dbPTM

H15_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H15_HUMAN
UniProt AC	P16401
Protein Name	Histone H1.5
Gene Name	HIST1H1B
Organism	Homo sapiens (Human).
Sequence Length	226
Subcellular Localization	Nucleus. Chromosome. According to PubMed:15911621 more commonly found in heterochromatin. According to PubMed:10997781 associates with actively transcribed chromatin and not heterochromatin.
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	MSETAPAETATPAPVEKSPAKKKATKKAAGAGAAKRKATGPPVSELITKAVAASKERNGLSLAALKKALAAGGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGATPKKAKKAAGAKKAVKKTPKKAKKPAAAGVKKVAKSPKKAKAAAKPKKATKSPAKPKAVKPKAAKPKAAKPKAAKPKAAKAKKAAAKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSETAPAET ------CCCCCCCCC	43.59	19691289
2	Phosphorylation	------MSETAPAET ------CCCCCCCCC	43.59	29255136
4	Phosphorylation	----MSETAPAETAT ----CCCCCCCCCCC	30.54	29255136
9	Phosphorylation	SETAPAETATPAPVE CCCCCCCCCCCCCCC	37.63	29255136
11	Phosphorylation	TAPAETATPAPVEKS CCCCCCCCCCCCCCC	27.66	29255136
17	Acetylation	ATPAPVEKSPAKKKA CCCCCCCCCHHHHHH	63.07	17043054
17	Malonylation	ATPAPVEKSPAKKKA CCCCCCCCCHHHHHH	63.07	26320211
17	Ubiquitination	ATPAPVEKSPAKKKA CCCCCCCCCHHHHHH	63.07	33845483
18	Phosphorylation	TPAPVEKSPAKKKAT CCCCCCCCHHHHHHH	19.31	29255136
21	Ubiquitination	PVEKSPAKKKATKKA CCCCCHHHHHHHHHH	59.18	22505724
22	Ubiquitination	VEKSPAKKKATKKAA CCCCHHHHHHHHHHH	50.15	-
23	Acetylation	EKSPAKKKATKKAAG CCCHHHHHHHHHHHC	61.66	20687029
25	Phosphorylation	SPAKKKATKKAAGAG CHHHHHHHHHHHCCH	41.79	26074081
26	Acetylation	PAKKKATKKAAGAGA HHHHHHHHHHHCCHH	45.32	15469825
26	Methylation	PAKKKATKKAAGAGA HHHHHHHHHHHCCHH	45.32	15469825
27	Lactylation	AKKKATKKAAGAGAA HHHHHHHHHHCCHHH	38.83	31645732
27	Methylation	AKKKATKKAAGAGAA HHHHHHHHHHCCHHH	38.83	19552482
35	2-Hydroxyisobutyrylation	AAGAGAAKRKATGPP HHCCHHHHHHCCCCC	54.63	-
35	Acetylation	AAGAGAAKRKATGPP HHCCHHHHHHCCCCC	54.63	7664325
35	Ubiquitination	AAGAGAAKRKATGPP HHCCHHHHHHCCCCC	54.63	22817900
37	"N6,N6-dimethyllysine"	GAGAAKRKATGPPVS CCHHHHHHCCCCCHH	49.98	-
37	Acetylation	GAGAAKRKATGPPVS CCHHHHHHCCCCCHH	49.98	26051181
37	Lactylation	GAGAAKRKATGPPVS CCHHHHHHCCCCCHH	49.98	31645732
37	Malonylation	GAGAAKRKATGPPVS CCHHHHHHCCCCCHH	49.98	26320211
37	Methylation	GAGAAKRKATGPPVS CCHHHHHHCCCCCHH	49.98	-
37	Other	GAGAAKRKATGPPVS CCHHHHHHCCCCCHH	49.98	-
37	Succinylation	GAGAAKRKATGPPVS CCHHHHHHCCCCCHH	49.98	-
37	Ubiquitination	GAGAAKRKATGPPVS CCHHHHHHCCCCCHH	49.98	22817900
39	Phosphorylation	GAAKRKATGPPVSEL HHHHHHCCCCCHHHH	53.94	23911959
44	Phosphorylation	KATGPPVSELITKAV HCCCCCHHHHHHHHH	32.24	23911959
