dbPTM

H2B3B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2B3B_HUMAN
UniProt AC	Q8N257
Protein Name	Histone H2B type 3-B
Gene Name	HIST3H2BB
Organism	Homo sapiens (Human).
Sequence Length	126
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	MPDPSKSAPAPKKGSKKAVTKAQKKDGKKRKRGRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREVQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MPDPSKSAP ------CCCCCCCCC	63.32	-
5	Phosphorylation	---MPDPSKSAPAPK ---CCCCCCCCCCCC	46.77	20873877
6	N6-crotonyl-L-lysine	--MPDPSKSAPAPKK --CCCCCCCCCCCCC	56.90	-
6	Acetylation	--MPDPSKSAPAPKK --CCCCCCCCCCCCC	56.90	16283522
6	Butyrylation	--MPDPSKSAPAPKK --CCCCCCCCCCCCC	56.90	27105113
6	Crotonylation	--MPDPSKSAPAPKK --CCCCCCCCCCCCC	56.90	21925322
6	Lactoylation	--MPDPSKSAPAPKK --CCCCCCCCCCCCC	56.90	31645732
6	Lactylation	--MPDPSKSAPAPKK --CCCCCCCCCCCCC	56.90	31645732
6	Other	--MPDPSKSAPAPKK --CCCCCCCCCCCCC	56.90	27105115
6	Sumoylation	--MPDPSKSAPAPKK --CCCCCCCCCCCCC	56.90	16283522
6	Ubiquitination	--MPDPSKSAPAPKK --CCCCCCCCCCCCC	56.90	33845483
7	Phosphorylation	-MPDPSKSAPAPKKG -CCCCCCCCCCCCCC	43.77	20873877
12	N6-crotonyl-L-lysine	SKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	-
12	Acetylation	SKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	32155916
12	Crotonylation	SKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	21925322
12	Lactoylation	SKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	31645732
12	Lactylation	SKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	31645732
12	Other	SKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	27105115
13	N6-crotonyl-L-lysine	KSAPAPKKGSKKAVT CCCCCCCCCCHHHHH	68.32	-
13	Acetylation	KSAPAPKKGSKKAVT CCCCCCCCCCHHHHH	68.32	16283522
13	Crotonylation	KSAPAPKKGSKKAVT CCCCCCCCCCHHHHH	68.32	21925322
13	Other	KSAPAPKKGSKKAVT CCCCCCCCCCHHHHH	68.32	24681537
15	Phosphorylation	APAPKKGSKKAVTKA CCCCCCCCHHHHHHH	39.60	1137958
16	N6-crotonyl-L-lysine	PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH	54.11	-
16	Acetylation	PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH	54.11	16283522
16	Crotonylation	PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH	54.11	21925322
16	Lactoylation	PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH	54.11	31645732
17	N6-crotonyl-L-lysine	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	-
17	Acetylation	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	16627869
17	Crotonylation	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	21925322
17	Glutarylation	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	31542297
17	Lactoylation	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	31645732
17	Other	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	27105115
17	Ubiquitination	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	25015289
21	N6-crotonyl-L-lysine	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	-
21	Acetylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	16283522
21	Butyrylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	27105113
21	Crotonylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	21925322
21	Lactoylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	31645732
21	Other	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	27105115
21	Sumoylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	16283522
21	Ubiquitination	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	25015289
24	N6-crotonyl-L-lysine	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	-
24	Acetylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	24431477
24	Crotonylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	21925322
24	Lactoylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	31645732
24	Other	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	24681537
24	Ubiquitination	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	25015289
25	Acetylation	AVTKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	24848081
25	Other	AVTKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	24681537
35	N6-crotonyl-L-lysine	KKRKRGRKESYSIYV CCCCCCCCHHHHHHH	54.56	-
35	Crotonylation	KKRKRGRKESYSIYV CCCCCCCCHHHHHHH	54.56	21925322
35	Glutarylation	KKRKRGRKESYSIYV CCCCCCCCHHHHHHH	54.56	31542297
35	Other	KKRKRGRKESYSIYV CCCCCCCCHHHHHHH	54.56	27105115
35	Succinylation	KKRKRGRKESYSIYV CCCCCCCCHHHHHHH	54.56	22389435
35	Ubiquitination	KKRKRGRKESYSIYV CCCCCCCCHHHHHHH	54.56	21890473
37	Phosphorylation	RKRGRKESYSIYVYK CCCCCCHHHHHHHHH	27.50	21712546
38	Phosphorylation	KRGRKESYSIYVYKV CCCCCHHHHHHHHHH	10.52	28152594
39	Phosphorylation	RGRKESYSIYVYKVL CCCCHHHHHHHHHHH	19.40	21712546
41	Phosphorylation	RKESYSIYVYKVLKQ CCHHHHHHHHHHHHH	7.56	28152594
43	Phosphorylation	ESYSIYVYKVLKQVH HHHHHHHHHHHHHHC	4.38	28152594
44	Acetylation	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	-
44	Glutarylation	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	31542297
44	Lactoylation	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	31645732
44	Other	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	24681537
44	Ubiquitination	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	23000965
47	Acetylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	37092721
47	Glutarylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	31542297
