CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002482
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone H1.0 
Protein Synonyms/Alias
 Histone H1'; Histone H1(0); Histone H1.0, N-terminally processed 
Gene Name
 H1F0 
Gene Synonyms/Alias
 H1FV 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
27KKSTDHPKYSDMIVAubiquitination[1, 2]
40VAAIQAEKNRAGSSRubiquitination[1, 2, 3]
52SSRQSIQKYIKSHYKacetylation[4]
52SSRQSIQKYIKSHYKubiquitination[1]
59KYIKSHYKVGENADSacetylation[4]
59KYIKSHYKVGENADSubiquitination[1, 2, 3]
82LVTTGVLKQTKGVGAubiquitination[1, 2]
85TGVLKQTKGVGASGSubiquitination[1]
164AKKPKTVKAKPVKASacetylation[5]
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] 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]
 [3] 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]
 [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] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330
Functional Description
 Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. The H1F0 histones are found in cells that are in terminal stages of differentiation or that have low rates of cell division. 
Sequence Annotation
 DOMAIN 24 97 H15.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 2 2 N-acetylthreonine; partial; in Histone
 MOD_RES 4 4 Deamidated asparagine; partial.  
Keyword
 Acetylation; Alternative splicing; Chromosome; Complete proteome; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; RNA editing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 194 AA 
Protein Sequence
MTENSTSAPA AKPKRAKASK KSTDHPKYSD MIVAAIQAEK NRAGSSRQSI QKYIKSHYKV 60
GENADSQIKL SIKRLVTTGV LKQTKGVGAS GSFRLAKSDE PKKSVAFKKT KKEIKKVATP 120
KKASKPKKAA SKAPTKKPKA TPVKKAKKKL AATPKKAKKP KTVKAKPVKA SKPKKAKPVK 180
PKAKSSAKRA GKKK 194 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0000786; C:nucleosome; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0006309; P:apoptotic DNA fragmentation; TAS:Reactome.
 GO:0006334; P:nucleosome assembly; IEA:InterPro. 
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.