MELK_HUMAN - dbPTM
MELK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MELK_HUMAN
UniProt AC Q14680
Protein Name Maternal embryonic leucine zipper kinase
Gene Name MELK
Organism Homo sapiens (Human).
Sequence Length 651
Subcellular Localization Cell membrane
Peripheral membrane protein .
Protein Description Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation and carcinogenesis. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14, possibly leading to affect mammary carcinogenesis by mediating inhibition of the pro-apoptotic function of BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis..
Protein Sequence MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRLRLSSFSCGQASATPFTDIKSNNWSLEDVTASDKNYVAGLIDYDWCEDDLSTGAATPRTSQFTKYWTESNGVESKSLTPALCRTPANKLKNKENVYTPKSAVKNEEYFMFPEPKTPVNKNQHKREILTTPNRYTTPSKARNQCLKETPIKIPVNSTGTDKLMTGVISPERRCRSVELDLNQAHMEETPKRKGAKVFGSLERGLDKVITVLTRSKRKGSARDGPRRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQKPDVVGIRRQRLKGDAWVYKRLVEDILSSCKV
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
2Ubiquitination------MKDYDELLK
------CCCHHHHHH		66.06-
4Phosphorylation----MKDYDELLKYY
----CCCHHHHHHHH		13.0520007894
9UbiquitinationKDYDELLKYYELHET
CCHHHHHHHHHHHHH		59.41-
11PhosphorylationYDELLKYYELHETIG
HHHHHHHHHHHHHHC		15.4927642862
24UbiquitinationIGTGGFAKVKLACHI
HCCCCHHHHHHHHEH		37.33-
44UbiquitinationVAIKIMDKNTLGSDL
EEEEECCCCCCCCCC		34.1621906983
49PhosphorylationMDKNTLGSDLPRIKT
CCCCCCCCCCHHHHH		38.8023312004
55SumoylationGSDLPRIKTEIEALK
CCCCHHHHHHHHHHH		41.19-
55SumoylationGSDLPRIKTEIEALK
CCCCHHHHHHHHHHH		41.19-
55UbiquitinationGSDLPRIKTEIEALK
CCCCHHHHHHHHHHH		41.1921890473
56PhosphorylationSDLPRIKTEIEALKN
CCCHHHHHHHHHHHH		39.5616216881
62UbiquitinationKTEIEALKNLRHQHI
HHHHHHHHHHCHHHH		62.0721906983
122PhosphorylationQIVSAVAYVHSQGYA
HHHHHHHHHHHCCCC		7.6626503514
125PhosphorylationSAVAYVHSQGYAHRD
HHHHHHHHCCCCCCC		18.4326503514
134UbiquitinationGYAHRDLKPENLLFD
CCCCCCCCHHHCCCC		55.3521890473
145UbiquitinationLLFDEYHKLKLIDFG
CCCCCCHHCCEEEEC		46.5521906983
147UbiquitinationFDEYHKLKLIDFGLC
CCCCHHCCEEEECEE		48.47-
156AcetylationIDFGLCAKPKGNKDY
EEECEECCCCCCCCC		46.3925953088
156UbiquitinationIDFGLCAKPKGNKDY
EEECEECCCCCCCCC		46.39-
161UbiquitinationCAKPKGNKDYHLQTC
ECCCCCCCCCCHHHH		69.22-
163PhosphorylationKPKGNKDYHLQTCCG
CCCCCCCCCHHHHHH		13.1616216881
167PhosphorylationNKDYHLQTCCGSLAY
CCCCCHHHHHHHHHH		19.0014976552
171PhosphorylationHLQTCCGSLAYAAPE
CHHHHHHHHHHHCHH		8.9116216881
225UbiquitinationYKKIMRGKYDVPKWL
HHHHHCCCCCCCCCC		28.10-
226PhosphorylationKKIMRGKYDVPKWLS
HHHHCCCCCCCCCCC		25.6220860994
