UniProt Accession

 HAT1_HUMAN; O14929; Q49A44; Q53QF0; Q53SU4; Q6P594; Q8WWB9 

Genbank Protein ID

 AF030424; AC015976; AC114745; CH471058; BC018682; BC045673; BC063003 

Genbank Nucleotide ID

 AAC02425.1; AAY14731.1; AAX93247.1; EAX11195.1; AAH18682.1; AAH63003.1 

Protein Name

 Histone acetyltransferase type B catalytic subunit 

Protein Synonyms/Alias

 Histone acetyltransferase 1 

Gene Name

 HAT1 

Gene Synonyms/Alias

 KAT1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
9	AGFGAMEKFLVEYKS	ubiquitination	[1, 2, 3]
15	EKFLVEYKSAVEKKL	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
20	EYKSAVEKKLAEYKC	ubiquitination	[8]
26	EKKLAEYKCNTNTAI	ubiquitination	[1, 2, 3]
36	TNTAIELKLVRFPED	ubiquitination	[2]
70	DETAFGYKGLKILLY	ubiquitination	[1, 3]
110	EADDVEGKIRQIIPP	ubiquitination	[2, 11, 12, 13]
280	ITAEDPSKSYVKLRD	ubiquitination	[2, 6, 13]
284	DPSKSYVKLRDFVLV	ubiquitination	[6]
304	LPCFSREKLMQGFNE	ubiquitination	[6]
320	MAIEAQQKFKINKQH	ubiquitination	[6]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] 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]
 [13] 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] 

Functional Description

 Acetylates soluble but not nucleosomal histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, acetylates histone H2A at 'Lys-5' (H2AK5ac). Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. May be involved in nucleosome assembly during DNA replication and repair as part of the histone H3.1 and H3.3 complexes. May play a role in DNA repair in response to free radical damage. 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine.  

Keyword

 3D-structure; Acetylation; Acyltransferase; Alternative splicing; Complete proteome; Cytoplasm; Nucleus; Polymorphism; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 419 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0004402; F:histone acetyltransferase activity; TAS:ProtInc.
 GO:0006348; P:chromatin silencing at telomere; IEA:InterPro.
 GO:0006323; P:DNA packaging; TAS:ProtInc.
 GO:0007584; P:response to nutrient; IEA:Compara. 

Interpro

 IPR016181; Acyl_CoA_acyltransferase.
 IPR019467; Hat1_N.
 IPR017380; Hist_AcTrfase_B-typ_cat-su. 

Pfam

 PF10394; Hat1_N 

SMART

  

PROSITE

  

PRINTS