UniProt Accession

 H14_HUMAN; P10412; Q4VB25 

Genbank Protein ID

 M60748; AF531302; AL353759; BC096168; BC096169; BC099632 

Genbank Nucleotide ID

 AAA63187.1; AAN06702.1; CAC04132.1; AAH96168.1; AAH96169.1; AAH99632.1 

Protein Name

 Histone H1.4 

Protein Synonyms/Alias

 Histone H1b; Histone H1s-4 

Gene Name

 HIST1H1E 

Gene Synonyms/Alias

 H1F4 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
17	AAPAPAEKTPVKKKA	acetylation	[1, 2, 3, 4, 5, 6]
17	AAPAPAEKTPVKKKA	ubiquitination	[6, 7, 8, 9]
21	PAEKTPVKKKARKSA	acetylation	[3]
21	PAEKTPVKKKARKSA	ubiquitination	[6, 7, 8, 9]
22	AEKTPVKKKARKSAG	ubiquitination	[9]
26	PVKKKARKSAGAAKR	acetylation	[10]
26	PVKKKARKSAGAAKR	methylation	[11, 12, 13]
34	SAGAAKRKASGPPVS	acetylation	[1]
34	SAGAAKRKASGPPVS	ubiquitination	[6, 7, 8, 9, 14]
46	PVSELITKAVAASKE	acetylation	[1, 2, 4, 5, 6]
46	PVSELITKAVAASKE	ubiquitination	[1, 6, 7, 8, 9, 14, 15, 16, 17, 18]
52	TKAVAASKERSGVSL	acetylation	[1]
52	TKAVAASKERSGVSL	ubiquitination	[14, 17]
63	GVSLAALKKALAAAG	acetylation	[2, 4, 5]
63	GVSLAALKKALAAAG	ubiquitination	[8, 9, 16, 18]
64	VSLAALKKALAAAGY	acetylation	[1]
64	VSLAALKKALAAAGY	ubiquitination	[6, 7, 8, 9, 14, 15, 17, 18]
75	AAGYDVEKNNSRIKL	acetylation	[3, 4, 5]
75	AAGYDVEKNNSRIKL	ubiquitination	[6, 7, 8, 9, 14, 15, 16, 17, 18]
85	SRIKLGLKSLVSKGT	acetylation	[1, 5]
85	SRIKLGLKSLVSKGT	ubiquitination	[6, 7, 8, 9, 19]
90	GLKSLVSKGTLVQTK	acetylation	[1, 2, 4, 5, 6]
90	GLKSLVSKGTLVQTK	ubiquitination	[6, 7, 8, 9, 14, 16, 18]
97	KGTLVQTKGTGASGS	acetylation	[1]
97	KGTLVQTKGTGASGS	ubiquitination	[6, 7, 8, 9, 14, 16, 18]
106	TGASGSFKLNKKAAS	acetylation	[2]
106	TGASGSFKLNKKAAS	ubiquitination	[6, 7, 9, 14, 16, 17, 18]
110	GSFKLNKKAASGEAK	ubiquitination	[9]
140	GAAKKPKKATGAATP	ubiquitination	[14]
148	ATGAATPKKSAKKTP	ubiquitination	[14]
160	KTPKKAKKPAAAAGA	ubiquitination	[14]
168	PAAAAGAKKAKSPKK	acetylation	[1]

Reference

 [1] 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]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [4] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [5] 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]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [9] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [10] Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin.
 Vaquero A, Scher M, Lee D, Erdjument-Bromage H, Tempst P, Reinberg D.
 Mol Cell. 2004 Oct 8;16(1):93-105. [PMID: 15469825]
 [11] Characterization of phosphorylation sites on histone H1 isoforms by tandem mass spectrometry.
 Garcia BA, Busby SA, Barber CM, Shabanowitz J, Allis CD, Hunt DF.
 J Proteome Res. 2004 Nov-Dec;3(6):1219-27. [PMID: 15595731]
 [12] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681]
 [13] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837]
 [14] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [15] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [16] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [17] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [18] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [19] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 

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 (By similarity). 

Sequence Annotation

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

Keyword

 3D-structure; Acetylation; Chromosome; Complete proteome; Direct protein sequencing; DNA-binding; Methylation; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 219 AA 

Protein Sequence

Gene Ontology

 GO:0000786; C:nucleosome; NAS:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003677; F:DNA binding; NAS:UniProtKB.
 GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
 GO:0016584; P:nucleosome positioning; IEA:Compara. 

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.