dbPTM

H2B1A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2B1A_HUMAN
UniProt AC	Q96A08
Protein Name	Histone H2B type 1-A
Gene Name	HIST1H2BA
Organism	Homo sapiens (Human).
Sequence Length	127
Subcellular Localization	Nucleus . Chromosome .
Protein Description	Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells (By similarity). Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones (By similarity). Core component of nucleosome (By similarity). Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template (By similarity). Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability (By similarity). DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity). Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear. [PubMed: 21249133]
Protein Sequence	MPEVSSKGATISKKGFKKAVVKTQKKEGKKRKRTRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIASEASRLAHYSKRSTISSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MPEVSSKGA ------CCCCCCCCC	51.18	-
5	Phosphorylation	---MPEVSSKGATIS ---CCCCCCCCCCCC	25.35	29759185
6	Phosphorylation	--MPEVSSKGATISK --CCCCCCCCCCCCC	40.04	29759185
7	"N6,N6-dimethyllysine"	-MPEVSSKGATISKK -CCCCCCCCCCCCCH	45.09	-
7	Acetylation	-MPEVSSKGATISKK -CCCCCCCCCCCCCH	45.09	16283522
7	Crotonylation	-MPEVSSKGATISKK -CCCCCCCCCCCCCH	45.09	21925322
7	Lactoylation	-MPEVSSKGATISKK -CCCCCCCCCCCCCH	45.09	31645732
7	Methylation	-MPEVSSKGATISKK -CCCCCCCCCCCCCH	45.09	-
7	Ubiquitination	-MPEVSSKGATISKK -CCCCCCCCCCCCCH	45.09	-
10	Phosphorylation	EVSSKGATISKKGFK CCCCCCCCCCCHHHH	34.16	27282143
12	Phosphorylation	SSKGATISKKGFKKA CCCCCCCCCHHHHHH	24.78	30622161
13	"N6,N6-dimethyllysine"	SKGATISKKGFKKAV CCCCCCCCHHHHHHH	53.73	-
13	Acetylation	SKGATISKKGFKKAV CCCCCCCCHHHHHHH	53.73	-
13	Crotonylation	SKGATISKKGFKKAV CCCCCCCCHHHHHHH	53.73	21925322
13	Lactoylation	SKGATISKKGFKKAV CCCCCCCCHHHHHHH	53.73	31645732
13	Methylation	SKGATISKKGFKKAV CCCCCCCCHHHHHHH	53.73	-
14	N6-crotonyl-L-lysine	KGATISKKGFKKAVV CCCCCCCHHHHHHHH	63.89	-
14	Acetylation	KGATISKKGFKKAVV CCCCCCCHHHHHHHH	63.89	16283522
14	Crotonylation	KGATISKKGFKKAVV CCCCCCCHHHHHHHH	63.89	21925322
17	N6-crotonyl-L-lysine	TISKKGFKKAVVKTQ CCCCHHHHHHHHHHC	48.79	-
17	Acetylation	TISKKGFKKAVVKTQ CCCCHHHHHHHHHHC	48.79	16283522
17	Crotonylation	TISKKGFKKAVVKTQ CCCCHHHHHHHHHHC	48.79	21925322
17	Lactoylation	TISKKGFKKAVVKTQ CCCCHHHHHHHHHHC	48.79	31645732
18	N6-crotonyl-L-lysine	ISKKGFKKAVVKTQK CCCHHHHHHHHHHCH	44.12	-
18	Acetylation	ISKKGFKKAVVKTQK CCCHHHHHHHHHHCH	44.12	20167786
18	Crotonylation	ISKKGFKKAVVKTQK CCCHHHHHHHHHHCH	44.12	21925322
18	Lactoylation	ISKKGFKKAVVKTQK CCCHHHHHHHHHHCH	44.12	31645732
22	N6-crotonyl-L-lysine	GFKKAVVKTQKKEGK HHHHHHHHHCHHCCC	38.34	-
22	Acetylation	GFKKAVVKTQKKEGK HHHHHHHHHCHHCCC	38.34	16283522
22	Crotonylation	GFKKAVVKTQKKEGK HHHHHHHHHCHHCCC	38.34	21925322
22	Lactoylation	GFKKAVVKTQKKEGK HHHHHHHHHCHHCCC	38.34	31645732
23	Phosphorylation	FKKAVVKTQKKEGKK HHHHHHHHCHHCCCC	33.73	30622161
25	N6-crotonyl-L-lysine	KAVVKTQKKEGKKRK HHHHHHCHHCCCCCC	59.01	-
25	Acetylation	KAVVKTQKKEGKKRK HHHHHHCHHCCCCCC	59.01	25953088
25	Crotonylation	KAVVKTQKKEGKKRK HHHHHHCHHCCCCCC	59.01	21925322
25	Lactoylation	KAVVKTQKKEGKKRK HHHHHHCHHCCCCCC	59.01	31645732
36	N6-crotonyl-L-lysine	KKRKRTRKESYSIYI CCCCCCCHHHHHHHH	50.85	-
