H31_MOUSE - dbPTM
H31_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H31_MOUSE
UniProt AC P68433
Protein Name Histone H3.1
Gene Name Hist1h3a
Organism Mus musculus (Mouse).
Sequence Length 136
Subcellular Localization Nucleus. Chromosome.
Protein Description 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 MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
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
3Asymmetric dimethylarginine-----MARTKQTARK
-----CCCCCHHHHH
40.95-
3Citrullination-----MARTKQTARK
-----CCCCCHHHHH
40.9515339660
3Methylation-----MARTKQTARK
-----CCCCCHHHHH
40.95-
3Phosphorylation-----MARTKQTARK
-----CCCCCHHHHH
40.95-
4Phosphorylation----MARTKQTARKS
----CCCCCHHHHHC
20.2614987995
5Allysine---MARTKQTARKST
---CCCCCHHHHHCC
39.85-
5Acetylation---MARTKQTARKST
---CCCCCHHHHHCC
39.8517194708
5Crotonylation---MARTKQTARKST
---CCCCCHHHHHCC
39.8521925322
5Deamination---MARTKQTARKST
---CCCCCHHHHHCC
39.85-
5Methylation---MARTKQTARKST
---CCCCCHHHHHCC
39.8517194708
5Other---MARTKQTARKST
---CCCCCHHHHHCC
39.8527105115
6Formation of an isopeptide bond--MARTKQTARKSTG
--CCCCCHHHHHCCC
39.52-
6Serotonylation--MARTKQTARKSTG
--CCCCCHHHHHCCC
39.5230867594
7Phosphorylation-MARTKQTARKSTGG
-CCCCCHHHHHCCCC
29.95-
9CitrullinationARTKQTARKSTGGKA
CCCCHHHHHCCCCCC
36.52-
9CitrullinationARTKQTARKSTGGKA
CCCCHHHHHCCCCCC
36.5215339660
9MethylationARTKQTARKSTGGKA
CCCCHHHHHCCCCCC
36.5215485929
10"N6,N6,N6-trimethyllysine"RTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.32-
10AcetylationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.3217194708
10CrotonylationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.3221925322
10LactoylationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.32-
10MethylationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.3217194708
10OtherRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.3227105115
11ADP-ribosylationTKQTARKSTGGKAPR
CCHHHHHCCCCCCCH
27.08-
11PhosphorylationTKQTARKSTGGKAPR
CCHHHHHCCCCCCCH
27.0818936171
12PhosphorylationKQTARKSTGGKAPRK
CHHHHHCCCCCCCHH
53.6518243098
15AcetylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.4712498683
15GlutarylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.47-
15LactoylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.4731645732
15MethylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.47-
15OtherARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.4727105115
15SuccinylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.47-
18Asymmetric dimethylarginineSTGGKAPRKQLATKA
CCCCCCCHHHHHHHH
44.18-
18CitrullinationSTGGKAPRKQLATKA
CCCCCCCHHHHHHHH
44.1815339660
18MethylationSTGGKAPRKQLATKA
CCCCCCCHHHHHHHH
44.1811751582
19N6-crotonyl-L-lysineTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
19AcetylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.9112498683
19ButyrylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.9127105113
19CrotonylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.9121925322
19GlutarylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
19HydroxylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.9124681537
19LactoylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.9131645732
19MalonylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.9126320211
19MethylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.9117194708
19OtherTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.9127105115
19UbiquitinationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.9127667366
24N6-crotonyl-L-lysinePRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.15-
24AcetylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.1512498683
24ButyrylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.1527105113
24CrotonylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.1521925322
24GlutarylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.15-
24HydroxylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.1524681537
24LactoylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.1531645732
24MalonylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.1526320211
24MethylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.1517194708
24OtherPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.1527105115
24SuccinylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.1523806337
24UbiquitinationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.1527667366
27CitrullinationQLATKAARKSAPATG
HHHHHHHHHHCCCCC
38.02-
27CitrullinationQLATKAARKSAPATG
HHHHHHHHHHCCCCC
38.0215339660
27MethylationQLATKAARKSAPATG
HHHHHHHHHHCCCCC
38.02-
28"N6,N6,N6-trimethyllysine"LATKAARKSAPATGG
HHHHHHHHHCCCCCC
46.36-
28AcetylationLATKAARKSAPATGG