48	Phosphorylation	PPVSELITKAVAASK CCHHHHHHHHHHHHH	26.10	26074081
49	2-Hydroxyisobutyrylation	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	-
49	Acetylation	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	25953088
49	Ubiquitination	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	23000965
54	Phosphorylation	ITKAVAASKERNGLS HHHHHHHHHHHCCCC	25.88	26546556
55	Acetylation	TKAVAASKERNGLSL HHHHHHHHHHCCCCH	56.84	7296747
55	Other	TKAVAASKERNGLSL HHHHHHHHHHCCCCH	56.84	-
55	Ubiquitination	TKAVAASKERNGLSL HHHHHHHHHHCCCCH	56.84	23000965
57	Citrullination	AVAASKERNGLSLAA HHHHHHHHCCCCHHH	46.37	-
57	Citrullination	AVAASKERNGLSLAA HHHHHHHHCCCCHHH	46.37	-
61	Phosphorylation	SKERNGLSLAALKKA HHHHCCCCHHHHHHH	19.84	19691289
66	2-Hydroxyisobutyrylation	GLSLAALKKALAAGG CCCHHHHHHHHHCCC	31.13	-
66	Acetylation	GLSLAALKKALAAGG CCCHHHHHHHHHCCC	31.13	25953088
66	Succinylation	GLSLAALKKALAAGG CCCHHHHHHHHHCCC	31.13	23954790
66	Ubiquitination	GLSLAALKKALAAGG CCCHHHHHHHHHCCC	31.13	22817900
67	2-Hydroxyisobutyrylation	LSLAALKKALAAGGY CCHHHHHHHHHCCCC	49.86	-
67	Acetylation	LSLAALKKALAAGGY CCHHHHHHHHHCCCC	49.86	26051181
67	Other	LSLAALKKALAAGGY CCHHHHHHHHHCCCC	49.86	-
67	Ubiquitination	LSLAALKKALAAGGY CCHHHHHHHHHCCCC	49.86	21906983
74	Nitration	KALAAGGYDVEKNNS HHHHCCCCCCCCCCC	18.85	-
74	Phosphorylation	KALAAGGYDVEKNNS HHHHCCCCCCCCCCC	18.85	22817900
78	2-Hydroxyisobutyrylation	AGGYDVEKNNSRIKL CCCCCCCCCCCCEEE	62.37	-
78	Acetylation	AGGYDVEKNNSRIKL CCCCCCCCCCCCEEE	62.37	23954790
78	Malonylation	AGGYDVEKNNSRIKL CCCCCCCCCCCCEEE	62.37	26320211
78	Ubiquitination	AGGYDVEKNNSRIKL CCCCCCCCCCCCEEE	62.37	21906983
81	Phosphorylation	YDVEKNNSRIKLGLK CCCCCCCCCEEEHHH	44.79	28634120
84	Ubiquitination	EKNNSRIKLGLKSLV CCCCCCEEEHHHHHH	35.08	23000965
88	Acetylation	SRIKLGLKSLVSKGT CCEEEHHHHHHHCCC	39.69	17043054
88	Other	SRIKLGLKSLVSKGT CCEEEHHHHHHHCCC	39.69	-
88	Ubiquitination	SRIKLGLKSLVSKGT CCEEEHHHHHHHCCC	39.69	23000965
89	Phosphorylation	RIKLGLKSLVSKGTL CEEEHHHHHHHCCCE	38.76	20860994
92	Phosphorylation	LGLKSLVSKGTLVQT EHHHHHHHCCCEEEE	30.57	17877366
93	Acetylation	GLKSLVSKGTLVQTK HHHHHHHCCCEEEEC	48.73	7692537
93	Other	GLKSLVSKGTLVQTK HHHHHHHCCCEEEEC	48.73	-
93	Ubiquitination	GLKSLVSKGTLVQTK HHHHHHHCCCEEEEC	48.73	23000965
95	Phosphorylation	KSLVSKGTLVQTKGT HHHHHCCCEEEECCC	27.74	17877366
99	Phosphorylation	SKGTLVQTKGTGASG HCCCEEEECCCCCCC	24.78	28111955
100	Succinylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	-
100	Ubiquitination	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	23000965
102	Phosphorylation	TLVQTKGTGASGSFK CEEEECCCCCCCCEE	31.00	26657352
