dbPTM

H2B1M_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2B1M_MOUSE
UniProt AC	P10854
Protein Name	Histone H2B type 1-M
Gene Name	Hist1h2bm
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	MPEPTKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MPEPTKSAP ------CCCCCCCCC	57.16	-
5	Phosphorylation	---MPEPTKSAPAPK ---CCCCCCCCCCCC	35.65	-
6	N6-crotonyl-L-lysine	--MPEPTKSAPAPKK --CCCCCCCCCCCCC	56.17	-
6	Acetylation	--MPEPTKSAPAPKK --CCCCCCCCCCCCC	56.17	23806337
6	Butyrylation	--MPEPTKSAPAPKK --CCCCCCCCCCCCC	56.17	-
6	Crotonylation	--MPEPTKSAPAPKK --CCCCCCCCCCCCC	56.17	21925322
6	Lactoylation	--MPEPTKSAPAPKK --CCCCCCCCCCCCC	56.17	31645732
6	Other	--MPEPTKSAPAPKK --CCCCCCCCCCCCC	56.17	27105115
6	Ubiquitination	--MPEPTKSAPAPKK --CCCCCCCCCCCCC	56.17	-
7	ADP-ribosylation	-MPEPTKSAPAPKKG -CCCCCCCCCCCCCC	41.80	-
7	Phosphorylation	-MPEPTKSAPAPKKG -CCCCCCCCCCCCCC	41.80	27600695
12	N6-crotonyl-L-lysine	TKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	-
12	Acetylation	TKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	23806337
12	Crotonylation	TKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	21925322
12	Lactoylation	TKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	31645732
12	Other	TKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	27105115
13	N6-crotonyl-L-lysine	KSAPAPKKGSKKAVT CCCCCCCCCCHHHHH	68.32	-
13	Acetylation	KSAPAPKKGSKKAVT CCCCCCCCCCHHHHH	68.32	158367
13	Crotonylation	KSAPAPKKGSKKAVT CCCCCCCCCCHHHHH	68.32	21925322
13	Other	KSAPAPKKGSKKAVT CCCCCCCCCCHHHHH	68.32	24681537
15	Phosphorylation	APAPKKGSKKAVTKA CCCCCCCCHHHHHHH	39.60	16039583
16	N6-crotonyl-L-lysine	PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH	54.11	-
16	Acetylation	PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH	54.11	158371
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	158375
17	Crotonylation	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	21925322
17	Glutarylation	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	-
17	Lactoylation	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	31645732
21	N6-crotonyl-L-lysine	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	-
21	Acetylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	158379
21	Butyrylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	-
21	Crotonylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	21925322
21	Lactoylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	31645732
21	Other	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	27105115
24	N6-crotonyl-L-lysine	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	-
24	Acetylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	158383
24	Crotonylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	21925322
24	Lactoylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	-
24	Other	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	24681537
25	Acetylation	AVTKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	158507
25	Other	AVTKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	24681537
33	Phosphorylation	DGKKRKRSRKESYSV CCCCCCCCCHHHHHH	51.22	21646345
35	N6-crotonyl-L-lysine	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	-
35	Crotonylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	21925322
35	Glutarylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	-
35	Other	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	27105115
35	Succinylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	-
35	Ubiquitination	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	-
37	Phosphorylation	RKRSRKESYSVYVYK CCCCCHHHHHHHHHH	26.24	23684622
38	Phosphorylation	KRSRKESYSVYVYKV CCCCHHHHHHHHHHH	11.84	25619855
39	Phosphorylation	RSRKESYSVYVYKVL CCCHHHHHHHHHHHH	19.09	25521595
41	Phosphorylation	RKESYSVYVYKVLKQ CHHHHHHHHHHHHHH	7.66	25619855
43	Phosphorylation	ESYSVYVYKVLKQVH HHHHHHHHHHHHHHC	4.25	25619855
44	Acetylation	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	38024259
44	Glutarylation	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	-
44	Lactoylation	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	-
44	Other	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	24681537
44	Ubiquitination	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	-
47	Acetylation	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	22631123
47	Glutarylation	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	-
47	Methylation	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	-
47	Other	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	24681537
47	Ubiquitination	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	-
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	Methylation	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	-
58	Other	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	24681537
58	Ubiquitination	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	-
65	Phosphorylation	KAMGIMNSFVNDIFE HHHHHHHHHHHHHHH	17.12	21082442
79	Phosphorylation	ERIAGEASRLAHYNK HHHHHHHHHHHHHCC	24.43	26643407
80	Methylation	RIAGEASRLAHYNKR HHHHHHHHHHHHCCC	42.83	-
84	Phosphorylation	EASRLAHYNKRSTIT HHHHHHHHCCCCCCC	19.44	22499769
86	"N6,N6,N6-trimethyllysine"	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	-
86	Acetylation	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	7609821
86	Lactoylation	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	31645732
86	Methylation	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	-
86	Other	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	24681537
86	Ubiquitination	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	-
87	Methylation	RLAHYNKRSTITSRE HHHHHCCCCCCCHHH	35.08	-
88	Phosphorylation	LAHYNKRSTITSREI HHHHCCCCCCCHHHH	26.27	26643407
89	Phosphorylation	AHYNKRSTITSREIQ HHHCCCCCCCHHHHH	32.10	26643407
91	Phosphorylation	YNKRSTITSREIQTA HCCCCCCCHHHHHHH	23.09	26643407
92	Phosphorylation	NKRSTITSREIQTAV CCCCCCCHHHHHHHH	24.86	30352176
93	Methylation	KRSTITSREIQTAVR CCCCCCHHHHHHHHH	36.07	-
97	Phosphorylation	ITSREIQTAVRLLLP CCHHHHHHHHHHHCC	32.55	26745281
109	Acetylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	163929
109	Glutarylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	-
109	Lactoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	31645732
109	Methylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	-
109	Other	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	27105115
109	Ubiquitination	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	-
113	O-linked_Glycosylation	ELAKHAVSEGTKAVT HHHHHHHHHHHHHHH	30.96	-
113	Phosphorylation	ELAKHAVSEGTKAVT HHHHHHHHHHHHHHH	30.96	26824392
116	Phosphorylation	KHAVSEGTKAVTKYT HHHHHHHHHHHHHHC	16.27	22817900
117	Glutarylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	-
117	Lactoylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	31645732
117	Methylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	-
117	Other	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	27105115
117	Succinylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	-
117	Ubiquitination	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	-
120	Phosphorylation	SEGTKAVTKYTSSK- HHHHHHHHHHCCCC-	24.16	17488778
121	Acetylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	1920963
121	Glutarylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	-
121	Lactoylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	-
121	Other	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	24681537
121	Succinylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	22389435
121	Ubiquitination	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	-
123	Phosphorylation	TKAVTKYTSSK---- HHHHHHHCCCC----	28.25	-
125	Phosphorylation	AVTKYTSSK------ HHHHHCCCC------	34.29	29514104
126	Acetylation	VTKYTSSK------- HHHHCCCC-------	65.21	7430965

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
Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation.
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.
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.
113	S	ubiquitylation	-
GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121.
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.
121	K	ubiquitylation	22389435
GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121.
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.

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of H2B1M_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of H2B1M_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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