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Q8C2B3

- HDAC7_MOUSE

UniProt

Q8C2B3 - HDAC7_MOUSE

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Protein

Histone deacetylase 7

Gene

Hdac7

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

Functioni

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors.1 Publication

Catalytic activityi

Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi520 – 5201ZincBy similarity
Metal bindingi522 – 5221ZincBy similarity
Metal bindingi528 – 5281ZincBy similarity
Metal bindingi605 – 6051ZincBy similarity
Active sitei657 – 6571By similarity
Sitei830 – 8301Contributes to catalysisBy similarity

GO - Molecular functioni

  1. 14-3-3 protein binding Source: UniProtKB
  2. chromatin binding Source: MGI
  3. histone deacetylase activity Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  6. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
  7. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
  8. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
  9. transcription corepressor activity Source: MGI
  10. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. B cell activation Source: UniProtKB
  2. B cell differentiation Source: UniProtKB
  3. cell-cell junction assembly Source: MGI
  4. chromatin modification Source: UniProtKB
  5. histone deacetylation Source: GOC
  6. inflammatory response Source: UniProtKB
  7. negative regulation of interleukin-2 production Source: Ensembl
  8. negative regulation of osteoblast differentiation Source: Ensembl
  9. negative regulation of striated muscle tissue development Source: UniProtKB
  10. negative regulation of transcription, DNA-templated Source: UniProtKB
  11. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  12. nervous system development Source: UniProtKB
  13. positive regulation of cell migration involved in sprouting angiogenesis Source: Ensembl
  14. transcription, DNA-templated Source: UniProtKB-KW
  15. vasculogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 7 (EC:3.5.1.98)
Short name:
HD7
Alternative name(s):
Histone deacetylase 7A
Short name:
HD7a
Gene namesi
Name:Hdac7
Synonyms:Hdac7a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1891835. Hdac7.

Subcellular locationi

Nucleus. Cytoplasm
Note: In the nucleus, it associates with distinct subnuclear dot-like structures. Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. histone deacetylase complex Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi178 – 1781S → A: Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE. 1 Publication
Mutagenesisi344 – 3441S → A: Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE. 1 Publication
Mutagenesisi479 – 4791S → A: Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE. 1 Publication
Mutagenesisi657 – 6571H → A: Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3. 2 Publications
Mutagenesisi692 – 6921D → A: Disrupts the dot-like nuclear pattern. 1 Publication
Mutagenesisi694 – 6941D → A: Disrupts the dot-like nuclear pattern. Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3. 1 Publication
Mutagenesisi717 – 7171H → A: Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 938938Histone deacetylase 7PRO_0000114706Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei132 – 1321PhosphoserineBy similarity
Modified residuei178 – 1781Phosphoserine; by MARK2, MARK3 and PKD/PRKD11 Publication
Modified residuei204 – 2041Phosphoserine; by PKD/PRKD2By similarity
Modified residuei344 – 3441Phosphoserine; by PKD/PRKD11 Publication
Modified residuei479 – 4791Phosphoserine; by PKD/PRKD11 Publication

Post-translational modificationi

May be phosphorylated by CaMK1. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylation at Ser-178 by MARK2, MARK3 and PRKD1 promotes interaction with 14-3-3 proteins and export from the nucleus. Phosphorylation at Ser-178 is a prerequisite for phosphorylation at Ser-204 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8C2B3.
PaxDbiQ8C2B3.
PRIDEiQ8C2B3.

PTM databases

PhosphoSiteiQ8C2B3.

Miscellaneous databases

PMAP-CutDBQ8C2B3.

Expressioni

Tissue specificityi

Highly expressed in heart and lung. Expressed at intermediate level in muscle.2 Publications

Gene expression databases

BgeeiQ8C2B3.
CleanExiMM_HDAC7.
ExpressionAtlasiQ8C2B3. baseline and differential.
GenevestigatoriQ8C2B3.

