Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Histone H3.1  

UniProtKB / Swiss-Prot ID :  H31_HUMAN

Gene Name (Synonyms) : 
HIST1H3A, H3FA
HIST1H3B, H3FL
HIST1H3C, H3FC
HIST1H3D, H3FB
HIST1H3E, H3FD
HIST1H3F, H3FI
HIST1H3G, H3FH
HIST1H3H, H3FK
HIST1H3I, H3FF
HIST1H3J, H3FJ  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Chromosome. 

Protein Function :  Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. 

Protein Sequence MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQR...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEEECCHHHHHHHHHHHHCCCCCHHHCCCHHH...
Protein Variant -
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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
Predicted PTM Sites
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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
35-methylarginine--MARTKQT
--CCCCCCC
40.95MeMo
Link
35-methylarginine--MARTKQT
--CCCCCCC
40.95Phosphositeplus
Link
3Asymmetric dimethylarginine; by PRMT6.--MARTKQT
--CCCCCCC
40.95UniProtKB
Link
3N2,N2-dimethylarginine--MARTKQT
--CCCCCCC
40.95Phosphositeplus
Link
4Phosphothreonine-MARTKQTA
-CCCCCCCC
20.26Phosphositeplus
Link
4Phosphothreonine (VRK1)-MARTKQTA
-CCCCCCCC
20.26PhosphoELM
Link
4Phosphothreonine; by GSG2.-MARTKQTA
-CCCCCCCC
20.26UniProtKB
Link
5Allysine; alternate.MARTKQTAR
CCCCCCCCC
39.85UniProtKB
Link-
5N6,N6,N6-trimethyllysineMARTKQTAR
CCCCCCCCC
39.85Phosphositeplus
Link-
5N6,N6,N6-trimethyllysine; alternate.MARTKQTAR
CCCCCCCCC
39.85UniProtKB
Link-
5N6,N6-dimethyllysineMARTKQTAR
CCCCCCCCC
39.85Phosphositeplus
Link-
5N6,N6-dimethyllysine; alternate.MARTKQTAR
CCCCCCCCC
39.85UniProtKB
Link-
5N6-acetyllysineMARTKQTAR
CCCCCCCCC
39.85Phosphositeplus
Link-
5N6-acetyllysine; alternate.MARTKQTAR
CCCCCCCCC
39.85UniProtKB
Link-
5N6-methylated lysineMARTKQTAR
CCCCCCCCC
39.85HPRD
Link-
5N6-methyllysineMARTKQTAR
CCCCCCCCC
39.85MeMo
Link-
5N6-methyllysineMARTKQTAR
CCCCCCCCC
39.85Phosphositeplus
Link-
5N6-methyllysine; alternate.MARTKQTAR
CCCCCCCCC
39.85UniProtKB
Link-
7PhosphothreonineRTKQTARKS
CCCCCCCCC
29.95Phosphositeplus
Link-
7Phosphothreonine; by PKC.RTKQTARKS
CCCCCCCCC
29.95UniProtKB
Link-
9Citrulline; alternate.KQTARKSTG
CCCCCCCCC
36.52UniProtKB
Link-
9N2,N2-dimethylarginineKQTARKSTG
CCCCCCCCC
36.52Phosphositeplus
Link-
10N6,N6,N6-trimethyllysineQTARKSTGG
CCCCCCCCC
50.32Phosphositeplus
Link-
10N6,N6,N6-trimethyllysine; alternate.QTARKSTGG
CCCCCCCCC
50.32UniProtKB
Link-
10N6,N6-dimethyllysineQTARKSTGG
CCCCCCCCC
50.32Phosphositeplus
Link-
10N6,N6-dimethyllysine; alternate.QTARKSTGG
CCCCCCCCC
50.32UniProtKB
Link-
10N6-acetyllysineQTARKSTGG
CCCCCCCCC
50.32Phosphositeplus
Link-
10N6-acetyllysine; alternate.QTARKSTGG
CCCCCCCCC
50.32UniProtKB
Link-
10N6-methylated lysineQTARKSTGG
CCCCCCCCC
50.32HPRD
Link-
10N6-methyllysineQTARKSTGG
CCCCCCCCC
50.32MeMo
