dbPTM

H11_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H11_HUMAN
UniProt AC	Q02539
Protein Name	Histone H1.1
Gene Name	HIST1H1A
Organism	Homo sapiens (Human).
Sequence Length	215
Subcellular Localization	Nucleus . Chromosome . Mainly localizes in euchromatin.
Protein Description	Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity)..
Protein Sequence	MSETVPPAPAASAAPEKPLAGKKAKKPAKAAAASKKKPAGPSVSELIVQAASSSKERGGVSLAALKKALAAAGYDVEKNNSRIKLGIKSLVSKGTLVQTKGTGASGSFKLNKKASSVETKPGASKVATKTKATGASKKLKKATGASKKSVKTPKKAKKPAATRKSSKNPKKPKTVKPKKVAKSPAKAKAVKPKAAKARVTKPKTAKPKKAAPKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSETVPPAP ------CCCCCCCCC	41.81	23663014
2	Acetylation	------MSETVPPAP ------CCCCCCCCC	41.81	-
4	Phosphorylation	----MSETVPPAPAA ----CCCCCCCCCCC	30.88	23663014
12	Phosphorylation	VPPAPAASAAPEKPL CCCCCCCCCCCCCCC	27.37	23663014
17	Acetylation	AASAAPEKPLAGKKA CCCCCCCCCCCCCCC	44.25	-
17	Ubiquitination	AASAAPEKPLAGKKA CCCCCCCCCCCCCCC	44.25	23000965
22	Acetylation	PEKPLAGKKAKKPAK CCCCCCCCCCCHHHH	43.90	17043054
22	Ubiquitination	PEKPLAGKKAKKPAK CCCCCCCCCCCHHHH	43.90	23000965
22	Methylation	PEKPLAGKKAKKPAK CCCCCCCCCCCHHHH	43.90	17043054
23	Ubiquitination	EKPLAGKKAKKPAKA CCCCCCCCCCHHHHH	65.60	23000965
23	Methylation	EKPLAGKKAKKPAKA CCCCCCCCCCHHHHH	65.60	17043054
26	Acetylation	LAGKKAKKPAKAAAA CCCCCCCHHHHHHHH	55.88	20167786
36	Ubiquitination	KAAAASKKKPAGPSV HHHHHHCCCCCCCCH	62.59	29967540
37	Ubiquitination	AAAASKKKPAGPSVS HHHHHCCCCCCCCHH	43.78	29967540
37	Other	AAAASKKKPAGPSVS HHHHHCCCCCCCCHH	43.78	-
42	Phosphorylation	KKKPAGPSVSELIVQ CCCCCCCCHHHHHHH	37.04	21406692
44	Phosphorylation	KPAGPSVSELIVQAA CCCCCCHHHHHHHHH	30.90	21406692
52	Phosphorylation	ELIVQAASSSKERGG HHHHHHHHCCCCCCC	37.85	21406692
53	Phosphorylation	LIVQAASSSKERGGV HHHHHHHCCCCCCCC	40.48	21406692
54	Phosphorylation	IVQAASSSKERGGVS HHHHHHCCCCCCCCC	35.72	21406692
55	Ubiquitination	VQAASSSKERGGVSL HHHHHCCCCCCCCCH	54.07	29967540
55	Other	VQAASSSKERGGVSL HHHHHCCCCCCCCCH	54.07	-
57	Citrullination	AASSSKERGGVSLAA HHHCCCCCCCCCHHH	51.40	-
57	Citrullination	AASSSKERGGVSLAA HHHCCCCCCCCCHHH	51.40	-
61	Phosphorylation	SKERGGVSLAALKKA CCCCCCCCHHHHHHH	18.63	24719451
66	Malonylation	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	26320211
66	Ubiquitination	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	23000965
67	Sumoylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	-
67	Ubiquitination	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	23000965
67	Sumoylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	-
67	Other	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	-
67	Acetylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	-
67	Malonylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	26320211
74	Phosphorylation	KALAAAGYDVEKNNS HHHHHCCCCCHHCCC	16.46	28152594
78	Acetylation	AAGYDVEKNNSRIKL HCCCCCHHCCCCEEE	62.37	158567
78	Ubiquitination	AAGYDVEKNNSRIKL HCCCCCHHCCCCEEE	62.37	21906983
81	Phosphorylation	YDVEKNNSRIKLGIK CCCHHCCCCEEEEHH	44.79	23401153
84	Ubiquitination	EKNNSRIKLGIKSLV HHCCCCEEEEHHHHH	39.28	23000965
88	Other	SRIKLGIKSLVSKGT CCEEEEHHHHHHCCC	35.62	-
88	Ubiquitination	SRIKLGIKSLVSKGT CCEEEEHHHHHHCCC	35.62	23000965
