CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001949
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone H4 
Protein Synonyms/Alias
  
Gene Name
 HHF1; HHF2 
Gene Synonyms/Alias
 YBR009C; YBR0122; YNL030W; N2752 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
6**MSGRGKGGKGLGKacetylation[1, 2, 3, 4, 5, 6, 7, 8, 9]
9SGRGKGGKGLGKGGAacetylation[1, 2, 3, 4, 7, 8, 9, 10]
9SGRGKGGKGLGKGGAbutyrylation[11]
13KGGKGLGKGGAKRHRacetylation[1, 2, 3, 4, 5, 6, 7, 8, 9, 12]
17GLGKGGAKRHRKILRacetylation[1, 2, 3, 4, 7, 8, 9, 10, 13]
21GGAKRHRKILRDNIQacetylation[14]
32DNIQGITKPAIRRLAacetylation[8]
32DNIQGITKPAIRRLAsuccinylation[15]
32DNIQGITKPAIRRLAubiquitination[16]
60EEVRAVLKSFLESVIubiquitination[16]
78VTYTEHAKRKTVTSLsuccinylation[15]
78VTYTEHAKRKTVTSLubiquitination[16]
92LDVVYALKRQGRTLYacetylation[8, 17]
92LDVVYALKRQGRTLYubiquitination[16]
Reference
 [1] Identification of a non-basic domain in the histone H4 N-terminus required for repression of the yeast silent mating loci.
 Johnson LM, Fisher-Adams G, Grunstein M.
 EMBO J. 1992 Jun;11(6):2201-9. [PMID: 1600945]
 [2] Yeast histone H4 N-terminal sequence is required for promoter activation in vivo.
 Durrin LK, Mann RK, Kayne PS, Grunstein M.
 Cell. 1991 Jun 14;65(6):1023-31. [PMID: 2044150]
 [3] Selective use of H4 acetylation sites in the yeast Saccharomyces cerevisiae.
 Clarke DJ, O'Neill LP, Turner BM.
 Biochem J. 1993 Sep 1;294 ( Pt 2):557-61. [PMID: 8373369]
 [4] Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern.
 Braunstein M, Sobel RE, Allis CD, Turner BM, Broach JR.
 Mol Cell Biol. 1996 Aug;16(8):4349-56. [PMID: 8754835]
 [5] Hif1 is a component of yeast histone acetyltransferase B, a complex mainly localized in the nucleus.
 Poveda A, Pamblanco M, Tafrov S, Tordera V, Sternglanz R, Sendra R.
 J Biol Chem. 2004 Apr 16;279(16):16033-43. [PMID: 14761951]
 [6] Site specificity of yeast histone acetyltransferase B complex in vivo.
 Poveda A, Sendra R.
 FEBS J. 2008 May;275(9):2122-36. [PMID: 18373695]
 [7] Nano-electrospray tandem mass spectrometric analysis of the acetylation state of histones H3 and H4 in stationary phase in Saccharomyces cerevisiae.
 Ngubo M, Kemp G, Patterton HG.
 BMC Biochem. 2011 Jul 4;12:34. [PMID: 21726436]
 [8] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [9] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591]
 [10] Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines.
 Kuo MH, Brownell JE, Sobel RE, Ranalli TA, Cook RG, Edmondson DG, Roth SY, Allis CD.
 Nature. 1996 Sep 19;383(6597):269-72. [PMID: 8805705]
 [11] Identification and verification of lysine propionylation and butyrylation in yeast core histones using PTMap software.
 Zhang K, Chen Y, Zhang Z, Zhao Y.
 J Proteome Res. 2009 Feb;8(2):900-6. [PMID: 19113941]
 [12] The major cytoplasmic histone acetyltransferase in yeast: links to chromatin replication and histone metabolism.
 Parthun MR, Widom J, Gottschling DE.
 Cell. 1996 Oct 4;87(1):85-94. [PMID: 8858151]
 [13] Sas4 and Sas5 are required for the histone acetyltransferase activity of Sas2 in the SAS complex.
 Sutton A, Shia WJ, Band D, Kaufman PD, Osada S, Workman JL, Sternglanz R.
 J Biol Chem. 2003 May 9;278(19):16887-92. [PMID: 12626510]
 [14] Organismal differences in post-translational modifications in histones H3 and H4.
 Garcia BA, Hake SB, Diaz RL, Kauer M, Morris SA, Recht J, Shabanowitz J, Mishra N, Strahl BD, Allis CD, Hunt DF.
 J Biol Chem. 2007 Mar 9;282(10):7641-55. [PMID: 17194708]
 [15] Lysine succinylation and lysine malonylation in histones.
 Xie Z, Dai J, Dai L, Tan M, Cheng Z, Wu Y, Boeke JD, Zhao Y.
 Mol Cell Proteomics. 2012 May;11(5):100-7. [PMID: 22389435]
 [16] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [17] Histone H4 lysine 91 acetylation a core domain modification associated with chromatin assembly.
 Ye J, Ai X, Eugeni EE, Zhang L, Carpenter LR, Jelinek MA, Freitas MA, Parthun MR.
 Mol Cell. 2005 Apr 1;18(1):123-30. [PMID: 15808514
Functional Description
 Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. Together with SPT15/TBP UAF seems to stimulate basal transcription to a fully activated level. 
Sequence Annotation
 DNA_BIND 17 21
 MOD_RES 6 6 N6-acetyllysine.
 MOD_RES 9 9 N6-acetyllysine.
 MOD_RES 13 13 N6-acetyllysine.
 MOD_RES 17 17 N6-acetyllysine.
 MOD_RES 61 61 Phosphoserine.
 MOD_RES 65 65 Phosphoserine.
 MOD_RES 80 80 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Chromosome; Complete proteome; Direct protein sequencing; DNA-binding; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 103 AA 
Protein Sequence
MSGRGKGGKG LGKGGAKRHR KILRDNIQGI TKPAIRRLAR RGGVKRISGL IYEEVRAVLK 60
SFLESVIRDS VTYTEHAKRK TVTSLDVVYA LKRQGRTLYG FGG 103 
Gene Ontology
 GO:0000788; C:nuclear nucleosome; TAS:SGD.
 GO:0031298; C:replication fork protection complex; IDA:SGD.
 GO:0003677; F:DNA binding; TAS:SGD.
 GO:0006333; P:chromatin assembly or disassembly; TAS:SGD.
 GO:0034729; P:histone H3-K79 methylation; IMP:SGD.
 GO:0006334; P:nucleosome assembly; IEA:InterPro.
 GO:0043935; P:sexual sporulation resulting in formation of a cellular spore; IMP:SGD. 
Interpro
 IPR009072; Histone-fold.
 IPR007125; Histone_core_D.
 IPR001951; Histone_H4.
 IPR019809; Histone_H4_CS. 
Pfam
 PF00125; Histone 
SMART
 SM00417; H4 
PROSITE
 PS00047; HISTONE_H4 
PRINTS
 PR00623; HISTONEH4.