105	Phosphorylation	QTKGTGASGSFKLNK EECCCCCCCCEECCC	35.99	25159151
107	Phosphorylation	KGTGASGSFKLNKKA CCCCCCCCEECCCCC	19.40	23401153
109	Acetylation	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	22648155
109	Other	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	-
109	Ubiquitination	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	27667366
112	Ubiquitination	SGSFKLNKKAASGEA CCCEECCCCCCCCCC	54.98	22817900
113	Ubiquitination	GSFKLNKKAASGEAK CCEECCCCCCCCCCC	48.38	21906983
116	Phosphorylation	KLNKKAASGEAKPKA ECCCCCCCCCCCHHH	41.86	26657352
120	Ubiquitination	KAASGEAKPKAKKAG CCCCCCCCHHHHHHC	42.63	21906983
122	Ubiquitination	ASGEAKPKAKKAGAA CCCCCCHHHHHHCHH	72.61	29967540
132	Acetylation	KAGAAKAKKPAGATP HHCHHHCCCCCCCCH	59.59	30584587
132	Ubiquitination	KAGAAKAKKPAGATP HHCHHHCCCCCCCCH	59.59	25015289
133	Acetylation	AGAAKAKKPAGATPK HCHHHCCCCCCCCHH	44.98	30584593
133	Ubiquitination	AGAAKAKKPAGATPK HCHHHCCCCCCCCHH	44.98	33845483
138	Phosphorylation	AKKPAGATPKKAKKA CCCCCCCCHHHHHHH	34.42	22167270
140	Acetylation	KPAGATPKKAKKAAG CCCCCCHHHHHHHHC	62.09	7369411
140	Ubiquitination	KPAGATPKKAKKAAG CCCCCCHHHHHHHHC	62.09	25015289
141	Ubiquitination	PAGATPKKAKKAAGA CCCCCHHHHHHHHCC	67.64	25015289
143	Acetylation	GATPKKAKKAAGAKK CCCHHHHHHHHCCHH	52.39	24431093
144	Acetylation	ATPKKAKKAAGAKKA CCHHHHHHHHCCHHH	48.61	24431101
149	Acetylation	AKKAAGAKKAVKKTP HHHHHCCHHHHHCCC	40.11	24431109
155	Phosphorylation	AKKAVKKTPKKAKKP CHHHHHCCCHHCCCC	34.32	16377619
157	Ubiquitination	KAVKKTPKKAKKPAA HHHHCCCHHCCCCHH	71.27	22817900
158	Acetylation	AVKKTPKKAKKPAAA HHHCCCHHCCCCHHH	67.64	17043054
158	Ubiquitination	AVKKTPKKAKKPAAA HHHCCCHHCCCCHHH	67.64	22817900
160	Acetylation	KKTPKKAKKPAAAGV HCCCHHCCCCHHHCH	69.07	25953088
160	Ubiquitination	KKTPKKAKKPAAAGV HCCCHHCCCCHHHCH	69.07	22817900
161	Ubiquitination	KTPKKAKKPAAAGVK CCCHHCCCCHHHCHH	44.76	21906983
168	2-Hydroxyisobutyrylation	KPAAAGVKKVAKSPK CCHHHCHHHHHCCHH	40.38	-
168	Acetylation	KPAAAGVKKVAKSPK CCHHHCHHHHHCCHH	40.38	19608861
168	Lactylation	KPAAAGVKKVAKSPK CCHHHCHHHHHCCHH	40.38	31645732
168	Ubiquitination	KPAAAGVKKVAKSPK CCHHHCHHHHHCCHH	40.38	22817900
169	Methylation	PAAAGVKKVAKSPKK CHHHCHHHHHCCHHH	45.05	17043054
169	Ubiquitination	PAAAGVKKVAKSPKK CHHHCHHHHHCCHHH	45.05	22817900
172	Ubiquitination	AGVKKVAKSPKKAKA HCHHHHHCCHHHHHH	70.99	22817900
173	Phosphorylation	GVKKVAKSPKKAKAA CHHHHHCCHHHHHHH	32.01	30278072
185	Ubiquitination	KAAAKPKKATKSPAK HHHHCCCCCCCCCCC	70.57	25015289
187	Phosphorylation	AAKPKKATKSPAKPK HHCCCCCCCCCCCCC	40.72	28176443