Link-
10N6-methyllysineQTARKSTGG
CCCCCCCCC
50.32Phosphositeplus
Link-
10N6-methyllysine; alternate.QTARKSTGG
CCCCCCCCC
50.32UniProtKB
Link-
11PhosphoserineTARKSTGGK
CCCCCCCCC
27.08Phosphositeplus
Link-
11Phosphoserine (Aurora A;Aurora B;Aurora B;VRK1)TARKSTGGK
CCCCCCCCC
27.08PhosphoELM
Link-
11Phosphoserine; by AURKB, AURKC, RPS6KA3,RPS6KA4 and RPS6KA5.TARKSTGGK
CCCCCCCCC
27.08UniProtKB
Link-
12PhosphothreonineARKSTGGKA
CCCCCCCCC
53.65Phosphositeplus
Link-
12Phosphothreonine (DAPK3)ARKSTGGKA
CCCCCCCCC
53.65PhosphoELM
Link-
12Phosphothreonine; by PKC and CHEK1.ARKSTGGKA
CCCCCCCCC
53.65UniProtKB
Link-
15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)STGGKAPRK
CCCCCCCCC
57.47Phosphositeplus
Link-
15N6,N6-dimethyllysineSTGGKAPRK
CCCCCCCCC
57.47Phosphositeplus
Link-
15N6-acetyllysineSTGGKAPRK
CCCCCCCCC
57.47Phosphositeplus
Link-
15N6-acetyllysine.STGGKAPRK
CCCCCCCCC
57.47UniProtKB
Link-
15N6-methyllysineSTGGKAPRK
CCCCCCCCC
57.47Phosphositeplus
Link-
185-methylarginineGKAPRKQLA
CCCCCCCCC
44.18MeMo
Link-
185-methylarginineGKAPRKQLA
CCCCCCCCC
44.18Phosphositeplus
Link-
18Asymmetric dimethylarginine; by CARM1;alternate.GKAPRKQLA
CCCCCCCCC
44.18UniProtKB
Link-
18Citrulline; alternate.GKAPRKQLA
CCCCCCCCC
44.18UniProtKB
Link-
18N2,N2-dimethylarginineGKAPRKQLA
CCCCCCCCC
44.18Phosphositeplus
Link-
19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KAPRKQLAT
CCCCCCCCC
48.91Phosphositeplus
Link-
19N6-acetyllysineKAPRKQLAT
CCCCCCCCC
48.91Phosphositeplus
Link-
19N6-acetyllysine; alternate.KAPRKQLAT
CCCCCCCCC
48.91UniProtKB
Link-
19N6-methyllysineKAPRKQLAT
CCCCCCCCC
48.91Phosphositeplus
Link-
19N6-methyllysine; alternate.KAPRKQLAT
CCCCCCCCC
48.91UniProtKB
Link-
24Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)QLATKAARK
CCCCCCCCC
34.15Phosphositeplus
Link-
24Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QLATKAARK
CCCCCCCCC
34.15Phosphositeplus
Link-
24N6-acetyllysineQLATKAARK
CCCCCCCCC
34.15Phosphositeplus
Link-
24N6-acetyllysine; alternate.QLATKAARK
CCCCCCCCC
34.15UniProtKB
Link-
24N6-methyllysineQLATKAARK
CCCCCCCCC
34.15Phosphositeplus
Link-
24N6-methyllysine; alternate.QLATKAARK
CCCCCCCCC
34.15UniProtKB
Link-
275-methylarginineTKAARKSAP
CCCCCCCCC
38.02MeMo
Link-
275-methylarginineTKAARKSAP
CCCCCCCCC
38.02Phosphositeplus
Link-
27N2,N2-dimethylarginineTKAARKSAP
CCCCCCCCC
38.02Phosphositeplus
Link-
28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KAARKSAPA
CCCCCCCCC
46.36Phosphositeplus
Link-
28N6,N6,N6-trimethyllysineKAARKSAPA
CCCCCCCCC
46.36Phosphositeplus
Link-
28N6,N6,N6-trimethyllysine; alternate.KAARKSAPA
CCCCCCCCC
46.36UniProtKB
Link-
28N6,N6-dimethyllysineKAARKSAPA
CCCCCCCCC
46.36Phosphositeplus
Link-
28N6,N6-dimethyllysine; alternate.KAARKSAPA
CCCCCCCCC
46.36UniProtKB
Link-
28N6-acetyllysineKAARKSAPA
CCCCCCCCC
46.36Phosphositeplus
Link-