HHHHHHHHHCCCCCC
46.3617194708
28ButyrylationLATKAARKSAPATGG
HHHHHHHHHCCCCCC
46.3627105113
28CrotonylationLATKAARKSAPATGG
HHHHHHHHHCCCCCC
46.3621925322
28GlutarylationLATKAARKSAPATGG
HHHHHHHHHCCCCCC
46.36-
28HydroxylationLATKAARKSAPATGG
HHHHHHHHHCCCCCC
46.3624681537
28LactoylationLATKAARKSAPATGG
HHHHHHHHHCCCCCC
46.3631645732
28MethylationLATKAARKSAPATGG
HHHHHHHHHCCCCCC
46.3617194708
28OtherLATKAARKSAPATGG
HHHHHHHHHCCCCCC
46.3624681537
28SuccinylationLATKAARKSAPATGG
HHHHHHHHHCCCCCC
46.3623806337
29ADP-ribosylationATKAARKSAPATGGV
HHHHHHHHCCCCCCC
33.65-
29PhosphorylationATKAARKSAPATGGV
HHHHHHHHCCCCCCC
33.6520129940
37"N6,N6,N6-trimethyllysine"APATGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.95-
37AcetylationAPATGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.9517189264
37ButyrylationAPATGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.9527105113
37HydroxylationAPATGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.9524681537
37MethylationAPATGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.9517194708
37OtherAPATGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.9524681537
38AcetylationPATGGVKKPHRYRPG
CCCCCCCCCCCCCCC
43.5822826441
38ButyrylationPATGGVKKPHRYRPG
CCCCCCCCCCCCCCC
43.5827105113
38MethylationPATGGVKKPHRYRPG
CCCCCCCCCCCCCCC
43.58-
41DimethylationGGVKKPHRYRPGTVA
CCCCCCCCCCCCCHH
37.37-
42PhosphorylationGVKKPHRYRPGTVAL
CCCCCCCCCCCCHHH
20.3728066266
46PhosphorylationPHRYRPGTVALREIR
CCCCCCCCHHHHHHH
12.8014729942
55PhosphorylationALREIRRYQKSTELL
HHHHHHHHHHCHHHH
15.5025159016
57"N6,N6,N6-trimethyllysine"REIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57AcetylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57CrotonylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.8721925322
57GlutarylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57LactoylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.8731645732
57MalonylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.8726320211
57MethylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57OtherREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.8727105115
57SuccinylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.8722389435
57UbiquitinationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.8727667366
58PhosphorylationEIRRYQKSTELLIRK
HHHHHHHCHHHHHHH
16.1626824392
59PhosphorylationIRRYQKSTELLIRKL
HHHHHHCHHHHHHHC
37.3725521595
65AcetylationSTELLIRKLPFQRLV
CHHHHHHHCCHHHHH
54.22-
65MethylationSTELLIRKLPFQRLV
CHHHHHHHCCHHHHH
54.22-
65OtherSTELLIRKLPFQRLV
CHHHHHHHCCHHHHH
54.2224681537
80"N6,N6,N6-trimethyllysine"REIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.79-
80AcetylationREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.79-
80ButyrylationREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.7927105113
80GlutarylationREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.79-
80LactoylationREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.79-
80MalonylationREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.7926320211
80MethylationREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.7917194708
80OtherREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.7924681537
80SuccinylationREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.7922389435
80UbiquitinationREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.7927667366
81PhosphorylationEIAQDFKTDLRFQSS
HHHHHHCCCHHHHHH
40.0125521595
87PhosphorylationKTDLRFQSSAVMALQ
CCCHHHHHHHHHHHH
19.97-
100PhosphorylationLQEACEAYLVGLFED
HHHHHHHHHHHHHCC
4.6126239621
108PhosphorylationLVGLFEDTNLCAIHA
HHHHHCCCCEEEEEE
23.9326239621
116AcetylationNLCAIHAKRVTIMPK
CEEEEEEEECEECHH
32.99-
116GlutarylationNLCAIHAKRVTIMPK
CEEEEEEEECEECHH
32.99-
119PhosphorylationAIHAKRVTIMPKDIQ
EEEEEECEECHHHHH
18.6529109428
121SulfoxidationHAKRVTIMPKDIQLA
EEEECEECHHHHHHH
2.1721406390
123AcetylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
123ButyrylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.5127105113
123GlutarylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
123MalonylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.5126320211
123MethylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.5113678296
123OtherKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.5124681537
123SuccinylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
123UbiquitinationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.5127667366
129MethylationPKDIQLARRIRGERA
HHHHHHHHHHHCCCC
43.05-
129PhosphorylationPKDIQLARRIRGERA
HHHHHHHHHHHCCCC
43.05-
130MethylationKDIQLARRIRGERA-
HHHHHHHHHHCCCC-
19.83-
130PhosphorylationKDIQLARRIRGERA-
HHHHHHHHHHCCCC-
19.83-
132PhosphorylationIQLARRIRGERA---
HHHHHHHHCCCC---
38.82-

