dbPTM

H2B1M_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2B1M_HUMAN
UniProt AC	Q99879
Protein Name	Histone H2B type 1-M
Gene Name	HIST1H2BM
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	MPEPVKSAPVPKKGSKKAINKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MPEPVKSAP ------CCCCCCCCC	55.38	-
6	N6-crotonyl-L-lysine	--MPEPVKSAPVPKK --CCCCCCCCCCCCC	52.17	-
6	Acetylation	--MPEPVKSAPVPKK --CCCCCCCCCCCCC	52.17	19608861
6	Butyrylation	--MPEPVKSAPVPKK --CCCCCCCCCCCCC	52.17	27105113
6	Crotonylation	--MPEPVKSAPVPKK --CCCCCCCCCCCCC	52.17	21925322
6	Lactoylation	--MPEPVKSAPVPKK --CCCCCCCCCCCCC	52.17	31645732
6	Lactylation	--MPEPVKSAPVPKK --CCCCCCCCCCCCC	52.17	31645732
6	Other	--MPEPVKSAPVPKK --CCCCCCCCCCCCC	52.17	27105115
6	Sumoylation	--MPEPVKSAPVPKK --CCCCCCCCCCCCC	52.17	28112733
6	Ubiquitination	--MPEPVKSAPVPKK --CCCCCCCCCCCCC	52.17	23000965
7	ADP-ribosylation	-MPEPVKSAPVPKKG -CCCCCCCCCCCCCC	37.73	27723750
7	Phosphorylation	-MPEPVKSAPVPKKG -CCCCCCCCCCCCCC	37.73	23403867
12	N6-crotonyl-L-lysine	VKSAPVPKKGSKKAI CCCCCCCCCCCHHHH	70.74	-
12	Acetylation	VKSAPVPKKGSKKAI CCCCCCCCCCCHHHH	70.74	25825284
12	Crotonylation	VKSAPVPKKGSKKAI CCCCCCCCCCCHHHH	70.74	21925322
12	Lactoylation	VKSAPVPKKGSKKAI CCCCCCCCCCCHHHH	70.74	31645732
12	Other	VKSAPVPKKGSKKAI CCCCCCCCCCCHHHH	70.74	27105115
12	Ubiquitination	VKSAPVPKKGSKKAI CCCCCCCCCCCHHHH	70.74	23000965
13	N6-crotonyl-L-lysine	KSAPVPKKGSKKAIN CCCCCCCCCCHHHHH	63.45	-
13	Acetylation	KSAPVPKKGSKKAIN CCCCCCCCCCHHHHH	63.45	19608861
13	Crotonylation	KSAPVPKKGSKKAIN CCCCCCCCCCHHHHH	63.45	21925322
13	Other	KSAPVPKKGSKKAIN CCCCCCCCCCHHHHH	63.45	24681537
15	Phosphorylation	APVPKKGSKKAINKA CCCCCCCCHHHHHHH	39.60	12757711
16	N6-crotonyl-L-lysine	PVPKKGSKKAINKAQ CCCCCCCHHHHHHHH	55.69	-
16	Acetylation	PVPKKGSKKAINKAQ CCCCCCCHHHHHHHH	55.69	19608861
16	Crotonylation	PVPKKGSKKAINKAQ CCCCCCCHHHHHHHH	55.69	21925322
16	Lactoylation	PVPKKGSKKAINKAQ CCCCCCCHHHHHHHH	55.69	31645732
17	N6-crotonyl-L-lysine	VPKKGSKKAINKAQK CCCCCCHHHHHHHHH	57.08	-
17	Acetylation	VPKKGSKKAINKAQK CCCCCCHHHHHHHHH	57.08	19608861
17	Crotonylation	VPKKGSKKAINKAQK CCCCCCHHHHHHHHH	57.08	21925322
17	Glutarylation	VPKKGSKKAINKAQK CCCCCCHHHHHHHHH	57.08	31542297
17	Lactoylation	VPKKGSKKAINKAQK CCCCCCHHHHHHHHH	57.08	31645732
17	Other	VPKKGSKKAINKAQK CCCCCCHHHHHHHHH	57.08	27105115
21	N6-crotonyl-L-lysine	GSKKAINKAQKKDGK CCHHHHHHHHHHCCC	46.19	-
21	Acetylation	GSKKAINKAQKKDGK CCHHHHHHHHHHCCC	46.19	19608861
21	Butyrylation	GSKKAINKAQKKDGK CCHHHHHHHHHHCCC	46.19	27105113
21	Crotonylation	GSKKAINKAQKKDGK CCHHHHHHHHHHCCC	46.19	21925322
21	Lactoylation	GSKKAINKAQKKDGK CCHHHHHHHHHHCCC	46.19	31645732
21	Lactylation	GSKKAINKAQKKDGK CCHHHHHHHHHHCCC	46.19	31645732
21	Other	GSKKAINKAQKKDGK CCHHHHHHHHHHCCC	46.19	27105115
21	Ubiquitination	GSKKAINKAQKKDGK CCHHHHHHHHHHCCC	46.19	27667366
24	N6-crotonyl-L-lysine	KAINKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	-
