dbPTM

H2B2E_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2B2E_HUMAN
UniProt AC	Q16778
Protein Name	Histone H2B type 2-E
Gene Name	HIST2H2BE
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	MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MPEPAKSAP ------CCCCCCCCC	57.17	-
6	N6-crotonyl-L-lysine	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	-
6	Acetylation	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	16283522
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	16627869
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	Glycation	AKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	-
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	Glycation	KSAPAPKKGSKKAVT CCCCCCCCCCHHHHH	68.32	-
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	Glycation	PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH	54.11	-
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	158407
24	Crotonylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	21925322
24	Lactoylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	31645732
24	Other	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	24681537
24	Ubiquitination	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	25015289
25	Acetylation	AVTKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	158513
25	Other	AVTKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	24681537
29	Ubiquitination	AQKKDGKKRKRSRKE HHHHCCCCCCCCHHH	69.54	23000965
31	Ubiquitination	KKDGKKRKRSRKESY HHCCCCCCCCHHHHH	64.70	23000965
33	Phosphorylation	DGKKRKRSRKESYSI CCCCCCCCHHHHHHH	51.22	10617636
35	N6-crotonyl-L-lysine	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	-
35	Crotonylation	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	21925322
35	Glutarylation	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	31542297
35	Glycation	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	-
35	Other	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	27105115
35	Succinylation	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	22389435
35	Ubiquitination	KKRKRSRKESYSIYV CCCCCCHHHHHHHHH	52.86	23000965
37	Phosphorylation	RKRSRKESYSIYVYK CCCCHHHHHHHHHHH	27.50	22617229
38	Phosphorylation	KRSRKESYSIYVYKV CCCHHHHHHHHHHHH	10.52	28152594
39	Phosphorylation	RSRKESYSIYVYKVL CCHHHHHHHHHHHHH	19.40	21712546
41	Phosphorylation	RKESYSIYVYKVLKQ HHHHHHHHHHHHHHH	7.56	27155012
43	Phosphorylation	ESYSIYVYKVLKQVH HHHHHHHHHHHHHHC	4.38	18180459
44	Acetylation	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	7933041
44	Glutarylation	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	31542297
44	Lactoylation	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	31645732
44	Other	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	24681537
44	Ubiquitination	SYSIYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	23000965
47	Acetylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	22631177
47	Glutarylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	31542297
47	Methylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	16627869
47	Other	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	24681537
47	Sumoylation	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	16627869
47	Ubiquitination	IYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	23000965
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	163975
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	7610013
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	27667366
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	163951
109	Glutarylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	31542297
109	Glycation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	-
109	Lactoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	31645732
109	Methylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	16627869
109	Neddylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	32015554
109	Other	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	24681537
109	Sumoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	16627869
109	Ubiquitination	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	21906983
113	O-linked_Glycosylation	ELAKHAVSEGTKAVT HHHHHHHHHHHHHHH	30.96	23222540
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	22389435
117	Glutarylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	31542297
117	Glycation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	-
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	22389435
117	Sumoylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	22389435
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	163835
121	Glutarylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	31542297
121	Lactoylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	31645732
121	Neddylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	32015554
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	22389435
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	7431057
126	Neddylation	VTKYTSSK------- HHHHCCCC-------	65.21	32015554
126	Ubiquitination	VTKYTSSK------- HHHHCCCC-------	65.21	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
33	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
37	S	Phosphorylation	Kinase	AMPK	Q9Y478	Uniprot
37	S	Phosphorylation	Kinase	AKT1	P31749	GPS
37	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
79	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
84	Y	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:15546622
-	K	Ubiquitination	E3 ubiquitin ligase	RNF40	O75150	PMID:16307923
-	K	Ubiquitination	E3 ubiquitin ligase	RNF20	Q5VTR2	PMID:21443952
-	K	Ubiquitination	E3 ubiquitin ligase	MSL2	Q9HCI7	PMID:21726816

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 H2B2E_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MDM2_HUMAN	MDM2	physical	15546622
DEK_HUMAN	DEK	physical	16696975
NUCL_HUMAN	NCL	physical	16601700
P66A_HUMAN	GATAD2A	physical	16415179
P66B_HUMAN	GATAD2B	physical	16415179
EP300_HUMAN	EP300	physical	15136563
AN32A_HUMAN	ANP32A	physical	15136563
TAF1B_HUMAN	TAF1B	physical	15136563
TAF1A_HUMAN	TAF1A	physical	15136563
UHRF1_MOUSE	Uhrf1	physical	14993289
BRD2_HUMAN	BRD2	physical	14731392
HIPK2_HUMAN	HIPK2	physical	22658722
TCF20_HUMAN	TCF20	physical	22081970
UIMC1_HUMAN	UIMC1	physical	19015238
LATS2_HUMAN	LATS2	physical	21041410
IL7RA_HUMAN	IL7R	physical	23151878
UBC_HUMAN	UBC	physical	24526689
UBP15_HUMAN	USP15	physical	24526689
SART3_HUMAN	SART3	physical	24526689
CDK9_HUMAN	CDK9	physical	24837678
RPB1_HUMAN	POLR2A	physical	24837678
H2AY_HUMAN	H2AFY	physical	25306110

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 H2B2E_HUMAN

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-6; 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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