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Q8C2B3 (HDAC7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase 7

Short name=HD7
EC=3.5.1.98
Alternative name(s):
Histone deacetylase 7A
Short name=HD7a
Gene names
Name:Hdac7
Synonyms:Hdac7a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length938 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

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

Subunit structure

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. Ref.1 Ref.4 Ref.5 Ref.6 Ref.11

Subcellular location

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. Ref.1 Ref.5 Ref.6

Tissue specificity

Highly expressed in heart and lung. Expressed at intermediate level in muscle. Ref.1 Ref.5

Domain

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

Post-translational modification

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. Ref.6 Ref.9

Miscellaneous

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

Sequence similarities

Belongs to the histone deacetylase family. HD type 2 subfamily.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Hydrolase
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell activation

Traceable author statement PubMed 12711221. Source: UniProtKB

B cell differentiation

Traceable author statement PubMed 12711221. Source: UniProtKB

cell-cell junction assembly

Inferred from mutant phenotype PubMed 16873063. Source: MGI

chromatin modification

Traceable author statement PubMed 12711221. Source: UniProtKB

histone deacetylation

Traceable author statement PubMed 12711221. Source: GOC

inflammatory response

Traceable author statement PubMed 12711221. Source: UniProtKB

negative regulation of interleukin-2 production

Inferred from electronic annotation. Source: Ensembl

negative regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of striated muscle tissue development

Traceable author statement PubMed 12711221. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1. Source: MGI

negative regulation of transcription, DNA-templated

Traceable author statement PubMed 12711221. Source: UniProtKB

nervous system development

Traceable author statement PubMed 12711221. Source: UniProtKB

positive regulation of cell migration involved in sprouting angiogenesis

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

vasculogenesis

Inferred from mutant phenotype PubMed 16873063. Source: MGI

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

histone deacetylase complex

Traceable author statement PubMed 12711221. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function14-3-3 protein binding

Inferred from sequence or structural similarity. Source: UniProtKB

NAD-dependent histone deacetylase activity (H3-K14 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K18 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K9 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H4-K16 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

chromatin binding

Inferred from direct assay PubMed 16109736. Source: MGI

histone deacetylase activity

Traceable author statement PubMed 12711221. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.6PubMed 15166223PubMed 16615898PubMed 16956611. Source: IntAct

transcription corepressor activity

Inferred from direct assay Ref.1. Source: MGI

transcription factor binding

Traceable author statement PubMed 12711221. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YwhaeP622596EBI-643830,EBI-356480

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8C2B3-1)

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.
Isoform 2 (identifier: Q8C2B3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: Missing.
     249-249: E → EALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAPAR
     376-382: Missing.
Isoform 3 (identifier: Q8C2B3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: Missing.
     249-249: E → EALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAPAR
Isoform 4 (identifier: Q8C2B3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     138-161: Missing.
     249-249: E → EALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAPAR
     376-382: Missing.
Isoform 5 (identifier: Q8C2B3-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: Missing.
Isoform 6 (identifier: Q8C2B3-6)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 938938Histone deacetylase 7
PRO_0000114706

Regions

Region1 – 121121Interaction with MEF2C
Region2 – 254253Transcription repression 1
Region72 – 172101Interaction with MEF2A
Region241 – 533293Transcription repression 2
Region505 – 852348Histone deacetylase
Region864 – 93875Interaction with SIN3A
Motif904 – 93835Nuclear export signal By similarity
Compositional bias220 – 2267Poly-Ser

Sites

Active site6571 By similarity
Metal binding5201Zinc By similarity
Metal binding5221Zinc By similarity
Metal binding5281Zinc By similarity
Metal binding6051Zinc By similarity
Site8301Contributes to catalysis By similarity

Amino acid modifications

Modified residue1321Phosphoserine By similarity
Modified residue1781Phosphoserine; by MARK2, MARK3 and PKD/PRKD1 Probable
Modified residue2041Phosphoserine; by PKD/PRKD2 By similarity
Modified residue3441Phosphoserine; by PKD/PRKD1 Ref.9
Modified residue4791Phosphoserine; by PKD/PRKD1 Ref.9