36	Crotonylation	KKRKRTRKESYSIYI CCCCCCCHHHHHHHH	50.85	21925322
36	Succinylation	KKRKRTRKESYSIYI CCCCCCCHHHHHHHH	50.85	-
38	Phosphorylation	RKRTRKESYSIYIYK CCCCCHHHHHHHHHH	27.50	-
42	Phosphorylation	RKESYSIYIYKVLKQ CHHHHHHHHHHHHHH	7.70	-
45	Acetylation	SYSIYIYKVLKQVHP HHHHHHHHHHHHHCC	31.37	25038526
45	Lactoylation	SYSIYIYKVLKQVHP HHHHHHHHHHHHHCC	31.37	31645732
45	Ubiquitination	SYSIYIYKVLKQVHP HHHHHHHHHHHHHCC	31.37	23000965
48	Acetylation	IYIYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	22631101
48	Methylation	IYIYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	-
48	Sumoylation	IYIYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	-
48	Ubiquitination	IYIYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	23000965
54	Phosphorylation	LKQVHPDTGISSKAM HHHHCCCCCCCHHHH	40.65	30266825
57	Phosphorylation	VHPDTGISSKAMSIM HCCCCCCCHHHHHHH	27.42	23401153
58	Phosphorylation	HPDTGISSKAMSIMN CCCCCCCHHHHHHHH	23.63	30266825
59	"N6,N6-dimethyllysine"	PDTGISSKAMSIMNS CCCCCCHHHHHHHHH	41.12	-
59	Acetylation	PDTGISSKAMSIMNS CCCCCCHHHHHHHHH	41.12	163983
59	Methylation	PDTGISSKAMSIMNS CCCCCCHHHHHHHHH	41.12	-
59	Ubiquitination	PDTGISSKAMSIMNS CCCCCCHHHHHHHHH	41.12	25015289
61	Sulfoxidation	TGISSKAMSIMNSFV CCCCHHHHHHHHHHH	2.99	28183972
62	Phosphorylation	GISSKAMSIMNSFVT CCCHHHHHHHHHHHH	24.44	23403867
64	Sulfoxidation	SSKAMSIMNSFVTDI CHHHHHHHHHHHHHH	2.42	28183972
66	Phosphorylation	KAMSIMNSFVTDIFE HHHHHHHHHHHHHHH	12.06	23403867
69	Phosphorylation	SIMNSFVTDIFERIA HHHHHHHHHHHHHHH	22.74	23403867
77	Phosphorylation	DIFERIASEASRLAH HHHHHHHHHHHHHHH	31.18	23403867
80	Phosphorylation	ERIASEASRLAHYSK HHHHHHHHHHHHHHC	24.63	21082442
81	Methylation	RIASEASRLAHYSKR HHHHHHHHHHHHHCC	42.83	21249133
86	Phosphorylation	ASRLAHYSKRSTISS HHHHHHHHCCCCCCH	16.24	21249133
87	"N6,N6,N6-trimethyllysine"	SRLAHYSKRSTISSR HHHHHHHCCCCCCHH	43.11	-
87	Acetylation	SRLAHYSKRSTISSR HHHHHHHCCCCCCHH	43.11	21249133
87	Lactoylation	SRLAHYSKRSTISSR HHHHHHHCCCCCCHH	43.11	31645732
87	Methylation	SRLAHYSKRSTISSR HHHHHHHCCCCCCHH	43.11	21249133
88	Methylation	RLAHYSKRSTISSRE HHHHHHCCCCCCHHH	32.85	21249133
89	Phosphorylation	LAHYSKRSTISSREI HHHHHCCCCCCHHHH	33.55	20860994
90	Phosphorylation	AHYSKRSTISSREIQ HHHHCCCCCCHHHHH	28.98	21406692
92	Phosphorylation	YSKRSTISSREIQTA HHCCCCCCHHHHHHH	24.35	20860994
93	Phosphorylation	SKRSTISSREIQTAV HCCCCCCHHHHHHHH	30.04	20860994
94	Methylation	KRSTISSREIQTAVR CCCCCCHHHHHHHHH	37.94	21249133
98	Phosphorylation	ISSREIQTAVRLLLP CCHHHHHHHHHHHCC	32.55	29802988
110	Ubiquitination	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	21890473
110	Sumoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	-
110	Acetylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	163935
110	Lactoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	31645732
110	Methylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	-
110	Neddylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	32015554
110	Sumoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	-
110	Ubiquitination	LLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	27667366
114	Phosphorylation	ELAKHAVSEGTKAVT HHHHHHHHHHCHHHH	30.96	28176443
117	Phosphorylation	KHAVSEGTKAVTKYT HHHHHHHCHHHHHHC	16.27	20068231
118	Sumoylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	-
