MAML1_HUMAN - dbPTM
MAML1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAML1_HUMAN
UniProt AC Q92585
Protein Name Mastermind-like protein 1
Gene Name MAML1 {ECO:0000312|HGNC:HGNC:13632}
Organism Homo sapiens (Human).
Sequence Length 1016
Subcellular Localization Nucleus speckle . Nuclear, in a punctate manner.
Protein Description Acts as a transcriptional coactivator for NOTCH proteins. Has been shown to amplify NOTCH-induced transcription of HES1. Enhances phosphorylation and proteolytic turnover of the NOTCH intracellular domain in the nucleus through interaction with CDK8. Binds to CREBBP/CBP which promotes nucleosome acetylation at NOTCH enhancers and activates transcription. Induces phosphorylation and localization of CREBBP to nuclear foci. Plays a role in hematopoietic development by regulating NOTCH-mediated lymphoid cell fate decisions..
Protein Sequence MVLPTCPMAEFALPRHSAVMERLRRRIELCRRHHSTCEARYEAVSPERLELERQHTFALHQRCIQAKAKRAGKHRQPPAATAPAPAAPAPRLDAADGPEHGRPATHLHDTVKRNLDSATSPQNGDQQNGYGDLFPGHKKTRREAPLGVAISSNGLPPASPLGQSDKPSGADALQSSGKHSLGLDSLNKKRLADSSLHLNGGSNPSESFPLSLNKELKQEPVEDLPCMITGTVGSISQSNLMPDLNLNEQEWKELIEELNRSVPDEDMKDLFNEDFEEKKDPESSGSATQTPLAQDINIKTEFSPAAFEQEQLGSPQVRAGSAGQTFLGPSSAPVSTDSPSLGGSQTLFHTSGQPRADNPSPNLMPASAQAQNAQRALAGVVLPSQGPGGASELSSAHQLQQIAAKQKREQMLQNPQQATPAPAPGQMSTWQQTGPSHSSLDVPYPMEKPASPSSYKQDFTNSKLLMMPSVNKSSPRPGGPYLQPSHVNLLSHQPPSNLNQNSANNQGSVLDYGNTKPLSHYKADCGQGSPGSGQSKPALMAYLPQQLSHISHEQNSLFLMKPKPGNMPFRSLVPPGQEQNPSSVPVQAQATSVGTQPPAVSVASSHNSSPYLSSQQQAAVMKQHQLLLDQQKQREQQQKHLQQQQFLQRQQHLLAEQEKQQFQRHLTRPPPQYQDPTQGSFPQQVGQFTGSSAAVPGMNTLGPSNSSCPRVFPQAGNLMPMGPGHASVSSLPTNSGQQDRGVAQFPGSQNMPQSSLYGMASGITQIVAQPPPQATNGHAHIPRQTNVGQNTSVSAAYGQNSLGSSGLSQQHNKGTLNPGLTKPPVPRVSPAMGGQNSSWQHQGMPNLSGQTPGNSNVSPFTAASSFHMQQQAHLKMSSPQFSQAVPNRPMAPMSSAAAVGSLLPPVSAQQRTSAPAPAPPPTAPQQGLPGLSPAGPELGAFSQSPASQMGGRAGLHCTQAYPVRTAGQELPFAYSGQPGGSGLSSVAGHTDLIDSLLKNRTSEEWMSDLDDLLGSQ
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
35PhosphorylationELCRRHHSTCEARYE
HHHHHCCCHHHHHHH		28.73-
41PhosphorylationHSTCEARYEAVSPER
CCHHHHHHHCCCHHH		18.4523403867
45PhosphorylationEARYEAVSPERLELE
HHHHHCCCHHHHHHH		28.2619664994
67SumoylationHQRCIQAKAKRAGKH
HHHHHHHHHHHCCCC		37.76-
75MethylationAKRAGKHRQPPAATA
HHHCCCCCCCCCCCC		54.94115482511
112AcetylationTHLHDTVKRNLDSAT
CCHHHHHHHHCCCCC		37.3525953088
117PhosphorylationTVKRNLDSATSPQNG
HHHHHCCCCCCCCCC		36.2930624053
119PhosphorylationKRNLDSATSPQNGDQ
HHHCCCCCCCCCCCC		44.9123927012
120PhosphorylationRNLDSATSPQNGDQQ
HHCCCCCCCCCCCCC		24.9723401153
130PhosphorylationNGDQQNGYGDLFPGH
CCCCCCCCCCCCCCC		18.2728634120
138AcetylationGDLFPGHKKTRREAP
CCCCCCCCCCCCCCC		62.8517300219
139AcetylationDLFPGHKKTRREAPL
CCCCCCCCCCCCCCC		41.4017300219
140PhosphorylationLFPGHKKTRREAPLG
CCCCCCCCCCCCCCC		39.50-
151PhosphorylationAPLGVAISSNGLPPA