88	Acetylation	SRIKLGIKSLVSKGT CCEEEEHHHHHHCCC	35.62	19608861
89	Phosphorylation	RIKLGIKSLVSKGTL CEEEEHHHHHHCCCE	31.89	20860994
92	Phosphorylation	LGIKSLVSKGTLVQT EEHHHHHHCCCEEEE	30.57	20860994
93	Ubiquitination	GIKSLVSKGTLVQTK EHHHHHHCCCEEEEC	48.73	23000965
93	Acetylation	GIKSLVSKGTLVQTK EHHHHHHCCCEEEEC	48.73	19608861
93	Malonylation	GIKSLVSKGTLVQTK EHHHHHHCCCEEEEC	48.73	26320211
93	Other	GIKSLVSKGTLVQTK EHHHHHHCCCEEEEC	48.73	-
95	Phosphorylation	KSLVSKGTLVQTKGT HHHHHCCCEEEECCC	27.74	29514088
99	Phosphorylation	SKGTLVQTKGTGASG HCCCEEEECCCCCCC	24.78	28111955
100	Ubiquitination	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	23000965
100	Acetylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	-
102	Phosphorylation	TLVQTKGTGASGSFK CEEEECCCCCCCCEE	31.00	26657352
105	Phosphorylation	QTKGTGASGSFKLNK EECCCCCCCCEEECC	35.99	25159151
107	Phosphorylation	KGTGASGSFKLNKKA CCCCCCCCEEECCCC	19.40	23401153
109	Acetylation	TGASGSFKLNKKASS CCCCCCEEECCCCCC	53.50	22648197
109	Ubiquitination	TGASGSFKLNKKASS CCCCCCEEECCCCCC	53.50	21963094
109	Other	TGASGSFKLNKKASS CCCCCCEEECCCCCC	53.50	-
112	Ubiquitination	SGSFKLNKKASSVET CCCEEECCCCCCCCC	61.22	22817900
113	Ubiquitination	GSFKLNKKASSVETK CCEEECCCCCCCCCC	53.05	22817900
115	Phosphorylation	FKLNKKASSVETKPG EEECCCCCCCCCCCC	43.74	30622161
116	Phosphorylation	KLNKKASSVETKPGA EECCCCCCCCCCCCC	28.91	30622161
119	Phosphorylation	KKASSVETKPGASKV CCCCCCCCCCCCCHH	40.14	30622161
120	Ubiquitination	KASSVETKPGASKVA CCCCCCCCCCCCHHC	28.13	23000965
124	Phosphorylation	VETKPGASKVATKTK CCCCCCCCHHCHHHC	33.31	29083192
125	Acetylation	ETKPGASKVATKTKA CCCCCCCHHCHHHCC	35.04	-
125	Lactylation	ETKPGASKVATKTKA CCCCCCCHHCHHHCC	35.04	31645732
125	Ubiquitination	ETKPGASKVATKTKA CCCCCCCHHCHHHCC	35.04	23000965
128	Phosphorylation	PGASKVATKTKATGA CCCCHHCHHHCCCCC	42.08	29083192
129	Lactylation	GASKVATKTKATGAS CCCHHCHHHCCCCCH	37.99	31645732
129	Ubiquitination	GASKVATKTKATGAS CCCHHCHHHCCCCCH	37.99	23000965
131	Ubiquitination	SKVATKTKATGASKK CHHCHHHCCCCCHHH	45.57	23000965
133	Phosphorylation	VATKTKATGASKKLK HCHHHCCCCCHHHHH	34.53	29396449
143	Phosphorylation	SKKLKKATGASKKSV HHHHHHHHCCCHHCC	42.01	29759185
146	Phosphorylation	LKKATGASKKSVKTP HHHHHCCCHHCCCCC	41.80	29759185
149	Phosphorylation	ATGASKKSVKTPKKA HHCCCHHCCCCCHHH	32.36	29759185
152	Phosphorylation	ASKKSVKTPKKAKKP CCHHCCCCCHHHCCC	37.88	20551309
162	Phosphorylation	KAKKPAATRKSSKNP HHCCCCCCCCCCCCC	40.51	22817900
165	Phosphorylation	KPAATRKSSKNPKKP CCCCCCCCCCCCCCC	43.16	20068231
166	Phosphorylation	PAATRKSSKNPKKPK CCCCCCCCCCCCCCC	39.21	20068231
174	Phosphorylation	KNPKKPKTVKPKKVA CCCCCCCCCCCCHHC	42.14	26657352
183	Phosphorylation	KPKKVAKSPAKAKAV CCCHHCCCHHHHHCC	21.98	20551309
204	Phosphorylation	ARVTKPKTAKPKKAA CCCCCCCCCCCCCCC	48.73	22817900

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
152	T	Phosphorylation	Kinase	CDK2	P24941	PSP
183	S	Phosphorylation	Kinase	CDK9	P50750	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	HUWE1	Q7Z6Z7	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
57	R	Citrullination		-
Citrullination at Arg-57 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance.

