dbPTM

H15_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H15_MOUSE
UniProt AC	P43276
Protein Name	Histone H1.5
Gene Name	Hist1h1b
Organism	Mus musculus (Mouse).
Sequence Length	223
Subcellular Localization	Nucleus. Chromosome. Mainly localizes in 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	MSETAPAETAAPAPVEKSPAKKKTTKKAGAAKRKATGPPVSELITKAVSASKERGGVSLPALKKALAAGGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKTGAAKAKKPAGATPKKPKKTAGAKKTVKKTPKKAKKPAAAGVKKVAKSPKKAKAAAKPKKAAKSPAKPKAVKSKASKPKVTKPKTAKPKAAKAKKAVSKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSETAPAET ------CCCCCCCCC	43.59	27087446
2	Acetylation	------MSETAPAET ------CCCCCCCCC	43.59	23806337
4	Phosphorylation	----MSETAPAETAA ----CCCCCCCCCCC	30.54	26824392
9	Phosphorylation	SETAPAETAAPAPVE CCCCCCCCCCCCCCC	30.17	23527152
17	Acetylation	AAPAPVEKSPAKKKT CCCCCCCCCCCCCCC	63.07	23806337
17	Ubiquitination	AAPAPVEKSPAKKKT CCCCCCCCCCCCCCC	63.07	-
17	Succinylation	AAPAPVEKSPAKKKT CCCCCCCCCCCCCCC	63.07	23806337
18	Phosphorylation	APAPVEKSPAKKKTT CCCCCCCCCCCCCCC	19.31	27087446
21	Methylation	PVEKSPAKKKTTKKA CCCCCCCCCCCCCCH	59.18	-
22	Methylation	VEKSPAKKKTTKKAG CCCCCCCCCCCCCHH	58.41	-
22	"N6,N6-dimethyllysine"	VEKSPAKKKTTKKAG CCCCCCCCCCCCCHH	58.41	-
23	Methylation	EKSPAKKKTTKKAGA CCCCCCCCCCCCHHH	61.80	-
26	Acetylation	PAKKKTTKKAGAAKR CCCCCCCCCHHHHHH	45.95	-
26	Methylation	PAKKKTTKKAGAAKR CCCCCCCCCHHHHHH	45.95	-
27	Methylation	AKKKTTKKAGAAKRK CCCCCCCCHHHHHHH	50.38	-
34	Succinylation	KAGAAKRKATGPPVS CHHHHHHHCCCCCHH	49.98	23806337
34	Other	KAGAAKRKATGPPVS CHHHHHHHCCCCCHH	49.98	-
34	Ubiquitination	KAGAAKRKATGPPVS CHHHHHHHCCCCCHH	49.98	-
34	Methylation	KAGAAKRKATGPPVS CHHHHHHHCCCCCHH	49.98	-
34	Acetylation	KAGAAKRKATGPPVS CHHHHHHHCCCCCHH	49.98	23806337
34	Succinylation	KAGAAKRKATGPPVS CHHHHHHHCCCCCHH	49.98	-
36	Phosphorylation	GAAKRKATGPPVSEL HHHHHHCCCCCHHHH	53.94	28833060
41	Phosphorylation	KATGPPVSELITKAV HCCCCCHHHHHHHHH	32.24	28833060
46	Acetylation	PVSELITKAVSASKE CHHHHHHHHHHHHHH	39.53	23806337
46	Ubiquitination	PVSELITKAVSASKE CHHHHHHHHHHHHHH	39.53	22790023
49	Phosphorylation	ELITKAVSASKERGG HHHHHHHHHHHHHCC	31.52	22817900
51	Phosphorylation	ITKAVSASKERGGVS HHHHHHHHHHHCCCC	27.78	26026062
52	Acetylation	TKAVSASKERGGVSL HHHHHHHHHHCCCCH	51.66	7296751
52	Ubiquitination	TKAVSASKERGGVSL HHHHHHHHHHCCCCH	51.66	-
52	Other	TKAVSASKERGGVSL HHHHHHHHHHCCCCH	51.66	-
54	Citrullination	AVSASKERGGVSLPA HHHHHHHHCCCCHHH	51.40	24463520
54	Citrullination	AVSASKERGGVSLPA HHHHHHHHCCCCHHH	51.40	-
58	Phosphorylation	SKERGGVSLPALKKA HHHHCCCCHHHHHHH	31.73	29176673
63	Succinylation	GVSLPALKKALAAGG CCCHHHHHHHHHCCC	37.80	23806337
63	Acetylation	GVSLPALKKALAAGG CCCHHHHHHHHHCCC	37.80	23806337
64	Succinylation	VSLPALKKALAAGGY CCHHHHHHHHHCCCC	49.86	23806337
64	Ubiquitination	VSLPALKKALAAGGY CCHHHHHHHHHCCCC	49.86	27667366
64	Other	VSLPALKKALAAGGY CCHHHHHHHHHCCCC	49.86	-
