UniProt Accession

 H14_MOUSE; P43274; Q5EBH3 

Genbank Protein ID

 L26163; L04141; Y12292; BC089600 

Genbank Nucleotide ID

 AAA37760.1; AAA37814.1; CAA72971.1; AAH89600.1 

Protein Name

 Histone H1.4 

Protein Synonyms/Alias

 H1 VAR.2; H1e 

Gene Name

 Hist1h1e 

Gene Synonyms/Alias

 H1f4 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
17	AAPAPAEKTPVKKKA	acetylation	[1, 2, 3, 4]
17	AAPAPAEKTPVKKKA	ubiquitination	[5]
21	PAEKTPVKKKARKAA	acetylation	[1]
32	RKAAGGAKRKTSGPP	acetylation	[1]
34	AAGGAKRKTSGPPVS	acetylation	[2, 4]
34	AAGGAKRKTSGPPVS	succinylation	[4]
34	AAGGAKRKTSGPPVS	ubiquitination	[5]
46	PVSELITKAVAASKE	acetylation	[2, 4, 6, 7]
46	PVSELITKAVAASKE	succinylation	[4]
46	PVSELITKAVAASKE	ubiquitination	[5]
52	TKAVAASKERSGVSL	acetylation	[6]
63	GVSLAALKKALAAAG	ubiquitination	[5]
64	VSLAALKKALAAAGY	ubiquitination	[5]
75	AAGYDVEKNNSRIKL	ubiquitination	[5]
85	SRIKLGLKSLVSKGT	acetylation	[6]
85	SRIKLGLKSLVSKGT	ubiquitination	[5]
90	GLKSLVSKGTLVQTK	acetylation	[1, 2, 4, 6, 7, 8]
90	GLKSLVSKGTLVQTK	succinylation	[4]
90	GLKSLVSKGTLVQTK	ubiquitination	[5]
97	KGTLVQTKGTGASGS	acetylation	[2, 4]
97	KGTLVQTKGTGASGS	ubiquitination	[5]
106	TGASGSFKLNKKAAS	ubiquitination	[5]
127	AKRAGAAKAKKPAGA	acetylation	[1]
136	KKPAGAAKKPKKAAG	acetylation	[1]
137	KPAGAAKKPKKAAGT	acetylation	[1]
149	AGTATAKKSTKKTPK	acetylation	[1]
159	KKTPKKAKKPAAAAG	acetylation	[6]
160	KTPKKAKKPAAAAGA	acetylation	[1, 6]
168	PAAAAGAKKAKSPKK	acetylation	[1, 6, 9]
192	PKSPAKAKTVKPKAA	acetylation	[10]

Reference

 [1] Comprehensive mapping of post-translational modifications on synaptic, nuclear, and histone proteins in the adult mouse brain.
 Tweedie-Cullen RY, Reck JM, Mansuy IM.
 J Proteome Res. 2009 Nov;8(11):4966-82. [PMID: 19737024]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [5] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [6] Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue.
 Wisniewski JR, Zougman A, Krüger S, Mann M.
 Mol Cell Proteomics. 2007 Jan;6(1):72-87. [PMID: 17043054]
 [7] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [8] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [9] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [10] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123] 

Functional 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. 

Sequence Annotation

 DOMAIN 36 109 H15.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 4 4 Phosphothreonine.
 MOD_RES 18 18 Phosphothreonine.
 MOD_RES 26 26 N6-acetyllysine; alternate (By
 MOD_RES 26 26 N6-methyllysine; alternate (By
 MOD_RES 36 36 Phosphoserine.
 MOD_RES 146 146 Phosphothreonine (By similarity).
 MOD_RES 187 187 Phosphoserine (By similarity).  

Keyword

 Acetylation; Chromosome; Complete proteome; DNA-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 219 AA 

Protein Sequence

Gene Ontology

 GO:0000786; C:nucleosome; IEA:InterPro.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IDA:MGI.
 GO:0006334; P:nucleosome assembly; IEA:InterPro.
 GO:0016584; P:nucleosome positioning; IMP:MGI. 

Interpro

 IPR005818; Histone_H1/H5.
 IPR005819; Histone_H5.
 IPR011991; WHTH_DNA-bd_dom. 

Pfam

 PF00538; Linker_histone 

SMART

 SM00526; H15 

PROSITE

 PS51504; H15 

PRINTS

 PR00624; HISTONEH5.