CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010958
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone H1.1 
Protein Synonyms/Alias
 Histone H1a 
Gene Name
 HIST1H1A 
Gene Synonyms/Alias
 H1F1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
17AASAAPEKPLAGKKAubiquitination[1]
22PEKPLAGKKAKKPAKacetylation[2]
26LAGKKAKKPAKAAAAacetylation[3]
67VSLAALKKALAAAGYacetylation[2]
67VSLAALKKALAAAGYubiquitination[1, 4]
78AAGYDVEKNNSRIKLubiquitination[1]
88SRIKLGIKSLVSKGTacetylation[5, 6]
88SRIKLGIKSLVSKGTubiquitination[7, 8]
93GIKSLVSKGTLVQTKacetylation[2]
93GIKSLVSKGTLVQTKubiquitination[1]
100KGTLVQTKGTGASGSacetylation[2]
100KGTLVQTKGTGASGSubiquitination[1, 4]
109TGASGSFKLNKKASSubiquitination[1]
125ETKPGASKVATKTKAubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [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
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 107 107 Phosphoserine (By similarity).  
Keyword
 Chromosome; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 215 AA 
Protein Sequence
MSETVPPAPA ASAAPEKPLA GKKAKKPAKA AAASKKKPAG PSVSELIVQA ASSSKERGGV 60
SLAALKKALA AAGYDVEKNN SRIKLGIKSL VSKGTLVQTK GTGASGSFKL NKKASSVETK 120
PGASKVATKT KATGASKKLK KATGASKKSV KTPKKAKKPA ATRKSSKNPK KPKTVKPKKV 180
AKSPAKAKAV KPKAAKARVT KPKTAKPKKA APKKK 215 
Gene Ontology
 GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
 GO:0000786; C:nucleosome; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0006334; P:nucleosome assembly; IEA:InterPro.
 GO:0007283; P:spermatogenesis; TAS:ProtInc. 
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.