236PhosphorylationPKWLSPSSILLLQQM
CCCCCHHHHHHHHHH		22.19-
249UbiquitinationQMLQVDPKKRISMKN
HHHCCCCCCCCCHHH		50.66-
250UbiquitinationMLQVDPKKRISMKNL
HHCCCCCCCCCHHHH		61.42-
253PhosphorylationVDPKKRISMKNLLNH
CCCCCCCCHHHHHCC		27.9516216881
255UbiquitinationPKKRISMKNLLNHPW
CCCCCCHHHHHCCCC		37.34-
267PhosphorylationHPWIMQDYNYPVEWQ
CCCHHCCCCCCCCCC		10.3326552605
269PhosphorylationWIMQDYNYPVEWQSK
CHHCCCCCCCCCCCC		11.4826552605
275PhosphorylationNYPVEWQSKNPFIHL
CCCCCCCCCCCCEEC		35.1626552605
335PhosphorylationKPVRLRLSSFSCGQA
CCEEEEEEECCCCCC		23.9329255136
336PhosphorylationPVRLRLSSFSCGQAS
CEEEEEEECCCCCCC		26.2729255136
338PhosphorylationRLRLSSFSCGQASAT
EEEEEECCCCCCCCC		21.2021712546
343PhosphorylationSFSCGQASATPFTDI
ECCCCCCCCCCCCCC		25.4516628004
345PhosphorylationSCGQASATPFTDIKS
CCCCCCCCCCCCCCC		19.2121815630
348PhosphorylationQASATPFTDIKSNNW
CCCCCCCCCCCCCCC		37.7129396449
352PhosphorylationTPFTDIKSNNWSLED
CCCCCCCCCCCCHHH		35.4130266825
356PhosphorylationDIKSNNWSLEDVTAS
CCCCCCCCHHHCCCC		24.8119664994
361PhosphorylationNWSLEDVTASDKNYV
CCCHHHCCCCCCCEE		32.5330266825
363PhosphorylationSLEDVTASDKNYVAG
CHHHCCCCCCCEEEE		39.4930266825
367PhosphorylationVTASDKNYVAGLIDY
CCCCCCCEEEEECCC		9.4516628004
374PhosphorylationYVAGLIDYDWCEDDL
EEEEECCCCCCCCCC		12.3529978859
387PhosphorylationDLSTGAATPRTSQFT
CCCCCCCCCCCHHHH		16.8716628004
391PhosphorylationGAATPRTSQFTKYWT
CCCCCCCHHHHHHHH		25.2816216881
395UbiquitinationPRTSQFTKYWTESNG
CCCHHHHHHHHHCCC		39.8321890473
395UbiquitinationPRTSQFTKYWTESNG
CCCHHHHHHHHHCCC		39.8321890473
395UbiquitinationPRTSQFTKYWTESNG
CCCHHHHHHHHHCCC		39.8321890473
395UbiquitinationPRTSQFTKYWTESNG
CCCHHHHHHHHHCCC		39.8321890473
395UbiquitinationPRTSQFTKYWTESNG
CCCHHHHHHHHHCCC		39.8321890473
395UbiquitinationPRTSQFTKYWTESNG
CCCHHHHHHHHHCCC		39.8321890473
395UbiquitinationPRTSQFTKYWTESNG
CCCHHHHHHHHHCCC		39.8321890473
395UbiquitinationPRTSQFTKYWTESNG
CCCHHHHHHHHHCCC		39.8321890473
398PhosphorylationSQFTKYWTESNGVES
HHHHHHHHHCCCCCC		26.8416628004
400PhosphorylationFTKYWTESNGVESKS
HHHHHHHCCCCCCCC		31.3525159151
405PhosphorylationTESNGVESKSLTPAL
HHCCCCCCCCCCHHH		25.7416628004
406SumoylationESNGVESKSLTPALC
HCCCCCCCCCCHHHH		35.66-
406SumoylationESNGVESKSLTPALC
HCCCCCCCCCCHHHH		35.66-
406UbiquitinationESNGVESKSLTPALC
HCCCCCCCCCCHHHH		35.66-
407PhosphorylationSNGVESKSLTPALCR
CCCCCCCCCCHHHHC		46.9122199227
409PhosphorylationGVESKSLTPALCRTP
CCCCCCCCHHHHCCC		17.3825159151
415PhosphorylationLTPALCRTPANKLKN
CCHHHHCCCHHHCCC		26.2525159151
423UbiquitinationPANKLKNKENVYTPK
CHHHCCCCCCCCCCH		49.42-
427PhosphorylationLKNKENVYTPKSAVK
CCCCCCCCCCHHHHC		28.9829396449
