H11_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H11_MOUSE
• UniProt AC: P43275
• Protein Name: Histone H1.1
• Gene Name: Hist1h1a
• Organism: Mus musculus (Mouse).
• Sequence Length: 213
• 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: MSETAPVAQAASTATEKPAAAKKTKKPAKAAAPRKKPAGPSVSELIVQAVSSSKERSGVSLAALKKSLAAAGYDVEKNNSRIKLGLKSLVNKGTLVQTKGTGAAGSFKLNKKAESKAITTKVSVKAKASGAAKKPKKTAGAAAKKTVKTPKKPKKPAVSKKTSKSPKKPKVVKAKKVAKSPAKAKAVKPKASKAKVTKPKTPAKPKKAAPKKK

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSETAPVAQ ------CCCCHHHHH	43.59	26824392
2	Acetylation	------MSETAPVAQ ------CCCCHHHHH	43.59	23806337
4	Phosphorylation	----MSETAPVAQAA ----CCCCHHHHHHH	29.02	26824392
12	Phosphorylation	APVAQAASTATEKPA HHHHHHHHHHCCCCH	22.91	26824392
13	Phosphorylation	PVAQAASTATEKPAA HHHHHHHHHCCCCHH	32.64	27566939
15	Phosphorylation	AQAASTATEKPAAAK HHHHHHHCCCCHHHH	44.63	25619855
17	Succinylation	AASTATEKPAAAKKT HHHHHCCCCHHHHHC	35.29	23806337
17	Methylation	AASTATEKPAAAKKT HHHHHCCCCHHHHHC	35.29	-
17	Ubiquitination	AASTATEKPAAAKKT HHHHHCCCCHHHHHC	35.29	-
17	Acetylation	AASTATEKPAAAKKT HHHHHCCCCHHHHHC	35.29	23806337
22	Acetylation	TEKPAAAKKTKKPAK CCCCHHHHHCCCCCH	57.14	17043054
23	Methylation	EKPAAAKKTKKPAKA CCCHHHHHCCCCCHH	61.93	-
35	Ubiquitination	AKAAAPRKKPAGPSV CHHCCCCCCCCCCCH	63.15	-
36	Ubiquitination	KAAAPRKKPAGPSVS HHCCCCCCCCCCCHH	41.18	-
36	Other	KAAAPRKKPAGPSVS HHCCCCCCCCCCCHH	41.18	-
41	Phosphorylation	RKKPAGPSVSELIVQ CCCCCCCCHHHHHHH	37.04	26239621
43	Phosphorylation	KPAGPSVSELIVQAV CCCCCCHHHHHHHHH	30.90	26239621
53	Phosphorylation	IVQAVSSSKERSGVS HHHHHHCCCCCCCCC	30.91	27600695
54	Other	VQAVSSSKERSGVSL HHHHHCCCCCCCCCH	60.12	-
54	Ubiquitination	VQAVSSSKERSGVSL HHHHHCCCCCCCCCH	60.12	-
54	Acetylation	VQAVSSSKERSGVSL HHHHHCCCCCCCCCH	60.12	22826441
56	Citrullination	AVSSSKERSGVSLAA HHHCCCCCCCCCHHH	42.31	24463520
56	Citrullination	AVSSSKERSGVSLAA HHHCCCCCCCCCHHH	42.31	-
57	Phosphorylation	VSSSKERSGVSLAAL HHCCCCCCCCCHHHH	44.64	24899341
60	Phosphorylation	SKERSGVSLAALKKS CCCCCCCCHHHHHHH	18.80	26745281
65	Ubiquitination	GVSLAALKKSLAAAG CCCHHHHHHHHHHCC	35.27	-
65	Acetylation	GVSLAALKKSLAAAG CCCHHHHHHHHHHCC	35.27	7616609
66	Ubiquitination	VSLAALKKSLAAAGY CCHHHHHHHHHHCCC	52.10	-
66	Succinylation	VSLAALKKSLAAAGY CCHHHHHHHHHHCCC	52.10	23806337
66	Acetylation	VSLAALKKSLAAAGY CCHHHHHHHHHHCCC	52.10	23806337
66	Other	VSLAALKKSLAAAGY CCHHHHHHHHHHCCC	52.10	-
67	Phosphorylation	SLAALKKSLAAAGYD CHHHHHHHHHHCCCC	22.96	-
77	Ubiquitination	AAGYDVEKNNSRIKL HCCCCCCCCCCCEEE	62.37	22790023