47	Methylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	16627869
47	Other	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	24681537
47	Sumoylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	16627869
47	Ubiquitination	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	21906983
53	Phosphorylation	LKQVHPDTGISSKAM HHHHCCCCCCCHHHH	40.65	30266825
56	Phosphorylation	VHPDTGISSKAMGIM HCCCCCCCHHHHHHH	27.42	23401153
57	Phosphorylation	HPDTGISSKAMGIMN CCCCCCCHHHHHHHH	23.63	30266825
58	"N6,N6-dimethyllysine"	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	-
58	Acetylation	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	24431487
58	Methylation	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	16627869
58	Other	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	24681537
58	Ubiquitination	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	21906983
60	Sulfoxidation	TGISSKAMGIMNSFV CCCCHHHHHHHHHHH	4.26	28183972
63	Sulfoxidation	SSKAMGIMNSFVNDI CHHHHHHHHHHHHHH	2.59	28183972
65	Phosphorylation	KAMGIMNSFVNDIFE HHHHHHHHHHHHHHH	17.12	22617229
73	Methylation	FVNDIFERIASEASR HHHHHHHHHHHHHHH	21.01	-
76	Phosphorylation	DIFERIASEASRLAH HHHHHHHHHHHHHHH	31.18	22817900
79	Phosphorylation	ERIASEASRLAHYNK HHHHHHHHHHHHHCC	24.63	22817900
80	Methylation	RIASEASRLAHYNKR HHHHHHHHHHHHCCC	42.83	-
84	Phosphorylation	EASRLAHYNKRSTIT HHHHHHHHCCCCCCC	19.44	25884760
86	"N6,N6,N6-trimethyllysine"	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	-
86	Acetylation	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	30589229
86	Lactoylation	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	31645732
86	Methylation	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	-
86	Other	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	27105115
86	Ubiquitination	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	27667366
87	Methylation	RLAHYNKRSTITSRE HHHHHCCCCCCCHHH	35.08	-
88	Phosphorylation	LAHYNKRSTITSREV HHHHCCCCCCCHHHH	26.27	30266825
89	Phosphorylation	AHYNKRSTITSREVQ HHHCCCCCCCHHHHH	32.10	30266825
91	Phosphorylation	YNKRSTITSREVQTA HCCCCCCCHHHHHHH	23.09	30266825
92	Phosphorylation	NKRSTITSREVQTAV CCCCCCCHHHHHHHH	23.69	20860994
93	Methylation	KRSTITSREVQTAVR CCCCCCHHHHHHHHH	39.18	-
100	Methylation	REVQTAVRLLLPGEL HHHHHHHHHHCCHHH	19.70	115387663
109	Ubiquitination	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	21890473
109	Sumoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	-
109	Acetylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	30589247
109	Glutarylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	31542297
109	Lactoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	31645732
109	Methylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	16627869
109	Neddylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	32015554
109	Other	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	24681537
109	Sumoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	16627869
109	Ubiquitination	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	23000965
113	O-linked_Glycosylation	ELAKHAVSEGTKAVT HHHHHHHHHHHHHHH	30.96	UniProtKB CARBOHYD
113	Phosphorylation	ELAKHAVSEGTKAVT HHHHHHHHHHHHHHH	30.96	28176443
116	Phosphorylation	KHAVSEGTKAVTKYT HHHHHHHHHHHHHHC	16.27	20068231
117	Sumoylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	-
117	Acetylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	22389435
117	Glutarylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	31542297
117	Lactoylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	31645732
117	Malonylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	22389435
117	Methylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	-
117	Neddylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	32015554
117	Other	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	27105115
117	Succinylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	22389435
117	Sumoylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	22389435
117	Ubiquitination	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	23000965
120	Phosphorylation	SEGTKAVTKYTSSK- HHHHHHHHHHCCCC-	24.16	20068231
121	Ubiquitination	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	21890473
121	Sumoylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	-
121	Acetylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	30589235
121	Glutarylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	31542297
121	Lactoylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	31645732
121	Neddylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	32015554
121	Other	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	27105115
121	Succinylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	22389435
121	Sumoylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	22389435
121	Ubiquitination	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	22389435
122	Phosphorylation	GTKAVTKYTSSK--- HHHHHHHHCCCC---	11.50	-
123	Phosphorylation	TKAVTKYTSSK---- HHHHHHHCCCC----	28.25	24719451
124	Phosphorylation	KAVTKYTSSK----- HHHHHHCCCC-----	32.80	27251275
126	Acetylation	VTKYTSSK------- HHHHCCCC-------	65.21	30589253
126	Neddylation	VTKYTSSK------- HHHHCCCC-------	65.21	32015554
126	Ubiquitination	VTKYTSSK------- HHHHCCCC-------	65.21	23000965

