dbPTM

H2B1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2B1B_HUMAN
UniProt AC	P33778
Protein Name	Histone H2B type 1-B
Gene Name	HIST1H2BB
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	MPEPSKSAPAPKKGSKKAITKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MPEPSKSAP ------CCCCCCCCC	63.31	-
5	Acetylation	---MPEPSKSAPAPK ---CCCCCCCCCCCC	37.27	29148549
5	Phosphorylation	---MPEPSKSAPAPK ---CCCCCCCCCCCC	37.27	24719451
6	N6-crotonyl-L-lysine	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	-
6	Acetylation	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	19608861
6	Butyrylation	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	27105113
6	Crotonylation	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	21925322
6	Hydroxylation	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	24681537
6	Lactoylation	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	31645732
6	Other	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	27105115
6	Ubiquitination	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	32015554
12	N6-crotonyl-L-lysine	SKSAPAPKKGSKKAI CCCCCCCCCCCHHHH	72.39	-
12	Acetylation	SKSAPAPKKGSKKAI CCCCCCCCCCCHHHH	72.39	21466224
12	Crotonylation	SKSAPAPKKGSKKAI CCCCCCCCCCCHHHH	72.39	21925322
12	Lactoylation	SKSAPAPKKGSKKAI CCCCCCCCCCCHHHH	72.39	31645732
12	Other	SKSAPAPKKGSKKAI CCCCCCCCCCCHHHH	72.39	27105115
13	N6-crotonyl-L-lysine	KSAPAPKKGSKKAIT CCCCCCCCCCHHHHH	68.32	-
13	Acetylation	KSAPAPKKGSKKAIT CCCCCCCCCCHHHHH	68.32	19608861
13	Crotonylation	KSAPAPKKGSKKAIT CCCCCCCCCCHHHHH	68.32	21925322
13	Other	KSAPAPKKGSKKAIT CCCCCCCCCCHHHHH	68.32	24681537
15	Phosphorylation	APAPKKGSKKAITKA CCCCCCCCHHHHHHH	39.60	16462032
16	N6-crotonyl-L-lysine	PAPKKGSKKAITKAQ CCCCCCCHHHHHHHH	55.69	-
16	Acetylation	PAPKKGSKKAITKAQ CCCCCCCHHHHHHHH	55.69	19608861
16	Crotonylation	PAPKKGSKKAITKAQ CCCCCCCHHHHHHHH	55.69	21925322
16	Lactoylation	PAPKKGSKKAITKAQ CCCCCCCHHHHHHHH	55.69	31645732
16	Methylation	PAPKKGSKKAITKAQ CCCCCCCHHHHHHHH	55.69	19608861
17	N6-crotonyl-L-lysine	APKKGSKKAITKAQK CCCCCCHHHHHHHHH	46.87	-
17	Acetylation	APKKGSKKAITKAQK CCCCCCHHHHHHHHH	46.87	19608861
17	Crotonylation	APKKGSKKAITKAQK CCCCCCHHHHHHHHH	46.87	21925322
17	Glutarylation	APKKGSKKAITKAQK CCCCCCHHHHHHHHH	46.87	31542297
17	Lactoylation	APKKGSKKAITKAQK CCCCCCHHHHHHHHH	46.87	31645732
17	Other	APKKGSKKAITKAQK CCCCCCHHHHHHHHH	46.87	27105115
20	Phosphorylation	KGSKKAITKAQKKDG CCCHHHHHHHHHHCC	25.78	-
21	N6-crotonyl-L-lysine	GSKKAITKAQKKDGK CCHHHHHHHHHHCCC	42.58	-
21	Acetylation	GSKKAITKAQKKDGK CCHHHHHHHHHHCCC	42.58	19608861
21	Butyrylation	GSKKAITKAQKKDGK CCHHHHHHHHHHCCC	42.58	27105113
21	Crotonylation	GSKKAITKAQKKDGK CCHHHHHHHHHHCCC	42.58	21925322
21	Lactoylation	GSKKAITKAQKKDGK CCHHHHHHHHHHCCC	42.58	31645732
21	Other	GSKKAITKAQKKDGK CCHHHHHHHHHHCCC	42.58	27105115
21	Ubiquitination	GSKKAITKAQKKDGK CCHHHHHHHHHHCCC	42.58	33845483
24	N6-crotonyl-L-lysine	KAITKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	-
24	Acetylation	KAITKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	19608861
24	Crotonylation	KAITKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	21925322
24	Lactoylation	KAITKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	31645732
24	Methylation	KAITKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	19608861
24	Other	KAITKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	24681537
25	Acetylation	AITKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	-
25	Other	AITKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	24681537
28	Acetylation	KAQKKDGKKRKRSRK HHHHHCCCCCCCCHH	60.58	106701403
29	Acetylation	AQKKDGKKRKRSRKE HHHHCCCCCCCCHHH	69.54	-
29	Ubiquitination	AQKKDGKKRKRSRKE HHHHCCCCCCCCHHH	69.54	23000965
31	Ubiquitination	KKDGKKRKRSRKESY HHCCCCCCCCHHHHH	64.70	23000965
33	Phosphorylation	DGKKRKRSRKESYSI CCCCCCCCHHHHHHH	51.22	10617636
35	N6-crotonyl-L-lysine	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	-
35	Crotonylation	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	21925322
35	Glutarylation	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	31542297
35	Other	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	27105115
35	Succinylation	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	22389435
35	Ubiquitination	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	23000965
37	O-linked_Glycosylation	RKRSRKESYSIYVYK CCCCHHHHHHHHHHH	27.50	21045127
37	Phosphorylation	RKRSRKESYSIYVYK CCCCHHHHHHHHHHH	27.50	22617229
38	Phosphorylation	KRSRKESYSIYVYKV CCCHHHHHHHHHHHH	10.52	28152594
39	Phosphorylation	RSRKESYSIYVYKVL CCHHHHHHHHHHHHH	19.40	21712546
41	Phosphorylation	RKESYSIYVYKVLKQ HHHHHHHHHHHHHHH	7.56	27155012
43	Phosphorylation	ESYSIYVYKVLKQVH HHHHHHHHHHHHHHC	4.38	18180459
44	Acetylation	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	-
44	Glutarylation	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	31542297
44	Lactoylation	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	31645732