77	Acetylation	AAGYDVEKNNSRIKL HCCCCCCCCCCCEEE	62.37	23806337
80	Phosphorylation	YDVEKNNSRIKLGLK CCCCCCCCCEEECHH	44.79	29176673
87	Acetylation	SRIKLGLKSLVNKGT CCEEECHHHHHHCCC	39.69	23806337
87	Ubiquitination	SRIKLGLKSLVNKGT CCEEECHHHHHHCCC	39.69	27667366
87	Other	SRIKLGLKSLVNKGT CCEEECHHHHHHCCC	39.69	-
88	Phosphorylation	RIKLGLKSLVNKGTL CEEECHHHHHHCCCE	42.46	27600695
92	Other	GLKSLVNKGTLVQTK CHHHHHHCCCEEEEC	45.88	-
92	Ubiquitination	GLKSLVNKGTLVQTK CHHHHHHCCCEEEEC	45.88	-
92	Acetylation	GLKSLVNKGTLVQTK CHHHHHHCCCEEEEC	45.88	23806337
98	Phosphorylation	NKGTLVQTKGTGAAG HCCCEEEECCCCCCC	24.78	25890499
99	Acetylation	KGTLVQTKGTGAAGS CCCEEEECCCCCCCC	37.07	23806337
99	Ubiquitination	KGTLVQTKGTGAAGS CCCEEEECCCCCCCC	37.07	-
99	Succinylation	KGTLVQTKGTGAAGS CCCEEEECCCCCCCC	37.07	23806337
106	Phosphorylation	KGTGAAGSFKLNKKA CCCCCCCCEECCCHH	17.93	24704852
108	Ubiquitination	TGAAGSFKLNKKAES CCCCCCEECCCHHCC	53.50	-
108	Acetylation	TGAAGSFKLNKKAES CCCCCCEECCCHHCC	53.50	22826441
108	Other	TGAAGSFKLNKKAES CCCCCCEECCCHHCC	53.50	-
116	Ubiquitination	LNKKAESKAITTKVS CCCHHCCCCEEEEHH	35.00	-
119	Phosphorylation	KAESKAITTKVSVKA HHCCCCEEEEHHHHH	25.98	28833060
120	Phosphorylation	AESKAITTKVSVKAK HCCCCEEEEHHHHHH	24.28	28833060
121	Acetylation	ESKAITTKVSVKAKA CCCCEEEEHHHHHHH	24.70	23806337
121	Ubiquitination	ESKAITTKVSVKAKA CCCCEEEEHHHHHHH	24.70	27667366
123	Phosphorylation	KAITTKVSVKAKASG CCEEEEHHHHHHHCC	21.32	28833060
129	Phosphorylation	VSVKAKASGAAKKPK HHHHHHHCCCCCCCC	28.40	22817900
145	Acetylation	TAGAAAKKTVKTPKK CCCHHHCCCCCCCCC	54.55	7718041
146	Phosphorylation	AGAAAKKTVKTPKKP CCHHHCCCCCCCCCC	26.91	28059163
151	Acetylation	KKTVKTPKKPKKPAV CCCCCCCCCCCCCCC	83.43	7718051
159	Phosphorylation	KPKKPAVSKKTSKSP CCCCCCCCCCCCCCC	30.46	27149854
165	Phosphorylation	VSKKTSKSPKKPKVV CCCCCCCCCCCCCEE	41.54	27149854
180	Phosphorylation	KAKKVAKSPAKAKAV ECHHHHCCHHHHHCC	21.98	24453211
197	Phosphorylation	KASKAKVTKPKTPAK CCHHCCCCCCCCCCC	40.71	27149854
201	Phosphorylation	AKVTKPKTPAKPKKA CCCCCCCCCCCCCCC	36.69	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
129	S	Phosphorylation	Kinase	PRKACA	P17612	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
56	R	Citrullination	Citrullination at Arg-56 (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.	24463520

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of H11_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of H11_MOUSE !!

Drug and Disease Associations

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