28N6-acetyllysine; alternate.KAARKSAPA
CCCCCCCCC
46.36UniProtKB
Link-
28N6-methyllysineKAARKSAPA
CCCCCCCCC
46.36MeMo
Link-
28N6-methyllysineKAARKSAPA
CCCCCCCCC
46.36Phosphositeplus
Link-
28N6-methyllysine; alternate.KAARKSAPA
CCCCCCCCC
46.36UniProtKB
Link-
29PhosphoserineAARKSAPAT
CCCCCCCCC
33.65HPRD
Link-
29PhosphoserineAARKSAPAT
CCCCCCCCC
33.65Phosphositeplus
Link-
29Phosphoserine (MAPK_group;Aurora B)AARKSAPAT
CCCCCCCCC
33.65PhosphoELM
Link-
29Phosphoserine; by AURKB, AURKC andRPS6KA5.AARKSAPAT
CCCCCCCCC
33.65UniProtKB
Link-
37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TGGVKKPHR
CCCCCCCEE
64.95Phosphositeplus
Link-
37N6,N6,N6-trimethyllysineTGGVKKPHR
CCCCCCCEE
64.95Phosphositeplus
Link-
37N6,N6,N6-trimethyllysine; alternate.TGGVKKPHR
CCCCCCCEE
64.95UniProtKB
Link-
37N6,N6-dimethyllysineTGGVKKPHR
CCCCCCCEE
64.95Phosphositeplus
Link-
37N6,N6-dimethyllysine; alternate.TGGVKKPHR
CCCCCCCEE
64.95UniProtKB
Link-
37N6-acetyllysineTGGVKKPHR
CCCCCCCEE
64.95Phosphositeplus
Link-
37N6-acetyllysine; alternate.TGGVKKPHR
CCCCCCCEE
64.95UniProtKB
Link-
37N6-methyllysineTGGVKKPHR
CCCCCCCEE
64.95MeMo
Link-
37N6-methyllysineTGGVKKPHR
CCCCCCCEE
64.95Phosphositeplus
Link-
37N6-methyllysine; alternate.TGGVKKPHR
CCCCCCCEE
64.95UniProtKB
Link-
38N6-acetyllysineGGVKKPHRY
CCCCCCEEE
43.58Phosphositeplus
Link-
38N6-methyllysine.GGVKKPHRY
CCCCCCEEE
43.58UniProtKB
Link-
42PhosphotyrosineKPHRYRPGT
CCEEECCHH
20.37Phosphositeplus
Link-
42Phosphotyrosine.KPHRYRPGT
CCEEECCHH
20.37UniProtKB
Link-
46PhosphothreonineYRPGTVALR
ECCHHHHHH
12.80Phosphositeplus
Link-
55PhosphotyrosineEIRRYQKST
HHHHHHCCC
15.50Phosphositeplus
Link-
57Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RRYQKSTEL
HHHHCCCCC
50.87Phosphositeplus
Link-
57N6,N6,N6-trimethyllysineRRYQKSTEL
HHHHCCCCC
50.87Phosphositeplus
Link-
57N6,N6,N6-trimethyllysine; alternate.RRYQKSTEL
HHHHCCCCC
50.87UniProtKB
Link-
57N6-acetyllysineRRYQKSTEL
HHHHCCCCC
50.87Phosphositeplus
Link-
57N6-acetyllysine; alternate.RRYQKSTEL
HHHHCCCCC
50.87UniProtKB
Link-
57N6-methyllysineRRYQKSTEL
HHHHCCCCC
50.87Phosphositeplus
Link-
57N6-methyllysine; by EHMT2; alternate.RRYQKSTEL
HHHHCCCCC
50.87UniProtKB
Link-
58PhosphoserineRYQKSTELL
HHHCCCCCH
16.16Phosphositeplus
Link-
58Phosphoserine.RYQKSTELL
HHHCCCCCH
16.16UniProtKB
Link-
65N6-methyllysineLLIRKLPFQ
CHHHCCCHH
54.22Phosphositeplus
Link-
65N6-methyllysine.LLIRKLPFQ
CHHHCCCHH
54.22UniProtKB
Link-
80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AQDFKTDLR
HHHCCCCCC
49.79Phosphositeplus
Link-
80N6,N6,N6-trimethyllysineAQDFKTDLR
HHHCCCCCC
49.79Phosphositeplus
Link-
80N6,N6-dimethyllysineAQDFKTDLR
HHHCCCCCC
49.79Phosphositeplus
Link-
80N6,N6-dimethyllysine; alternate.AQDFKTDLR
HHHCCCCCC
49.79UniProtKB
Link-
80N6-acetyllysineAQDFKTDLR
HHHCCCCCC
49.79Phosphositeplus
Link-
80N6-acetyllysine; alternate.AQDFKTDLR
HHHCCCCCC
49.79UniProtKB