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
4TPhosphorylationKinaseGSG2Q9Z0R0
GPS
7TPhosphorylationKinasePKC-Uniprot
10SPhosphorylationKinaseAURBQ96GD4
PSP
10SPhosphorylationKinaseAURBO70126
PSP
10SPhosphorylationKinaseMSK1Q8C050
PSP
10SPhosphorylationKinaseERK2P63085
PSP
10SPhosphorylationKinaseAURCO88445
PSP
10SPhosphorylationKinaseMST2Q13188
PSP
10SPhosphorylationKinaseMSK1O75582
PSP
10SPhosphorylationKinaseCHK1O14757
PSP
10SPhosphorylationKinaseMSK2O75676
PSP
10SPhosphorylationKinaseP38AQ16539
PSP
10SPhosphorylationKinaseRSK2P18654
PSP
11SPhosphorylationKinaseRPS6KA5Q8C050
GPS
11SPhosphorylationKinaseRPS6KA4Q9Z2B9
GPS
11SPhosphorylationKinaseRPS6KA3P18654
GPS
11SPhosphorylationKinaseCHEK1O14757
GPS
11TPhosphorylationKinaseCHK1O14757
PSP
11SPhosphorylationKinaseAURKCO88445
GPS
11SPhosphorylationKinaseAURKBO70126
GPS
11SPhosphorylationKinaseALTERNATE-Uniprot
12TPhosphorylationKinasePKC-Uniprot
12TPhosphorylationKinaseCHEK1O35280
Uniprot
28SPhosphorylationKinaseMSK1Q8C050
PSP
28SPhosphorylationKinaseMSK1O75582
PSP
28SPhosphorylationKinaseMST2Q13188
PSP
28SPhosphorylationKinaseAURBO70126
PSP
28SPhosphorylationKinaseAURBQ96GD4
PSP
29SPhosphorylationKinaseRPS6KA5Q8C050
GPS
29SPhosphorylationKinaseAURKCO88445
GPS
29SPhosphorylationKinaseAURKBO70126
GPS
29SPhosphorylationKinaseALTERNATE-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
3RMethylation