CCCCEEECCCCCCCC		14.1729255136
152PhosphorylationPLGVAISSNGLPPAS
CCCEEECCCCCCCCC		28.8929255136
159PhosphorylationSNGLPPASPLGQSDK
CCCCCCCCCCCCCCC		26.8229255136
164PhosphorylationPASPLGQSDKPSGAD
CCCCCCCCCCCCHHH		45.8929255136
166AcetylationSPLGQSDKPSGADAL
CCCCCCCCCCHHHHH		46.4626051181
168PhosphorylationLGQSDKPSGADALQS
CCCCCCCCHHHHHHH		52.9729255136
175PhosphorylationSGADALQSSGKHSLG
CHHHHHHHCCCCCCC		41.7429255136
176PhosphorylationGADALQSSGKHSLGL
HHHHHHHCCCCCCCC		38.6129255136
178AcetylationDALQSSGKHSLGLDS
HHHHHCCCCCCCCCC		31.7826051181
185PhosphorylationKHSLGLDSLNKKRLA
CCCCCCCCCCCHHHC		38.5921712546
188UbiquitinationLGLDSLNKKRLADSS
CCCCCCCCHHHCCCC		44.5619608861
188AcetylationLGLDSLNKKRLADSS
CCCCCCCCHHHCCCC		44.5617300219
189AcetylationGLDSLNKKRLADSSL
CCCCCCCHHHCCCCC		52.1217300219
214AcetylationSFPLSLNKELKQEPV
CCCCCCCHHHHCCCC		70.4926051181
217SumoylationLSLNKELKQEPVEDL
CCCCHHHHCCCCCCC		54.42-
217SumoylationLSLNKELKQEPVEDL
CCCCHHHHCCCCCCC		54.42-
261PhosphorylationLIEELNRSVPDEDMK
HHHHHHHCCCCHHHH		36.6122199227
268UbiquitinationSVPDEDMKDLFNEDF
CCCCHHHHHHHCCCH		64.7029967540
278AcetylationFNEDFEEKKDPESSG
HCCCHHHHCCCCCCC		56.1017300219
279AcetylationNEDFEEKKDPESSGS
CCCHHHHCCCCCCCC		80.1117300219
283PhosphorylationEEKKDPESSGSATQT
HHHCCCCCCCCCCCC		45.4425159151
284PhosphorylationEKKDPESSGSATQTP
HHCCCCCCCCCCCCC		34.8025159151
286PhosphorylationKDPESSGSATQTPLA
CCCCCCCCCCCCCHH		30.0525159151
288PhosphorylationPESSGSATQTPLAQD
CCCCCCCCCCCHHHC		34.3725159151
290PhosphorylationSSGSATQTPLAQDIN
CCCCCCCCCHHHCCC		18.8625159151
299SumoylationLAQDINIKTEFSPAA
HHHCCCCCCCCCHHH		37.20-
299SumoylationLAQDINIKTEFSPAA
HHHCCCCCCCCCHHH		37.20-
300PhosphorylationAQDINIKTEFSPAAF
HHCCCCCCCCCHHHH		38.1729255136
303PhosphorylationINIKTEFSPAAFEQE
CCCCCCCCHHHHHHH		13.8529255136
314PhosphorylationFEQEQLGSPQVRAGS
HHHHHHCCCCCCCCC		22.2825159151
321PhosphorylationSPQVRAGSAGQTFLG
CCCCCCCCCCCCCCC		28.3923401153
325PhosphorylationRAGSAGQTFLGPSSA
CCCCCCCCCCCCCCC		21.6526074081
330PhosphorylationGQTFLGPSSAPVSTD
CCCCCCCCCCCCCCC		37.0228450419
331PhosphorylationQTFLGPSSAPVSTDS
CCCCCCCCCCCCCCC		39.4628450419
335PhosphorylationGPSSAPVSTDSPSLG
CCCCCCCCCCCCCCC		25.9928450419
336PhosphorylationPSSAPVSTDSPSLGG
CCCCCCCCCCCCCCC		40.5028450419
338PhosphorylationSAPVSTDSPSLGGSQ
CCCCCCCCCCCCCCC		19.2428450419
340PhosphorylationPVSTDSPSLGGSQTL
CCCCCCCCCCCCCEE		43.5328450419
344PhosphorylationDSPSLGGSQTLFHTS
CCCCCCCCCEEEECC		20.4228450419
346PhosphorylationPSLGGSQTLFHTSGQ
CCCCCCCEEEECCCC		32.8428450419
350PhosphorylationGSQTLFHTSGQPRAD
CCCEEEECCCCCCCC		27.5028450419
351PhosphorylationSQTLFHTSGQPRADN
CCEEEECCCCCCCCC		27.1928450419
360PhosphorylationQPRADNPSPNLMPAS
CCCCCCCCCCCCCHH		32.4529255136
367PhosphorylationSPNLMPASAQAQNAQ
CCCCCCHHHHHHHHH		18.2923403867
405AcetylationQLQQIAAKQKREQML