24	Acetylation	KAINKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	19608861
24	Crotonylation	KAINKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	21925322
24	Lactoylation	KAINKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	31645732
24	Other	KAINKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	24681537
25	Acetylation	AINKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	7493399
25	Other	AINKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	24681537
29	Ubiquitination	AQKKDGKKRKRSRKE HHHHCCCCCCCCHHH	69.54	23000965
31	Ubiquitination	KKDGKKRKRSRKESY HHCCCCCCCCHHHHH	64.70	23000965
33	Phosphorylation	DGKKRKRSRKESYSV CCCCCCCCHHHHHHH	51.22	28152594
35	N6-crotonyl-L-lysine	KKRKRSRKESYSVYV CCCCCCHHHHHHHHH	52.86	-
35	Acetylation	KKRKRSRKESYSVYV CCCCCCHHHHHHHHH	52.86	22389435
35	Crotonylation	KKRKRSRKESYSVYV CCCCCCHHHHHHHHH	52.86	21925322
35	Glutarylation	KKRKRSRKESYSVYV CCCCCCHHHHHHHHH	52.86	31542297
35	Other	KKRKRSRKESYSVYV CCCCCCHHHHHHHHH	52.86	27105115
35	Succinylation	KKRKRSRKESYSVYV CCCCCCHHHHHHHHH	52.86	22389435
35	Ubiquitination	KKRKRSRKESYSVYV CCCCCCHHHHHHHHH	52.86	23000965
37	Phosphorylation	RKRSRKESYSVYVYK CCCCHHHHHHHHHHH	26.24	23401153
38	Phosphorylation	KRSRKESYSVYVYKV CCCHHHHHHHHHHHH	11.84	21082442
39	Phosphorylation	RSRKESYSVYVYKVL CCHHHHHHHHHHHHH	19.09	25159151
41	Phosphorylation	RKESYSVYVYKVLKQ HHHHHHHHHHHHHHH	7.66	27155012
43	Phosphorylation	ESYSVYVYKVLKQVH HHHHHHHHHHHHHHC	4.25	27273156
44	Acetylation	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	30779513
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	Acetylation	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	185143
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	-
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	163991
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	30846556
63	Sulfoxidation	SSKAMGIMNSFVNDI CHHHHHHHHHHHHHH	2.59	30846556
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	7681419
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	Sumoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	-
109	Acetylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	163955
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	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	Sumoylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	-
121	Acetylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	22389435
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	7431197
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
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 H2B1M_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
A4_HUMAN	APP	physical	21832049

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 H2B1M_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-13; LYS-16; LYS-17;LYS-21 AND 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-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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