Natural variations

Alternative sequence1 – 2222Missing in isoform 2, isoform 3 and isoform 5.
VSP_007432
Alternative sequence138 – 16124Missing in isoform 4 and isoform 6.
VSP_007433
Alternative sequence2491E → EALLGQRLRLQETSLAPFAL PTVSLLPAITLGLPAPAR in isoform 2, isoform 3 and isoform 4.
VSP_007434
Alternative sequence376 – 3827Missing in isoform 2 and isoform 4.
VSP_007435

Experimental info

Mutagenesis1781S → A: Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE. Ref.6
Mutagenesis3441S → A: Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE. Ref.6
Mutagenesis4791S → A: Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE. Ref.6
Mutagenesis6571H → A: Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3. Ref.4 Ref.5
Mutagenesis6921D → A: Disrupts the dot-like nuclear pattern. Ref.4
Mutagenesis6941D → A: Disrupts the dot-like nuclear pattern. Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3. Ref.4
Mutagenesis7171H → A: Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3. Ref.4
Sequence conflict1691E → G in BAC27161. Ref.2
Sequence conflict1831K → M in BAC29493. Ref.2
Sequence conflict2281P → T in BAC27161. Ref.2
Sequence conflict4871L → M in AAF31419. Ref.1
Sequence conflict4871L → M in BAC40598. Ref.2
Sequence conflict4871L → M in BAC40666. Ref.2
Sequence conflict6451K → R in BAC29493. Ref.2
Sequence conflict6611S → P in BAC40598. Ref.2
Sequence conflict7371G → A in AAF31419. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 16, 2003. Version 2.
Checksum: 8D4B455CE6F95483

FASTA938101,287
        10         20         30         40         50         60 
MHSPGAGCPA LQPDTPGSQP QPMDLRVGQR PTVEPPPEPA LLTLQHPQRL HRHLFLAGLH 

        70         80         90        100        110        120 
QQQRSAEPMR LSMDPPMPEL QGGQQEQELR QLLNKDKSKR SAVASSVVKQ KLAEVILKKQ 

       130        140        150        160        170        180 
QAALERTVHP SSPSIPYRTL EPLDTEGAAR SVLSSFLPPV PSLPTEPPEH FPLRKTVSEP 

       190        200        210        220        230        240 
NLKLRYKPKK SLERRKNPLL RKESAPPSLR RRPAETLGDS SPSSSSTPAS GCSSPNDSEH 

       250        260        270        280        290        300 
GPNPALGSEA DGDRRTHSTL GPRGPVLGNP HAPLFLHHGL EPEAGGTLPS RLQPILLLDP 

       310        320        330        340        350        360 
SVSHAPLWTV PGLGPLPFHF AQPLLTTERL SGSGLHRPLN RTRSEPLPPS ATASPLLAPL 

       370        380        390        400        410        420 
QPRQDRLKPH VQLIKPAISP PQRPAKPSEK PRLRQIPSAE DLETDGGGVG PMANDGLEHR 

       430        440        450        460        470        480 
ESGRGPPEGR GSISLQQHQQ VPPWEQQHLA GRLSQGSPGD SVLIPLAQVG HRPLSRTQSS 

       490        500        510        520        530        540 
PAAPVSLLSP EPTCQTQVLN SSETPATGLV YDSVMLKHQC SCGDNSKHPE HAGRIQSIWS 

       550        560        570        580        590        600 
RLQERGLRSQ CECLRGRKAS LEELQSVHSE RHVLLYGTNP LSRLKLDNGK LTGLLAQRTF 

       610        620        630        640        650        660 
VMLPCGGVGV DTDTIWNELH SSNAARWAAG SVTDLAFKVA SRELKNGFAV VRPPGHHADH 

       670        680        690        700        710        720 
STAMGFCFFN SVAIACRQLQ QHGKASKILI VDWDVHHGNG TQQTFYQDPS VLYISLHRHD 

       730        740        750        760        770        780 
DGNFFPGSGA VDEVGTGSGE GFNVNVAWAG GLDPPMGDPE YLAAFRIVVM PIAREFAPDL 

       790        800        810        820        830        840 
VLVSAGFDAA EGHPAPLGGY HVSAKCFGYM TQQLMNLAGG AVVLALEGGH DLTAICDASE 

       850        860        870        880        890        900 
ACVAALLGNK VDPLSEESWK QKPNLSAIRS LEAVVRVHRK YWGCMQRLAS CPDSWLPRVP 

       910        920        930 
GADAEVEAVT ALASLSVGIL AEDRPSERLV EEEEPMNL 

« Hide

Isoform 2 [UniParc].

