H2B1C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2B1C_HUMAN
• UniProt AC: P62807
• Protein Name: Histone H2B type 1-C/E/F/G/I
• Gene Name: HIST1H2BC
• 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.; Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid..
• Protein Sequence: MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MPEPAKSAP ------CCCCCCCCC	57.17	-
5	Phosphorylation	---MPEPAKSAPAPK ---CCCCCCCCCCCC	19.44	-
6	N6-crotonyl-L-lysine	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	-
6	Acetylation	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	19608861
6	Butyrylation	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	27105113
6	Crotonylation	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	21925322
6	Lactoylation	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	31645732
6	Methylation	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	16283522
6	Other	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	27105115
6	Sumoylation	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	19608861
6	Ubiquitination	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	23000965
7	Phosphorylation	-MPEPAKSAPAPKKG -CCCCCCCCCCCCCC	41.41	23401153
12	N6-crotonyl-L-lysine	AKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	-
12	Acetylation	AKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	16627869
12	Crotonylation	AKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	21925322
12	Lactoylation	AKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	31645732
12	Other	AKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	27105115
12	Ubiquitination	AKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	23000965
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
17	Ubiquitination	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	25015289
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	25015289
24	N6-crotonyl-L-lysine	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	-
24	Acetylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	158385
24	Crotonylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	21925322
24	Lactoylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	31645732
24	Methylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	-
24	Other	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	24681537
24	Ubiquitination	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	25015289
25	Acetylation	AVTKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	158509
25	Other	AVTKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	24681537
29	Ubiquitination	AQKKDGKKRKRSRKE HHHHCCCCCCCCCHH	69.54	23000965
30	Ubiquitination	QKKDGKKRKRSRKES HHHCCCCCCCCCHHH	43.01	23000965
31	Ubiquitination	KKDGKKRKRSRKESY HHCCCCCCCCCHHHH	64.70	23000965
33	Phosphorylation	DGKKRKRSRKESYSV CCCCCCCCCHHHHHH	51.22	28152594
35	N6-crotonyl-L-lysine	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	-
35	Acetylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	22389435
35	Crotonylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	21925322
35	Glutarylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	31542297
35	Malonylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	26320211
35	Other	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	27105115
35	Succinylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	22389435
35	Ubiquitination	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	23000965
36	Ubiquitination	KRKRSRKESYSVYVY CCCCCCHHHHHHHHH	54.52	23000965
37	Phosphorylation	RKRSRKESYSVYVYK CCCCCHHHHHHHHHH	26.24	25159151
38	Phosphorylation	KRSRKESYSVYVYKV CCCCHHHHHHHHHHH	11.84	21082442
39	Phosphorylation	RSRKESYSVYVYKVL CCCHHHHHHHHHHHH	19.09	25159151
41	Phosphorylation	RKESYSVYVYKVLKQ CHHHHHHHHHHHHHH	7.66	27155012
41	Ubiquitination	RKESYSVYVYKVLKQ CHHHHHHHHHHHHHH	7.66	25015289
43	Phosphorylation	ESYSVYVYKVLKQVH HHHHHHHHHHHHHHC	4.25	27273156
44	Acetylation	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	38024255
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
45	Ubiquitination	YSVYVYKVLKQVHPD HHHHHHHHHHHHCCC	4.40	25015289
47	Acetylation	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	22631109
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	21906983
48	Ubiquitination	YVYKVLKQVHPDTGI HHHHHHHHHCCCCCC	34.29	25015289
53	Phosphorylation	LKQVHPDTGISSKAM HHHHCCCCCCCHHHH	40.65	30266825
53	Ubiquitination	LKQVHPDTGISSKAM HHHHCCCCCCCHHHH	40.65	23000965
55	Ubiquitination	QVHPDTGISSKAMGI HHCCCCCCCHHHHHH	4.57	23000965
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	163971
58	Methylation	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	16627869
58	Other	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	24681537
58	Ubiquitination	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	21906983
59	Ubiquitination	DTGISSKAMGIMNSF CCCCCHHHHHHHHHH	11.90	23000965
65	Phosphorylation	KAMGIMNSFVNDIFE HHHHHHHHHHHHHHH	17.12	22617229
68	Ubiquitination	GIMNSFVNDIFERIA HHHHHHHHHHHHHHH	34.35	23000965
71	Ubiquitination	NSFVNDIFERIAGEA HHHHHHHHHHHHHHH	6.02	23000965
73	Methylation	FVNDIFERIAGEASR HHHHHHHHHHHHHHH	17.20	-
79	Phosphorylation	ERIAGEASRLAHYNK HHHHHHHHHHHHHCC	24.43	22617229
80	Methylation	RIAGEASRLAHYNKR HHHHHHHHHHHHCCC	42.83	-
82	Ubiquitination	AGEASRLAHYNKRST HHHHHHHHHHCCCCC	11.29	22817900
84	Phosphorylation	EASRLAHYNKRSTIT HHHHHHHHCCCCCCC	19.44	25884760
86	"N6,N6,N6-trimethyllysine"	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	-
86	Acetylation	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	7610065
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	21906983
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	19608861
109	Glutarylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	31542297
109	Lactoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	31645732
109	Methylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	19608861
109	Neddylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	32015554
109	Other	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	24681537
109	Sumoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	19608861
109	Ubiquitination	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	27667366
110	Ubiquitination	LPGELAKHAVSEGTK CCHHHHHHHHHHHHH	26.25	27667366
113	O-linked_Glycosylation	ELAKHAVSEGTKAVT HHHHHHHHHHHHHHH	30.96	22121020
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	19608861
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	19608861
117	Sumoylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	19608861
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	163829
121	Glutarylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	31542297
121	Lactoylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	31645732
121	Methylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	-
121	Neddylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	32015554
121	Other	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	27105115
121	Succinylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	19608861
121	Sumoylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	19608861
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	Neddylation	VTKYTSSK------- HHHHCCCC-------	65.21	32015554
126	Ubiquitination	VTKYTSSK------- HHHHCCCC-------	65.21	23000965
133	Ubiquitination	K-------------- C--------------		23000965
141	Ubiquitination	---------------------- ----------------------		23000965
145	Ubiquitination	-------------------------- --------------------------		23000965
150	Ubiquitination	------------------------------- -------------------------------		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
15	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
15	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
33	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
33	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
37	S	Phosphorylation	Kinase	AMPK	Q9Y478	Uniprot
37	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
37	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
79	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
84	Y	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	RNF20	Q5VTR2	PMID:16307923
-	K	Ubiquitination	E3 ubiquitin ligase	MSL2	Q9HCI7	PMID:16627869