118	Acetylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	158621
118	Lactoylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	31645732
118	Methylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	-
118	Neddylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	32015554
118	Succinylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	21890473
118	Sumoylation	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	-
118	Ubiquitination	HAVSEGTKAVTKYTS HHHHHHCHHHHHHCC	52.28	23000965
121	Phosphorylation	SEGTKAVTKYTSSK- HHHCHHHHHHCCCC-	24.16	20068231
122	Ubiquitination	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	21890473
122	Sumoylation	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	-
122	Acetylation	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	163843
122	Lactoylation	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	31645732
122	Neddylation	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	32015554
122	Succinylation	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	21890473
122	Sumoylation	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	-
122	Ubiquitination	EGTKAVTKYTSSK-- HHCHHHHHHCCCC--	39.67	25015289
123	Phosphorylation	GTKAVTKYTSSK--- HCHHHHHHCCCC---	11.50	-
124	Phosphorylation	TKAVTKYTSSK---- CHHHHHHCCCC----	28.25	24719451
125	Phosphorylation	KAVTKYTSSK----- HHHHHHCCCC-----	32.80	27251275
127	Acetylation	VTKYTSSK------- HHHHCCCC-------	65.21	7431175
127	Neddylation	VTKYTSSK------- HHHHCCCC-------	65.21	32015554
127	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
-	K	Ubiquitination	E3 ubiquitin ligase	RNF40	O75150	PMID:16307923
-	K	Ubiquitination	E3 ubiquitin ligase	RNF20	Q5VTR2	PMID:16307923
-	K	Ubiquitination	E3 ubiquitin ligase	BRCA1	P38398	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	RNF8	O76064	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	HUWE1	Q7Z6Z7	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
4	K	Methylation	31645732
Monoubiquitination at Lys-36 (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	31645732
Similarly, monoubiquitination at Lys-122 (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	31645732
Monoubiquitination at Lys-36 (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	31645732
Similarly, monoubiquitination at Lys-122 (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.
36	K	Methylation	21925322
Monoubiquitination at Lys-36 (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.
36	K	ubiquitylation	21925322
Monoubiquitination at Lys-36 (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	16307923
Monoubiquitination at Lys-36 (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	16307923
Similarly, monoubiquitination at Lys-122 (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	16307923
Monoubiquitination at Lys-36 (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	16307923
Similarly, monoubiquitination at Lys-122 (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.
117	T	Phosphorylation	-
Phosphorylated at Thr-117 in spermatogonia, spermatocytes and round spermatids.
118	K	Methylation	-
Methylated at Lys-118 in spermatogonia, spermatocytes and round spermatids.
122	K	Methylation	16307923
Similarly, monoubiquitination at Lys-122 (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.
