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Q8BY71 (HAT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone acetyltransferase type B catalytic subunit

EC=2.3.1.48
Alternative name(s):
Histone acetyltransferase 1
Gene names
Name:Hat1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Subunit structure

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.

Subcellular location

Nucleus matrix By similarity.

Sequence similarities

Belongs to the HAT1 family.

Ontologies

Keywords
   Cellular componentNucleus
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin silencing at telomere

Inferred from electronic annotation. Source: InterPro

response to nutrient

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhistone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 416415Histone acetyltransferase type B catalytic subunit
PRO_0000227729

Amino acid modifications

Modified residue21N-acetylalanine
Modified residue61N6-acetyllysine
Modified residue121N6-acetyllysine

Sequences

Sequence LengthMass (Da)Tools
Q8BY71 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: A20D53ABF1A7C824

FASTA41649,278
        10         20         30         40         50         60 
MAALEKFLVE YKSAVEKKLA EYKCNTNTAI ELKLVRFPED LENDIRTFFP EYTHQLFGDD 

        70         80         90        100        110        120 
ETAFGYKGLK ILLYYIAGSL STLFRVEYSS KVDENFDCVE ADDVEGKIRQ IIPPGFCTNT 

       130        140        150        160        170        180 
NDFLSLLEKE TNFKPFGTLL HTYTVPSQTG GETFTFQIHK ADMTCRGFRE YHERLQTFLM 

       190        200        210        220        230        240 
WFIETASFID VDDERWHYFL VFEKYNKDGA TLFATVGYMT VYNYYVYPDK TRPRVSQMLI 

       250        260        270        280        290        300 
LTPFQGQGHG AQLLETVHRY YISFPTVLDI TAEDPSRSYL KLRDFVLVKF CQFLPSFSRE 

       310        320        330        340        350        360 
RLLQGFSEDM AIQAQQMFKI NKQHARRVYE ILRLLVTDMS DAEQYRSYRL DIKRRLISPY 

       370        380        390        400        410 
KKKQRDLAKM KKCLRPEELT NQMNQIEISV QHEQLEERFQ ELVEDYRRVI ERLAQE 

« Hide

References

[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. expand/collapse author list , 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(2005) [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(2004) [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(2013) [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK041700 mRNA. Translation: BAC31038.1.
AK169315 mRNA. Translation: BAE41070.1.
BC055460 mRNA. Translation: AAH55460.1.
RefSeqNP_080391.2. NM_026115.4.
UniGeneMm.272472.

3D structure databases

ProteinModelPortalQ8BY71.
SMRQ8BY71. Positions 20-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BY71. 3 interactions.

PTM databases

PhosphoSiteQ8BY71.

Proteomic databases

PaxDbQ8BY71.
PRIDEQ8BY71.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028408; ENSMUSP00000028408; ENSMUSG00000027018.
GeneID107435.
KEGGmmu:107435.
UCSCuc008kap.1. mouse.

Organism-specific databases

CTD8520.
MGIMGI:96013. Hat1.

Phylogenomic databases

eggNOGNOG326277.
GeneTreeENSGT00390000007069.
HOGENOMHOG000231943.
HOVERGENHBG005945.
KOK11303.

Gene expression databases

ArrayExpressQ8BY71.
BgeeQ8BY71.
CleanExMM_HAT1.
GenevestigatorQ8BY71.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
[Graphical view]
PANTHERPTHR12046. PTHR12046. 1 hit.
PfamPF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMSSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Other

ChiTaRSHAT1. mouse.
NextBio358792.
PROQ8BY71.
SOURCESearch...

Entry information

Entry nameHAT1_MOUSE
AccessionPrimary (citable) accession number: Q8BY71
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 1, 2003
Last modified: March 19, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot