Q8C2B3 (HDAC7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	938 AA.
Sequence status	Complete.
Protein existence	Evidence 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.10
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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell differentiation Traceable author statement PubMed 12711221. Source: UniProtKB cell-cell junction assembly Inferred from mutant phenotype PubMed 16873063. Source: MGI histone H3 deacetylation Inferred from electronic annotation. Source: GOC histone H4 deacetylation Inferred from electronic annotation. Source: GOC inflammatory response Traceable author statement PubMed 12711221. Source: UniProtKB negative regulation of interleukin-2 production Inferred from electronic annotation. Source: Compara negative regulation of osteoblast differentiation Inferred from electronic annotation. Source: Compara 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 nervous system development Traceable author statement PubMed 12711221. Source: UniProtKB positive regulation of cell migration involved in sprouting angiogenesis Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW vasculogenesis Inferred from mutant phenotype PubMed 16873063. Source: MGI
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB histone deacetylase complex Traceable author statement PubMed 12711221. Source: UniProtKB
Molecular_function	14-3-3 protein binding Inferred from sequence or structural similarity. Source: UniProtKB NAD-dependent histone deacetylase activity (H3-K14 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K18 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K9 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H4-K16 specific) Inferred from electronic annotation. Source: 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 transcription corepressor activity Inferred from direct assay Ref.1. Source: MGI transcription factor binding Traceable author statement PubMed 12711221. Source: UniProtKB
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 938	938	Histone deacetylase 7		PRO_0000114706
Regions
	Region	1 – 121	121	Interaction with MEF2C
	Region	2 – 254	253	Transcription repression 1
	Region	72 – 172	101	Interaction with MEF2A
	Region	241 – 533	293	Transcription repression 2
	Region	505 – 852	348	Histone deacetylase
	Region	864 – 938	75	Interaction with SIN3A
	Motif	904 – 938	35	Nuclear export signal By similarity
	Compositional bias	220 – 226	7	Poly-Ser
Sites
	Active site	657	1	By similarity
	Metal binding	520	1	Zinc By similarity
	Metal binding	522	1	Zinc By similarity
	Metal binding	528	1	Zinc By similarity
	Metal binding	605	1	Zinc By similarity
	Site	830	1	Contributes to catalysis By similarity
Amino acid modifications
	Modified residue	132	1	Phosphoserine By similarity
	Modified residue	178	1	Phosphoserine; by MARK2, MARK3 and PKD/PRKD1 Probable
	Modified residue	204	1	Phosphoserine; by PKD/PRKD2 By similarity
	Modified residue	344	1	Phosphoserine; by PKD/PRKD1 Ref.8 Ref.9
