Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Histone-lysine N-methyltransferase MLL4  

UniProtKB / Swiss-Prot ID :  MLL4_HUMAN

Gene Name (Synonyms) : 
WBP7, HRX2, KIAA0304, KMT2D, MLL2, MLL4, TRX2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (By similarity). 

Protein Function :  Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. 

Protein Sequence MAAAAGGGSCPGPGSARGRFPGRPRGAGGGGGRGGRGNGAERVRVALRRGGGATGPGGAEPGEDTALLRL...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
172T -> I (in dbSNP:rs60207923). VAR_061913
587P -> R (in dbSNP:rs2242519). VAR_046563
754P -> L (in dbSNP:rs179686). VAR_046564
1097P -> L (in dbSNP:rs34014681). VAR_046565
1829P -> L (in dbSNP:rs16970649). VAR_052653
2364D -> G (in dbSNP:rs231591). VAR_052654
2408K -> N (in dbSNP:rs36062432). VAR_052655
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAAAG
---
19.67UniProtKB
Link-
158PhosphothreonineRKHKTTPLP
33.11HPRD
Link-
159PhosphothreonineKHKTTPLPP
27.86HPRD
Link-
159PhosphothreonineKHKTTPLPP
27.86PhosphoELM
Link-
159PhosphothreonineKHKTTPLPP
27.86Phosphositeplus
Link-
159PhosphothreonineKHKTTPLPP
27.86SysPTM
Link-
159Phosphothreonine.KHKTTPLPP
27.86UniProtKB
Link-
172PhosphothreonineDVAPTPPKT
42.35HPRD
Link-
172PhosphothreonineDVAPTPPKT
42.35PhosphoELM
Link-
172PhosphothreonineDVAPTPPKT
42.35Phosphositeplus
Link-
172PhosphothreonineDVAPTPPKT
42.35SysPTM
Link-
172Phosphothreonine.DVAPTPPKT
42.35UniProtKB
Link-
176PhosphothreonineTPPKTPARK
28.14HPRD
Link-
176PhosphothreonineTPPKTPARK
28.14PhosphoELM
Link-
176PhosphothreonineTPPKTPARK
28.14Phosphositeplus
Link-
176PhosphothreonineTPPKTPARK
28.14SysPTM
Link-
176Phosphothreonine.TPPKTPARK
28.14UniProtKB
Link-
351PhosphoserineGQGGSPCWK
24.57HPRD
Link-
351PhosphoserineGQGGSPCWK
24.57Phosphositeplus
Link-
351Phosphoserine.GQGGSPCWK
24.57UniProtKB
Link-
797Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FSLLKRAKV
56.45Phosphositeplus
Link-
821PhosphoserineSMPLSPGGQ
18.67HPRD
Link-
821PhosphoserineSMPLSPGGQ
18.67PhosphoELM
Link-
821PhosphoserineSMPLSPGGQ
18.67Phosphositeplus
Link-
821PhosphoserineSMPLSPGGQ
18.67SysPTM
Link-
821Phosphoserine.SMPLSPGGQ
18.67UniProtKB
Link-
844PhosphoserineGPVRSEDES
50.03HPRD
Link-
844PhosphoserineGPVRSEDES
50.03PhosphoELM
Link-
844PhosphoserineGPVRSEDES
50.03Phosphositeplus
Link-
844PhosphoserineGPVRSEDES
50.03SysPTM
Link-
844Phosphoserine.GPVRSEDES
50.03UniProtKB
Link-
848PhosphoserineSEDESVEAK
37.26HPRD
Link-
848PhosphoserineSEDESVEAK
37.26SysPTM
Link-
857PhosphoserineRERPSGPES
73.52HPRD
Link-
861PhosphoserineSGPESPVQG
33.24HPRD
Link-
861PhosphoserineSGPESPVQG
33.24PhosphoELM
Link-
861PhosphoserineSGPESPVQG
33.24Phosphositeplus
Link-
861PhosphoserineSGPESPVQG
33.24SysPTM
Link-
861Phosphoserine.SGPESPVQG
33.24UniProtKB
Link-
926N6-acetyllysineSRRGKVEAA
34.78HPRD
Link-
926N6-acetyllysineSRRGKVEAA
34.78Phosphositeplus
Link-
926N6-acetyllysine.SRRGKVEAA
34.78UniProtKB
Link-
