dbPTM

H2B2E_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2B2E_MOUSE
UniProt AC	Q64524
Protein Name	Histone H2B type 2-E
Gene Name	Hist2h2be
Organism	Mus musculus (Mouse).
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	MPELAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIANEASRLAHYNKRSTITSREIQTSVRLLLPGELAKHAVSEGTKAVTKYTSAK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MPELAKSAP ------CCHHHHCCC	45.36	-
6	Lactoylation	--MPELAKSAPAPKK --CCHHHHCCCCCCC	60.83	31645732
6	Malonylation	--MPELAKSAPAPKK --CCHHHHCCCCCCC	60.83	26320211
6	Other	--MPELAKSAPAPKK --CCHHHHCCCCCCC	60.83	27105115
6	Crotonylation	--MPELAKSAPAPKK --CCHHHHCCCCCCC	60.83	21925322
6	Butyrylation	--MPELAKSAPAPKK --CCHHHHCCCCCCC	60.83	-
6	Acetylation	--MPELAKSAPAPKK --CCHHHHCCCCCCC	60.83	-
6	N6-crotonyl-L-lysine	--MPELAKSAPAPKK --CCHHHHCCCCCCC	60.83	-
7	Phosphorylation	-MPELAKSAPAPKKG -CCHHHHCCCCCCCC	33.60	29472430
12	N6-crotonyl-L-lysine	AKSAPAPKKGSKKAV HHCCCCCCCCCHHHH	72.39	-
12	Lactoylation	AKSAPAPKKGSKKAV HHCCCCCCCCCHHHH	72.39	31645732
12	Crotonylation	AKSAPAPKKGSKKAV HHCCCCCCCCCHHHH	72.39	21925322
12	Other	AKSAPAPKKGSKKAV HHCCCCCCCCCHHHH	72.39	27105115
12	Acetylation	AKSAPAPKKGSKKAV HHCCCCCCCCCHHHH	72.39	158471
13	Other	KSAPAPKKGSKKAVT HCCCCCCCCCHHHHH	68.32	24681537
13	N6-crotonyl-L-lysine	KSAPAPKKGSKKAVT HCCCCCCCCCHHHHH	68.32	-
13	Acetylation	KSAPAPKKGSKKAVT HCCCCCCCCCHHHHH	68.32	158475
13	Crotonylation	KSAPAPKKGSKKAVT HCCCCCCCCCHHHHH	68.32	21925322
15	Phosphorylation	APAPKKGSKKAVTKA CCCCCCCCHHHHHHH	39.60	16039583
16	Acetylation	PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH	54.11	158479
16	Lactoylation	PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH	54.11	31645732
16	N6-crotonyl-L-lysine	PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH	54.11	-
16	Crotonylation	PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH	54.11	21925322
17	Acetylation	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	158483
17	Lactoylation	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	31645732
17	N6-crotonyl-L-lysine	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	-
17	Glutarylation	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	-
17	Crotonylation	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	21925322
21	Crotonylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	21925322
21	Acetylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	158487
21	Butyrylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	-
21	N6-crotonyl-L-lysine	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	-
21	Lactoylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	31645732
21	Other	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	27105115
24	Crotonylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	21925322
24	Lactoylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	-
24	N6-crotonyl-L-lysine	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	-
24	Other	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	24681537
24	Acetylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	158491
25	Other	AVTKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	24681537
25	Acetylation	AVTKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	158533
35	Succinylation	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	-
35	Other	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	27105115
35	Glutarylation	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	-
35	N6-crotonyl-L-lysine	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	-
35	Crotonylation	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	21925322
37	Phosphorylation	RKRSRKESYSIYVYK CCCCHHHHHHHHHHH	27.50	20647423
39	Phosphorylation	RSRKESYSIYVYKVL CCHHHHHHHHHHHHH	19.40	27600695
44	Lactoylation	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	-
44	Other	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	24681537
44	Glutarylation	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	-
47	Acetylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	22733758
47	Glutarylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	-
47	Methylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	-
47	Other	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	24681537
47	Ubiquitination	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	22790023
53	Phosphorylation	LKQVHPDTGISSKAM HHHHCCCCCCCHHHH	40.65	23737553
56	Phosphorylation	VHPDTGISSKAMGIM HCCCCCCCHHHHHHH	27.42	25521595
57	Phosphorylation	HPDTGISSKAMGIMN CCCCCCCHHHHHHHH	23.63	25521595
58	"N6,N6-dimethyllysine"	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	-
58	Ubiquitination	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	-
58	Methylation	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	-
58	Other	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	24681537
65	Phosphorylation	KAMGIMNSFVNDIFE HHHHHHHHHHHHHHH	17.12	21082442
80	Methylation	RIANEASRLAHYNKR HHHHHHHHHHHHCCC	42.83	-
84	Phosphorylation	EASRLAHYNKRSTIT HHHHHHHHCCCCCCC	19.44	22499769
86	Lactoylation	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	31645732
86	Other	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	24681537
86	Methylation	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	-
86	"N6,N6,N6-trimethyllysine"	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	-
86	Ubiquitination	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	27667366
86	Acetylation	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	7610021
87	Methylation	RLAHYNKRSTITSRE HHHHHCCCCCCCHHH	35.08	-
88	Phosphorylation	LAHYNKRSTITSREI HHHHCCCCCCCHHHH	26.27	-
89	Phosphorylation	AHYNKRSTITSREIQ HHHCCCCCCCHHHHH	32.10	29514104
93	Methylation	KRSTITSREIQTSVR CCCCCCHHHHHHHHH	36.07	-
109	Ubiquitination	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	27667366
109	Acetylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	163945
109	Glutarylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	-
109	Lactoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	31645732
109	Methylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	-
109	Other	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	27105115
113	Phosphorylation	ELAKHAVSEGTKAVT HHHHHHHHHHCHHHH	30.96	23684622
116	Phosphorylation	KHAVSEGTKAVTKYT HHHHHHHCHHHHHHC	16.27	28066266
117	Succinylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	-
117	Ubiquitination	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	27667366
117	Glutarylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	-
117	Lactoylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	31645732
117	Methylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	-
117	Other	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	27105115
121	Ubiquitination	EGTKAVTKYTSAK-- HHCHHHHHHCCCC--	39.67	27667366
121	Succinylation	EGTKAVTKYTSAK-- HHCHHHHHHCCCC--	39.67	22389435
121	Other	EGTKAVTKYTSAK-- HHCHHHHHHCCCC--	39.67	24681537
121	Malonylation	EGTKAVTKYTSAK-- HHCHHHHHHCCCC--	39.67	26320211
121	Lactoylation	EGTKAVTKYTSAK-- HHCHHHHHHCCCC--	39.67	-
121	Glutarylation	EGTKAVTKYTSAK-- HHCHHHHHHCCCC--	39.67	-
121	Acetylation	EGTKAVTKYTSAK-- HHCHHHHHHCCCC--	39.67	23806337
123	Phosphorylation	TKAVTKYTSAK---- CHHHHHHCCCC----	24.62	-