Interactioni

Subunit structurei

Interacts with KDM5B (By similarity). Interacts with KAT5 and EDNRA. Interacts with HDAC1, HDAC2, HDAC3, HDAC4, HDAC5, NCOR1, NCOR2, SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1, SAP30 and MBD3. Interacts with the 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C. Interacts with ZMYND15. Interacts with PML (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
YwhaeP622596EBI-643830,EBI-356480

Protein-protein interaction databases

BioGridi207862. 5 interactions.
DIPiDIP-42594N.
IntActiQ8C2B3. 4 interactions.
MINTiMINT-1551781.

Structurei

3D structure databases

ProteinModelPortaliQ8C2B3.
SMRiQ8C2B3. Positions 507-887.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 121121Interaction with MEF2CAdd
BLAST
Regioni2 – 254253Transcription repression 1Add
BLAST
Regioni72 – 172101Interaction with MEF2AAdd
BLAST
Regioni241 – 533293Transcription repression 2Add
BLAST
Regioni505 – 852348Histone deacetylaseAdd
BLAST
Regioni864 – 93875Interaction with SIN3AAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi904 – 93835Nuclear export signalBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi220 – 2267Poly-Ser

Domaini

The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm.By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0123.
GeneTreeiENSGT00530000062809.
HOGENOMiHOG000232065.
HOVERGENiHBG057100.
InParanoidiQ8C2B3.
KOiK11408.
OMAiAFRIVVM.
OrthoDBiEOG7RFTH5.
PhylomeDBiQ8C2B3.
TreeFamiTF106173.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR017320. Histone_deAcase_II_euk.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037911. HDAC_II_euk. 1 hit.
PRINTSiPR01270. HDASUPER.

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8C2B3-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MHSPGAGCPA LQPDTPGSQP QPMDLRVGQR PTVEPPPEPA LLTLQHPQRL
60 70 80 90 100
HRHLFLAGLH QQQRSAEPMR LSMDPPMPEL QGGQQEQELR QLLNKDKSKR
110 120 130 140 150
SAVASSVVKQ KLAEVILKKQ QAALERTVHP SSPSIPYRTL EPLDTEGAAR
160 170 180 190 200
SVLSSFLPPV PSLPTEPPEH FPLRKTVSEP NLKLRYKPKK SLERRKNPLL
210 220 230 240 250
RKESAPPSLR RRPAETLGDS SPSSSSTPAS GCSSPNDSEH GPNPALGSEA
260 270 280 290 300
DGDRRTHSTL GPRGPVLGNP HAPLFLHHGL EPEAGGTLPS RLQPILLLDP
310 320 330 340 350
SVSHAPLWTV PGLGPLPFHF AQPLLTTERL SGSGLHRPLN RTRSEPLPPS
360 370 380 390 400
ATASPLLAPL QPRQDRLKPH VQLIKPAISP PQRPAKPSEK PRLRQIPSAE
410 420 430 440 450
DLETDGGGVG PMANDGLEHR ESGRGPPEGR GSISLQQHQQ VPPWEQQHLA
460 470 480 490 500
GRLSQGSPGD SVLIPLAQVG HRPLSRTQSS PAAPVSLLSP EPTCQTQVLN
510 520 530 540 550
SSETPATGLV YDSVMLKHQC SCGDNSKHPE HAGRIQSIWS RLQERGLRSQ
560 570 580 590 600
CECLRGRKAS LEELQSVHSE RHVLLYGTNP LSRLKLDNGK LTGLLAQRTF
610 620 630 640 650
VMLPCGGVGV DTDTIWNELH SSNAARWAAG SVTDLAFKVA SRELKNGFAV
660 670 680 690 700
VRPPGHHADH STAMGFCFFN SVAIACRQLQ QHGKASKILI VDWDVHHGNG
710 720 730 740 750
TQQTFYQDPS VLYISLHRHD DGNFFPGSGA VDEVGTGSGE GFNVNVAWAG
760 770 780 790 800
GLDPPMGDPE YLAAFRIVVM PIAREFAPDL VLVSAGFDAA EGHPAPLGGY
810 820 830 840 850
HVSAKCFGYM TQQLMNLAGG AVVLALEGGH DLTAICDASE ACVAALLGNK
860 870 880 890 900
VDPLSEESWK QKPNLSAIRS LEAVVRVHRK YWGCMQRLAS CPDSWLPRVP
910 920 930
GADAEVEAVT ALASLSVGIL AEDRPSERLV EEEEPMNL
Length:938
Mass (Da):101,287
Last modified:May 16, 2003 - v2
Checksum:i8D4B455CE6F95483
GO
Isoform 2 (identifier: Q8C2B3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: Missing.
     249-249: E → EALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAPAR
     376-382: Missing.