428PhosphorylationKNKENVYTPKSAVKN
CCCCCCCCCHHHHCC		21.6921815630
431PhosphorylationENVYTPKSAVKNEEY
CCCCCCHHHHCCCCC		39.2321945579
434SumoylationYTPKSAVKNEEYFMF
CCCHHHHCCCCCCCC		59.36-
434SumoylationYTPKSAVKNEEYFMF
CCCHHHHCCCCCCCC		59.36-
434UbiquitinationYTPKSAVKNEEYFMF
CCCHHHHCCCCCCCC		59.3621890473
438PhosphorylationSAVKNEEYFMFPEPK
HHHCCCCCCCCCCCC		8.3121945579
446PhosphorylationFMFPEPKTPVNKNQH
CCCCCCCCCCCCCHH		43.0925159151
459PhosphorylationQHKREILTTPNRYTT
HHHHHCCCCCCCCCC		45.9628450419
460PhosphorylationHKREILTTPNRYTTP
HHHHCCCCCCCCCCC		18.3429255136
463MethylationEILTTPNRYTTPSKA
HCCCCCCCCCCCHHH		31.23115483141
464PhosphorylationILTTPNRYTTPSKAR
CCCCCCCCCCCHHHH		22.9328450419
465PhosphorylationLTTPNRYTTPSKARN
CCCCCCCCCCHHHHH		29.0628450419
466PhosphorylationTTPNRYTTPSKARNQ
CCCCCCCCCHHHHHH		19.3428450419
468PhosphorylationPNRYTTPSKARNQCL
CCCCCCCHHHHHHHH		36.5322199227
469UbiquitinationNRYTTPSKARNQCLK
CCCCCCHHHHHHHHH		53.20-
476UbiquitinationKARNQCLKETPIKIP
HHHHHHHHCCCCEEE		68.14-
478PhosphorylationRNQCLKETPIKIPVN
HHHHHHCCCCEEECC		28.8225159151
481UbiquitinationCLKETPIKIPVNSTG
HHHCCCCEEECCCCC		42.0121890473
486PhosphorylationPIKIPVNSTGTDKLM
CCEEECCCCCCCCCC		28.5718691976
487PhosphorylationIKIPVNSTGTDKLMT
CEEECCCCCCCCCCC		38.6128555341
489PhosphorylationIPVNSTGTDKLMTGV
EECCCCCCCCCCCCC		30.01-
491UbiquitinationVNSTGTDKLMTGVIS
CCCCCCCCCCCCCCC		39.7421906983
494PhosphorylationTGTDKLMTGVISPER
CCCCCCCCCCCCHHH		38.4428102081
495UbiquitinationGTDKLMTGVISPERR
CCCCCCCCCCCHHHH		10.7821890473
498PhosphorylationKLMTGVISPERRCRS
CCCCCCCCHHHHHCE		20.5029255136
505PhosphorylationSPERRCRSVELDLNQ
CHHHHHCEEECCCCH		24.4629255136
518PhosphorylationNQAHMEETPKRKGAK
CHHHHHHCCCHHCCC		22.3223927012
520UbiquitinationAHMEETPKRKGAKVF
HHHHHCCCHHCCCHH		74.33-
522UbiquitinationMEETPKRKGAKVFGS
HHHCCCHHCCCHHHH		70.15-
525SumoylationTPKRKGAKVFGSLER
CCCHHCCCHHHHHHH		46.92-
525SumoylationTPKRKGAKVFGSLER
CCCHHCCCHHHHHHH		46.92-
525UbiquitinationTPKRKGAKVFGSLER
CCCHHCCCHHHHHHH		46.92-
529PhosphorylationKGAKVFGSLERGLDK
HCCCHHHHHHHHHHH		18.6529255136
536UbiquitinationSLERGLDKVITVLTR
HHHHHHHHHHHHHCC		40.3521890473
536UbiquitinationSLERGLDKVITVLTR
HHHHHHHHHHHHHCC		40.3521890473
536UbiquitinationSLERGLDKVITVLTR
HHHHHHHHHHHHHCC		40.3521890473
536UbiquitinationSLERGLDKVITVLTR
HHHHHHHHHHHHHCC		40.3521890473
536UbiquitinationSLERGLDKVITVLTR
HHHHHHHHHHHHHCC		40.3521890473
536UbiquitinationSLERGLDKVITVLTR
HHHHHHHHHHHHHCC		40.3521890473
536UbiquitinationSLERGLDKVITVLTR
HHHHHHHHHHHHHCC		40.3521890473
536UbiquitinationSLERGLDKVITVLTR
HHHHHHHHHHHHHCC		40.3521890473