15339660
4TPhosphorylation

15681610
5KAcetylation

11747826
5KMethylation

11747826
5Kubiquitylation

11747826
5KMethylation

11747826
5KMethylation

11747826
5KMethylation

11747826
5KMethylation

11747826
5KMethylation

11747826
5KPhosphorylation

11747826
7TPhosphorylation

13678296
7TMethylation

13678296
9RMethylation

15339660
9RMethylation

15339660
9RMethylation

15339660
9RCitrullination

15339660
9RAcetylation

15339660
10KPhosphorylation

13678296
10KPhosphorylation

13678296
10KPhosphorylation

13678296
10KPhosphorylation

13678296
10KMethylation

13678296
10KMethylation

13678296
10KMethylation

13678296
10KMethylation

13678296
10KAcetylation

13678296
10KAcetylation

13678296
10KAcetylation

13678296
10KAcetylation

13678296
10KAcetylation

13678296
10KPhosphorylation

13678296
10KMethylation

13678296
10KMethylation

13678296
11SMethylation

10464286
11SMethylation

10464286
11SAcetylation

10464286
11SAcetylation

10464286
11SAcetylation

10464286
11SPhosphorylation

10464286
11SPhosphorylation

10464286
11SPhosphorylation

10464286
11SPhosphorylation

10464286
11SPhosphorylation

10464286
11SPhosphorylation

10464286
11SPhosphorylation

10464286
12TPhosphorylation

18243098
12TAcetylation

18243098
12TMethylation

18243098
12TPhosphorylation

18243098
12TPhosphorylation

18243098
18RCitrullination

11747826
18RAcetylation

11747826
18RMethylation

11747826
18RMethylation

11747826
18RMethylation

11747826
19KMethylation

12498683
19KAcetylation

12498683
24KMethylation

12498683
24KAcetylation

12498683
28KMethylation

13678296
28KMethylation

13678296
29SPhosphorylation

10464286
37KMethylation

13678296
57KMethylation

21925322
80Kubiquitylation

13678296
80KMethylation

13678296
80KMethylation

13678296
80KMethylation

13678296
80KSuccinylation

13678296
120Kubiquitylation

13678296
120KMethylation

13678296
123KSuccinylation

13678296
123KAcetylation

13678296

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 H31_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of H31_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of H31_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
"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 AND LYS-28,METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 ANDLYS-80, AND MASS SPECTROMETRY.
"Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 andnegatively regulates expression of ST7 and NM23 tumor suppressorgenes.";
Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.;
Mol. Cell. Biol. 24:9630-9645(2004).
Cited for: METHYLATION AT ARG-9, AND ACETYLATION AT LYS-10.
"Identification of methylation and acetylation sites on mouse histoneH3 using matrix-assisted laser desorption/ionization time-of-flightand nanoelectrospray ionization tandem mass spectrometry.";
Cocklin R.R., Wang M.;
J. Protein Chem. 22:327-334(2003).
Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-10;LYS-28; LYS-37; LYS-80 AND LYS-123, AND MASS SPECTROMETRY.
"Crosstalk between CARM1 methylation and CBP acetylation on histoneH3.";
Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.;
Curr. Biol. 12:2090-2097(2002).
Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, AND METHYLATION AT ARG-18.
Methylation
ReferencePubMed
"Arginine methyltransferase CARM1 is a promoter-specific regulator ofNF-kappaB-dependent gene expression.";
Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C.,Imhof R., Bedford M.T., Natoli G., Hottiger M.O.;
EMBO J. 24:85-96(2005).
Cited for: METHYLATION AT ARG-18.
"Methylation at arginine 17 of histone H3 is linked to geneactivation.";
Bauer U.-M., Daujat S., Nielsen S.J., Nightingale K., Kouzarides T.;
EMBO Rep. 3:39-44(2002).
Cited for: METHYLATION AT ARG-18.
"Crosstalk between CARM1 methylation and CBP acetylation on histoneH3.";
Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.;
Curr. Biol. 12:2090-2097(2002).
Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, AND METHYLATION AT ARG-18.
"Hormone-dependent, CARM1-directed, arginine-specific methylation ofhistone H3 on a steroid-regulated promoter.";
Ma H., Baumann C.T., Li H., Strahl B.D., Rice R., Jelinek M.A.,Aswad D.W., Allis C.D., Hager G.L., Stallcup M.R.;
Curr. Biol. 11:1981-1985(2001).
Cited for: METHYLATION AT LYS-5 AND 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 AND LYS-28,METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 ANDLYS-80, AND MASS SPECTROMETRY.
"Identification of methylation and acetylation sites on mouse histoneH3 using matrix-assisted laser desorption/ionization time-of-flightand nanoelectrospray ionization tandem mass spectrometry.";
Cocklin R.R., Wang M.;
J. Protein Chem. 22:327-334(2003).
Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-10;LYS-28; LYS-37; LYS-80 AND LYS-123, AND MASS SPECTROMETRY.
"Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 andnegatively regulates expression of ST7 and NM23 tumor suppressorgenes.";
Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.;
Mol. Cell. Biol. 24:9630-9645(2004).
Cited for: METHYLATION AT ARG-9, AND ACETYLATION AT LYS-10.
Phosphorylation
ReferencePubMed
"Stimulation of the Ras-MAPK pathway leads to independentphosphorylation of histone H3 on serine 10 and 28.";
Dunn K.L., Davie J.R.;
Oncogene 24:3492-3502(2005).
Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
"MAP kinase-mediated phosphorylation of distinct pools of histone H3at S10 or S28 via mitogen- and stress-activated kinase 1/2.";
Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J.,Nightingale K., Iborra F.J., Mahadevan L.C.;
J. Cell Sci. 118:2247-2259(2005).
Cited for: PHOSPHORYLATION AT 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.
"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 AND SER-11.
"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.
"Ultraviolet B-induced phosphorylation of histone H3 at serine 28 ismediated by MSK1.";
Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M.,Ma W.-Y., Dong Z.;
J. Biol. Chem. 276:33213-33219(2001).
Cited for: PHOSPHORYLATION AT SER-29.
"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: PHOSPHORYLATION AT SER-11 AND SER-29.

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