	Modified residue	479	1	Phosphoserine; by PKD/PRKD1 Ref.9
Natural variations
	Alternative sequence	1 – 22	22	Missing in isoform 2, isoform 3 and isoform 5.		VSP_007432
	Alternative sequence	138 – 161	24	Missing in isoform 4 and isoform 6.		VSP_007433
	Alternative sequence	249	1	E → EALLGQRLRLQETSLAPFAL PTVSLLPAITLGLPAPAR in isoform 2, isoform 3 and isoform 4.		VSP_007434
	Alternative sequence	376 – 382	7	Missing in isoform 2 and isoform 4.		VSP_007435
Experimental info
	Mutagenesis	178	1	S → A: Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE. Ref.6
	Mutagenesis	344	1	S → A: Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE. Ref.6
	Mutagenesis	479	1	S → A: Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE. Ref.6
	Mutagenesis	657	1	H → A: Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3. Ref.4 Ref.5
	Mutagenesis	692	1	D → A: Disrupts the dot-like nuclear pattern. Ref.4
	Mutagenesis	694	1	D → A: Disrupts the dot-like nuclear pattern. Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3. Ref.4
	Mutagenesis	717	1	H → A: Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3. Ref.4
	Sequence conflict	169	1	E → G in BAC27161. Ref.2
	Sequence conflict	183	1	K → M in BAC29493. Ref.2
	Sequence conflict	228	1	P → T in BAC27161. Ref.2
	Sequence conflict	487	1	L → M in AAF31419. Ref.1
	Sequence conflict	487	1	L → M in BAC40598. Ref.2
	Sequence conflict	487	1	L → M in BAC40666. Ref.2
	Sequence conflict	645	1	K → R in BAC29493. Ref.2
	Sequence conflict	661	1	S → P in BAC40598. Ref.2
	Sequence conflict	737	1	G → A in AAF31419. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 16, 2003. Version 2. Checksum: 8D4B455CE6F95483	FASTA	938	101,287
	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
	Isoform 2 [UniParc]. Checksum: 035DE255A4F44F7E	FASTA	946	102,289
	10 20 30 40 50 60 MDLRVGQRPT VEPPPEPALL TLQHPQRLHR HLFLAGLHQQ QRSAEPMRLS MDPPMPELQG 70 80 90 100 110 120 GQQEQELRQL LNKDKSKRSA VASSVVKQKL AEVILKKQQA ALERTVHPSS PSIPYRTLEP 130 140 150 160 170 180 LDTEGAARSV LSSFLPPVPS LPTEPPEHFP LRKTVSEPNL KLRYKPKKSL ERRKNPLLRK 190 200 210 220 230 240 ESAPPSLRRR PAETLGDSSP SSSSTPASGC SSPNDSEHGP NPALGSEALL GQRLRLQETS 250 260 270 280 290 300 LAPFALPTVS LLPAITLGLP APARADGDRR THSTLGPRGP VLGNPHAPLF LHHGLEPEAG 310 320 330 340 350 360 GTLPSRLQPI LLLDPSVSHA PLWTVPGLGP LPFHFAQPLL TTERLSGSGL HRPLNRTRSE 370 380 390 400 410 420 PLPPSATASP LLAPLQPRQD RLKPHVQLIK RPAKPSEKPR LRQIPSAEDL ETDGGGVGPM 430 440 450 460 470 480 ANDGLEHRES GRGPPEGRGS ISLQQHQQVP PWEQQHLAGR LSQGSPGDSV LIPLAQVGHR 490 500 510 520 530 540 PLSRTQSSPA APVSLLSPEP TCQTQVLNSS ETPATGLVYD SVMLKHQCSC GDNSKHPEHA 550 560 570 580 590 600 GRIQSIWSRL QERGLRSQCE CLRGRKASLE ELQSVHSERH VLLYGTNPLS RLKLDNGKLT 610 620 630 640 650 660 GLLAQRTFVM LPCGGVGVDT DTIWNELHSS NAARWAAGSV TDLAFKVASR ELKNGFAVVR 670 680 690 700 710 720 PPGHHADHST AMGFCFFNSV AIACRQLQQH GKASKILIVD WDVHHGNGTQ QTFYQDPSVL 730 740 750 760 770 780 YISLHRHDDG NFFPGSGAVD EVGTGSGEGF NVNVAWAGGL DPPMGDPEYL AAFRIVVMPI 790 800 810 820 830 840 AREFAPDLVL VSAGFDAAEG HPAPLGGYHV SAKCFGYMTQ QLMNLAGGAV VLALEGGHDL 850 860 870 880 890 900 TAICDASEAC VAALLGNKVD PLSEESWKQK PNLSAIRSLE AVVRVHRKYW GCMQRLASCP 910 920 930 940 DSWLPRVPGA DAEVEAVTAL ASLSVGILAE DRPSERLVEE EEPMNL