Link-
80N6-methyllysineAQDFKTDLR
HHHCCCCCC
49.79MeMo
Link-
80N6-methyllysineAQDFKTDLR
HHHCCCCCC
49.79Phosphositeplus
Link-
80N6-methyllysine; alternate.AQDFKTDLR
HHHCCCCCC
49.79UniProtKB
Link-
81Phosphothreonine.QDFKTDLRF
HHCCCCCCC
40.01UniProtKB
Link-
100PhosphotyrosineACEAYLVGL
HHHHHHHHH
4.61Phosphositeplus
Link-
116N6-acetyllysineAIHAKRVTI
HHHCCCEEE
32.99Phosphositeplus
Link-
123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TIMPKDIQL
EEEECHHHH
50.51Phosphositeplus
Link-
123N6,N6-dimethyllysineTIMPKDIQL
EEEECHHHH
50.51Phosphositeplus
Link-
123N6-acetyllysineTIMPKDIQL
EEEECHHHH
50.51Phosphositeplus
Link-
123N6-methyllysineTIMPKDIQL
EEEECHHHH
50.51MeMo
Link-
123N6-methyllysineTIMPKDIQL
EEEECHHHH
50.51Phosphositeplus
Link-
123N6-methyllysine.TIMPKDIQL
EEEECHHHH
50.51UniProtKB
Link-
1295-methylarginineIQLARRIRG
HHHHHHHCC
43.05MeMo
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ANM5_HUMANmethylation reactionMINT-56507MINT15670829
JHD3A_HUMANdirect interactionMINT-2829722MINT16415788
JHD3A_HUMANdirect interactionMINT-2830454MINT16415788
JHD3A_HUMANdirect interactionMINT-2830478MINT16415788
JHD3A_HUMANdirect interactionMINT-2830611MINT16415788
JHD3A_HUMANdirect interactionMINT-2829063MINT16415788
JHD3A_HUMANdirect interactionMINT-2829698MINT16415788
CBX5_HUMANdirect interactionMINT-2830941MINT16415788
WDR5_HUMANdirect interactionMINT-3293375MINT16946699
WDR5_HUMANdirect interactionMINT-3319516MINT16946699
WDR5_HUMANdirect interactionMINT-3319546MINT16946699
WDR5_HUMANdirect interactionMINT-3293337MINT16946699
WDR5_HUMANdirect interactionMINT-3319259MINT16946699
WDR5_HUMANdirect interactionMINT-3319477MINT16946699
WDR5_HUMANdirect interactionMINT-3293300MINT16946699
GRB2_HUMANphysical interactionMINT-61561MINT12577067
TP53B_HUMANdirect interactionMINT-2829755MINT16415788
TP53B_HUMANdirect interactionMINT-2830088MINT16415788
TP53B_HUMANdirect interactionMINT-2830502MINT16415788
TP53B_HUMANdirect interactionMINT-2831063MINT16415788
TP53B_HUMANdirect interactionMINT-2829648MINT16415788
CBX3_HUMANdirect interactionMINT-2830686MINT16415788
CBX3_HUMANdirect interactionMINT-2831013MINT16415788
PHF20_HUMANdirect interactionMINT-2829329MINT16415788
PHF20_HUMANdirect interactionMINT-2830536MINT16415788
Q9Y381_HUMANdirect interactionMINT-2830238MINT16415788
SETD7_HUMANmethylation
direct interaction
EBI-1270528
EBI-1268600
intact12540855
16415881
CAF1B_HUMANphysical interactionEBI-1165514
intact17081972
CAF1A_HUMANphysical interactionEBI-1165514
intact17081972
EGFR_HUMANcolocalizationEBI-298046
intact12577067
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Modifications of human histone H3 variants during mitosis.";
Garcia B.A., Barber C.M., Hake S.B., Ptak C., Turner F.B., Busby S.A.,Shabanowitz J., Moran R.G., Allis C.D., Hunt D.F.;
Biochemistry 44:13202-13213(2005).
