dbPTM

H1X_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H1X_HUMAN
UniProt AC	Q92522
Protein Name	Histone H1x
Gene Name	H1FX
Organism	Homo sapiens (Human).
Sequence Length	213
Subcellular Localization	Nucleus. Chromosome.
Protein Description	Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures..
Protein Sequence	MSVELEEALPVTTAEGMAKKVTKAGGSAALSPSKKRKNSKKKNQPGKYSQLVVETIRRLGERNGSSLAKIYTEAKKVPWFDQQNGRTYLKYSIKALVQNDTLLQVKGTGANGSFKLNRKKLEGGGERRGAPAAATAPAPTAHKAKKAAPGAAGSRRADKKPARGQKPEQRSHKKGAGAKKDKGGKAKKTAAAGGKKVKKAAKPSVPKVPKGRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSVELEEAL ------CCCCHHHHC	25.05	30266825
2	Acetylation	------MSVELEEAL ------CCCCHHHHC	25.05	19691289
12	Phosphorylation	LEEALPVTTAEGMAK HHHHCCCCCHHHHHH	20.53	30266825
13	Phosphorylation	EEALPVTTAEGMAKK HHHCCCCCHHHHHHH	23.97	30266825
17	Sulfoxidation	PVTTAEGMAKKVTKA CCCCHHHHHHHHHHC	3.58	21406390
19	Ubiquitination	TTAEGMAKKVTKAGG CCHHHHHHHHHHCCC	38.59	32015554
19	2-Hydroxyisobutyrylation	TTAEGMAKKVTKAGG CCHHHHHHHHHHCCC	38.59	-
19	Acetylation	TTAEGMAKKVTKAGG CCHHHHHHHHHHCCC	38.59	25953088
20	Ubiquitination	TAEGMAKKVTKAGGS CHHHHHHHHHHCCCC	45.67	29967540
22	Phosphorylation	EGMAKKVTKAGGSAA HHHHHHHHHCCCCCC	24.85	-
23	Ubiquitination	GMAKKVTKAGGSAAL HHHHHHHHCCCCCCC	48.28	33845483
27	Phosphorylation	KVTKAGGSAALSPSK HHHHCCCCCCCCHHH	14.95	23927012
31	Phosphorylation	AGGSAALSPSKKRKN CCCCCCCCHHHHCCC	23.54	29255136
33	Phosphorylation	GSAALSPSKKRKNSK CCCCCCHHHHCCCCC	47.65	29255136
34	2-Hydroxyisobutyrylation	SAALSPSKKRKNSKK CCCCCHHHHCCCCCC	61.04	-
34	Ubiquitination	SAALSPSKKRKNSKK CCCCCHHHHCCCCCC	61.04	29967540
34	Acetylation	SAALSPSKKRKNSKK CCCCCHHHHCCCCCC	61.04	25953088
41	Ubiquitination	KKRKNSKKKNQPGKY HHCCCCCCCCCCCCH	57.70	23000965
42	Ubiquitination	KRKNSKKKNQPGKYS HCCCCCCCCCCCCHH	65.63	23000965
47	Acetylation	KKKNQPGKYSQLVVE CCCCCCCCHHHHHHH	48.70	19608861
47	2-Hydroxyisobutyrylation	KKKNQPGKYSQLVVE CCCCCCCCHHHHHHH	48.70	-
47	Ubiquitination	KKKNQPGKYSQLVVE CCCCCCCCHHHHHHH	48.70	23000965
48	Phosphorylation	KKNQPGKYSQLVVET CCCCCCCHHHHHHHH	13.94	28152594
49	Phosphorylation	KNQPGKYSQLVVETI CCCCCCHHHHHHHHH	22.11	28152594
57	Methylation	QLVVETIRRLGERNG HHHHHHHHHHHHHCC	34.88	-
62	Citrullination	TIRRLGERNGSSLAK HHHHHHHHCCCHHHH	51.52	-
62	Citrullination	TIRRLGERNGSSLAK HHHHHHHHCCCHHHH	51.52	-
65	Phosphorylation	RLGERNGSSLAKIYT HHHHHCCCHHHHHHH	26.23	29396449
66	Phosphorylation	LGERNGSSLAKIYTE HHHHCCCHHHHHHHH	33.47	29396449
75	2-Hydroxyisobutyrylation	AKIYTEAKKVPWFDQ HHHHHHHHCCCCEEC	48.33	-
75	Acetylation	AKIYTEAKKVPWFDQ HHHHHHHHCCCCEEC	48.33	25953088
76	Ubiquitination	KIYTEAKKVPWFDQQ HHHHHHHCCCCEECC	61.65	16196087
90	Ubiquitination	QNGRTYLKYSIKALV CCCCEEEEEEHHHHH	26.91	29967540
92	Phosphorylation	GRTYLKYSIKALVQN CCEEEEEEHHHHHCC	18.94	24719451
101	O-linked_Glycosylation	KALVQNDTLLQVKGT HHHHCCCCEEEEECC	36.60	21224338
106	Ubiquitination	NDTLLQVKGTGANGS CCCEEEEECCCCCCC	37.48	23000965
