dbPTM

H13_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H13_HUMAN
UniProt AC	P16402
Protein Name	Histone H1.3
Gene Name	HIST1H1D
Organism	Homo sapiens (Human).
Sequence Length	221
Subcellular Localization	Nucleus. Chromosome. According to PubMed:15911621 more commonly found in euchromatin. According to PubMed:10997781 is associated with inactive chromatin.
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	MSETAPLAPTIPAPAEKTPVKKKAKKAGATAGKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEGKPKAKKAGAAKPRKPAGAAKKPKKVAGAATPKKSIKKTPKKVKKPATAAGTKKVAKSAKKVKTPQPKKAAKSPAKAKAPKPKAAKPKSGKPKVTKAKKAAPKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSETAPLAP ------CCCCCCCCC	43.59	21406692
2	Phosphorylation	------MSETAPLAP ------CCCCCCCCC	43.59	23401153
4	Phosphorylation	----MSETAPLAPTI ----CCCCCCCCCCC	26.69	23401153
10	Phosphorylation	ETAPLAPTIPAPAEK CCCCCCCCCCCCCCC	33.70	23401153
17	Acetylation	TIPAPAEKTPVKKKA CCCCCCCCCCCHHHH	61.30	23749302
17	Methylation	TIPAPAEKTPVKKKA CCCCCCCCCCCHHHH	61.30	17043054
17	Ubiquitination	TIPAPAEKTPVKKKA CCCCCCCCCCCHHHH	61.30	22817900
18	Phosphorylation	IPAPAEKTPVKKKAK CCCCCCCCCCHHHHH	25.48	29255136
21	Ubiquitination	PAEKTPVKKKAKKAG CCCCCCCHHHHHHCC	50.16	33845483
22	Ubiquitination	AEKTPVKKKAKKAGA CCCCCCHHHHHHCCC	59.19	22817900
30	Phosphorylation	KAKKAGATAGKRKAS HHHHCCCCCCCCCCC	34.72	26074081
33	Acetylation	KAGATAGKRKASGPP HCCCCCCCCCCCCCC	48.54	7708193
35	Acetylation	GATAGKRKASGPPVS CCCCCCCCCCCCCHH	50.84	17043054
35	Glycation	GATAGKRKASGPPVS CCCCCCCCCCCCCHH	50.84	-
35	Methylation	GATAGKRKASGPPVS CCCCCCCCCCCCCHH	50.84	-
35	Other	GATAGKRKASGPPVS CCCCCCCCCCCCCHH	50.84	27105115
35	Ubiquitination	GATAGKRKASGPPVS CCCCCCCCCCCCCHH	50.84	32142685
37	Phosphorylation	TAGKRKASGPPVSEL CCCCCCCCCCCHHHH	55.67	29255136
42	Phosphorylation	KASGPPVSELITKAV CCCCCCHHHHHHHHH	32.24	30266825
46	Phosphorylation	PPVSELITKAVAASK CCHHHHHHHHHHHHH	26.10	30266825
47	Ubiquitination	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	21890473
47	Acetylation	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	22641323
47	Glycation	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	-
47	Other	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	27105115
47	Ubiquitination	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	25015289
52	Phosphorylation	ITKAVAASKERSGVS HHHHHHHHHHCCCCC	25.88	26546556
53	Acetylation	TKAVAASKERSGVSL HHHHHHHHHCCCCCH	53.04	7296757
53	Other	TKAVAASKERSGVSL HHHHHHHHHCCCCCH	53.04	27105115
53	Ubiquitination	TKAVAASKERSGVSL HHHHHHHHHCCCCCH	53.04	23000965
55	Citrullination	AVAASKERSGVSLAA HHHHHHHCCCCCHHH	42.31	-
55	Citrullination	AVAASKERSGVSLAA HHHHHHHCCCCCHHH	42.31	-
55	Methylation	AVAASKERSGVSLAA HHHHHHHCCCCCHHH	42.31	-
56	Phosphorylation	VAASKERSGVSLAAL HHHHHHCCCCCHHHH	44.64	30266825
59	Phosphorylation	SKERSGVSLAALKKA HHHCCCCCHHHHHHH	18.80	30266825
64	Acetylation	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	163887
64	Ubiquitination	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	23000965
65	Ubiquitination	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	21890473
65	Sumoylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	-
65	Acetylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	-
65	Methylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	-
65	Other	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	27105115
65	Sumoylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	-
65	Ubiquitination	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	23000965
72	Phosphorylation	KALAAAGYDVEKNNS HHHHHCCCCCHHCCC	16.46	28152594
76	Ubiquitination	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	21890473
76	Acetylation	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	158555
76	Other	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	27105115
76	Ubiquitination	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	23000965
79	Phosphorylation	YDVEKNNSRIKLGLK CCCHHCCCCCCCCHH	44.79	23401153
82	Ubiquitination	EKNNSRIKLGLKSLV HHCCCCCCCCHHHHH	35.08	23000965
86	Ubiquitination	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	21890473
86	Acetylation	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	72630449
86	Other	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	27105115
86	Ubiquitination	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	23000965