539PhosphorylationRGLDKVITVLTRSKR
HHHHHHHHHHCCCCC		16.6714976552
542PhosphorylationDKVITVLTRSKRKGS
HHHHHHHCCCCCCCC		28.6722199227
544PhosphorylationVITVLTRSKRKGSAR
HHHHHCCCCCCCCCC		31.4122199227
558UbiquitinationRDGPRRLKLHYNVTT
CCCCCCEEEEEEEEE		31.26-
561PhosphorylationPRRLKLHYNVTTTRL
CCCEEEEEEEEECCC		23.0523312004
564PhosphorylationLKLHYNVTTTRLVNP
EEEEEEEEECCCCCH		20.8623312004
565PhosphorylationKLHYNVTTTRLVNPD
EEEEEEEECCCCCHH		12.9723312004
566PhosphorylationLHYNVTTTRLVNPDQ
EEEEEEECCCCCHHH		16.7923312004
585UbiquitinationIMSILPKKHVDFVQK
HHHHCCHHHCCHHHC		47.09-
592UbiquitinationKHVDFVQKGYTLKCQ
HHCCHHHCCCEEEEE		48.89-
597UbiquitinationVQKGYTLKCQTQSDF
HHCCCEEEEECCCCC		19.25-
632UbiquitinationGIRRQRLKGDAWVYK
EEECCCCCCCHHHHH		57.862190698
639TrimethylationKGDAWVYKRLVEDIL
CCCHHHHHHHHHHHH		29.63-
639MethylationKGDAWVYKRLVEDIL
CCCHHHHHHHHHHHH		29.6323644510
639UbiquitinationKGDAWVYKRLVEDIL
CCCHHHHHHHHHHHH		29.63-
650TrimethylationEDILSSCKV------
HHHHHHCCC------		53.58-
650MethylationEDILSSCKV------
HHHHHHCCC------		53.5823644510
650UbiquitinationEDILSSCKV------
HHHHHHCCC------		53.58-
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
56TPhosphorylationKinaseMELKQ14680
PSP
163YPhosphorylationKinaseMELKQ14680
PSP
167TPhosphorylationKinaseSTK11Q15831
PhosphoELM
167TPhosphorylationKinaseMELKQ14680
PSP
171SPhosphorylationKinaseMELKQ14680
PSP
253SPhosphorylationKinaseMELKQ14680
PSP
336SPhosphorylationKinaseMELKQ14680
PSP
343SPhosphorylationKinaseMELKQ14680
PSP
356SPhosphorylationKinaseMELKQ14680
PSP
367YPhosphorylationKinaseMELKQ14680
PSP
387TPhosphorylationKinaseMELKQ14680
PSP
391SPhosphorylationKinaseMELKQ14680
PSP
398TPhosphorylationKinaseMELKQ14680
PSP
405SPhosphorylationKinaseMELKQ14680
PSP
407SPhosphorylationKinaseMELKQ14680
PSP
409TPhosphorylationKinaseMELKQ14680
PSP
431SPhosphorylationKinaseMELKQ14680
PSP
438YPhosphorylationKinaseMELKQ14680
PSP
494TPhosphorylationKinaseMELKQ14680
PSP
505SPhosphorylationKinaseMELKQ14680
PSP
529SPhosphorylationKinaseMELKQ14680
PSP
539TPhosphorylationKinaseMELKQ14680
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
167TPhosphorylation

14976552
171SPhosphorylation

16216881
478TPhosphorylation

14699119
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 MELK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPIP2_HUMANCDC25Bphysical
12400006
ZN622_HUMANZNF622physical
11802789
ACACA_RATAcacaphysical
16216881
EIF2A_YEASTYGR054Wphysical
16216881
CASA1_BOVINCSN1S1physical
16216881
LMNB1_HUMANLMNB1physical
16216881
MBP_HUMANMBPphysical
16216881
MELK_HUMANMELKphysical
16216881
KI13B_HUMANKIF13Bphysical
