dbPTM

H2B2F_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2B2F_HUMAN
UniProt AC	Q5QNW6
Protein Name	Histone H2B type 2-F
Gene Name	HIST2H2BF
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	MPDPAKSAPAPKKGSKKAVTKVQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MPDPAKSAP ------CCCHHHCCC	57.18	-
6	N6-crotonyl-L-lysine	--MPDPAKSAPAPKK --CCCHHHCCCCCCC	53.17	-
6	Acetylation	--MPDPAKSAPAPKK --CCCHHHCCCCCCC	53.17	19608861
6	Butyrylation	--MPDPAKSAPAPKK --CCCHHHCCCCCCC	53.17	27105113
6	Crotonylation	--MPDPAKSAPAPKK --CCCHHHCCCCCCC	53.17	21925322
6	Lactoylation	--MPDPAKSAPAPKK --CCCHHHCCCCCCC	53.17	31645732
6	Other	--MPDPAKSAPAPKK --CCCHHHCCCCCCC	53.17	27105115
6	Sumoylation	--MPDPAKSAPAPKK --CCCHHHCCCCCCC	53.17	19608861
6	Ubiquitination	--MPDPAKSAPAPKK --CCCHHHCCCCCCC	53.17	33845483
7	Phosphorylation	-MPDPAKSAPAPKKG -CCCHHHCCCCCCCC	41.41	23403867
12	N6-crotonyl-L-lysine	AKSAPAPKKGSKKAV HHCCCCCCCCCCHHH	72.39	-
12	Acetylation	AKSAPAPKKGSKKAV HHCCCCCCCCCCHHH	72.39	158409
12	Crotonylation	AKSAPAPKKGSKKAV HHCCCCCCCCCCHHH	72.39	21925322
12	Lactoylation	AKSAPAPKKGSKKAV HHCCCCCCCCCCHHH	72.39	31645732
12	Lactylation	AKSAPAPKKGSKKAV HHCCCCCCCCCCHHH	72.39	31645732
12	Other	AKSAPAPKKGSKKAV HHCCCCCCCCCCHHH	72.39	27105115
12	Ubiquitination	AKSAPAPKKGSKKAV HHCCCCCCCCCCHHH	72.39	25015289
13	N6-crotonyl-L-lysine	KSAPAPKKGSKKAVT HCCCCCCCCCCHHHH	68.32	-
13	Acetylation	KSAPAPKKGSKKAVT HCCCCCCCCCCHHHH	68.32	19608861
13	Crotonylation	KSAPAPKKGSKKAVT HCCCCCCCCCCHHHH	68.32	21925322
13	Other	KSAPAPKKGSKKAVT HCCCCCCCCCCHHHH	68.32	24681537
15	Phosphorylation	APAPKKGSKKAVTKV CCCCCCCCCHHHHHH	39.60	12757711
16	N6-crotonyl-L-lysine	PAPKKGSKKAVTKVQ CCCCCCCCHHHHHHH	54.11	-
16	Acetylation	PAPKKGSKKAVTKVQ CCCCCCCCHHHHHHH	54.11	19608861
16	Crotonylation	PAPKKGSKKAVTKVQ CCCCCCCCHHHHHHH	54.11	21925322
16	Lactoylation	PAPKKGSKKAVTKVQ CCCCCCCCHHHHHHH	54.11	31645732
17	N6-crotonyl-L-lysine	APKKGSKKAVTKVQK CCCCCCCHHHHHHHH	50.19	-
17	Acetylation	APKKGSKKAVTKVQK CCCCCCCHHHHHHHH	50.19	19608861
17	Crotonylation	APKKGSKKAVTKVQK CCCCCCCHHHHHHHH	50.19	21925322
17	Glutarylation	APKKGSKKAVTKVQK CCCCCCCHHHHHHHH	50.19	31542297
17	Lactoylation	APKKGSKKAVTKVQK CCCCCCCHHHHHHHH	50.19	31645732
17	Lactylation	APKKGSKKAVTKVQK CCCCCCCHHHHHHHH	50.19	31645732
17	Other	APKKGSKKAVTKVQK CCCCCCCHHHHHHHH	50.19	27105115
21	N6-crotonyl-L-lysine	GSKKAVTKVQKKDGK CCCHHHHHHHHCCCC	35.75	-
21	Acetylation	GSKKAVTKVQKKDGK CCCHHHHHHHHCCCC	35.75	19608861
21	Butyrylation	GSKKAVTKVQKKDGK CCCHHHHHHHHCCCC	35.75	27105113
21	Crotonylation	GSKKAVTKVQKKDGK CCCHHHHHHHHCCCC	35.75	21925322
21	Lactoylation	GSKKAVTKVQKKDGK CCCHHHHHHHHCCCC	35.75	31645732
21	Lactylation	GSKKAVTKVQKKDGK CCCHHHHHHHHCCCC	35.75	31645732
21	Other	GSKKAVTKVQKKDGK CCCHHHHHHHHCCCC	35.75	27105115
21	Sumoylation	GSKKAVTKVQKKDGK CCCHHHHHHHHCCCC	35.75	28112733
21	Ubiquitination	GSKKAVTKVQKKDGK CCCHHHHHHHHCCCC	35.75	33845483
24	N6-crotonyl-L-lysine	KAVTKVQKKDGKKRK HHHHHHHHCCCCCCC	56.68	-
24	Acetylation	KAVTKVQKKDGKKRK HHHHHHHHCCCCCCC	56.68	23749302
24	Crotonylation	KAVTKVQKKDGKKRK HHHHHHHHCCCCCCC	56.68	21925322
24	Lactoylation	KAVTKVQKKDGKKRK HHHHHHHHCCCCCCC	56.68	31645732
24	Lactylation	KAVTKVQKKDGKKRK HHHHHHHHCCCCCCC	56.68	31645732
24	Other	KAVTKVQKKDGKKRK HHHHHHHHCCCCCCC	56.68	24681537
25	Acetylation	AVTKVQKKDGKKRKR HHHHHHHCCCCCCCC	55.40	12635587
25	Other	AVTKVQKKDGKKRKR HHHHHHHCCCCCCCC	55.40	24681537
29	Ubiquitination	VQKKDGKKRKRSRKE HHHCCCCCCCCCCHH	69.54	23000965
31	Ubiquitination	KKDGKKRKRSRKESY HCCCCCCCCCCHHHH	64.70	23000965
33	Phosphorylation	DGKKRKRSRKESYSV CCCCCCCCCHHHHHH	51.22	28152594
35	Ubiquitination	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	21890473
35	N6-crotonyl-L-lysine	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	-
35	Acetylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	19608861
35	Crotonylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	21925322
35	Glutarylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	31542297
35	Other	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	27105115
35	Succinylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	19608861
35	Ubiquitination	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	23000965
37	Phosphorylation	RKRSRKESYSVYVYK CCCCCHHHHHHHHHH	26.24	23401153
38	Phosphorylation	KRSRKESYSVYVYKV CCCCHHHHHHHHHHH	11.84	21082442
39	Phosphorylation	RSRKESYSVYVYKVL CCCHHHHHHHHHHHH	19.09	25159151
41	Phosphorylation	RKESYSVYVYKVLKQ CHHHHHHHHHHHHHH	7.66	27155012
43	Phosphorylation	ESYSVYVYKVLKQVH HHHHHHHHHHHHHHC	4.25	27273156
44	Ubiquitination	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	21890473
44	Acetylation	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	30779545
44	Glutarylation	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	31542297
44	Lactoylation	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	31645732
44	Methylation	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	-