122	K	ubiquitylation	16307923
Similarly, monoubiquitination at Lys-122 (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 H2B1A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PARP1_HUMAN	PARP1	physical	20525793
A4_HUMAN	APP	physical	21832049
HDAC1_HUMAN	HDAC1	physical	24722339
HDAC2_HUMAN	HDAC2	physical	24722339
HDAC3_HUMAN	HDAC3	physical	24722339
NP1L1_HUMAN	NAP1L1	physical	26186194
RUVB1_HUMAN	RUVBL1	physical	26186194
MIER1_HUMAN	MIER1	physical	26186194
HDAC1_HUMAN	HDAC1	physical	26186194
EP400_HUMAN	EP400	physical	26186194
GON4L_HUMAN	GON4L	physical	26186194
EAF6_HUMAN	MEAF6	physical	26186194
H2AW_HUMAN	H2AFY2	physical	26186194
H2AY_HUMAN	H2AFY	physical	26186194
SP16H_HUMAN	SUPT16H	physical	26186194
DNLI3_HUMAN	LIG3	physical	26186194
ACL6A_HUMAN	ACTL6A	physical	26186194
ACL6B_HUMAN	ACTL6B	physical	26186194
EPC1_HUMAN	EPC1	physical	26186194
EPC2_HUMAN	EPC2	physical	26186194
PARP2_HUMAN	PARP2	physical	26186194
PHF14_HUMAN	PHF14	physical	26186194
PARP1_HUMAN	PARP1	physical	26186194
SRCAP_HUMAN	SRCAP	physical	26186194
DMAP1_HUMAN	DMAP1	physical	26186194
TCF20_HUMAN	TCF20	physical	26186194
ARI5B_HUMAN	ARID5B	physical	26186194
TRRAP_HUMAN	TRRAP	physical	26186194
CP087_HUMAN	C16orf87	physical	26186194
HLTF_HUMAN	HLTF	physical	26186194
MCM7_HUMAN	MCM7	physical	26186194
MCM2_HUMAN	MCM2	physical	26186194
IPO9_HUMAN	IPO9	physical	26186194
BRD8_HUMAN	BRD8	physical	26186194
H1T_HUMAN	HIST1H1T	physical	26186194
PPM1G_HUMAN	PPM1G	physical	26186194
VPS72_HUMAN	VPS72	physical	26186194
EHMT1_HUMAN	EHMT1	physical	26186194
EHMT2_HUMAN	EHMT2	physical	26186194
H2B1J_HUMAN	HIST1H2BJ	physical	26186194
H2B1L_HUMAN	HIST1H2BL	physical	26186194
MMS22_HUMAN	MMS22L	physical	26186194
MCM6_HUMAN	MCM6	physical	26186194
SSRP1_HUMAN	SSRP1	physical	26186194
ING3_HUMAN	ING3	physical	26186194
H2AZ_HUMAN	H2AFZ	physical	26186194
H2A2B_HUMAN	HIST2H2AB	physical	26186194
TEX10_HUMAN	TEX10	physical	26186194
BAHD1_HUMAN	BAHD1	physical	26186194
MIER3_HUMAN	MIER3	physical	26186194
RUVB2_HUMAN	RUVBL2	physical	26186194
CRML_HUMAN	CRAMP1L	physical	26186194
CHD1L_HUMAN	CHD1L	physical	26186194
AN32E_HUMAN	ANP32E	physical	26186194
MCM4_HUMAN	MCM4	physical	26186194
ARP6_HUMAN	ACTR6	physical	26186194
XPC_HUMAN	XPC	physical	26186194
CFDP1_HUMAN	CFDP1	physical	26186194
KAT5_HUMAN	KAT5	physical	26186194
CETN2_HUMAN	CETN2	physical	26186194
UBE2O_HUMAN	UBE2O	physical	26186194
KBTB7_HUMAN	KBTBD7	physical	26186194
MBTD1_HUMAN	MBTD1	physical	26186194
MO4L1_HUMAN	MORF4L1	physical	26186194
MO4L2_HUMAN	MORF4L2	physical	26186194
MRGBP_HUMAN	MRGBP	physical	26186194
TONSL_HUMAN	TONSL	physical	26186194
SENP3_HUMAN	SENP3	physical	26186194
CDYL_HUMAN	CDYL	physical	26186194
YETS4_HUMAN	YEATS4	physical	26186194
PELP1_HUMAN	PELP1	physical	26186194
XRCC1_HUMAN	XRCC1	physical	26186194
APLF_HUMAN	APLF	physical	26186194
ZNHI1_HUMAN	ZNHIT1	physical	26186194
HM20A_HUMAN	HMG20A	physical	26186194
TRI41_HUMAN	TRIM41	physical	26186194