108	Phosphorylation	TLLQVKGTGANGSFK CEEEEECCCCCCCEE	27.66	21406692
113	Phosphorylation	KGTGANGSFKLNRKK ECCCCCCCEEECCCC	21.00	25159151
115	Ubiquitination	TGANGSFKLNRKKLE CCCCCCEEECCCCCC	46.69	29967540
115	Acetylation	TGANGSFKLNRKKLE CCCCCCEEECCCCCC	46.69	25953088
128	Methylation	LEGGGERRGAPAAAT CCCCCCCCCCCCCCC	41.12	-
143	Ubiquitination	APAPTAHKAKKAAPG CCCCCHHHHHHHCCC	60.48	33845483
143	Acetylation	APAPTAHKAKKAAPG CCCCCHHHHHHHCCC	60.48	25953088
145	Ubiquitination	APTAHKAKKAAPGAA CCCHHHHHHHCCCCC	47.99	-
146	Ubiquitination	PTAHKAKKAAPGAAG CCHHHHHHHCCCCCC	55.42	29967540
146	Lactylation	PTAHKAKKAAPGAAG CCHHHHHHHCCCCCC	55.42	31645732
146	Methylation	PTAHKAKKAAPGAAG CCHHHHHHHCCCCCC	55.42	-
174	Acetylation	PEQRSHKKGAGAKKD HHHHCCCCCCCCCCC	48.87	158585
179	Acetylation	HKKGAGAKKDKGGKA CCCCCCCCCCCCCCC	61.66	19608861
180	Acetylation	KKGAGAKKDKGGKAK CCCCCCCCCCCCCCC	65.23	19608861
182	Acetylation	GAGAKKDKGGKAKKT CCCCCCCCCCCCCCC	77.70	19608861
185	Acetylation	AKKDKGGKAKKTAAA CCCCCCCCCCCCHHC	66.75	19608861
195	Acetylation	KTAAAGGKKVKKAAK CCHHCCCHHCHHHCC	54.17	22362497
196	Acetylation	TAAAGGKKVKKAAKP CHHCCCHHCHHHCCC	63.66	12634897
196	Methylation	TAAAGGKKVKKAAKP CHHCCCHHCHHHCCC	63.66	-
198	Acetylation	AAGGKKVKKAAKPSV HCCCHHCHHHCCCCC	45.64	12634907
199	Acetylation	AGGKKVKKAAKPSVP CCCHHCHHHCCCCCC	57.47	12634917
202	Ubiquitination	KKVKKAAKPSVPKVP HHCHHHCCCCCCCCC	42.56	33845483
204	Phosphorylation	VKKAAKPSVPKVPKG CHHHCCCCCCCCCCC	50.80	29802988
207	Methylation	AAKPSVPKVPKGRK- HCCCCCCCCCCCCC-	69.85	-
210	Methylation	PSVPKVPKGRK---- CCCCCCCCCCC----	74.47	-

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 H1X_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
62	R	Citrullination		-
Citrullination at Arg-62 (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 H1X_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IL7RA_HUMAN	IL7R	physical	23151878
ACPH_HUMAN	APEH	physical	22863883
CYHR1_HUMAN	CYHR1	physical	22863883
EXOS4_HUMAN	EXOSC4	physical	22863883
H15_HUMAN	HIST1H1B	physical	22863883
NMI_HUMAN	NMI	physical	22863883
GLYM_HUMAN	SHMT2	physical	22863883
VP26A_HUMAN	VPS26A	physical	22863883

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 H1X_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47; LYS-179; LYS-180;LYS-182 AND LYS-185, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASSSPECTROMETRY.	19690332 [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 SER-31, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-31, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-33, AND MASSSPECTROMETRY.	19007248 [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 SER-31, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASSSPECTROMETRY.	17924679 [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 SER-2 AND SER-31, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASSSPECTROMETRY.	15302935 [Abstract]

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