44	Other	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	24681537
44	Ubiquitination	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	23000965
47	Ubiquitination	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	21890473
47	Acetylation	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	19608861
47	Glutarylation	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	31542297
47	Methylation	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	-
47	Other	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	24681537
47	Sumoylation	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	19608861
47	Ubiquitination	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	27667366
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	163977
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	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	19608861
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	Ubiquitination	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	21890473
109	Sumoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	-
109	Acetylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	163953
109	Glutarylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	31542297
109	Lactoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	31645732
109	Methylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	-
109	Neddylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	32015554
109	Other	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	24681537
109	Sumoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	-
109	Ubiquitination	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	21906983
113	O-linked_Glycosylation	ELAKHAVSEGTKAVT HHHHHHHHHHCHHHH	30.96	UniProtKB CARBOHYD
113	Phosphorylation	ELAKHAVSEGTKAVT HHHHHHHHHHCHHHH	30.96	28176443
116	Phosphorylation	KHAVSEGTKAVTKYT HHHHHHHCHHHHHHC	16.27	20068231
117	Ubiquitination	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	21890473
117	Sumoylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	-
117	Acetylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	22389435
117	Glutarylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	31542297
117	Lactoylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	31645732
117	Malonylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	22389435
117	Methylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	-
117	Neddylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	32015554
117	Other	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	27105115
117	Succinylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	22389435
117	Sumoylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	22389435
117	Ubiquitination	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	23000965
120	Phosphorylation	SEGTKAVTKYTSSK- HHHCHHHHHHCCCC-	24.16	20068231
121	Ubiquitination	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	21890473
121	Sumoylation	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	-
121	Acetylation	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	163839
121	Glutarylation	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	31542297
121	Lactoylation	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	31645732
121	Neddylation	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	32015554
121	Other	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	27105115
121	Succinylation	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	22389435
121	Sumoylation	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	22389435
121	Ubiquitination	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	27667366
122	Phosphorylation	GTKAVTKYTSSK--- HCHHHHHHCCCC---	11.50	-
123	Phosphorylation	TKAVTKYTSSK---- CHHHHHHCCCC----	28.25	24719451
124	Phosphorylation	KAVTKYTSSK----- HHHHHHCCCC-----	32.80	27251275
126	Acetylation	VTKYTSSK------- HHHHCCCC-------	65.21	7431069
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
37	S	Phosphorylation	Kinase	AKT1	P31749	PSP
79	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
84	Y	Phosphorylation	Kinase	AURKB	Q96GD4	GPS

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	12757711
Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity).
79	K	Methylation	-
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	-
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	-
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	-
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 H2B2F_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of H2B2F_HUMAN !!

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 H2B2F_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-6; LYS-17 AND LYS-21, ANDMASS 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-6; 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]
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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