64	Acetylation	VSLPALKKALAAGGY CCHHHHHHHHHCCCC	49.86	23806337
75	Ubiquitination	AGGYDVEKNNSRIKL CCCCCCCCCCCCEEE	62.37	22790023
75	Acetylation	AGGYDVEKNNSRIKL CCCCCCCCCCCCEEE	62.37	23806337
78	Phosphorylation	YDVEKNNSRIKLGLK CCCCCCCCCEEEHHH	44.79	29176673
85	Ubiquitination	SRIKLGLKSLVSKGT CCEEEHHHHHHHCCC	39.69	27667366
85	Other	SRIKLGLKSLVSKGT CCEEEHHHHHHHCCC	39.69	-
86	Phosphorylation	RIKLGLKSLVSKGTL CEEEHHHHHHHCCCE	38.76	24704852
89	Phosphorylation	LGLKSLVSKGTLVQT EHHHHHHHCCCEEEE	30.57	29176673
90	Acetylation	GLKSLVSKGTLVQTK HHHHHHHCCCEEEEC	48.73	7760121
90	Ubiquitination	GLKSLVSKGTLVQTK HHHHHHHCCCEEEEC	48.73	27667366
90	Other	GLKSLVSKGTLVQTK HHHHHHHCCCEEEEC	48.73	-
92	Phosphorylation	KSLVSKGTLVQTKGT HHHHHCCCEEEECCC	27.74	27600695
97	Succinylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	-
97	Ubiquitination	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	27667366
99	Phosphorylation	TLVQTKGTGASGSFK CEEEECCCCCCCCEE	31.00	29899451
102	Phosphorylation	QTKGTGASGSFKLNK EECCCCCCCCEECCC	35.99	26824392
104	Phosphorylation	KGTGASGSFKLNKKA CCCCCCCCEECCCCC	19.40	25521595
106	Ubiquitination	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	27667366
106	Other	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	-
106	Acetylation	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	22648157
109	Ubiquitination	SGSFKLNKKAASGEA CCCEECCCCCCCCCC	54.98	-
117	Acetylation	KAASGEAKPKAKKTG CCCCCCCCCCHHHCC	42.63	7616619
119	Acetylation	ASGEAKPKAKKTGAA CCCCCCCCHHHCCCC	72.61	7616629
135	Phosphorylation	AKKPAGATPKKPKKT CCCCCCCCCCCCCCC	34.42	26824392
147	Acetylation	KKTAGAKKTVKKTPK CCCCCCCCCCCCCCH	59.00	19853439
151	Acetylation	GAKKTVKKTPKKAKK CCCCCCCCCCHHCCC	66.77	19853447
152	Phosphorylation	AKKTVKKTPKKAKKP CCCCCCCCCHHCCCC	34.32	-
158	Acetylation	KTPKKAKKPAAAGVK CCCHHCCCCHHHCHH	44.76	17043054
165	Acetylation	KPAAAGVKKVAKSPK CCHHHCHHHHHCCHH	40.38	17043054
166	Acetylation	PAAAGVKKVAKSPKK CHHHCHHHHHCCHHH	45.05	20612021
170	Phosphorylation	GVKKVAKSPKKAKAA CHHHHHCCHHHHHHH	32.01	23684622
185	Methylation	AKPKKAAKSPAKPKA HCCHHHCCCCCCCHH	62.93	-
186	Phosphorylation	KPKKAAKSPAKPKAV CCHHHCCCCCCCHHH	25.93	18779572

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
Oops, there are no upstream regulatory protein records of H15_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
54	R	Citrullination		24463520
Citrullination at Arg-54 (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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of H15_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of H15_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION ATSER-18, AND MASS SPECTROMETRY.	16452087 [Abstract]
Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION ATSER-18, AND MASS SPECTROMETRY.	16452087 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4, AND MASSSPECTROMETRY.	17242355 [Abstract]

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