Q8WUI4 (HDAC7_HUMAN) 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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	952 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 By similarity. May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene. Ref.12
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	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 By similarity. Interacts with KAT5 and EDNRA. Interacts with KDM5B. Interacts with ZMYND15 By similarity. Interacts with PML (isoform PML-4). Ref.10 Ref.11 Ref.13 Ref.16 Ref.22
Subcellular location	Nucleus. Cytoplasm. Note: In the nucleus, it associates with distinct subnuclear dot-like structures. Shuttles between the nucleus and the cytoplasm. Treatment with EDN1 results in shuttling from the nucleus to the perinuclear region. The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation. Ref.10 Ref.14
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-155 by MARK2, MARK3 and PRKD1 promotes interaction with 14-3-3 proteins and export from the nucleus. Phosphorylation at Ser-155 is a prerequisite for phosphorylation at Ser-181. Ref.14 Ref.15 Ref.19
Miscellaneous	Its activity is inhibited by Trichostatin A (TSA), a known histone deacetylase inhibitor By similarity.
Sequence similarities	Belongs to the histone deacetylase family. HD type 2 subfamily.
Sequence caution	The sequence AAF63491.1 differs from that shown. Reason: Frameshift at position 877. The sequence BAA91474.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA91545.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB15759.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB55363.1 differs from that shown. Reason: Erroneous initiation. The sequence BAC56929.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling pathway Traceable author statement. Source: Reactome cell-cell junction assembly Inferred from electronic annotation. Source: Compara histone H3 deacetylation Inferred from electronic annotation. Source: GOC histone H4 deacetylation Inferred from electronic annotation. Source: GOC negative regulation of interleukin-2 production Inferred from direct assay PubMed 17360565. Source: BHF-UCL negative regulation of osteoblast differentiation Inferred from mutant phenotype PubMed 17997710. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of cell migration involved in sprouting angiogenesis Inferred from mutant phenotype PubMed 19351956. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW vasculogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay Ref.14PubMed 17997710. Source: UniProtKB histone deacetylase complex Inferred from electronic annotation. Source: InterPro nucleus Inferred from direct assay Ref.14PubMed 17997710. Source: UniProtKB
Molecular_function	14-3-3 protein binding Inferred from direct assay Ref.14. 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 electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW transcription corepressor activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 10 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8WUI4-1)

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: Q8WUI4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-472: Missing.
     473-520: LAQGGHRPLS...TPARTLPFTT → MQACVGVRGV...WVPALTLAPA

Note: No experimental confirmation available.

Isoform 3 (identifier: Q8WUI4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     227-263: Missing.

Isoform 4 (identifier: Q8WUI4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     227-256: Missing.

Note: No experimental confirmation available.

Isoform 5 (identifier: Q8WUI4-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHSPGADGTQVSPGAHYCSPTGAGCPRPCADTPGPQPQPM

Isoform 6 (identifier: Q8WUI4-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHSPGAGCPRPCADTPGPQPQPM

Isoform 7 (identifier: Q8WUI4-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHSPGADGTQVSPGAHYCSPTGAGCPRPCADTPGPQPQPM
     227-263: Missing.

Isoform 8 (identifier: Q8WUI4-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSDLRKRELGALFTSRGTGGVEWDGTQVSPGAHYCSPTGAGCPRPCADTPGPQPQPM
     892-952: SKYWGCMQRL...LVEEEEPMNL → MGALTLSQIP...QGLTKKKWRQ

Isoform 9 (identifier: Q8WUI4-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-527: Missing.

Isoform 10 (identifier: Q8WUI4-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1-338: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 952

952

Histone deacetylase 7

PRO_0000114705

Regions

Region

1 – 268

268

Transcription repression 1 By similarity

Region

1 – 98

98

Interaction with MEF2C By similarity

Region

49 – 149

101

Interaction with MEF2A By similarity

Region

218 – 546

329

Transcription repression 2 By similarity

Region

518 – 865

348

Histone deacetylase

Region

877 – 952

76

Interaction with SIN3A By similarity

Motif

918 – 952

35

Nuclear export signal By similarity

Compositional bias

197 – 203

7

Poly-Ser

Compositional bias

368 – 373

6

Poly-Pro

Sites

Active site

670

1

By similarity

Metal binding

533

1

Zinc

Metal binding

535

1

Zinc

Metal binding

541

1

Zinc

Metal binding

618

1

Zinc

Site

843

1

Contributes to catalysis

Amino acid modifications

Modified residue

109

1

Phosphoserine Ref.17

Modified residue

155

1

Phosphoserine; by MARK2, MARK3 and PKD/PRKD1 Probable

Modified residue

181

1

Phosphoserine; by PKD/PRKD2 Ref.14 Ref.15 Ref.20 Ref.21

Modified residue

283

1

Phosphoserine Ref.17 Ref.20

Modified residue

286

1

Phosphothreonine Ref.17 Ref.20

Modified residue

358

1

Phosphoserine; by PKD/PRKD1 By similarity

Modified residue

486

1

Phosphoserine Ref.17 Ref.18 Ref.21

Natural variations

Alternative sequence

1 – 527

527

Missing in isoform 9.