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
4	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.	16627869
4	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.	16627869
4	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.	16627869
4	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.	16627869
15	S	Phosphorylation	Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation.	12757711
15	S	Phosphorylation	Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination.	12757711
35	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.	21726816
35	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.	21726816
37	S	Phosphorylation	Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity).	12757711
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.	16627869
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.	16627869
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.	16627869
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.	16627869
113	S	ubiquitylation	GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121.	22121020
121	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.	16627869
121	K	ubiquitylation	GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121.	16627869
121	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.	16627869

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
17	Acetylation	27 (10)	G ⇒ S;R;C	rs7766641	Height	28270201
17	Crotonylation	27 (10)	G ⇒ S;R;C	rs7766641	Height	28270201
21	Acetylation	27 (6)	G ⇒ S;R;C	rs7766641	Height	28270201
21	Crotonylation	27 (6)	G ⇒ S;R;C	rs7766641	Height	28270201
24	Acetylation	27 (3)	G ⇒ S;R;C	rs7766641	Height	28270201
24	Crotonylation	27 (3)	G ⇒ S;R;C	rs7766641	Height	28270201
25	Acetylation	27 (2)	G ⇒ S;R;C	rs7766641	Height	28270201
33	Phosphorylation	27 (6)	G ⇒ S;R;C	rs7766641	Height	28270201
35	Acetylation	27 (8)	G ⇒ S;R;C	rs7766641	Height	28270201
35	Crotonylation	27 (8)	G ⇒ S;R;C	rs7766641	Height	28270201
35	Ubiquitination	27 (8)	G ⇒ S;R;C	rs7766641	Height	28270201
37	Phosphorylation	27 (10)	G ⇒ S;R;C	rs7766641	Height	28270201

Protein-Protein Interaction

Oops, there are no PPI records of H2B1C_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• There are no disease associations of PTM sites.
• There are no disease associations of PTM sites.
• There are no disease associations of PTM sites.
• There are no disease associations of PTM sites.
• 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.
• There are no disease associations of PTM sites.
• There are no disease associations of PTM sites.
• There are no disease associations of PTM sites.
• There are no disease associations of PTM sites.
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"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-6; LYS-12; LYS-13; LYS-16;LYS-17; LYS-21; LYS-24 AND LYS-109, AND MASS SPECTROMETRY.
PubMed: 16916647

"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.
PubMed: 16283522

"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.
PubMed: 16627869

"Characterization of histones H2A and H2B variants and their post-translational modifications by mass spectrometry.";
Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.;
Mol. Cell. Proteomics 5:541-552(2006).
Cited for: PROTEIN SEQUENCE OF 2-26, ACETYLATION AT LYS-13; LYS-16 AND LYS-21,AND MASS SPECTROMETRY.
PubMed: 16319397

Methylation

"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.
PubMed: 16627869

O-linked Glycosylation

"GlcNAcylation of histone H2B facilitates its monoubiquitination.";
Fujiki R., Hashiba W., Sekine H., Yokoyama A., Chikanishi T., Ito S.,Imai Y., Kim J., He H.H., Igarashi K., Kanno J., Ohtake F.,Kitagawa H., Roeder R.G., Brown M., Kato S.;
Nature 480:557-560(2011).
Cited for: GLYCOSYLATION AT SER-113, AND UBIQUITINATION AT LYS-121.
PubMed: 22121020

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY.
PubMed: 19413330

"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.
PubMed: 12757711

Ubiquitylation

"GlcNAcylation of histone H2B facilitates its monoubiquitination.";
Fujiki R., Hashiba W., Sekine H., Yokoyama A., Chikanishi T., Ito S.,Imai Y., Kim J., He H.H., Igarashi K., Kanno J., Ohtake F.,Kitagawa H., Roeder R.G., Brown M., Kato S.;
Nature 480:557-560(2011).
Cited for: GLYCOSYLATION AT SER-113, AND UBIQUITINATION AT LYS-121.
PubMed: 22121020

"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.
PubMed: 16713563

"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.
PubMed: 16307923

"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.
PubMed: 16627869