Cited for: PROTEIN SEQUENCE OF 2-20, METHYLATION AT LYS-10; LYS-28 AND LYS-37,PHOSPHORYLATION AT THR-4; SER-11 AND SER-29, ACETYLATION AT LYS-10 ANDLYS-15, AND MASS SPECTROMETRY.
"Expression patterns and post-translational modifications associatedwith mammalian histone H3 variants.";
Hake S.B., Garcia B.A., Duncan E.M., Kauer M., Dellaire G.,Shabanowitz J., Bazett-Jones D.P., Allis C.D., Hunt D.F.;
J. Biol. Chem. 281:559-568(2006).
Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19 AND LYS-24, METHYLATION ATLYS-5; LYS-10; LYS-19; LYS-28; LYS-37; LYS-65; LYS-80 AND LYS-123, ANDMASS SPECTROMETRY.
"Mass spectrometric characterization of human histone H3: a bird's eyeview.";
Thomas C.E., Kelleher N.L., Mizzen C.A.;
J. Proteome Res. 5:240-247(2006).
Cited for: METHYLATION AT LYS-5 AND LYS-10, ACETYLATION AT LYS-10; LYS-15 ANDLYS-24, PHOSPHORYLATION AT SER-11 AND SER-29, AND MASS SPECTROMETRY.
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-15; LYS-19; LYS-24;LYS-28 AND LYS-37, AND MASS SPECTROMETRY.
"Quantitative proteomic analysis of post-translational modificationsof human histones.";
Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M.,Finn P., Grauslund M., Hansen A.M., Jensen O.N.;
Mol. Cell. Proteomics 5:1314-1325(2006).
Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, METHYLATIONAT LYS-28; LYS-37 AND LYS-80, AND MASS SPECTROMETRY.
"Coactivator-associated arginine methyltransferase-1 enhances nuclearfactor-kappaB-mediated gene transcription through methylation ofhistone H3 at arginine 17.";
Miao F., Li S., Chavez V., Lanting L., Natarajan R.;
Mol. Endocrinol. 20:1562-1573(2006).
Cited for: ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT ARG-18, ANDCITRULLINATION AT ARG-18.
"Organismal differences in post-translational modifications inhistones H3 and H4.";
Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.;
J. Biol. Chem. 282:7641-7655(2007).
Cited for: ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37;LYS-57 AND LYS-80, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24;LYS-28; LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123, AND MASSSPECTROMETRY.
"Identification of histone H3 lysine 36 acetylation as a highlyconserved histone modification.";
Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L.,Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
J. Biol. Chem. 282:7632-7640(2007).
Cited for: ACETYLATION AT LYS-37.
Methylation
ReferencePubMed
"Modifications of human histone H3 variants during mitosis.";
Garcia B.A., Barber C.M., Hake S.B., Ptak C., Turner F.B., Busby S.A.,Shabanowitz J., Moran R.G., Allis C.D., Hunt D.F.;
Biochemistry 44:13202-13213(2005).
Cited for: PROTEIN SEQUENCE OF 2-20, METHYLATION AT LYS-10; LYS-28 AND LYS-37,PHOSPHORYLATION AT THR-4; SER-11 AND SER-29, ACETYLATION AT LYS-10 ANDLYS-15, AND MASS SPECTROMETRY.
"Methylation of histone H3 lysine 9 creates a binding site for HP1proteins.";
Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.;
Nature 410:116-120(2001).
Cited for: METHYLATION AT LYS-10.