27173435
GGYF1_HUMANGIGYF1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
SRS12_HUMANSRSF12physical
27173435
SYDE1_HUMANSYDE1physical
27173435
CING_HUMANCGNphysical
27173435
F110B_HUMANFAM110Bphysical
27173435
HDAC4_HUMANHDAC4physical
27173435
F110A_HUMANFAM110Aphysical
27173435
CBY1_HUMANCBY1physical
27173435
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 MELK_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-356, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-356; THR-460;SER-498; SER-505; THR-518 AND SER-529, 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-431 AND SER-505, ANDMASS 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-356; THR-446; THR-460;THR-478; THR-494; SER-498; SER-505; THR-518 AND SER-529, 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 SER-505, AND MASSSPECTROMETRY.
"Substrate specificity and activity regulation of protein kinaseMELK.";
Beullens M., Vancauwenbergh S., Morrice N., Derua R., Ceulemans H.,Waelkens E., Bollen M.;
J. Biol. Chem. 280:40003-40011(2005).
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION,CALCIUM-BINDING, PHOSPHORYLATION AT THR-56; TYR-163; THR-167; SER-171;SER-253; SER-336; SER-343; SER-356; SER-391; THR-398; SER-407;SER-431; THR-494; SER-505; SER-529 AND THR-539, AND MUTAGENESIS OFCYS-29; CYS-70; CYS-89; ASP-150; CYS-154; TYR-163; CYS-168; CYS-169;SER-171; CYS-204; 283-ASP--ASP-285; CYS-286 AND CYS-339.
"M-phase MELK activity is regulated by MPF and MAPK.";
Badouel C., Korner R., Frank-Vaillant M., Couturier A., Nigg E.A.,Tassan J.P.;
Cell Cycle 5:883-889(2006).
Cited for: PHOSPHORYLATION AT THR-167; SER-343; SER-356; TYR-367; THR-398;THR-409; SER-431; THR-494; SER-505 AND SER-529.
"LKB1 is a master kinase that activates 13 kinases of the AMPKsubfamily, including MARK/PAR-1.";
Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A.,Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G.,Alessi D.R.;
EMBO J. 23:833-843(2004).
Cited for: PHOSPHORYLATION AT THR-167, AUTOPHOSPHORYLATION, AND MUTAGENESIS OFTHR-167.
"Inhibition of spliceosome assembly by the cell cycle-regulatedprotein kinase MELK and involvement of splicing factor NIPP1.";
Vulsteke V., Beullens M., Boudrez A., Keppens S., Van Eynde A.,Rider M.H., Stalmans W., Bollen M.;
J. Biol. Chem. 279:8642-8647(2004).
Cited for: INTERACTION WITH PPP1R8, AUTOPHOSPHORYLATION, MUTAGENESIS OF ASP-150;THR-345; THR-387; THR-409; THR-415; THR-428; THR-446; THR-460;THR-466; THR-478 AND THR-518, PHOSPHORYLATION AT THR-478, ANDFUNCTION.

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