dbPTM

H14_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H14_MOUSE
UniProt AC	P43274
Protein Name	Histone H1.4
Gene Name	Hist1h1e
Organism	Mus musculus (Mouse).
Sequence Length	219
Subcellular Localization	Nucleus. Chromosome. Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus..
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..
Protein Sequence	MSETAPAAPAAPAPAEKTPVKKKARKAAGGAKRKTSGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKRAGAAKAKKPAGAAKKPKKAAGTATAKKSTKKTPKKAKKPAAAAGAKKAKSPKKAKATKAKKAPKSPAKAKTVKPKAAKPKTSKPKAAKPKKTAAKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSETAPAAP ------CCCCCCCCC	43.59	23806337
2	Phosphorylation	------MSETAPAAP ------CCCCCCCCC	43.59	23527152
4	Phosphorylation	----MSETAPAAPAA ----CCCCCCCCCCC	30.54	23527152
17	Malonylation	AAPAPAEKTPVKKKA CCCCCCCCCCCHHHH	61.30	26320211
17	Methylation	AAPAPAEKTPVKKKA CCCCCCCCCCCHHHH	61.30	-
17	Acetylation	AAPAPAEKTPVKKKA CCCCCCCCCCCHHHH	61.30	23806337
17	"N6,N6-dimethyllysine"	AAPAPAEKTPVKKKA CCCCCCCCCCCHHHH	61.30	-
17	Ubiquitination	AAPAPAEKTPVKKKA CCCCCCCCCCCHHHH	61.30	-
18	Phosphorylation	APAPAEKTPVKKKAR CCCCCCCCCCHHHHH	25.48	26824392
21	Acetylation	PAEKTPVKKKARKAA CCCCCCCHHHHHHHH	50.16	19737024
21	"N6,N6-dimethyllysine"	PAEKTPVKKKARKAA CCCCCCCHHHHHHHH	50.16	-
21	Methylation	PAEKTPVKKKARKAA CCCCCCCHHHHHHHH	50.16	-
22	Methylation	AEKTPVKKKARKAAG CCCCCCHHHHHHHHC	52.48	-
22	"N6,N6-dimethyllysine"	AEKTPVKKKARKAAG CCCCCCHHHHHHHHC	52.48	-
23	Acetylation	EKTPVKKKARKAAGG CCCCCHHHHHHHHCC	47.94	19854271
23	Methylation	EKTPVKKKARKAAGG CCCCCHHHHHHHHCC	47.94	-
23	"N6,N6-dimethyllysine"	EKTPVKKKARKAAGG CCCCCHHHHHHHHCC	47.94	-
26	Acetylation	PVKKKARKAAGGAKR CCHHHHHHHHCCCCC	47.66	19853925
26	Methylation	PVKKKARKAAGGAKR CCHHHHHHHHCCCCC	47.66	-
32	Acetylation	RKAAGGAKRKTSGPP HHHHCCCCCCCCCCC	58.67	19737024
34	Succinylation	AAGGAKRKTSGPPVS HHCCCCCCCCCCCHH	46.46	-
34	Methylation	AAGGAKRKTSGPPVS HHCCCCCCCCCCCHH	46.46	-
34	Other	AAGGAKRKTSGPPVS HHCCCCCCCCCCCHH	46.46	-
34	Ubiquitination	AAGGAKRKTSGPPVS HHCCCCCCCCCCCHH	46.46	27667366
34	Succinylation	AAGGAKRKTSGPPVS HHCCCCCCCCCCCHH	46.46	23806337
34	Malonylation	AAGGAKRKTSGPPVS HHCCCCCCCCCCCHH	46.46	26320211
34	Acetylation	AAGGAKRKTSGPPVS HHCCCCCCCCCCCHH	46.46	23806337
35	Phosphorylation	AGGAKRKTSGPPVSE HCCCCCCCCCCCHHH	42.84	26824392
36	Phosphorylation	GGAKRKTSGPPVSEL CCCCCCCCCCCHHHH	52.95	27087446
41	Phosphorylation	KTSGPPVSELITKAV CCCCCCHHHHHHHHH	32.24	23984901
45	Phosphorylation	PPVSELITKAVAASK CCHHHHHHHHHHHCH	26.10	25619855
46	Succinylation	PVSELITKAVAASKE CHHHHHHHHHHHCHH	33.59	-
46	Ubiquitination	PVSELITKAVAASKE CHHHHHHHHHHHCHH	33.59	22790023
46	Acetylation	PVSELITKAVAASKE CHHHHHHHHHHHCHH	33.59	-
52	Other	TKAVAASKERSGVSL HHHHHHCHHCCCCCH	53.04	-
52	Ubiquitination	TKAVAASKERSGVSL HHHHHHCHHCCCCCH	53.04	-
52	Acetylation	TKAVAASKERSGVSL HHHHHHCHHCCCCCH	53.04	7296731
54	Citrullination	AVAASKERSGVSLAA HHHHCHHCCCCCHHH	42.31	-
54	Citrullination	AVAASKERSGVSLAA HHHHCHHCCCCCHHH	42.31	24463520
55	Phosphorylation	VAASKERSGVSLAAL HHHCHHCCCCCHHHH	44.64	24899341
58	Phosphorylation	SKERSGVSLAALKKA CHHCCCCCHHHHHHH	18.80	26745281
63	Acetylation	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	163869
63	Ubiquitination	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	22790023
63	Malonylation	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	26320211
64	Malonylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	26320211
64	Ubiquitination	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	22790023
64	Other	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	-
71	Phosphorylation	KALAAAGYDVEKNNS HHHHHCCCCCHHCCC	16.46	26026062
75	Acetylation	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	158553
75	Ubiquitination	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	22790023
78	Phosphorylation	YDVEKNNSRIKLGLK CCCHHCCCCCCCCHH	44.79	29176673
85	Other	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	-
85	Ubiquitination	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	22790023
85	Malonylation	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	26320211
85	Acetylation	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	17043054
86	Phosphorylation	RIKLGLKSLVSKGTL CCCCCHHHHHHCCCE	38.76	24704852
89	Phosphorylation	LGLKSLVSKGTLVQT CCHHHHHHCCCEEEE	30.57	29176673
90	Other	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	-
90	Ubiquitination	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	27667366
90	Malonylation	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	26320211
90	Acetylation	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	22826441
90	Succinylation	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	-
92	Phosphorylation	KSLVSKGTLVQTKGT HHHHHCCCEEEECCC	27.74	27600695
97	Succinylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	-
97	Acetylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	23806337
97	Malonylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	26320211
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	Acetylation	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	22641363
106	Other	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	-
106	Malonylation	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	26073543
106	Ubiquitination	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	27667366
109	Ubiquitination	SGSFKLNKKAASGEA CCCEECCCCCCCCCC	54.98	-
127	Acetylation	AKRAGAAKAKKPAGA HHHHCHHHCCCCCCC	61.27	19737024
129	Acetylation	RAGAAKAKKPAGAAK HHCHHHCCCCCCCCC	59.59	163873
130	Acetylation	AGAAKAKKPAGAAKK HCHHHCCCCCCCCCC	44.98	163877
136	Acetylation	KKPAGAAKKPKKAAG CCCCCCCCCCCCCCC	69.90	19737024
137	Acetylation	KPAGAAKKPKKAAGT CCCCCCCCCCCCCCC	58.29	19737024
146	Phosphorylation	KKAAGTATAKKSTKK CCCCCCCCCCCCCCC	38.56	-
149	Acetylation	AGTATAKKSTKKTPK CCCCCCCCCCCCCCH	61.98	19737024
150	ADP-ribosylation	GTATAKKSTKKTPKK CCCCCCCCCCCCCHH	44.76	-
154	Phosphorylation	AKKSTKKTPKKAKKP CCCCCCCCCHHHCCH	41.73	18779572
159	Acetylation	KKTPKKAKKPAAAAG CCCCHHHCCHHHHHC	69.07	17043054
160	Acetylation	KTPKKAKKPAAAAGA CCCHHHCCHHHHHCH	44.76	19737024
168	Acetylation	PAAAAGAKKAKSPKK HHHHHCHHHCCCHHH	52.96	23864654
172	Phosphorylation	AGAKKAKSPKKAKAT HCHHHCCCHHHHHHH	46.97	-
186	Methylation	TKAKKAPKSPAKAKT HHCCCCCCCCCCCCC	74.14	-
187	Phosphorylation	KAKKAPKSPAKAKTV HCCCCCCCCCCCCCC	29.09	26824392
192	Acetylation	PKSPAKAKTVKPKAA CCCCCCCCCCCCCCC	53.82	23201123

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 H14_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
26	K	Acetylation	-
Acetylated at Lys-26.
26	K	Acetylation	-
Deacetylated at Lys-26 by SIRT1.
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 H14_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CBX1_MOUSE	Cbx1	physical	16127177
CBX5_MOUSE	Cbx5	physical	16127177

Drug and Disease Associations

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

Regulatory Network of H14_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, AND MASS SPECTROMETRY.	16452087 [Abstract]
Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASSSPECTROMETRY.	14729942 [Abstract]
"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 THR-18, AND MASSSPECTROMETRY.	19131326 [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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