HHHHHHHHHHHHHHH		47.5319608861
407AcetylationQQIAAKQKREQMLQN
HHHHHHHHHHHHHHC		58.1425953088
419PhosphorylationLQNPQQATPAPAPGQ
HHCHHHCCCCCCCCC		18.6923401153
428PhosphorylationAPAPGQMSTWQQTGP
CCCCCCCCCCCCCCC		20.7123401153
429PhosphorylationPAPGQMSTWQQTGPS
CCCCCCCCCCCCCCC		23.1923401153
433PhosphorylationQMSTWQQTGPSHSSL
CCCCCCCCCCCCCCC		35.6423401153
444PhosphorylationHSSLDVPYPMEKPAS
CCCCCCCCCCCCCCC		18.3026074081
451PhosphorylationYPMEKPASPSSYKQD
CCCCCCCCCCHHCCC		33.5725849741
453PhosphorylationMEKPASPSSYKQDFT
CCCCCCCCHHCCCCC		43.7526074081
454PhosphorylationEKPASPSSYKQDFTN
CCCCCCCHHCCCCCC		39.4726074081
455PhosphorylationKPASPSSYKQDFTNS
CCCCCCHHCCCCCCC		19.6026074081
463AcetylationKQDFTNSKLLMMPSV
CCCCCCCCEEECCCC		47.9425953088
472AcetylationLMMPSVNKSSPRPGG
EECCCCCCCCCCCCC		50.5925953088
516AcetylationVLDYGNTKPLSHYKA
CCCCCCCCCCCCCCC		48.2226051181
529PhosphorylationKADCGQGSPGSGQSK
CCCCCCCCCCCCCCH		20.4225849741
536AcetylationSPGSGQSKPALMAYL
CCCCCCCHHHHHHHC		26.8226051181
632UbiquitinationQLLLDQQKQREQQQK
HHHHHHHHHHHHHHH		45.7729967540
794O-linked_GlycosylationVGQNTSVSAAYGQNS
CCCCCCCHHHCCCCC		13.6230059200
813AcetylationGLSQQHNKGTLNPGL
CCCCCCCCCCCCCCC		51.6626051181
822AcetylationTLNPGLTKPPVPRVS
CCCCCCCCCCCCCCC		52.9819608861
827MethylationLTKPPVPRVSPAMGG
CCCCCCCCCCCCCCC		41.60115482503
965O-linked_GlycosylationTQAYPVRTAGQELPF
CEEEECCCCCCCCCE		35.0630059200
995PhosphorylationGHTDLIDSLLKNRTS
CCHHHHHHHHCCCCC		28.7124719451
1001PhosphorylationDSLLKNRTSEEWMSD
HHHHCCCCCHHHHHH		50.3026552605
1002PhosphorylationSLLKNRTSEEWMSDL
HHHCCCCCHHHHHHH		30.2226552605
1007PhosphorylationRTSEEWMSDLDDLLG
CCCHHHHHHHHHHHC		35.7726552605
1015PhosphorylationDLDDLLGSQ------
HHHHHHCCC------		32.4626552605
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 MAML1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MAML1_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 MAML1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EP300_HUMANEP300physical
12391150
EP300_HUMANEP300physical
12050117
CBP_HUMANCREBBPphysical
12050117
NOTC1_HUMANNOTCH1physical
11101851
NOTC2_HUMANNOTCH2physical
11101851
NOTC4_HUMANNOTCH4physical
11101851
NOTC3_HUMANNOTCH3physical
11101851
HDAC9_HUMANHDAC9physical
20203086
NOTC1_HUMANNOTCH1physical
22100894
SUH_HUMANRBPJphysical
23022380
NOTC1_HUMANNOTCH1physical
23022380
PHF8_HUMANPHF8physical
23022380
SMCA4_HUMANSMARCA4physical
23022380
PB1_HUMANPBRM1physical
23022380
EP300_HUMANEP300physical
15546612
CDK8_HUMANCDK8physical
15546612
RND3_HUMANRND3physical
26108681
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 MAML1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-822, AND MASS SPECTROMETRY.
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-314 AND SER-360, ANDMASS SPECTROMETRY.

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