dbPTM

H10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H10_HUMAN
UniProt AC	P07305
Protein Name	Histone H1.0
Gene Name	H1F0
Organism	Homo sapiens (Human).
Sequence Length	194
Subcellular Localization	Nucleus . Chromosome . The RNA edited version has been localized to nuclear speckles. During mitosis, it appears in the vicinity of condensed chromosomes.
Protein Description	Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. The H1F0 histones are found in cells that are in terminal stages of differentiation or that have low rates of cell division..
Protein Sequence	MTENSTSAPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYKVGENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKSDEPKKSVAFKKTKKEIKKVATPKKASKPKKAASKAPTKKPKATPVKKAKKKLAATPKKAKKPKTVKAKPVKASKPKKAKPVKPKAKSSAKRAGKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MTENSTSA -------CCCCCCCC	10.80	19413330
2	Acetylation	------MTENSTSAP ------CCCCCCCCC	43.82	19691289
2	Phosphorylation	------MTENSTSAP ------CCCCCCCCC	43.82	19413330
4	Deamidation	----MTENSTSAPAA ----CCCCCCCCCCC	41.23	9582379
4	Deamidated asparagine	----MTENSTSAPAA ----CCCCCCCCCCC	41.23	-
5	Phosphorylation	---MTENSTSAPAAK ---CCCCCCCCCCCC	19.94	27794612
6	Phosphorylation	--MTENSTSAPAAKP --CCCCCCCCCCCCC	40.25	19691289
7	Phosphorylation	-MTENSTSAPAAKPK -CCCCCCCCCCCCCC	31.88	29396449
12	Methylation	STSAPAAKPKRAKAS CCCCCCCCCCHHCCC	53.85	17043054
12	Acetylation	STSAPAAKPKRAKAS CCCCCCCCCCHHCCC	53.85	17043054
12	Ubiquitination	STSAPAAKPKRAKAS CCCCCCCCCCHHCCC	53.85	33845483
14	Acetylation	SAPAAKPKRAKASKK CCCCCCCCHHCCCCC	65.37	7669719
14	Ubiquitination	SAPAAKPKRAKASKK CCCCCCCCHHCCCCC	65.37	24816145
21	Ubiquitination	KRAKASKKSTDHPKY CHHCCCCCCCCCCCH	56.97	23000965
27	Acetylation	KKSTDHPKYSDMIVA CCCCCCCCHHHHHHH	54.70	25825284
27	Ubiquitination	KKSTDHPKYSDMIVA CCCCCCCCHHHHHHH	54.70	23000965
40	Ubiquitination	VAAIQAEKNRAGSSR HHHHHHHHHCCCCCH	55.54	23000965
42	Citrullination	AIQAEKNRAGSSRQS HHHHHHHCCCCCHHH	51.93	-
42	Citrullination	AIQAEKNRAGSSRQS HHHHHHHCCCCCHHH	51.93	-
52	Ubiquitination	SSRQSIQKYIKSHYK CCHHHHHHHHHHHHC	47.47	23000965
52	Acetylation	SSRQSIQKYIKSHYK CCHHHHHHHHHHHHC	47.47	25825284
55	2-Hydroxyisobutyrylation	QSIQKYIKSHYKVGE HHHHHHHHHHHCCCC	28.26	-
55	Ubiquitination	QSIQKYIKSHYKVGE HHHHHHHHHHHCCCC	28.26	23000965
58	Phosphorylation	QKYIKSHYKVGENAD HHHHHHHHCCCCCCC	17.92	-
59	Methylation	KYIKSHYKVGENADS HHHHHHHCCCCCCCH	38.04	-
59	Ubiquitination	KYIKSHYKVGENADS HHHHHHHCCCCCCCH	38.04	23000965
59	Acetylation	KYIKSHYKVGENADS HHHHHHHCCCCCCCH	38.04	22424773
66	Phosphorylation	KVGENADSQIKLSIK CCCCCCCHHHHHHHH	31.25	17525332
82	Methylation	LVTTGVLKQTKGVGA HHHHCCCCCCCCCCC	54.22	-
82	Ubiquitination	LVTTGVLKQTKGVGA HHHHCCCCCCCCCCC	54.22	23000965
82	2-Hydroxyisobutyrylation	LVTTGVLKQTKGVGA HHHHCCCCCCCCCCC	54.22	-
84	Phosphorylation	TTGVLKQTKGVGASG HHCCCCCCCCCCCCC	28.33	-
85	Ubiquitination	TGVLKQTKGVGASGS HCCCCCCCCCCCCCC	49.45	23000965
90	Phosphorylation	QTKGVGASGSFRLAK CCCCCCCCCCEEECC	29.10	30266825
92	Phosphorylation	KGVGASGSFRLAKSD CCCCCCCCEEECCCC	12.51	30266825
102	Methylation	LAKSDEPKKSVAFKK ECCCCCCCCCCCCHH	56.48	-
104	ADP-ribosylation	KSDEPKKSVAFKKTK CCCCCCCCCCCHHHH	25.46	27723750
104	Phosphorylation	KSDEPKKSVAFKKTK CCCCCCCCCCCHHHH	25.46	23312004
108	Methylation	PKKSVAFKKTKKEIK CCCCCCCHHHHHHHH	50.20	-
108	Acetylation	PKKSVAFKKTKKEIK CCCCCCCHHHHHHHH	50.20	12431253
119	Phosphorylation	KEIKKVATPKKASKP HHHHHHCCCCCCCCC	38.33	28985074
121	Acetylation	IKKVATPKKASKPKK HHHHCCCCCCCCCCH	57.53	12437633
124	Phosphorylation	VATPKKASKPKKAAS HCCCCCCCCCCHHHH	59.37	20068231
141	Phosphorylation	PTKKPKATPVKKAKK CCCCCCCCCHHHHHH	34.44	20339515
149	Lactylation	PVKKAKKKLAATPKK CHHHHHHHHCCCCCC	42.52	31645732
149	Ubiquitination	PVKKAKKKLAATPKK CHHHHHHHHCCCCCC	42.52	29967540
153	Phosphorylation	AKKKLAATPKKAKKP HHHHHCCCCCCCCCC	29.99	30266825
155	Ubiquitination	KKLAATPKKAKKPKT HHHCCCCCCCCCCCC	62.09	33845483
155	2-Hydroxyisobutyrylation	KKLAATPKKAKKPKT HHHCCCCCCCCCCCC	62.09	-
155	Methylation	KKLAATPKKAKKPKT HHHCCCCCCCCCCCC	62.09	-
161	Acetylation	PKKAKKPKTVKAKPV CCCCCCCCCCCCCCC	74.87	7364673
164	Acetylation	AKKPKTVKAKPVKAS CCCCCCCCCCCCCCC	56.79	21339330
171	Phosphorylation	KAKPVKASKPKKAKP CCCCCCCCCCCCCCC	43.72	20068231

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 H10_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
17	S	Phosphorylation		18993075
Phosphorylated on Ser-17 in RNA edited version.

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 H10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
XBP1_HUMAN	XBP1	physical	20211142
A4_HUMAN	APP	physical	21832049

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 H10_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-5, AND MASSSPECTROMETRY.	19007248 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND MASSSPECTROMETRY.	17525332 [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-171, AND MASSSPECTROMETRY.	17081983 [Abstract]

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