"Ligand-dependent activation of the farnesoid X-receptor directsarginine methylation of histone H3 by CARM1.";
Ananthanarayanan M., Li S., Balasubramaniyan N., Suchy F.J.,Walsh M.J.;
J. Biol. Chem. 279:54348-54357(2004).
Cited for: METHYLATION AT ARG-18.
"Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strandbreaks.";
Huyen Y., Zgheib O., Ditullio R.A. Jr., Gorgoulis V.G., Zacharatos P.,Petty T.J., Sheston E.A., Mellert H.S., Stavridi E.S.,Halazonetis T.D.;
Nature 432:406-411(2004).
Cited for: METHYLATION AT LYS-80.
"Human PAD4 regulates histone arginine methylation levels viademethylimination.";
Wang Y., Wysocka J., Sayegh J., Lee Y.-H., Perlin J.R., Leonelli L.,Sonbuchner L.S., McDonald C.H., Cook R.G., Dou Y., Roeder R.G.,Clarke S., Stallcup M.R., Allis C.D., Coonrod S.A.;
Science 306:279-283(2004).
Cited for: CITRULLINATION AT ARG-9 AND ARG-18, AND METHYLATION AT ARG-18.
"Protein identification using sequential ion/ion reactions and tandemmass spectrometry.";
Coon J.J., Ueberheide B., Syka J.E.P., Dryhurst D.D., Ausio J.,Shabanowitz J., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 102:9463-9468(2005).
Cited for: METHYLATION AT LYS-37 AND LYS-38, AND MASS SPECTROMETRY.
"Expression patterns and post-translational modifications associatedwith mammalian histone H3 variants.";
Hake S.B., Garcia B.A., Duncan E.M., Kauer M., Dellaire G.,Shabanowitz J., Bazett-Jones D.P., Allis C.D., Hunt D.F.;
J. Biol. Chem. 281:559-568(2006).
Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19 AND LYS-24, METHYLATION ATLYS-5; LYS-10; LYS-19; LYS-28; LYS-37; LYS-65; LYS-80 AND LYS-123, ANDMASS SPECTROMETRY.
"Mass spectrometric characterization of human histone H3: a bird's eyeview.";
Thomas C.E., Kelleher N.L., Mizzen C.A.;
J. Proteome Res. 5:240-247(2006).
Cited for: METHYLATION AT LYS-5 AND LYS-10, ACETYLATION AT LYS-10; LYS-15 ANDLYS-24, PHOSPHORYLATION AT SER-11 AND SER-29, AND MASS SPECTROMETRY.
"Quantitative proteomic analysis of post-translational modificationsof human histones.";
Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M.,Finn P., Grauslund M., Hansen A.M., Jensen O.N.;
Mol. Cell. Proteomics 5:1314-1325(2006).
Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, METHYLATIONAT LYS-28; LYS-37 AND LYS-80, AND MASS SPECTROMETRY.
"Coactivator-associated arginine methyltransferase-1 enhances nuclearfactor-kappaB-mediated gene transcription through methylation ofhistone H3 at arginine 17.";
Miao F., Li S., Chavez V., Lanting L., Natarajan R.;
Mol. Endocrinol. 20:1562-1573(2006).
Cited for: ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT ARG-18, ANDCITRULLINATION AT ARG-18.
"PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4trimethylation.";
Hyllus D., Stein C., Schnabel K., Schiltz E., Imhof A., Dou Y.,Hsieh J., Bauer U.M.;
Genes Dev. 21:3369-3380(2007).
Cited for: METHYLATION AT ARG-3 BY PRMT6.
"Organismal differences in post-translational modifications inhistones H3 and H4.";
Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.;
J. Biol. Chem. 282:7641-7655(2007).
Cited for: ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37;LYS-57 AND LYS-80, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24;LYS-28; LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123, AND MASSSPECTROMETRY.
"Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex aremutually exclusive.";
Guccione E., Bassi C., Casadio F., Martinato F., Cesaroni M.,Schuchlautz H., Luescher B., Amati B.;
Nature 449:933-937(2007).
Cited for: METHYLATION AT ARG-3 BY PRMT6.
"Arginine methylation of the histone H3 tail impedes effectorbinding.";
Iberg A.N., Espejo A., Cheng D., Kim D., Michaud-Levesque J.,Richard S., Bedford M.T.;
J. Biol. Chem. 283:3006-3010(2008).
Cited for: METHYLATION AT ARG-3 BY PRMT6.