87	Phosphorylation	RIKLGLKSLVSKGTL CCCCCHHHHHHCCCE	38.76	20860994
90	Phosphorylation	LGLKSLVSKGTLVQT CCHHHHHHCCCEEEE	30.57	17877366
91	Ubiquitination	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	21890473
91	Acetylation	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	7692547
91	Other	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	27105115
91	Ubiquitination	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	23000965
93	Phosphorylation	KSLVSKGTLVQTKGT HHHHHCCCEEEECCC	27.74	17877366
97	Phosphorylation	SKGTLVQTKGTGASG HCCCEEEECCCCCCC	24.78	28111955
98	Ubiquitination	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	21890473
98	Acetylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	-
98	Methylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	-
98	Ubiquitination	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	23000965
100	Phosphorylation	TLVQTKGTGASGSFK CEEEECCCCCCCCEE	31.00	26657352
103	Phosphorylation	QTKGTGASGSFKLNK EECCCCCCCCEEECC	35.99	21712546
105	Phosphorylation	KGTGASGSFKLNKKA CCCCCCCCEEECCCC	19.40	23401153
107	Ubiquitination	TGASGSFKLNKKAAS CCCCCCEEECCCCCC	53.50	21890473
107	Acetylation	TGASGSFKLNKKAAS CCCCCCEEECCCCCC	53.50	22641329
107	Methylation	TGASGSFKLNKKAAS CCCCCCEEECCCCCC	53.50	-
107	Other	TGASGSFKLNKKAAS CCCCCCEEECCCCCC	53.50	27105115
107	Ubiquitination	TGASGSFKLNKKAAS CCCCCCEEECCCCCC	53.50	21906983
110	Ubiquitination	SGSFKLNKKAASGEG CCCEEECCCCCCCCC	54.98	22817900
111	Ubiquitination	GSFKLNKKAASGEGK CCEEECCCCCCCCCC	48.38	22817900
114	Phosphorylation	KLNKKAASGEGKPKA EECCCCCCCCCCCCH	42.09	24825855
118	Ubiquitination	KAASGEGKPKAKKAG CCCCCCCCCCHHHCC	38.76	33845483
141	Lactylation	GAAKKPKKVAGAATP CCCCCCCCCCCCCCC	45.93	31645732
141	Ubiquitination	GAAKKPKKVAGAATP CCCCCCCCCCCCCCC	45.93	33845483
147	Phosphorylation	KKVAGAATPKKSIKK CCCCCCCCCCHHCCC	34.80	22167270
149	Ubiquitination	VAGAATPKKSIKKTP CCCCCCCCHHCCCCC	55.59	33845483
151	Phosphorylation	GAATPKKSIKKTPKK CCCCCCHHCCCCCCC	45.85	28111955
155	Phosphorylation	PKKSIKKTPKKVKKP CCHHCCCCCCCCCCC	35.03	15595731
160	Ubiquitination	KKTPKKVKKPATAAG CCCCCCCCCCCCHHC	63.02	29967540
161	Ubiquitination	KTPKKVKKPATAAGT CCCCCCCCCCCHHCH	42.76	33845483
164	Phosphorylation	KKVKKPATAAGTKKV CCCCCCCCHHCHHHH	26.10	20860994
168	Phosphorylation	KPATAAGTKKVAKSA CCCCHHCHHHHHHHH	23.98	21406692
169	Acetylation	PATAAGTKKVAKSAK CCCHHCHHHHHHHHC	44.31	17043054
169	Ubiquitination	PATAAGTKKVAKSAK CCCHHCHHHHHHHHC	44.31	33845483
170	Acetylation	ATAAGTKKVAKSAKK CCHHCHHHHHHHHCC	47.46	24847165
170	Methylation	ATAAGTKKVAKSAKK CCHHCHHHHHHHHCC	47.46	17043054
170	Other	ATAAGTKKVAKSAKK CCHHCHHHHHHHHCC	47.46	27105115
173	Acetylation	AGTKKVAKSAKKVKT HCHHHHHHHHCCCCC	54.67	24847173
176	Acetylation	KKVAKSAKKVKTPQP HHHHHHHCCCCCCCC	66.25	24847181
179	Acetylation	AKSAKKVKTPQPKKA HHHHCCCCCCCCHHH	64.47	25953088
179	Ubiquitination	AKSAKKVKTPQPKKA HHHHCCCCCCCCHHH	64.47	33845483
180	Phosphorylation	KSAKKVKTPQPKKAA HHHCCCCCCCCHHHC	30.09	28674151
188	Acetylation	PQPKKAAKSPAKAKA CCCHHHCCCCHHHCC	62.93	164433
189	Phosphorylation	QPKKAAKSPAKAKAP CCHHHCCCCHHHCCC	25.93	16377619
207	Acetylation	AAKPKSGKPKVTKAK CCCCCCCCCCCCCCH	49.08	163959
209	Acetylation	KPKSGKPKVTKAKKA CCCCCCCCCCCCHHC	67.05	158577
212	Acetylation	SGKPKVTKAKKAAPK CCCCCCCCCHHCCCC	62.28	158347

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		-
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of H13_HUMAN !!

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 H13_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Human spleen histone H1. Isolation and amino acid sequences of threeminor variants, H1a, H1c, and H1d."; Ohe Y., Hayashi H., Iwai K.; J. Biochem. 106:844-857(1989). Cited for: PROTEIN SEQUENCE OF 2-221.	2613692 [Abstract]
Phosphorylation
Reference	PubMed
"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 SER-37, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASSSPECTROMETRY.	19367720 [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-18 AND SER-37, AND MASSSPECTROMETRY.	17081983 [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 THR-4 AND THR-18, AND MASSSPECTROMETRY.	19413330 [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 THR-180, AND MASSSPECTROMETRY.	17287340 [Abstract]

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