Show »
Length:946
Mass (Da):102,289
Checksum:i035DE255A4F44F7E
GO
Isoform 3 (identifier: Q8C2B3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: Missing.
     249-249: E → EALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAPAR

Show »
Length:953
Mass (Da):102,980
Checksum:i4D87C0E22274202C
GO
Isoform 4 (identifier: Q8C2B3-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     138-161: Missing.
     249-249: E → EALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAPAR
     376-382: Missing.

Show »
Length:944
Mass (Da):101,910
Checksum:i5DD4D8F2A30A8C16
GO
Isoform 5 (identifier: Q8C2B3-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: Missing.

Show »
Length:916
Mass (Da):99,131
Checksum:i1586B7308A24964A
GO
Isoform 6 (identifier: Q8C2B3-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     138-161: Missing.

Show »
Length:914
Mass (Da):98,752
Checksum:i23AD714981D53FC7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691E → G in BAC27161. (PubMed:16141072)Curated
Sequence conflicti183 – 1831K → M in BAC29493. (PubMed:16141072)Curated
Sequence conflicti228 – 2281P → T in BAC27161. (PubMed:16141072)Curated
Sequence conflicti487 – 4871L → M in AAF31419. (PubMed:10640276)Curated
Sequence conflicti487 – 4871L → M in BAC40598. (PubMed:16141072)Curated
Sequence conflicti487 – 4871L → M in BAC40666. (PubMed:16141072)Curated
Sequence conflicti645 – 6451K → R in BAC29493. (PubMed:16141072)Curated
Sequence conflicti661 – 6611S → P in BAC40598. (PubMed:16141072)Curated
Sequence conflicti737 – 7371G → A in AAF31419. (PubMed:10640276)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2222Missing in isoform 2, isoform 3 and isoform 5. 1 PublicationVSP_007432Add
BLAST
Alternative sequencei138 – 16124Missing in isoform 4 and isoform 6. 1 PublicationVSP_007433Add
BLAST
Alternative sequencei249 – 2491E → EALLGQRLRLQETSLAPFAL PTVSLLPAITLGLPAPAR in isoform 2, isoform 3 and isoform 4. 1 PublicationVSP_007434
Alternative sequencei376 – 3827Missing in isoform 2 and isoform 4. 1 PublicationVSP_007435

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF207749 mRNA. Translation: AAF31419.1.
AK030863 mRNA. Translation: BAC27161.1.
AK036586 mRNA. Translation: BAC29493.1.
AK044287 mRNA. Translation: BAC31856.1.
AK088828 mRNA. Translation: BAC40598.1.
AK088945 mRNA. Translation: BAC40666.1.
BC057332 mRNA. Translation: AAH57332.1.
CCDSiCCDS37188.1. [Q8C2B3-1]
CCDS57004.1. [Q8C2B3-5]
CCDS57005.1. [Q8C2B3-2]
CCDS57006.1. [Q8C2B3-3]
CCDS57007.1. [Q8C2B3-4]
RefSeqiNP_001191204.1. NM_001204275.1. [Q8C2B3-3]
NP_001191205.1. NM_001204276.1. [Q8C2B3-2]
NP_001191206.1. NM_001204277.1. [Q8C2B3-4]
NP_001191207.1. NM_001204278.1. [Q8C2B3-5]
NP_062518.2. NM_019572.3. [Q8C2B3-1]
XP_006521268.1. XM_006521205.1.
XP_006521269.1. XM_006521206.1. [Q8C2B3-3]
XP_006521270.1. XM_006521207.1. [Q8C2B3-3]
XP_006521271.1. XM_006521208.1. [Q8C2B3-3]
XP_006521272.1. XM_006521209.1. [Q8C2B3-3]
XP_006521273.1. XM_006521210.1. [Q8C2B3-3]
UniGeneiMm.384027.

