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Protein

Histone acetyltransferase type B catalytic subunit

Gene

Hat1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei196 – 1961Interaction with histone H4 N-terminusBy similarity
Active sitei273 – 2731Proton donor/acceptorBy similarity

GO - Molecular functioni

  1. H4 histone acetyltransferase activity Source: UniProtKB

GO - Biological processi

  1. chromatin silencing at telomere Source: InterPro
  2. DNA replication-dependent nucleosome assembly Source: MGI
  3. DNA replication-independent nucleosome assembly Source: MGI
  4. histone H4 acetylation Source: UniProtKB
  5. response to nutrient Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_291621. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase type B catalytic subunit (EC:2.3.1.48By similarity)
Alternative name(s):
Histone acetyltransferase 1
Gene namesi
Name:Hat1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:96013. Hat1.

Subcellular locationi

Nucleus matrix By similarity

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: MGI
  2. nuclear chromatin Source: MGI
  3. nuclear matrix Source: UniProtKB-SubCell
  4. nucleoplasm Source: MGI
  5. protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 416415Histone acetyltransferase type B catalytic subunitPRO_0000227729Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei6 – 61N6-acetyllysine1 Publication
Modified residuei12 – 121N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8BY71.
PaxDbiQ8BY71.
PRIDEiQ8BY71.

PTM databases

PhosphoSiteiQ8BY71.

Expressioni

Gene expression databases

BgeeiQ8BY71.
CleanExiMM_HAT1.
ExpressionAtlasiQ8BY71. baseline and differential.
GenevestigatoriQ8BY71.

Interactioni

Subunit structurei

Catalytic subunit of the type B histone acetyltransferase (HAT) complex, composed of RBBP7 and HAT1. Interacts with histones H4 and H2A. The interaction is dependent of the ability of RBBP7 to bind to the N-terminus of histones. Component of the histone H3.1 and H3.3 complexes.By similarity

Protein-protein interaction databases

IntActiQ8BY71. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8BY71.
SMRiQ8BY71. Positions 20-338.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni59 – 613Interaction with histone H4 N-terminusBy similarity
Regioni222 – 2243Interaction with histone H4 N-terminusBy similarity
Regioni238 – 2403Acetyl-CoA bindingBy similarity
Regioni245 – 2517Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Belongs to the HAT1 family.Curated

Phylogenomic databases

eggNOGiNOG326277.
GeneTreeiENSGT00390000007069.
HOGENOMiHOG000231943.
HOVERGENiHBG005945.
InParanoidiQ8BY71.
KOiK11303.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
[Graphical view]
PANTHERiPTHR12046. PTHR12046. 1 hit.
PfamiPF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMiSSF55729. SSF55729. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BY71-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALEKFLVE YKSAVEKKLA EYKCNTNTAI ELKLVRFPED LENDIRTFFP
60 70 80 90 100
EYTHQLFGDD ETAFGYKGLK ILLYYIAGSL STLFRVEYSS KVDENFDCVE
110 120 130 140 150
ADDVEGKIRQ IIPPGFCTNT NDFLSLLEKE TNFKPFGTLL HTYTVPSQTG
160 170 180 190 200
GETFTFQIHK ADMTCRGFRE YHERLQTFLM WFIETASFID VDDERWHYFL
210 220 230 240 250
VFEKYNKDGA TLFATVGYMT VYNYYVYPDK TRPRVSQMLI LTPFQGQGHG
260 270 280 290 300
AQLLETVHRY YISFPTVLDI TAEDPSRSYL KLRDFVLVKF CQFLPSFSRE
310 320 330 340 350
RLLQGFSEDM AIQAQQMFKI NKQHARRVYE ILRLLVTDMS DAEQYRSYRL
360 370 380 390 400
DIKRRLISPY KKKQRDLAKM KKCLRPEELT NQMNQIEISV QHEQLEERFQ
410
ELVEDYRRVI ERLAQE
Length:416
Mass (Da):49,278
Last modified:March 1, 2003 - v1
Checksum:iA20D53ABF1A7C824
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK041700 mRNA. Translation: BAC31038.1.
AK169315 mRNA. Translation: BAE41070.1.
BC055460 mRNA. Translation: AAH55460.1.
CCDSiCCDS16114.1.
RefSeqiNP_080391.2. NM_026115.4.
UniGeneiMm.272472.

Genome annotation databases

EnsembliENSMUST00000028408; ENSMUSP00000028408; ENSMUSG00000027018.
GeneIDi107435.
KEGGimmu:107435.
UCSCiuc008kap.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK041700 mRNA. Translation: BAC31038.1.
AK169315 mRNA. Translation: BAE41070.1.
BC055460 mRNA. Translation: AAH55460.1.
CCDSiCCDS16114.1.
RefSeqiNP_080391.2. NM_026115.4.
UniGeneiMm.272472.

3D structure databases

ProteinModelPortaliQ8BY71.
SMRiQ8BY71. Positions 20-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BY71. 3 interactions.

PTM databases

PhosphoSiteiQ8BY71.

Proteomic databases

MaxQBiQ8BY71.
PaxDbiQ8BY71.
PRIDEiQ8BY71.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028408; ENSMUSP00000028408; ENSMUSG00000027018.
GeneIDi107435.
KEGGimmu:107435.
UCSCiuc008kap.1. mouse.

Organism-specific databases

CTDi8520.
MGIiMGI:96013. Hat1.

Phylogenomic databases

eggNOGiNOG326277.
GeneTreeiENSGT00390000007069.
HOGENOMiHOG000231943.
HOVERGENiHBG005945.
InParanoidiQ8BY71.
KOiK11303.

Enzyme and pathway databases

ReactomeiREACT_291621. HATs acetylate histones.

Miscellaneous databases

ChiTaRSiHat1. mouse.
NextBioi358792.
PROiQ8BY71.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BY71.
CleanExiMM_HAT1.
ExpressionAtlasiQ8BY71. baseline and differential.
GenevestigatoriQ8BY71.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
[Graphical view]
PANTHERiPTHR12046. PTHR12046. 1 hit.
PfamiPF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMiSSF55729. SSF55729. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Heart and Thymus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-6 AND LYS-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiHAT1_MOUSE
AccessioniPrimary (citable) accession number: Q8BY71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 1, 2003
Last modified: April 1, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.