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 H11_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CTCFL_HUMAN	CTCFL	physical	17048991
DEK_HUMAN	DEK	physical	16696975
EZH2_HUMAN	EZH2	physical	16431907
SUZ12_HUMAN	SUZ12	physical	16431907
EED_HUMAN	EED	physical	16431907
RBBP4_HUMAN	RBBP4	physical	16431907
AEBP2_HUMAN	AEBP2	physical	16431907
UHRF1_MOUSE	Uhrf1	physical	14993289
LYOX_HUMAN	LOX	physical	12686141
NSD3_HUMAN	WHSC1L1	physical	23455924
CTR9_HUMAN	CTR9	physical	24360965
LEO1_HUMAN	LEO1	physical	24360965
PAF1_HUMAN	PAF1	physical	24360965
CDC73_HUMAN	CDC73	physical	24360965
WDR61_HUMAN	WDR61	physical	24360965
CUL4A_HUMAN	CUL4A	physical	24360965
DDB1_HUMAN	DDB1	physical	24360965
RBX1_HUMAN	RBX1	physical	24360965
WDR5_HUMAN	WDR5	physical	24360965
DCAF1_HUMAN	VPRBP	physical	24360965
LARP7_HUMAN	LARP7	physical	26186194
YBOX2_HUMAN	YBX2	physical	26186194
KNOP1_HUMAN	KNOP1	physical	26186194
SF3B1_HUMAN	SF3B1	physical	26186194
POP1_HUMAN	POP1	physical	26186194
DDX24_HUMAN	DDX24	physical	26186194
SPB1_HUMAN	FTSJ3	physical	26186194
RS3_HUMAN	RPS3	physical	26186194
SF3B2_HUMAN	SF3B2	physical	26186194
ZN574_HUMAN	ZNF574	physical	26186194
ZN668_HUMAN	ZNF668	physical	26186194
RRP12_HUMAN	RRP12	physical	26186194
ZNF70_HUMAN	ZNF70	physical	26186194
MET17_HUMAN	METTL17	physical	26186194
RL10A_HUMAN	RPL10A	physical	26186194
DKC1_HUMAN	DKC1	physical	26186194
RENT1_HUMAN	UPF1	physical	26186194
STAU2_HUMAN	STAU2	physical	26186194
STAU1_HUMAN	STAU1	physical	26186194
PABP4_HUMAN	PABPC4	physical	26186194
DHX30_HUMAN	DHX30	physical	26186194
ELAV2_HUMAN	ELAVL2	physical	26186194
ZSC25_HUMAN	ZSCAN25	physical	26186194
HP1B3_HUMAN	HP1BP3	physical	26186194
DDX27_HUMAN	DDX27	physical	26186194
TRUB2_HUMAN	TRUB2	physical	26186194
NOP14_HUMAN	NOP14	physical	26186194
RS3A_HUMAN	RPS3A	physical	26186194
RS5_HUMAN	RPS5	physical	26186194
KRI1_HUMAN	KRI1	physical	26186194
MOV10_HUMAN	MOV10	physical	26186194
CG050_HUMAN	C7orf50	physical	26186194
ZCRB1_HUMAN	ZCRB1	physical	26186194
ZCCHV_HUMAN	ZC3HAV1	physical	26186194
RL1D1_HUMAN	RSL1D1	physical	26186194
UTP23_HUMAN	UTP23	physical	26186194
ZCHC3_HUMAN	ZCCHC3	physical	26186194
RBM19_HUMAN	RBM19	physical	26186194
DHX57_HUMAN	DHX57	physical	26186194
SURF6_HUMAN	SURF6	physical	26186194
NOG1_HUMAN	GTPBP4	physical	26186194
LARP1_HUMAN	LARP1	physical	26186194
SYFM_HUMAN	FARS2	physical	26186194
PTCD1_HUMAN	PTCD1	physical	26186194
CTCF_HUMAN	CTCF	physical	26186194
RL36L_HUMAN	RPL36AL	physical	26186194
MK67I_HUMAN	NIFK	physical	26186194
RS15_HUMAN	RPS15	physical	26186194
RBM34_HUMAN	RBM34	physical	26186194
LN28B_HUMAN	LIN28B	physical	26186194
GLE1_HUMAN	GLE1	physical	26186194
RSBN1_HUMAN	RSBN1	physical	26186194
NOC4L_HUMAN	NOC4L	physical	26186194
ZC3H8_HUMAN	ZC3H8	physical	26186194
PARN_HUMAN	PARN	physical	26186194
RRS1_HUMAN	RRS1	physical	26186194
KRR1_HUMAN	KRR1	physical	26186194
RSSA_HUMAN	RPSA	physical	26186194
NOG2_HUMAN	GNL2	physical	26186194
ZN771_HUMAN	ZNF771	physical	26186194
NMNA1_HUMAN	NMNAT1	physical	26186194
UIF_HUMAN	FYTTD1	physical	26186194
RBMS1_HUMAN	RBMS1	physical	26186194
PRD15_HUMAN	PRDM15	physical	26186194
RPF2_HUMAN	RPF2	physical	26186194
LIN41_HUMAN	TRIM71	physical	26186194
NGDN_HUMAN	NGDN	physical	26186194
NSA2_HUMAN	NSA2	physical	26186194
CI114_HUMAN	C9orf114	physical	26186194
ZNF22_HUMAN	ZNF22	physical	26186194
NOL12_HUMAN	NOL12	physical	26186194
ZN189_HUMAN	ZNF189	physical	26186194
TOE1_HUMAN	TOE1	physical	26186194
H2A2B_HUMAN	HIST2H2AB	physical	26186194
SREK1_HUMAN	SREK1	physical	26186194
ZNF48_HUMAN	ZNF48	physical	26186194
TPPP_HUMAN	TPPP	physical	26186194
NHP2_HUMAN	NHP2	physical	26186194
STAU1_HUMAN	STAU1	physical	28514442
PUM3_HUMAN	KIAA0020	physical	28514442
YBOX2_HUMAN	YBX2	physical	28514442
RRP8_HUMAN	RRP8	physical	28514442
RL36L_HUMAN	RPL36AL	physical	28514442
LIN41_HUMAN	TRIM71	physical	28514442
NOP14_HUMAN	NOP14	physical	28514442
NOC4L_HUMAN	NOC4L	physical	28514442
TPPP_HUMAN	TPPP	physical	28514442
RSSA_HUMAN	RPSA	physical	28514442
DHX57_HUMAN	DHX57	physical	28514442
NMNA1_HUMAN	NMNAT1	physical	28514442
SYFM_HUMAN	FARS2	physical	28514442
RS15_HUMAN	RPS15	physical	28514442
ZCCHV_HUMAN	ZC3HAV1	physical	28514442
DDX24_HUMAN	DDX24	physical	28514442
ZSC25_HUMAN	ZSCAN25	physical	28514442
ZN189_HUMAN	ZNF189	physical	28514442
RBMS1_HUMAN	RBMS1	physical	28514442
STAU2_HUMAN	STAU2	physical	28514442
RRP12_HUMAN	RRP12	physical	28514442
ZC3H8_HUMAN	ZC3H8	physical	28514442
GLE1_HUMAN	GLE1	physical	28514442
MOV10_HUMAN	MOV10	physical	28514442
TOE1_HUMAN	TOE1	physical	28514442
RBM19_HUMAN	RBM19	physical	28514442
SURF6_HUMAN	SURF6	physical	28514442
PARN_HUMAN	PARN	physical	28514442
ZNF22_HUMAN	ZNF22	physical	28514442
ELAV2_HUMAN	ELAVL2	physical	28514442
LARP1_HUMAN	LARP1	physical	28514442
LARP7_HUMAN	LARP7	physical	28514442
DHX30_HUMAN	DHX30	physical	28514442
RS5_HUMAN	RPS5	physical	28514442
ZN771_HUMAN	ZNF771	physical	28514442
RBM34_HUMAN	RBM34	physical	28514442
RS3_HUMAN	RPS3	physical	28514442
RENT1_HUMAN	UPF1	physical	28514442
RS2_HUMAN	RPS2	physical	28514442
TRUB2_HUMAN	TRUB2	physical	28514442
CI114_HUMAN	C9orf114	physical	28514442
ZN668_HUMAN	ZNF668	physical	28514442
NOG1_HUMAN	GTPBP4	physical	28514442
UTP23_HUMAN	UTP23	physical	28514442
ZNF48_HUMAN	ZNF48	physical	28514442
ZNF70_HUMAN	ZNF70	physical	28514442
PRD15_HUMAN	PRDM15	physical	28514442
RPF2_HUMAN	RPF2	physical	28514442
ZN574_HUMAN	ZNF574	physical	28514442
RS10_HUMAN	RPS10	physical	28514442
H2A2B_HUMAN	HIST2H2AB	physical	28514442
NOL12_HUMAN	NOL12	physical	28514442
NOG2_HUMAN	GNL2	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 H11_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-88, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-162, AND MASSSPECTROMETRY.	17287340 [Abstract]

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