Genome annotation databases

EnsembliENSMUST00000079838; ENSMUSP00000078766; ENSMUSG00000022475. [Q8C2B3-4]
ENSMUST00000088402; ENSMUSP00000085744; ENSMUSG00000022475. [Q8C2B3-1]
ENSMUST00000116408; ENSMUSP00000112109; ENSMUSG00000022475. [Q8C2B3-5]
ENSMUST00000116409; ENSMUSP00000112110; ENSMUSG00000022475. [Q8C2B3-3]
ENSMUST00000118294; ENSMUSP00000113380; ENSMUSG00000022475. [Q8C2B3-2]
GeneIDi56233.
KEGGimmu:56233.
UCSCiuc007xle.2. mouse. [Q8C2B3-1]
uc007xlf.2. mouse. [Q8C2B3-2]
uc007xlg.2. mouse. [Q8C2B3-4]
uc007xlh.2. mouse. [Q8C2B3-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF207749 mRNA. Translation: AAF31419.1 .
AK030863 mRNA. Translation: BAC27161.1 .
AK036586 mRNA. Translation: BAC29493.1 .
AK044287 mRNA. Translation: BAC31856.1 .
AK088828 mRNA. Translation: BAC40598.1 .
AK088945 mRNA. Translation: BAC40666.1 .
BC057332 mRNA. Translation: AAH57332.1 .
CCDSi CCDS37188.1. [Q8C2B3-1 ]
CCDS57004.1. [Q8C2B3-5 ]
CCDS57005.1. [Q8C2B3-2 ]
CCDS57006.1. [Q8C2B3-3 ]
CCDS57007.1. [Q8C2B3-4 ]
RefSeqi NP_001191204.1. NM_001204275.1. [Q8C2B3-3 ]
NP_001191205.1. NM_001204276.1. [Q8C2B3-2 ]
NP_001191206.1. NM_001204277.1. [Q8C2B3-4 ]
NP_001191207.1. NM_001204278.1. [Q8C2B3-5 ]
NP_062518.2. NM_019572.3. [Q8C2B3-1 ]
XP_006521268.1. XM_006521205.1.
XP_006521269.1. XM_006521206.1. [Q8C2B3-3 ]
XP_006521270.1. XM_006521207.1. [Q8C2B3-3 ]
XP_006521271.1. XM_006521208.1. [Q8C2B3-3 ]
XP_006521272.1. XM_006521209.1. [Q8C2B3-3 ]
XP_006521273.1. XM_006521210.1. [Q8C2B3-3 ]
UniGenei Mm.384027.

3D structure databases

ProteinModelPortali Q8C2B3.
SMRi Q8C2B3. Positions 507-887.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207862. 5 interactions.
DIPi DIP-42594N.
IntActi Q8C2B3. 4 interactions.
MINTi MINT-1551781.

PTM databases

PhosphoSitei Q8C2B3.

Proteomic databases

MaxQBi Q8C2B3.
PaxDbi Q8C2B3.
PRIDEi Q8C2B3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000079838 ; ENSMUSP00000078766 ; ENSMUSG00000022475 . [Q8C2B3-4 ]
ENSMUST00000088402 ; ENSMUSP00000085744 ; ENSMUSG00000022475 . [Q8C2B3-1 ]
ENSMUST00000116408 ; ENSMUSP00000112109 ; ENSMUSG00000022475 . [Q8C2B3-5 ]
ENSMUST00000116409 ; ENSMUSP00000112110 ; ENSMUSG00000022475 . [Q8C2B3-3 ]
ENSMUST00000118294 ; ENSMUSP00000113380 ; ENSMUSG00000022475 . [Q8C2B3-2 ]
GeneIDi 56233.
KEGGi mmu:56233.
UCSCi uc007xle.2. mouse. [Q8C2B3-1 ]
uc007xlf.2. mouse. [Q8C2B3-2 ]
uc007xlg.2. mouse. [Q8C2B3-4 ]
uc007xlh.2. mouse. [Q8C2B3-3 ]

Organism-specific databases

CTDi 51564.
MGIi MGI:1891835. Hdac7.