	Isoform 3 [UniParc]. Checksum: 4D87C0E22274202C	FASTA	953	102,980
	10 20 30 40 50 60 MDLRVGQRPT VEPPPEPALL TLQHPQRLHR HLFLAGLHQQ QRSAEPMRLS MDPPMPELQG 70 80 90 100 110 120 GQQEQELRQL LNKDKSKRSA VASSVVKQKL AEVILKKQQA ALERTVHPSS PSIPYRTLEP 130 140 150 160 170 180 LDTEGAARSV LSSFLPPVPS LPTEPPEHFP LRKTVSEPNL KLRYKPKKSL ERRKNPLLRK 190 200 210 220 230 240 ESAPPSLRRR PAETLGDSSP SSSSTPASGC SSPNDSEHGP NPALGSEALL GQRLRLQETS 250 260 270 280 290 300 LAPFALPTVS LLPAITLGLP APARADGDRR THSTLGPRGP VLGNPHAPLF LHHGLEPEAG 310 320 330 340 350 360 GTLPSRLQPI LLLDPSVSHA PLWTVPGLGP LPFHFAQPLL TTERLSGSGL HRPLNRTRSE 370 380 390 400 410 420 PLPPSATASP LLAPLQPRQD RLKPHVQLIK PAISPPQRPA KPSEKPRLRQ IPSAEDLETD 430 440 450 460 470 480 GGGVGPMAND GLEHRESGRG PPEGRGSISL QQHQQVPPWE QQHLAGRLSQ GSPGDSVLIP 490 500 510 520 530 540 LAQVGHRPLS RTQSSPAAPV SLLSPEPTCQ TQVLNSSETP ATGLVYDSVM LKHQCSCGDN 550 560 570 580 590 600 SKHPEHAGRI QSIWSRLQER GLRSQCECLR GRKASLEELQ SVHSERHVLL YGTNPLSRLK 610 620 630 640 650 660 LDNGKLTGLL AQRTFVMLPC GGVGVDTDTI WNELHSSNAA RWAAGSVTDL AFKVASRELK 670 680 690 700 710 720 NGFAVVRPPG HHADHSTAMG FCFFNSVAIA CRQLQQHGKA SKILIVDWDV HHGNGTQQTF 730 740 750 760 770 780 YQDPSVLYIS LHRHDDGNFF PGSGAVDEVG TGSGEGFNVN VAWAGGLDPP MGDPEYLAAF 790 800 810 820 830 840 RIVVMPIARE FAPDLVLVSA GFDAAEGHPA PLGGYHVSAK CFGYMTQQLM NLAGGAVVLA 850 860 870 880 890 900 LEGGHDLTAI CDASEACVAA LLGNKVDPLS EESWKQKPNL SAIRSLEAVV RVHRKYWGCM 910 920 930 940 950 QRLASCPDSW LPRVPGADAE VEAVTALASL SVGILAEDRP SERLVEEEEP MNL
	Isoform 4 [UniParc]. Checksum: 5DD4D8F2A30A8C16	FASTA	944	101,910
	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 SSPSIPYSLP TEPPEHFPLR KTVSEPNLKL RYKPKKSLER RKNPLLRKES 190 200 210 220 230 240 APPSLRRRPA ETLGDSSPSS SSTPASGCSS PNDSEHGPNP ALGSEALLGQ RLRLQETSLA 250 260 270 280 290 300 PFALPTVSLL PAITLGLPAP ARADGDRRTH STLGPRGPVL GNPHAPLFLH HGLEPEAGGT 310 320 330 340 350 360 LPSRLQPILL LDPSVSHAPL WTVPGLGPLP FHFAQPLLTT ERLSGSGLHR PLNRTRSEPL 370 380 390 400 410 420 PPSATASPLL APLQPRQDRL KPHVQLIKRP AKPSEKPRLR QIPSAEDLET DGGGVGPMAN 430 440 450 460 470 480 DGLEHRESGR GPPEGRGSIS LQQHQQVPPW EQQHLAGRLS QGSPGDSVLI PLAQVGHRPL 490 500 510 520 530 540 SRTQSSPAAP VSLLSPEPTC QTQVLNSSET PATGLVYDSV MLKHQCSCGD NSKHPEHAGR 550 560 570 580 590 600 IQSIWSRLQE RGLRSQCECL RGRKASLEEL QSVHSERHVL LYGTNPLSRL KLDNGKLTGL 610 620 630 640 650 660 LAQRTFVMLP CGGVGVDTDT IWNELHSSNA ARWAAGSVTD LAFKVASREL KNGFAVVRPP 670 680 690 700 710 720 GHHADHSTAM GFCFFNSVAI ACRQLQQHGK ASKILIVDWD VHHGNGTQQT FYQDPSVLYI 730 740 750 760 770 780 SLHRHDDGNF FPGSGAVDEV GTGSGEGFNV NVAWAGGLDP PMGDPEYLAA FRIVVMPIAR 790 800 810 820 830 840 EFAPDLVLVS AGFDAAEGHP APLGGYHVSA KCFGYMTQQL MNLAGGAVVL ALEGGHDLTA 850 860 870 880 890 900 ICDASEACVA ALLGNKVDPL SEESWKQKPN LSAIRSLEAV VRVHRKYWGC MQRLASCPDS 910 920 930 940 WLPRVPGADA EVEAVTALAS LSVGILAEDR PSERLVEEEE PMNL
