CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004458
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone H1.5 
Protein Synonyms/Alias
 Histone H1a; Histone H1b; Histone H1s-3 
Gene Name
 HIST1H1B 
Gene Synonyms/Alias
 H1F5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
17ATPAPVEKSPAKKKAacetylation[1]
17ATPAPVEKSPAKKKAubiquitination[2, 3]
21PVEKSPAKKKATKKAubiquitination[3, 4]
22VEKSPAKKKATKKAAubiquitination[4]
37GAGAAKRKATGPPVSubiquitination[3, 4, 5, 6]
49PVSELITKAVAASKEacetylation[1]
49PVSELITKAVAASKEubiquitination[2, 3, 4, 5, 6, 7, 8, 9]
67LSLAALKKALAAGGYubiquitination[2, 3, 4, 5, 6]
78AGGYDVEKNNSRIKLubiquitination[2, 3, 4, 5, 6]
88SRIKLGLKSLVSKGTacetylation[1]
161KTPKKAKKPAAAGVKubiquitination[5]
168KPAAAGVKKVAKSPKacetylation[1, 10]
168KPAAAGVKKVAKSPKubiquitination[5]
199KPKAVKPKAAKPKAAacetylation[10]
202AVKPKAAKPKAAKPKacetylation[10]
204KPKAAKPKAAKPKAAacetylation[10]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [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] 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]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [10] 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
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 39 112 H15.
 MOD_RES 2 2 N-acetylserine; partial.
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 4 4 Phosphothreonine (By similarity).
 MOD_RES 11 11 Phosphothreonine; by GSK3.
 MOD_RES 18 18 Phosphoserine.
 MOD_RES 27 27 N6-methyllysine.
 MOD_RES 39 39 Phosphothreonine.
 MOD_RES 138 138 Phosphothreonine.
 MOD_RES 168 168 N6-acetyllysine.
 MOD_RES 173 173 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
 226 AA 
Protein Sequence
MSETAPAETA TPAPVEKSPA KKKATKKAAG AGAAKRKATG PPVSELITKA VAASKERNGL 60
SLAALKKALA AGGYDVEKNN SRIKLGLKSL VSKGTLVQTK GTGASGSFKL NKKAASGEAK 120
PKAKKAGAAK AKKPAGATPK KAKKAAGAKK AVKKTPKKAK KPAAAGVKKV AKSPKKAKAA 180
AKPKKATKSP AKPKAVKPKA AKPKAAKPKA AKPKAAKAKK AAAKKK 226 
Gene Ontology
 GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
 GO:0000786; C:nucleosome; NAS:UniProtKB.
 GO:0003677; F:DNA binding; NAS:UniProtKB.
 GO:0006334; P:nucleosome assembly; NAS:UniProtKB. 
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.