Phylogenomic databases

eggNOGi COG0123.
GeneTreei ENSGT00530000062809.
HOGENOMi HOG000232065.
HOVERGENi HBG057100.
InParanoidi Q8C2B3.
KOi K11408.
OMAi AFRIVVM.
OrthoDBi EOG7RFTH5.
PhylomeDBi Q8C2B3.
TreeFami TF106173.

Enzyme and pathway databases

Reactomei REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.

Miscellaneous databases

ChiTaRSi Hdac7. mouse.
NextBioi 312136.
PMAP-CutDB Q8C2B3.
PROi Q8C2B3.
SOURCEi Search...

Gene expression databases

Bgeei Q8C2B3.
CleanExi MM_HDAC7.
ExpressionAtlasi Q8C2B3. baseline and differential.
Genevestigatori Q8C2B3.

Family and domain databases

Gene3Di 3.40.800.20. 1 hit.
InterProi IPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR017320. Histone_deAcase_II_euk.
[Graphical view ]
PANTHERi PTHR10625. PTHR10625. 1 hit.
Pfami PF00850. Hist_deacetyl. 1 hit.
[Graphical view ]
PIRSFi PIRSF037911. HDAC_II_euk. 1 hit.
PRINTSi PR01270. HDASUPER.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression."
    Kao H.-Y., Downes M., Ordentlich P., Evans R.M.
    Genes Dev. 14:55-66(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NCOR2 AND SIN3A.
    Strain: C57BL/6.
    Tissue: Brain.
  2. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5 AND 6).
    Strain: C57BL/6J and NOD.
    Tissue: Bone, Retina and Thymus.
  3. "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] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Brain.
  4. Cited for: INTERACTION WITH HDAC1; HDAC2; HDAC3; HDAC4; HDAC5; NCOR1; NCOR2; SIN3A; SIN3B; RBBP4; RBBP7; MTA1L1; SAP30 AND MBD3, MUTAGENESIS OF HIS-657; ASP-692; ASP-694 AND HIS-717.
  5. "A dynamic role for HDAC7 in MEF2-mediated muscle differentiation."
    Dressel U., Bailey P.J., Wang S.-C.M., Downes M., Evans R.M., Muscat G.E.O.
    J. Biol. Chem. 276:17007-17013(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH MEF2C, MUTAGENESIS OF HIS-657.
  6. "Mechanism for nucleocytoplasmic shuttling of histone deacetylase 7."
    Kao H.-Y., Verdel A., Tsai C.-C., Simon C., Juguilon H., Khochbin S.
    J. Biol. Chem. 276:47496-47507(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH YWHAE; MEF2A; MEF2B AND MEF2C, MUTAGENESIS OF SER-178; SER-344 AND SER-479.
  7. "Identification of a signal-responsive nuclear export sequence in class II histone deacetylases."
    McKinsey T.A., Zhang C.-L., Olson E.N.
    Mol. Cell. Biol. 21:6312-6321(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEAR EXPORT SIGNAL.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Control of endothelial cell proliferation and migration by VEGF signaling to histone deacetylase 7."
    Wang S., Li X., Parra M., Verdin E., Bassel-Duby R., Olson E.N.
    Proc. Natl. Acad. Sci. U.S.A. 105:7738-7743(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-178; SER-344 AND SER-479.
  10. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  11. "Zmynd15 encodes a histone deacetylase-dependent transcriptional repressor essential for spermiogenesis and male fertility."
    Yan W., Si Y., Slaymaker S., Li J., Zheng H., Young D.L., Aslanian A., Saunders L., Verdin E., Charo I.F.
    J. Biol. Chem. 285:31418-31426(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZMYND15.

Entry informationi

Entry nameiHDAC7_MOUSE
AccessioniPrimary (citable) accession number: Q8C2B3
Secondary accession number(s): Q8C2C9
, Q8C8X4, Q8CB80, Q8CDA3, Q9JL72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 16, 2003
Last modified: November 26, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Its activity is inhibited by Trichostatin A (TSA), a known histone deacetylase inhibitor.

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