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
15	S	Phosphorylation	Kinase	MST1	P26927	Uniprot
15	S	Phosphorylation	Kinase	STK4	Q13043	GPS
37	S	Phosphorylation	Kinase	AMPK	Q9Y478	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
4	K	Methylation	16627869
Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci.
4	K	Methylation	16627869
Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.
4	K	ubiquitylation	16627869
Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci.
4	K	ubiquitylation	16627869
Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.
15	S	Phosphorylation	12757711
Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation.
15	S	Phosphorylation	12757711
Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination.
35	K	Methylation	21925322
Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci.
35	K	ubiquitylation	21925322
Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci.
37	S	Phosphorylation	12757711
Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity).
79	K	Methylation	16627869
Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci.
79	K	Methylation	16627869
Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.
79	K	ubiquitylation	16627869
Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci.
79	K	ubiquitylation	16627869
Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.
113	S	ubiquitylation	-
GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121.
121	K	ubiquitylation	16627869
Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.
121	K	ubiquitylation	16627869
GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121.
121	K	Methylation	16627869
Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.

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 H2B3B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC1_HUMAN	HDAC1	physical	21846774
CDN2A_HUMAN	CDKN2A	physical	21846774
ARF_HUMAN	CDKN2A	physical	21846774
RL5_HUMAN	RPL5	physical	21846774
HUWE1_HUMAN	HUWE1	physical	21846774

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 H2B3B_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-86 AND LYS-121, AND MASSSPECTROMETRY.	19608861 [Abstract]
"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-12; LYS-13; LYS-16; LYS-17;LYS-21; LYS-24 AND LYS-109, AND MASS SPECTROMETRY.	16916647 [Abstract]
"Inhibition of core histones acetylation by carcinogenic nickel(II)."; Golebiowski F., Kasprzak K.S.; Mol. Cell. Biochem. 279:133-139(2005). Cited for: ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21.	16283522 [Abstract]
"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: PROTEIN SEQUENCE OF 7-24, ACETYLATION AT LYS-6; LYS-12; LYS-13;LYS-16; LYS-17 AND LYS-21, METHYLATION AT LYS-47; LYS-58 AND LYS-109,UBIQUITINATION AT LYS-121, AND MASS SPECTROMETRY.	16627869 [Abstract]
Methylation
Reference	PubMed
"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: PROTEIN SEQUENCE OF 7-24, ACETYLATION AT LYS-6; LYS-12; LYS-13;LYS-16; LYS-17 AND LYS-21, METHYLATION AT LYS-47; LYS-58 AND LYS-109,UBIQUITINATION AT LYS-121, AND MASS SPECTROMETRY.	16627869 [Abstract]
Phosphorylation
Reference	PubMed
"Apoptotic phosphorylation of histone H2B is mediated by mammaliansterile twenty kinase."; Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A.,Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.; Cell 113:507-517(2003). Cited for: PHOSPHORYLATION AT SER-15.	12757711 [Abstract]
Ubiquitylation
Reference	PubMed
"Histone H2B monoubiquitination functions cooperatively with FACT toregulate elongation by RNA polymerase II."; Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A.,Reinberg D.; Cell 125:703-717(2006). Cited for: UBIQUITINATION AT LYS-121.	16713563 [Abstract]
"Monoubiquitination of human histone H2B: the factors involved andtheir roles in HOX gene regulation."; Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H.,Tempst P., Reinberg D.; Mol. Cell 20:601-611(2005). Cited for: UBIQUITINATION AT LYS-121.	16307923 [Abstract]
"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: PROTEIN SEQUENCE OF 7-24, ACETYLATION AT LYS-6; LYS-12; LYS-13;LYS-16; LYS-17 AND LYS-21, METHYLATION AT LYS-47; LYS-58 AND LYS-109,UBIQUITINATION AT LYS-121, AND MASS SPECTROMETRY.	16627869 [Abstract]

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