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	P26928	Uniprot
15	S	Phosphorylation	Kinase	STK4	Q61036	GPS
37	S	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
37	S	Phosphorylation	Kinase	AMPK	-	Uniprot

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	15197225
Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination.
15	S	Phosphorylation	15197225
Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation.
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	20647423
Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription.
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.
121	K	Methylation	22389435
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	22389435
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 H2B2E_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
WDTC1_MOUSE	Wdtc1	physical	17767906

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of H2B2E_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-21, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"Signaling kinase AMPK activates stress-promoted transcription viahistone H2B phosphorylation."; Bungard D., Fuerth B.J., Zeng P.Y., Faubert B., Maas N.L., Viollet B.,Carling D., Thompson C.B., Jones R.G., Berger S.L.; Science 329:1201-1205(2010). Cited for: PHOSPHORYLATION AT SER-37.	20647423 [Abstract]
"Histone modifications associated with somatic hypermutation."; Odegard V.H., Kim S.T., Anderson S.M., Shlomchik M.J., Schatz D.G.; Immunity 23:101-110(2005). Cited for: PHOSPHORYLATION AT SER-15.	16039583 [Abstract]
"Phosphorylation of histone H2B at DNA double-strand breaks."; Fernandez-Capetillo O., Allis C.D., Nussenzweig A.; J. Exp. Med. 199:1671-1677(2004). Cited for: PHOSPHORYLATION AT SER-15.	15197225 [Abstract]

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