UniProt Accession

 H12_HUMAN; P16403; A8K4I2 

Genbank Protein ID

 X57129; AF531300; AK290947; AB451259; AB451385; U91328; CH471087; BC002649 

Genbank Nucleotide ID

 CAA40408.1; AAN06700.1; BAF83636.1; BAG70073.1; BAG70199.1; EAW55515.1 

Protein Name

 Histone H1.2 

Protein Synonyms/Alias

 Histone H1c; Histone H1d; Histone H1s-1 

Gene Name

 HIST1H1C 

Gene Synonyms/Alias

 H1F2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
17	AAAPPAEKAPVKKKA	acetylation	[1, 2, 3, 4]
17	AAAPPAEKAPVKKKA	ubiquitination	[4, 5, 6, 7, 8, 9]
21	PAEKAPVKKKAAKKA	glycation	[10]
21	PAEKAPVKKKAAKKA	ubiquitination	[4, 9]
22	AEKAPVKKKAAKKAG	glycation	[10]
22	AEKAPVKKKAAKKAG	ubiquitination	[9]
23	EKAPVKKKAAKKAGG	glycation	[10]
27	VKKKAAKKAGGTPRK	glycation	[10]
34	KAGGTPRKASGPPVS	acetylation	[1]
34	KAGGTPRKASGPPVS	crotonylation	[11]
34	KAGGTPRKASGPPVS	methylation	[12]
34	KAGGTPRKASGPPVS	ubiquitination	[7, 8, 9, 13, 14, 15]
46	PVSELITKAVAASKE	acetylation	[1]
46	PVSELITKAVAASKE	ubiquitination	[6, 7, 8, 9, 13, 14, 15, 16, 17]
52	TKAVAASKERSGVSL	acetylation	[1]
52	TKAVAASKERSGVSL	ubiquitination	[14]
63	GVSLAALKKALAAAG	ubiquitination	[7, 15, 18]
64	VSLAALKKALAAAGY	acetylation	[1]
64	VSLAALKKALAAAGY	crotonylation	[11]
64	VSLAALKKALAAAGY	ubiquitination	[6, 7, 13, 14, 15]
75	AAGYDVEKNNSRIKL	ubiquitination	[6, 7, 13, 14, 15]
85	SRIKLGLKSLVSKGT	acetylation	[1]
85	SRIKLGLKSLVSKGT	crotonylation	[11]
85	SRIKLGLKSLVSKGT	ubiquitination	[7, 13]
90	GLKSLVSKGTLVQTK	acetylation	[1]
90	GLKSLVSKGTLVQTK	crotonylation	[11]
90	GLKSLVSKGTLVQTK	ubiquitination	[7, 8, 13, 14, 15]
97	KGTLVQTKGTGASGS	acetylation	[1]
97	KGTLVQTKGTGASGS	crotonylation	[11]
97	KGTLVQTKGTGASGS	ubiquitination	[7, 8, 13, 14, 15]
106	TGASGSFKLNKKAAS	ubiquitination	[8, 13, 14, 15]
110	GSFKLNKKAASGEAK	ubiquitination	[14]
117	KAASGEAKPKVKKAG	ubiquitination	[14]
127	VKKAGGTKPKKPVGA	ubiquitination	[14]
136	KKPVGAAKKPKKAAG	glycation	[10]
136	KKPVGAAKKPKKAAG	ubiquitination	[15]
140	GAAKKPKKAAGGATP	ubiquitination	[14]
157	SAKKTPKKAKKPAAA	glycation	[10]
159	KKTPKKAKKPAAATV	crotonylation	[11]
159	KKTPKKAKKPAAATV	ubiquitination	[14, 15]
160	KTPKKAKKPAAATVT	ubiquitination	[14, 15]
168	PAAATVTKKVAKSPK	acetylation	[1]
168	PAAATVTKKVAKSPK	crotonylation	[11]
168	PAAATVTKKVAKSPK	ubiquitination	[7, 14, 15]
172	TVTKKVAKSPKKAKV	glycation	[10]
175	KKVAKSPKKAKVAKP	glycation	[10]
191	KAAKSAAKAVKPKAA	acetylation	[1]
199	AVKPKAAKPKVVKPK	glycation	[10]
201	KPKAAKPKVVKPKKA	glycation	[10]
206	KPKVVKPKKAAPKKK	ubiquitination	[19]

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] 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]
 [3] 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]
 [4] 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]
 [5] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
 Meierhofer D, Wang X, Huang L, Kaiser P.
 J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
 [6] 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]
 [7] 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]
 [8] 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]
 [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] Glycation and oxidation of histones H2B and H1: in vitro study and characterization by mass spectrometry.
 Guedes S, Vitorino R, Domingues MR, Amado F, Domingues P.
 Anal Bioanal Chem. 2011 Apr;399(10):3529-39. [PMID: 21274518]
 [11] Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification.
 Tan M, Luo H, Lee S, Jin F, Yang JS, Montellier E, Buchou T, Cheng Z, Rousseaux S, Rajagopal N, Lu Z, Ye Z, Zhu Q, Wysocka J, Ye Y, Khochbin S, Ren B, Zhao Y.
 Cell. 2011 Sep 16;146(6):1016-28. [PMID: 21925322]
 [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] 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]
 [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] 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]
 [16] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [17] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [18] 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]
 [19] Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry.
 Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D.
 Proteomics. 2007 Mar;7(6):868-74. [PMID: 17370265] 

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; partial.
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 34 34 N6-crotonyl-L-lysine; alternate.
 MOD_RES 34 34 N6-methyllysine; alternate.
 MOD_RES 64 64 N6-crotonyl-L-lysine.
 MOD_RES 85 85 N6-crotonyl-L-lysine.
 MOD_RES 90 90 N6-crotonyl-L-lysine.
 MOD_RES 97 97 N6-crotonyl-L-lysine.
 MOD_RES 104 104 Phosphoserine; by PKC (By similarity).
 MOD_RES 146 146 Phosphothreonine.
 MOD_RES 159 159 N6-crotonyl-L-lysine.
 MOD_RES 168 168 N6-crotonyl-L-lysine.
 MOD_RES 187 187 N6-methyllysine; by EHMT1 and EHMT2.
 CROSSLNK 17 17 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 206 206 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 Acetylation; Chromosome; Complete proteome; Direct protein sequencing; DNA-binding; Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 213 AA 

Protein Sequence

Gene Ontology

 GO:0000786; C:nucleosome; NAS:UniProtKB.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 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.