188	Lactylation	AKPKKATKSPAKPKA HCCCCCCCCCCCCCC	60.34	31645732
188	Methylation	AKPKKATKSPAKPKA HCCCCCCCCCCCCCC	60.34	-
188	Ubiquitination	AKPKKATKSPAKPKA HCCCCCCCCCCCCCC	60.34	25015289
189	Phosphorylation	KPKKATKSPAKPKAV CCCCCCCCCCCCCCC	26.24	28176443
192	Ubiquitination	KATKSPAKPKAVKPK CCCCCCCCCCCCCCC	50.89	25015289
194	Ubiquitination	TKSPAKPKAVKPKAA CCCCCCCCCCCCCCC	66.17	25015289
197	Ubiquitination	PAKPKAVKPKAAKPK CCCCCCCCCCCCCCC	45.73	25015289
199	Acetylation	KPKAVKPKAAKPKAA CCCCCCCCCCCCCCC	56.08	19608861
199	Ubiquitination	KPKAVKPKAAKPKAA CCCCCCCCCCCCCCC	56.08	25015289
202	Acetylation	AVKPKAAKPKAAKPK CCCCCCCCCCCCCCC	52.49	19608861
202	Ubiquitination	AVKPKAAKPKAAKPK CCCCCCCCCCCCCCC	52.49	25015289
204	Acetylation	KPKAAKPKAAKPKAA CCCCCCCCCCCCCCC	61.34	19608861
204	Ubiquitination	KPKAAKPKAAKPKAA CCCCCCCCCCCCCCC	61.34	25015289
207	Ubiquitination	AAKPKAAKPKAAKPK CCCCCCCCCCCCCHH	52.49	25015289
209	Acetylation	KPKAAKPKAAKPKAA CCCCCCCCCCCHHHH	61.34	-
209	Ubiquitination	KPKAAKPKAAKPKAA CCCCCCCCCCCHHHH	61.34	25015289
212	Ubiquitination	AAKPKAAKPKAAKAK CCCCCCCCHHHHHHH	52.49	25015289
214	Ubiquitination	KPKAAKPKAAKAKKA CCCCCCHHHHHHHHH	61.34	25015289

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
11	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
11	T	Phosphorylation	Kinase	GSK3	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	HUWE1	Q7Z6Z7	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
11	T	Phosphorylation	16377619
Phosphorylated at Thr-11 by GSK3B during mitosis in prometaphase and dephosphorylated in telophase.
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 H15_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FOXP3_HUMAN	FOXP3	physical	21654845
CUL5_HUMAN	CUL5	physical	22863883
CYHR1_HUMAN	CYHR1	physical	22863883
NMI_HUMAN	NMI	physical	22863883
GLYM_HUMAN	SHMT2	physical	22863883

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 H15_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-93; LYS-109; LYS-168 ANDLYS-209, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-18, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; SER-18 AND THR-39,AND MASS SPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-11; SER-18;THR-39; SER-44; THR-187 AND SER-189, AND MASS SPECTROMETRY.	19007248 [Abstract]
"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 SER-107, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4 AND SER-18, AND MASSSPECTROMETRY.	16083285 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138, AND MASSSPECTROMETRY.	17081983 [Abstract]

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