRPPEGKHITTPRE
CCCCCCCCCCCCCCC		30.1226051181
2295PhosphorylationPPEGKHITTPREPLP
CCCCCCCCCCCCCCC		30.3922199227
2296PhosphorylationPEGKHITTPREPLPP
CCCCCCCCCCCCCCC		21.5325159151
2306PhosphorylationEPLPPIVTFQLIPKG
CCCCCEEEEEEEECC		13.3422199227
2314PhosphorylationFQLIPKGSIAQPAGA
EEEEECCCCCCCCCC		22.3721945579
2326PhosphorylationAGAPQPQSTCPPAVA
CCCCCCCCCCCCCCC		38.3621945579
2327PhosphorylationGAPQPQSTCPPAVAG
CCCCCCCCCCCCCCC		24.6321945579
2338PhosphorylationAVAGPLPTMYQIPEM
CCCCCCCCCCCCHHH		35.8721945579
2340PhosphorylationAGPLPTMYQIPEMAR
CCCCCCCCCCHHHHC		13.0321945579
2350PhosphorylationPEMARLPSVAFPTAM
HHHHCCCCCCCCCCC		30.5727642862
2368PhosphorylationQDGQVAQTILPAYHP
CCCCCCHHHCHHCCC		18.1029978859
2373PhosphorylationAQTILPAYHPFPASV
CHHHCHHCCCCCCCC		14.2127259358
2379PhosphorylationAYHPFPASVGKYPTP
HCCCCCCCCCCCCCC		31.4729978859
2382AcetylationPFPASVGKYPTPPSQ
CCCCCCCCCCCCHHH		45.9926051181
2383PhosphorylationFPASVGKYPTPPSQH
CCCCCCCCCCCHHHC		13.3527080861
2385PhosphorylationASVGKYPTPPSQHSY
CCCCCCCCCHHHCCC		44.7525159151
2388PhosphorylationGKYPTPPSQHSYASS
CCCCCCHHHCCCCCC		41.5525159151
2391PhosphorylationPTPPSQHSYASSNAA
CCCHHHCCCCCCCCC		18.1125627689
2392PhosphorylationTPPSQHSYASSNAAE
CCHHHCCCCCCCCCC		14.3727080861
2460PhosphorylationRGPGTHMSEPPHNNM
CCCCCCCCCCCCCCC		39.0728555341
2470PhosphorylationPHNNMQVYA------
CCCCCCCCC------		6.9527259358
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 NOTC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOTC2_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 NOTC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CNTN1_HUMANCNTN1physical
14567914
GSK3B_HUMANGSK3Bphysical
12794074
SUH_HUMANRBPJphysical
9032325
DLL1_HUMANDLL1physical
10958687
JAG1_HUMANJAG1physical
10958687
JAG2_HUMANJAG2physical
10958687
SC24C_HUMANSEC24Cphysical
22939629
PIMT_HUMANPCMT1physical
22939629
PSB1_HUMANPSMB1physical
22939629
ZO1_HUMANTJP1physical
22939629
SIN3A_HUMANSIN3Aphysical
22939629
UPAR_HUMANPLAURphysical
22939629
EF2_HUMANEEF2physical
26344197
AFAD_HUMANMLLT4physical
26344197
PDIA6_HUMANPDIA6physical
26344197
CYTM_HUMANCST6physical
25640309
ESIP1_HUMANEPSTI1physical
25640309
FA84B_HUMANFAM84Bphysical
25640309
I13R2_HUMANIL13RA2physical
25640309
IL24_HUMANIL24physical
25640309
ITIH5_HUMANITIH5physical
25640309
KLK5_HUMANKLK5physical
25640309
MTA3_HUMANMTA3physical
25640309
HOP2_HUMANPSMC3IPphysical
25640309
ST14_HUMANST14physical
25640309
Drug and Disease Associations
Kegg Disease
H00409 Type II diabetes mellitus
H00551 Alagille syndrome
H00623 Hajdu-Cheney syndrome
OMIM Disease
610205Alagille syndrome 2 (ALGS2)
102500Hajdu-Cheney syndrome (HJCYS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NOTC2_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-1778 AND SER-1845, ANDMASS 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 THR-1716; SER-1778;THR-1802; SER-1804; THR-1808; SER-2070; THR-2074; SER-2081 ANDTHR-2097, AND MASS SPECTROMETRY.
"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 SER-1841; SER-1842 ANDSER-1845, AND MASS 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 THR-1808 AND SER-2070, ANDMASS SPECTROMETRY.

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