44	Methylation	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	-
44	Other	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	24681537
44	Ubiquitination	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	23000965
47	Acetylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	19608861
47	Glutarylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	31542297
47	Methylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	19608861
47	Other	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	24681537
47	Sumoylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	19608861
47	Ubiquitination	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	23000965
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	Methylation	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	-
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	FVNDIFERIAGEASR HHHHHHHHHHHHHHH	17.20	-
79	O-linked_Glycosylation	ERIAGEASRLAHYNK HHHHHHHHHHHHHCC	24.43	21045127
79	Phosphorylation	ERIAGEASRLAHYNK HHHHHHHHHHHHHCC	24.43	22617229
80	Methylation	RIAGEASRLAHYNKR 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	-
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	LAHYNKRSTITSREI HHHHCCCCCCCHHHH	26.27	30266825
89	Phosphorylation	AHYNKRSTITSREIQ HHHCCCCCCCHHHHH	32.10	30266825
91	Phosphorylation	YNKRSTITSREIQTA HCCCCCCCHHHHHHH	23.09	30266825
92	Phosphorylation	NKRSTITSREIQTAV CCCCCCCHHHHHHHH	24.86	23401153
93	Methylation	KRSTITSREIQTAVR CCCCCCHHHHHHHHH	36.07	-
97	Phosphorylation	ITSREIQTAVRLLLP CCHHHHHHHHHHHCC	32.55	23403867
100	Methylation	REIQTAVRLLLPGEL HHHHHHHHHHCCHHH	19.70	-
109	Acetylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	-
109	Glutarylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	31542297
109	Lactoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	31645732
109	Methylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	-
109	Neddylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	32015554
109	Other	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	24681537
109	Sumoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	-
109	Ubiquitination	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	21906983
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	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	22389435
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	O-linked_Glycosylation	SEGTKAVTKYTSSK- HHHHHHHHHHCCCC-	24.16	21045127
120	Phosphorylation	SEGTKAVTKYTSSK- HHHHHHHHHHCCCC-	24.16	20068231
121	Acetylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	22389435
121	Glutarylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	31542297
121	Lactoylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	31645732
121	Methylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	22389435
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	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
14	S	Phosphorylation	Kinase	STK4	Q13043	GPS
15	S	Phosphorylation	Kinase	MST1	P26927	Uniprot
15	S	Phosphorylation	Kinase	STK4	Q13043	PhosphoELM
32	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
32	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
32	S	Phosphorylation	Kinase	MAP3K8	P41279	GPS
36	S	Phosphorylation	Kinase	PRKAA1	Q5EG47	GPS
36	S	Phosphorylation	Kinase	AKT1	P31749	PSP
36	S	Phosphorylation	Kinase	RPS6KB1	P23443	GPS
37	S	Phosphorylation	Kinase	AMPK	Q9Y478	Uniprot
78	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
83	Y	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	HUWE1	Q7Z6Z7	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
4	K	Methylation	24681537
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	24681537
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	24681537
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	24681537
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	11709551
Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity).
79	K	Methylation	11709551
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	11709551
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	11709551
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	11709551
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	16307923
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	16307923
GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121.
121	K	Methylation	16307923
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 H2B1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ERCC6_HUMAN	ERCC6	physical	11003660
A4_HUMAN	APP	physical	21832049
SSRP1_HUMAN	SSRP1	physical	22939629

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 H2B1B_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-13; LYS-16; LYS-17; LYS-21AND LYS-24, AND MASS SPECTROMETRY.	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-17AND 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]
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]

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