dbPTM

H2B1N_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2B1N_HUMAN
UniProt AC	Q99877
Protein Name	Histone H2B type 1-N
Gene Name	HIST1H2BN
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	MPEPSKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MPEPSKSAP ------CCCCCCCCC	63.31	-
5	Phosphorylation	---MPEPSKSAPAPK ---CCCCCCCCCCCC	37.27	24719451
6	N6-crotonyl-L-lysine	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	-
6	Acetylation	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	16283522
6	Butyrylation	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	27105113
6	Crotonylation	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	21925322
6	Lactoylation	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	31645732
6	Other	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	27105115
6	Sumoylation	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	16283522
6	Ubiquitination	--MPEPSKSAPAPKK --CCCCCCCCCCCCC	62.44	16283522
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	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
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	16283522
24	N6-crotonyl-L-lysine	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	-
24	Acetylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	158457
24	Crotonylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	21925322
24	Lactoylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	31645732
24	Other	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	24681537
25	Acetylation	AVTKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	158527
25	Other	AVTKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	24681537
33	Phosphorylation	DGKKRKRSRKESYSV CCCCCCCCCHHHHHH	51.22	28152594
35	N6-crotonyl-L-lysine	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	-
35	Acetylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	22631171
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	22389435
35	Ubiquitination	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	21890473
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	Acetylation	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	38024279
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	21890473
47	Acetylation	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	22631165
47	Glutarylation	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	31542297
47	Methylation	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	16627869
47	Other	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	24681537
47	Sumoylation	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	16627869
47	Ubiquitination	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	473
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	163987
58	Methylation	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	16627869
58	Other	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	24681537
58	Ubiquitination	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	21906983
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	7610003
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	-
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	163939
109	Glutarylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	31542297
109	Lactoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	31645732
109	Methylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	16627869
109	Other	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	24681537
109	Sumoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	16627869
109	Ubiquitination	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	20639865
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	158625
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	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	22389435
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	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	16627869
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	7431187
126	Ubiquitination	VTKYTSSK------- HHHHCCCC-------	65.21	-

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	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 H2B1N_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
BCCIP_HUMAN	BCCIP	physical	16189514

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 H2B1N_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-12 AND LYS-13, 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-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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