	Isoform 5 [UniParc]. Checksum: 1586B7308A24964A	FASTA	916	99,131
	10 20 30 40 50 60 MDLRVGQRPT VEPPPEPALL TLQHPQRLHR HLFLAGLHQQ QRSAEPMRLS MDPPMPELQG 70 80 90 100 110 120 GQQEQELRQL LNKDKSKRSA VASSVVKQKL AEVILKKQQA ALERTVHPSS PSIPYRTLEP 130 140 150 160 170 180 LDTEGAARSV LSSFLPPVPS LPTEPPEHFP LRKTVSEPNL KLRYKPKKSL ERRKNPLLRK 190 200 210 220 230 240 ESAPPSLRRR PAETLGDSSP SSSSTPASGC SSPNDSEHGP NPALGSEADG DRRTHSTLGP 250 260 270 280 290 300 RGPVLGNPHA PLFLHHGLEP EAGGTLPSRL QPILLLDPSV SHAPLWTVPG LGPLPFHFAQ 310 320 330 340 350 360 PLLTTERLSG SGLHRPLNRT RSEPLPPSAT ASPLLAPLQP RQDRLKPHVQ LIKPAISPPQ 370 380 390 400 410 420 RPAKPSEKPR LRQIPSAEDL ETDGGGVGPM ANDGLEHRES GRGPPEGRGS ISLQQHQQVP 430 440 450 460 470 480 PWEQQHLAGR LSQGSPGDSV LIPLAQVGHR PLSRTQSSPA APVSLLSPEP TCQTQVLNSS 490 500 510 520 530 540 ETPATGLVYD SVMLKHQCSC GDNSKHPEHA GRIQSIWSRL QERGLRSQCE CLRGRKASLE 550 560 570 580 590 600 ELQSVHSERH VLLYGTNPLS RLKLDNGKLT GLLAQRTFVM LPCGGVGVDT DTIWNELHSS 610 620 630 640 650 660 NAARWAAGSV TDLAFKVASR ELKNGFAVVR PPGHHADHST AMGFCFFNSV AIACRQLQQH 670 680 690 700 710 720 GKASKILIVD WDVHHGNGTQ QTFYQDPSVL YISLHRHDDG NFFPGSGAVD EVGTGSGEGF 730 740 750 760 770 780 NVNVAWAGGL DPPMGDPEYL AAFRIVVMPI AREFAPDLVL VSAGFDAAEG HPAPLGGYHV 790 800 810 820 830 840 SAKCFGYMTQ QLMNLAGGAV VLALEGGHDL TAICDASEAC VAALLGNKVD PLSEESWKQK 850 860 870 880 890 900 PNLSAIRSLE AVVRVHRKYW GCMQRLASCP DSWLPRVPGA DAEVEAVTAL ASLSVGILAE 910 DRPSERLVEE EEPMNL
	Isoform 6 [UniParc]. Checksum: 23AD714981D53FC7	FASTA	914	98,752
	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 SSPSIPYSLP TEPPEHFPLR KTVSEPNLKL RYKPKKSLER RKNPLLRKES 190 200 210 220 230 240 APPSLRRRPA ETLGDSSPSS SSTPASGCSS PNDSEHGPNP ALGSEADGDR RTHSTLGPRG 250 260 270 280 290 300 PVLGNPHAPL FLHHGLEPEA GGTLPSRLQP ILLLDPSVSH APLWTVPGLG PLPFHFAQPL 310 320 330 340 350 360 LTTERLSGSG LHRPLNRTRS EPLPPSATAS PLLAPLQPRQ DRLKPHVQLI KPAISPPQRP 370 380 390 400 410 420 AKPSEKPRLR QIPSAEDLET DGGGVGPMAN DGLEHRESGR GPPEGRGSIS LQQHQQVPPW 430 440 450 460 470 480 EQQHLAGRLS QGSPGDSVLI PLAQVGHRPL SRTQSSPAAP VSLLSPEPTC QTQVLNSSET 490 500 510 520 530 540 PATGLVYDSV MLKHQCSCGD NSKHPEHAGR IQSIWSRLQE RGLRSQCECL RGRKASLEEL 550 560 570 580 590 600 QSVHSERHVL LYGTNPLSRL KLDNGKLTGL LAQRTFVMLP CGGVGVDTDT IWNELHSSNA 610 620 630 640 650 660 ARWAAGSVTD LAFKVASREL KNGFAVVRPP GHHADHSTAM GFCFFNSVAI ACRQLQQHGK 670 680 690 700 710 720 ASKILIVDWD VHHGNGTQQT FYQDPSVLYI SLHRHDDGNF FPGSGAVDEV GTGSGEGFNV 730 740 750 760 770 780 NVAWAGGLDP PMGDPEYLAA FRIVVMPIAR EFAPDLVLVS AGFDAAEGHP APLGGYHVSA 790 800 810 820 830 840 KCFGYMTQQL MNLAGGAVVL ALEGGHDLTA ICDASEACVA ALLGNKVDPL SEESWKQKPN 850 860 870 880 890 900 LSAIRSLEAV VRVHRKYWGC MQRLASCPDS WLPRVPGADA EVEAVTALAS LSVGILAEDR 910 PSERLVEEEE PMNL

References

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[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]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, MASS SPECTROMETRY. 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]	"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.
IPI	IPI00227380. IPI00315371. IPI00315372. IPI00315373. IPI00315375. IPI00315376.
RefSeq	NP_001191204.1. NM_001204275.1. NP_001191205.1. NM_001204276.1. NP_001191206.1. NM_001204277.1. NP_001191207.1. NM_001204278.1. NP_062518.2. NM_019572.3.
UniGene	Mm.384027.
3D structure databases
ProteinModelPortal	Q8C2B3.
SMR	Q8C2B3. Positions 507-887.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-42594N.
IntAct	Q8C2B3. 1 interaction.
MINT	MINT-1551781.
PTM databases
PhosphoSite	Q8C2B3.
Proteomic databases
PaxDb	Q8C2B3.
PRIDE	Q8C2B3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000079838; ENSMUSP00000078766; ENSMUSG00000022475. ENSMUST00000088402; ENSMUSP00000085744; ENSMUSG00000022475. ENSMUST00000116408; ENSMUSP00000112109; ENSMUSG00000022475. ENSMUST00000116409; ENSMUSP00000112110; ENSMUSG00000022475. ENSMUST00000118294; ENSMUSP00000113380; ENSMUSG00000022475.
GeneID	56233.
KEGG	mmu:56233.
UCSC	uc007xld.1. mouse. uc007xle.1. mouse. uc007xlf.1. mouse. uc007xlg.1. mouse. uc007xlh.1. mouse. uc007xlj.1. mouse.
Organism-specific databases
CTD	51564.
MGI	MGI:1891835. Hdac7.
Phylogenomic databases
eggNOG	COG0123.
GeneTree	ENSGT00530000062809.
HOGENOM	HOG000232065.
HOVERGEN	HBG057100.
KO	K11408.
OMA	AFRIVVM.
OrthoDB	EOG4NKBV4.
Gene expression databases
ArrayExpress	Q8C2B3.
Bgee	Q8C2B3.
CleanEx	MM_HDAC7.
Genevestigator	Q8C2B3.
GermOnline	ENSMUSG00000022475. Mus musculus.
Family and domain databases
Gene3D	3.40.800.20. 1 hit.
InterPro	IPR000286. His_deacetylse. IPR023801. His_deacetylse_dom. IPR017320. Histone_deAcase_II_euk. [Graphical view]
PANTHER	PTHR10625. PTHR10625. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PIRSF	PIRSF037911. HDAC_II_euk. 1 hit.
PRINTS	PR01270. HDASUPER.
ProtoNet	Search...
Other
BindingDB	Q8C2B3.
ChEMBL	CHEMBL4219.
ChiTaRS	HDAC7. mouse.
NextBio	312136.
PMAP-CutDB	Q8C2B3.
SOURCE	Search...

Entry information

Entry name

HDAC7_MOUSE

Accession

Primary (citable) accession number: Q8C2B3
Secondary accession number(s): Q8C2C9 , Q8C8X4, Q8CB80, Q8CDA3, Q9JL72

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2003
Last sequence update:	May 16, 2003
Last modified:	May 1, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program