Checksum: 035DE255A4F44F7E
Show »

FASTA946102,289
Isoform 3 [UniParc].

Checksum: 4D87C0E22274202C
Show »

FASTA953102,980
Isoform 4 [UniParc].

Checksum: 5DD4D8F2A30A8C16
Show »

FASTA944101,910
Isoform 5 [UniParc].

Checksum: 1586B7308A24964A
Show »

FASTA91699,131
Isoform 6 [UniParc].

Checksum: 23AD714981D53FC7
Show »

FASTA91498,752

References

« Hide 'large scale' references
[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. 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] (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]"Identification of a nuclear domain with deacetylase activity."
Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.
Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS37188.1. [Q8C2B3-1]
CCDS57004.1. [Q8C2B3-5]
CCDS57005.1. [Q8C2B3-2]
CCDS57006.1. [Q8C2B3-3]
CCDS57007.1. [Q8C2B3-4]
RefSeqNP_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]
UniGeneMm.384027.

3D structure databases

ProteinModelPortalQ8C2B3.
SMRQ8C2B3. Positions 507-887.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207862. 5 interactions.
DIPDIP-42594N.
IntActQ8C2B3. 4 interactions.
MINTMINT-1551781.

Chemistry

BindingDBQ8C2B3.

PTM databases

PhosphoSiteQ8C2B3.

Proteomic databases

PaxDbQ8C2B3.
PRIDEQ8C2B3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000079838; ENSMUSP00000078766; ENSMUSG00000022475. [Q8C2B3-4]
ENSMUST00000088402; ENSMUSP00000085744; ENSMUSG00000022475. [Q8C2B3-1]
ENSMUST00000116408; ENSMUSP00000112109; ENSMUSG00000022475. [Q8C2B3-5]
ENSMUST00000116409; ENSMUSP00000112110; ENSMUSG00000022475. [Q8C2B3-3]
ENSMUST00000118294; ENSMUSP00000113380; ENSMUSG00000022475. [Q8C2B3-2]
GeneID56233.
KEGGmmu:56233.
UCSCuc007xle.2. mouse. [Q8C2B3-1]
uc007xlf.2. mouse. [Q8C2B3-2]
uc007xlg.2. mouse. [Q8C2B3-4]
uc007xlh.2. mouse. [Q8C2B3-3]

Organism-specific databases

CTD51564.
MGIMGI:1891835. Hdac7.

Phylogenomic databases

eggNOGCOG0123.
GeneTreeENSGT00530000062809.
HOGENOMHOG000232065.
HOVERGENHBG057100.
KOK11408.
OMAAFRIVVM.
OrthoDBEOG7RFTH5.
PhylomeDBQ8C2B3.
TreeFamTF106173.

Gene expression databases

ArrayExpressQ8C2B3.
BgeeQ8C2B3.
CleanExMM_HDAC7.
GenevestigatorQ8C2B3.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR017320. Histone_deAcase_II_euk.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037911. HDAC_II_euk. 1 hit.
PRINTSPR01270. HDASUPER.
ProtoNetSearch...

Other

ChiTaRSHDAC7. mouse.
NextBio312136.
PMAP-CutDBQ8C2B3.
PROQ8C2B3.
SOURCESearch...

Entry information

Entry nameHDAC7_MOUSE
AccessionPrimary (citable) accession number: Q8C2B3
Secondary accession number(s): Q8C2C9 expand/collapse secondary AC list , Q8C8X4, Q8CB80, Q8CDA3, Q9JL72
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 16, 2003
Last modified: July 9, 2014
This is version 123 of the entry and version 2 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