"Histone H3 lysine 56 methylation regulates DNA replication throughits interaction wwith PCNA.";
Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A.,Carey M.F., Grunstein M.;
Mol. Cell 46:7-17(2012).
Cited for: METHYLATION AT LYS-57.
Phosphorylation
ReferencePubMed
"Modifications of human histone H3 variants during mitosis.";
Garcia B.A., Barber C.M., Hake S.B., Ptak C., Turner F.B., Busby S.A.,Shabanowitz J., Moran R.G., Allis C.D., Hunt D.F.;
Biochemistry 44:13202-13213(2005).
Cited for: PROTEIN SEQUENCE OF 2-20, METHYLATION AT LYS-10; LYS-28 AND LYS-37,PHOSPHORYLATION AT THR-4; SER-11 AND SER-29, ACETYLATION AT LYS-10 ANDLYS-15, AND MASS SPECTROMETRY.
"Identification of a novel phosphorylation site on histone H3 coupledwith mitotic chromosome condensation.";
Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M.,Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.;
J. Biol. Chem. 274:25543-25549(1999).
Cited for: PROTEIN SEQUENCE OF 58-64; 117-120 AND 124-135, AND PHOSPHORYLATION ATSER-11 AND SER-29.
"Aurora-B phosphorylates Histone H3 at serine28 with regard to themitotic chromosome condensation.";
Goto H., Yasui Y., Nigg E.A., Inagaki M.;
Genes Cells 7:11-17(2002).
Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
"Novel mitosis-specific phosphorylation of histone H3 at Thr11mediated by Dlk/ZIP kinase.";
Preuss U., Landsberg G., Scheidtmann K.H.;
Nucleic Acids Res. 31:878-885(2003).
Cited for: PHOSPHORYLATION AT SER-11 AND THR-12.
"The kinase haspin is required for mitotic histone H3 Thr 3phosphorylation and normal metaphase chromosome alignment.";
Dai J., Sultan S., Taylor S.S., Higgins J.M.G.;
Genes Dev. 19:472-488(2005).
Cited for: PHOSPHORYLATION AT THR-4; SER-11 AND SER-29.
"Phosphorylation of Ser28 in histone H3 mediated by mixed lineagekinase-like mitogen-activated protein triple kinase alpha.";
Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.;
J. Biol. Chem. 280:13545-13553(2005).
Cited for: PHOSPHORYLATION AT SER-29.
"Mass spectrometric characterization of human histone H3: a bird's eyeview.";
Thomas C.E., Kelleher N.L., Mizzen C.A.;
J. Proteome Res. 5:240-247(2006).
Cited for: METHYLATION AT LYS-5 AND LYS-10, ACETYLATION AT LYS-10; LYS-15 ANDLYS-24, PHOSPHORYLATION AT SER-11 AND SER-29, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASSSPECTROMETRY.
"Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-induced transcriptional repression.";
Shimada M., Niida H., Zineldeen D.H., Tagami H., Tanaka M., Saito H.,Nakanishi M.;
Cell 132:221-232(2008).
Cited for: PHOSPHORYLATION AT THR-12 BY CHEK1.
"Phosphorylation of histone H3 at threonine 11 establishes a novelchromatin mark for transcriptional regulation.";
Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K.,Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H.,Buettner R., Schule R.;
Nat. Cell Biol. 10:53-60(2008).
Cited for: PHOSPHORYLATION AT THR-12.
"JAK2 phosphorylates histone H3Y41 and excludes HP1alpha fromchromatin.";
Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T.,Green A.R., Kouzarides T.;
Nature 461:819-822(2009).
Cited for: PHOSPHORYLATION AT TYR-42.
"Quantitative interaction proteomics and genome-wide profiling ofepigenetic histone marks and their readers.";
Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S.,Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G.,Mann M.;
Cell 142:967-980(2010).
Cited for: PHOSPHORYLATION AT SER-58 AND THR-81.
"Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylationat histone H3K4.";
Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N.,Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N.,Beisenherz-Huss C., Gunther T., Buettner R., Schule R.;
Nature 464:792-796(2010).
Cited for: PHOSPHORYLATION AT THR-7.
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