Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

Hdac2 protein

Gene

Hdac2

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

  • core promoter binding Source: RGD
  • enzyme binding Source: RGD
  • heat shock protein binding Source: RGD
  • histone deacetylase activity Source: RGD
  • transcription factor binding Source: RGD

GO - Biological processi

  • behavioral response to ethanol Source: RGD
  • cardiac muscle hypertrophy Source: RGD
  • cellular response to dopamine Source: RGD
  • cellular response to heat Source: RGD
  • cellular response to hydrogen peroxide Source: RGD
  • cellular response to retinoic acid Source: RGD
  • cellular response to transforming growth factor beta stimulus Source: RGD
  • histone deacetylation Source: RGD
  • histone H3 deacetylation Source: RGD
  • negative regulation of dendritic spine development Source: RGD
  • negative regulation of DNA binding Source: RGD
  • negative regulation of neuron projection development Source: RGD
  • negative regulation of peptidyl-lysine acetylation Source: RGD
  • negative regulation of transcription, DNA-templated Source: RGD
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of epithelial to mesenchymal transition Source: RGD
  • positive regulation of interleukin-1 production Source: RGD
  • positive regulation of oligodendrocyte differentiation Source: RGD
  • positive regulation of tumor necrosis factor production Source: RGD
  • positive regulation of tyrosine phosphorylation of Stat3 protein Source: RGD
  • response to amphetamine Source: RGD
  • response to caffeine Source: RGD
  • response to cocaine Source: RGD
  • response to drug Source: RGD
  • response to hyperoxia Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to nicotine Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Hdac2 proteinImported
Gene namesi
Name:Hdac2Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Organism-specific databases

RGDi619976. Hdac2.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: RGD
  • cytoplasm Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2095943.

PTM / Processingi

Proteomic databases

PaxDbiB1WBY8.

Expressioni

Gene expression databases

GenevisibleiB1WBY8. RN.

Interactioni

GO - Molecular functioni

  • enzyme binding Source: RGD
  • heat shock protein binding Source: RGD
  • transcription factor binding Source: RGD

Protein-protein interaction databases

IntActiB1WBY8. 1 interaction.
MINTiMINT-7138457.
STRINGi10116.ENSRNOP00000000742.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 376290Hist_deacetylInterPro annotationAdd
BLAST

Phylogenomic databases

eggNOGiKOG1342. Eukaryota.
COG0123. LUCA.
HOGENOMiHOG000225180.
HOVERGENiHBG057112.
KOiK06067.
PhylomeDBiB1WBY8.
TreeFamiTF106171.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSiPR01270. HDASUPER.
PR01271. HISDACETLASE.

Sequencei

Sequence statusi: Fragment.

B1WBY8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ALRSRALPAP ARRPAPGCPC CEGRRARRLP QPSCLAAGPR RARAAGGGAA
60 70 80 90 100
ARRRRPEPMA YSQGGGKKKV CYYYDGDIGN YYYGQGHPMK PHRIRMTHNL
110 120 130 140 150
LLNYGLYRKM EIYRPHKATA EEMTKYHSDE YIKFLRSIRP DNMSEYSKQM
160 170 180 190 200
QRFNVGEDCP VFDGLFEFCQ LSTGGSVAGA VKLNRQQTDM AVNWAGGLHH
210 220 230 240 250
AKKSEASGFC YVNDIVLAVL ELLKYHQRVL YIDIDIHHGD GVEEAFYTTD
260 270 280 290 300
RVMTVSFHKY GEYFPGTGDL RDIGAGKGKY YAVNFPMRDG IDDESYGQIF
310 320 330 340 350
KPIISKVMEM YQPSAVVLQC GADSLSGDRL GCFNLTVKGH AKCVEVVKTF
360 370 380 390 400
NLPLLMLGGG GYTIRNVARC WTYETAVALD CEIPNELPYN DYFEYFGPDF
410 420 430 440 450
KLHISPSNMT NQNTPEYMEK IKQRLFENLR MLPHAPGVQM QAIPEDAVHE
460 470 480 490 500
DSGDEDGEDP DKRISIRASD KRIACDEEFS DSEDEGEGGR RNVADHKKGA
510 520 530 540
KKARIEEDKK EAEDKRTDVK EEDKSKDNSG EKTDTKGAKS EQLNNP
Length:546
Mass (Da):61,422
Last modified:May 20, 2008 - v1
Checksum:iB57901BFDD8773A1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC161939 mRNA. Translation: AAI61939.1.
RefSeqiNP_445899.1. NM_053447.1.
UniGeneiRn.1797.

Genome annotation databases

GeneIDi84577.
KEGGirno:84577.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC161939 mRNA. Translation: AAI61939.1.
RefSeqiNP_445899.1. NM_053447.1.
UniGeneiRn.1797.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiB1WBY8. 1 interaction.
MINTiMINT-7138457.
STRINGi10116.ENSRNOP00000000742.

Chemistry

ChEMBLiCHEMBL2095943.

Proteomic databases

PaxDbiB1WBY8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi84577.
KEGGirno:84577.

Organism-specific databases

CTDi3066.
RGDi619976. Hdac2.

Phylogenomic databases

eggNOGiKOG1342. Eukaryota.
COG0123. LUCA.
HOGENOMiHOG000225180.
HOVERGENiHBG057112.
KOiK06067.
PhylomeDBiB1WBY8.
TreeFamiTF106171.

Gene expression databases

GenevisibleiB1WBY8. RN.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSiPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: KidneyImported.

Entry informationi

Entry nameiB1WBY8_RAT
AccessioniPrimary (citable) accession number: B1WBY8
Entry historyi
Integrated into UniProtKB/TrEMBL: May 20, 2008
Last sequence update: May 20, 2008
Last modified: June 8, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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 one 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.