dbPTM

H13_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H13_MOUSE
UniProt AC	P43277
Protein Name	Histone H1.3
Gene Name	Hist1h1d
Organism	Mus musculus (Mouse).
Sequence Length	221
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	MSETAPAAPAAPAPVEKTPVKKKAKKTGAAAGKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGAAKKPKKATGAATPKKTAKKTPKKAKKPAAAAGAKKVSKSPKKVKAAKPKKAAKSPAKAKAPKAKASKPKASKPKATKAKKAAPRKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSETAPAAP ------CCCCCCCCC	43.59	23527152
2	Acetylation	------MSETAPAAP ------CCCCCCCCC	43.59	23806337
4	Phosphorylation	----MSETAPAAPAA ----CCCCCCCCCCC	30.54	23527152
17	Ubiquitination	AAPAPVEKTPVKKKA CCCCCCCCCCCCHHH	59.36	-
17	Acetylation	AAPAPVEKTPVKKKA CCCCCCCCCCCCHHH	59.36	23806337
17	Malonylation	AAPAPVEKTPVKKKA CCCCCCCCCCCCHHH	59.36	26320211
18	Phosphorylation	APAPVEKTPVKKKAK CCCCCCCCCCCHHHH	21.58	26824392
23	Acetylation	EKTPVKKKAKKTGAA CCCCCCHHHHHHCCC	60.77	7385605
26	Acetylation	PVKKKAKKTGAAAGK CCCHHHHHHCCCCCC	57.98	7385603
27	Phosphorylation	VKKKAKKTGAAAGKR CCHHHHHHCCCCCCC	31.20	18779572
33	Acetylation	KTGAAAGKRKASGPP HHCCCCCCCCCCCCC	46.10	23864654
33	Other	KTGAAAGKRKASGPP HHCCCCCCCCCCCCC	46.10	27105115
35	Ubiquitination	GAAAGKRKASGPPVS CCCCCCCCCCCCCHH	50.84	22790023
35	Other	GAAAGKRKASGPPVS CCCCCCCCCCCCCHH	50.84	27105115
35	Malonylation	GAAAGKRKASGPPVS CCCCCCCCCCCCCHH	50.84	26320211
37	Phosphorylation	AAGKRKASGPPVSEL CCCCCCCCCCCHHHH	55.67	27087446
42	Phosphorylation	KASGPPVSELITKAV CCCCCCHHHHHHHHH	32.24	24068923
46	Phosphorylation	PPVSELITKAVAASK CCHHHHHHHHHHHHH	26.10	24068923
47	Ubiquitination	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	22790023
47	Acetylation	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	22641325
53	Acetylation	TKAVAASKERSGVSL HHHHHHHHHCCCCCH	53.04	7296761
53	Ubiquitination	TKAVAASKERSGVSL HHHHHHHHHCCCCCH	53.04	-
53	Other	TKAVAASKERSGVSL HHHHHHHHHCCCCCH	53.04	27105115
55	Citrullination	AVAASKERSGVSLAA HHHHHHHCCCCCHHH	42.31	-
55	Citrullination	AVAASKERSGVSLAA HHHHHHHCCCCCHHH	42.31	24463520
56	Phosphorylation	VAASKERSGVSLAAL HHHHHHCCCCCHHHH	44.64	24899341
59	Phosphorylation	SKERSGVSLAALKKA HHHCCCCCHHHHHHH	18.80	26745281
64	Acetylation	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	163889
64	Ubiquitination	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	-
65	Other	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	27105115
65	Ubiquitination	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	-
72	Phosphorylation	KALAAAGYDVEKNNS HHHHHCCCCCHHCCC	16.46	26026062
76	Acetylation	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	158557
76	Ubiquitination	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	-
79	Phosphorylation	YDVEKNNSRIKLGLK CCCHHCCCCCCCCHH	44.79	29176673
86	Other	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	27105115
86	Acetylation	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	-
86	Ubiquitination	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	-
87	Phosphorylation	RIKLGLKSLVSKGTL CCCCCHHHHHHCCCE	38.76	24704852
90	Phosphorylation	LGLKSLVSKGTLVQT CCHHHHHHCCCEEEE	30.57	29176673
91	Other	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	27105115
91	Ubiquitination	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	-
91	Acetylation	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	7760101
93	Phosphorylation	KSLVSKGTLVQTKGT HHHHHCCCEEEECCC	27.74	27600695
98	Ubiquitination	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	-
100	Phosphorylation	TLVQTKGTGASGSFK CEEEECCCCCCCCEE	31.00	29899451
103	Phosphorylation	QTKGTGASGSFKLNK EECCCCCCCCEECCC	35.99	26824392
105	Phosphorylation	KGTGASGSFKLNKKA CCCCCCCCEECCCCC	19.40	25521595
107	Ubiquitination	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	-
107	Acetylation	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	22641331
107	Other	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	27105115
110	Ubiquitination	SGSFKLNKKAASGEA CCCEECCCCCCCCCC	54.98	-
118	Acetylation	KAASGEAKPKAKKAG CCCCCCCCHHHHHHC	42.63	7616639
120	Acetylation	ASGEAKPKAKKAGAA CCCCCCHHHHHHCHH	72.61	7616649
128	Acetylation	AKKAGAAKAKKPAGA HHHHCHHHCCCCCCC	61.27	20612029
130	Acetylation	KAGAAKAKKPAGAAK HHCHHHCCCCCCCCC	59.59	165987
131	Acetylation	AGAAKAKKPAGAAKK HCHHHCCCCCCCCCC	44.98	165991
137	Acetylation	KKPAGAAKKPKKATG CCCCCCCCCCCCCCC	69.90	165995
138	Acetylation	KPAGAAKKPKKATGA CCCCCCCCCCCCCCC	58.29	165999
141	Other	GAAKKPKKATGAATP CCCCCCCCCCCCCCC	60.76	27105115
147	Phosphorylation	KKATGAATPKKTAKK CCCCCCCCCCCCCCC	34.80	26824392
151	Phosphorylation	GAATPKKTAKKTPKK CCCCCCCCCCCCCHH	50.24	22817900
155	Phosphorylation	PKKTAKKTPKKAKKP CCCCCCCCCHHHCCH	39.37	23384938
161	Acetylation	KTPKKAKKPAAAAGA CCCHHHCCHHHHHCC	44.76	19861025
169	Acetylation	PAAAAGAKKVSKSPK HHHHHCCCCCCCCHH	53.44	19737024
172	Phosphorylation	AAGAKKVSKSPKKVK HHCCCCCCCCHHHHH	35.97	22817900
174	Phosphorylation	GAKKVSKSPKKVKAA CCCCCCCCHHHHHCC	34.15	22817900
189	Phosphorylation	KPKKAAKSPAKAKAP CCHHHCCCHHHHCCC	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
105	S	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
55	R	Citrullination		24463520
Citrullination at Arg-55 (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 H13_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of H13_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of H13_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-37, 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-37, 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]

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