1032PhosphoserineLPWDSDESP
39.13HPRD
Link-
1032PhosphoserineLPWDSDESP
39.13PhosphoELM
Link-
1032PhosphoserineLPWDSDESP
39.13Phosphositeplus
Link-
1032PhosphoserineLPWDSDESP
39.13SysPTM
Link-
1032Phosphoserine.LPWDSDESP
39.13UniProtKB
Link-
1035PhosphoserineDSDESPEAS
32.79HPRD
Link-
1035PhosphoserineDSDESPEAS
32.79PhosphoELM
Link-
1035PhosphoserineDSDESPEAS
32.79Phosphositeplus
Link-
1035PhosphoserineDSDESPEAS
32.79SysPTM
Link-
1035Phosphoserine.DSDESPEAS
32.79UniProtKB
Link-
1039PhosphoserineSPEASPGPP
28.82HPRD
Link-
1092PhosphoserineIFEDSDDSE
35.80HPRD
Link-
1092PhosphoserineIFEDSDDSE
35.80Phosphositeplus
Link-
1095PhosphoserineDSDDSEPGG
51.16HPRD
Link-
1095PhosphoserineDSDDSEPGG
51.16Phosphositeplus
Link-
1164PhosphoserineGKQKSPDGV
26.23HPRD
Link-
1164PhosphoserineGKQKSPDGV
26.23PhosphoELM
Link-
1164PhosphoserineGKQKSPDGV
26.23Phosphositeplus
Link-
1164PhosphoserineGKQKSPDGV
26.23SysPTM
Link-
1164Phosphoserine.GKQKSPDGV
26.23UniProtKB
Link-
1930PhosphoserineSRWASPPLK
21.79HPRD
Link-
1930PhosphoserineSRWASPPLK
21.79PhosphoELM
Link-
1930PhosphoserineSRWASPPLK
21.79Phosphositeplus
Link-
1930PhosphoserineSRWASPPLK
21.79SysPTM
Link-
1930Phosphoserine.SRWASPPLK
21.79UniProtKB
Link-
1935PhosphothreoninePPLKTSPQL
54.01HPRD
Link-
1935PhosphothreoninePPLKTSPQL
54.01PhosphoELM
Link-
1935PhosphothreoninePPLKTSPQL
54.01SysPTM
Link-
1935Phosphothreonine.PPLKTSPQL
54.01UniProtKB
Link-
1936PhosphoserinePLKTSPQLR
14.73HPRD
Link-
1936PhosphoserinePLKTSPQLR
14.73PhosphoELM
Link-
1936PhosphoserinePLKTSPQLR
14.73Phosphositeplus
Link-
2068PhosphothreonineVDDGTDSEA
43.26Phosphositeplus
Link-
2070PhosphoserineDGTDSEAEA
38.25HPRD
Link-
2070PhosphoserineDGTDSEAEA
38.25Phosphositeplus
Link-
2083PhosphothreonineRGQGTPPSG
24.92HPRD
Link-
2083PhosphothreonineRGQGTPPSG
24.92Phosphositeplus
Link-
2083Phosphothreonine.RGQGTPPSG
24.92UniProtKB
Link-
2196Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ILVNKLGQV
46.65Phosphositeplus
Link-
2270PhosphoserineSGPASPPRQ
38.27HPRD
Link-
2296N6-acetyllysinePPPYKAPRL
58.66HPRD
Link-
2296N6-acetyllysinePPPYKAPRL
58.66Phosphositeplus
Link-
2296N6-acetyllysine.PPPYKAPRL
58.66UniProtKB
Link-
2604PhosphotyrosineMVIEYSGIV
10.89Phosphositeplus
Link-
2605PhosphoserineVIEYSGIVI
14.84Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-351; SER-821 AND THR-2083, AND MASSSPECTROMETRY.
"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-926 AND LYS-2296, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-172; THR-176; SER-821;SER-844; SER-1032; SER-1035; SER-1930 AND THR-1935, AND MASSSPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-351; SER-821 AND THR-2083, AND MASSSPECTROMETRY.
"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-821 AND THR-2083, 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 THR-159, 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-861 AND SER-1164, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures