dbPTM

H2B3B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2B3B_MOUSE
UniProt AC	Q8CGP0
Protein Name	Histone H2B type 3-B
Gene Name	Hist3h2bb
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	MPDPSKSAPAPKKGSKKAVTKAQKKDGKKRKRGRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREVQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MPDPSKSAP ------CCCCCCCCC	63.32	-
6	N6-crotonyl-L-lysine	--MPDPSKSAPAPKK --CCCCCCCCCCCCC	56.90	-
6	Acetylation	--MPDPSKSAPAPKK --CCCCCCCCCCCCC	56.90	-
6	Butyrylation	--MPDPSKSAPAPKK --CCCCCCCCCCCCC	56.90	-
6	Crotonylation	--MPDPSKSAPAPKK --CCCCCCCCCCCCC	56.90	21925322
6	Lactoylation	--MPDPSKSAPAPKK --CCCCCCCCCCCCC	56.90	31645732
6	Other	--MPDPSKSAPAPKK --CCCCCCCCCCCCC	56.90	27105115
7	Phosphorylation	-MPDPSKSAPAPKKG -CCCCCCCCCCCCCC	43.77	-
12	N6-crotonyl-L-lysine	SKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	-
12	Acetylation	SKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	19737024
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	24431441
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	24431451
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	24431461
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	24431471
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	24431481
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	24848085
25	Other	AVTKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	24681537
35	N6-crotonyl-L-lysine	KKRKRGRKESYSIYV CCCCCCCCHHHHHHH	54.56	-
35	Crotonylation	KKRKRGRKESYSIYV CCCCCCCCHHHHHHH	54.56	21925322
35	Glutarylation	KKRKRGRKESYSIYV CCCCCCCCHHHHHHH	54.56	-
35	Other	KKRKRGRKESYSIYV CCCCCCCCHHHHHHH	54.56	27105115
35	Succinylation	KKRKRGRKESYSIYV CCCCCCCCHHHHHHH	54.56	-
37	Phosphorylation	RKRGRKESYSIYVYK CCCCCCHHHHHHHHH	27.50	20647423
39	Phosphorylation	RGRKESYSIYVYKVL CCCCHHHHHHHHHHH	19.40	27600695
44	Glutarylation	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	-
44	Lactoylation	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	-
44	Other	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	24681537
47	Acetylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	37418361
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	-
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
76	Phosphorylation	DIFERIASEASRLAH HHHHHHHHHHHHHHH	31.18	24453211
79	Phosphorylation	ERIASEASRLAHYNK HHHHHHHHHHHHHCC	24.63	28066266
80	Methylation	RIASEASRLAHYNKR 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	-
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	LAHYNKRSTITSREV HHHHCCCCCCCHHHH	26.27	-
89	Phosphorylation	AHYNKRSTITSREVQ HHHCCCCCCCHHHHH	32.10	29514104
91	Phosphorylation	YNKRSTITSREVQTA HCCCCCCCHHHHHHH	23.09	22817900
92	Phosphorylation	NKRSTITSREVQTAV CCCCCCCHHHHHHHH	23.69	22817900
93	Methylation	KRSTITSREVQTAVR CCCCCCHHHHHHHHH	39.18	-
109	Acetylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	30589249
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	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	30589237
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

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

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 H2B3B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of H2B3B_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of H2B3B_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]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	19367708 [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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