RUVB1_HUMAN	RUVBL1	physical	26344197
SSRP1_HUMAN	SSRP1	physical	26344197
MIER3_HUMAN	MIER3	physical	28514442
BAHD1_HUMAN	BAHD1	physical	28514442
PHF14_HUMAN	PHF14	physical	28514442
H2B1L_HUMAN	HIST1H2BL	physical	28514442
MIER1_HUMAN	MIER1	physical	28514442
GON4L_HUMAN	GON4L	physical	28514442
ZNHI1_HUMAN	ZNHIT1	physical	28514442
KAT5_HUMAN	KAT5	physical	28514442
TONSL_HUMAN	TONSL	physical	28514442
ARP6_HUMAN	ACTR6	physical	28514442
ARI5B_HUMAN	ARID5B	physical	28514442
EPC2_HUMAN	EPC2	physical	28514442
VPS72_HUMAN	VPS72	physical	28514442
SRCAP_HUMAN	SRCAP	physical	28514442
EPC1_HUMAN	EPC1	physical	28514442
CRML_HUMAN	CRAMP1L	physical	28514442
MMS22_HUMAN	MMS22L	physical	28514442
CFDP1_HUMAN	CFDP1	physical	28514442
EP400_HUMAN	EP400	physical	28514442
SP16H_HUMAN	SUPT16H	physical	28514442
MBTD1_HUMAN	MBTD1	physical	28514442
DMAP1_HUMAN	DMAP1	physical	28514442
TRRAP_HUMAN	TRRAP	physical	28514442
PARP2_HUMAN	PARP2	physical	28514442
EAF6_HUMAN	MEAF6	physical	28514442
ACL6B_HUMAN	ACTL6B	physical	28514442
APLF_HUMAN	APLF	physical	28514442
ING3_HUMAN	ING3	physical	28514442
CDYL_HUMAN	CDYL	physical	28514442
XPC_HUMAN	XPC	physical	28514442
IPO9_HUMAN	IPO9	physical	28514442
HM20A_HUMAN	HMG20A	physical	28514442
TRI41_HUMAN	TRIM41	physical	28514442
BRD8_HUMAN	BRD8	physical	28514442
H2AY_HUMAN	H2AFY	physical	28514442
SSRP1_HUMAN	SSRP1	physical	28514442
H2AW_HUMAN	H2AFY2	physical	28514442
DNLI3_HUMAN	LIG3	physical	28514442
PPM1G_HUMAN	PPM1G	physical	28514442
JAZF1_HUMAN	JAZF1	physical	28514442
MCM2_HUMAN	MCM2	physical	28514442
AN32E_HUMAN	ANP32E	physical	28514442
TCF20_HUMAN	TCF20	physical	28514442
MCM4_HUMAN	MCM4	physical	28514442
H2A2B_HUMAN	HIST2H2AB	physical	28514442
YETS4_HUMAN	YEATS4	physical	28514442
MRGBP_HUMAN	MRGBP	physical	28514442
MO4L1_HUMAN	MORF4L1	physical	28514442
XRCC1_HUMAN	XRCC1	physical	28514442
RUVB1_HUMAN	RUVBL1	physical	28514442
EHMT2_HUMAN	EHMT2	physical	28514442
NP1L1_HUMAN	NAP1L1	physical	28514442
H2AZ_HUMAN	H2AFZ	physical	28514442
MCM6_HUMAN	MCM6	physical	28514442
RUVB2_HUMAN	RUVBL2	physical	28514442
CP087_HUMAN	C16orf87	physical	28514442
MCM7_HUMAN	MCM7	physical	28514442
H1T_HUMAN	HIST1H1T	physical	28514442
PARP1_HUMAN	PARP1	physical	28514442
HDAC1_HUMAN	HDAC1	physical	28514442
ACL6A_HUMAN	ACTL6A	physical	28514442
CETN2_HUMAN	CETN2	physical	28514442
TEX10_HUMAN	TEX10	physical	28514442
UBE2O_HUMAN	UBE2O	physical	28514442
NP1L4_HUMAN	NAP1L4	physical	28514442
PSF3_HUMAN	GINS3	physical	28514442
HDAC2_HUMAN	HDAC2	physical	28514442
HLTF_HUMAN	HLTF	physical	28514442

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 H2B1A_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-110, 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-7; LYS-14; LYS-17 AND LYS-22.	16283522 [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-122.	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-122.	16307923 [Abstract]

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