VSP_038102

Alternative sequence

1 – 472

472

Missing in isoform 2.

VSP_007429

Alternative sequence

1 – 338

338

Missing in isoform 10.

VSP_038103

Alternative sequence

1

1

M → MHSPGADGTQVSPGAHYCSP TGAGCPRPCADTPGPQPQPM in isoform 5 and isoform 7.

VSP_038104

Alternative sequence

1

1

M → MHSPGAGCPRPCADTPGPQP QPM in isoform 6.

VSP_038105

Alternative sequence

1

1

M → MSDLRKRELGALFTSRGTGG VEWDGTQVSPGAHYCSPTGA GCPRPCADTPGPQPQPM in isoform 8.

VSP_038106

Alternative sequence

227 – 263

37

Missing in isoform 3 and isoform 7.

VSP_008772

Alternative sequence

227 – 256

30

Missing in isoform 4.

VSP_007430

Alternative sequence

473 – 520

48

LAQGG…LPFTT → MQACVGVRGVYPPGSMWVPA VAVLACSLQPRPWGVRTPWV PALTLAPA in isoform 2.

VSP_007431

Alternative sequence

892 – 952

61

SKYWG…EPMNL → MGALTLSQIPGHGSSQQQAG GAFSRPGHPCRAAVVMVNTG AACSAWPPVQTPGCLECQGL TKKKWRQ in isoform 8.

VSP_038107

Natural variant

43

1

V → M in a breast cancer sample; somatic mutation. Ref.24

VAR_036043

Experimental info

Mutagenesis

150

1

L → A: Abolishes phosphorylation at S-155. Ref.14

Mutagenesis

155

1

S → A: Abolishes nuclear export; when associated with A-181; A-358 and A-486. Abolishes phosphorylation by MARK2 and MARK3, interaction with 14-3-3 and localization to the cytoplasm. Ref.14

Mutagenesis

181

1

S → A: Abolishes nuclear export; when associated with A-155; A-358 and A-486. Ref.14

Mutagenesis

358

1

S → A: Abolishes nuclear export; when associated with A-192; A-1118 and A-486. Ref.14

Mutagenesis

486

1

S → A: Abolishes nuclear export; when associated with A-192; A-1118 and A-358. Ref.14

Mutagenesis

843

1

H → A: Enhanced deacetylase activity. Ref.23

Mutagenesis

843

1

H → F: Enhanced deacetylase activity. Ref.23

Mutagenesis

843

1

H → Y: 6000 fold increase in deacetylase activity. Ref.23

Sequence conflict

50

1

M → T in BAG64517. Ref.5

Sequence conflict

225 – 264

40

Missing in AAF63491. Ref.1

Sequence conflict

276

1

P → L in BAA91545. Ref.5

Sequence conflict

561

1

R → L in BAA91545. Ref.5

Sequence conflict

614

1

V → E in AAF63491. Ref.1

Sequence conflict

644

1

S → R in BAB15759. Ref.5

Sequence conflict

665

1

R → W in BAA91474. Ref.5

Sequence conflict

700

1

K → KASK in AAF63491. Ref.1

Sequence conflict

750

1

G → S in BAA91545. Ref.5

Sequence conflict

777

1

A → T in BAB55363. Ref.5

Sequence conflict

825

1

Q → H in BAA91474. Ref.5

Secondary structure

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952

Helix Strand Turn

Details...

Beta strand

520 – 523

4

Helix

526 – 530

5

Helix

538 – 540

3

Helix

546 – 557

12

Helix

561 – 563

3

Beta strand

564 – 567

4

Helix

574 – 577

4

Turn

578 – 580

3

Helix

583 – 590

8

Helix

601 – 609

9

Beta strand

621 – 626

6

Turn

631 – 633

3

Helix

634 – 653

20

Beta strand

656 – 662

7

Beta strand

680 – 682

3

Helix

684 – 695

12

Beta strand

701 – 705

5

Beta strand

707 – 709

3

Helix

712 – 718

7

Beta strand

724 – 731

8

Turn

733 – 736

4

Helix

750 – 752

3

Beta strand

756 – 761

6

Beta strand

765 – 767

3

Helix

771 – 780

10

Helix

782 – 789

8

Beta strand

792 – 798

7

Helix

808 – 810

3

Helix

817 – 827

11

Helix

831 – 833

3

Beta strand

835 – 839

5

Helix

845 – 860

16

Helix

866 – 868

3

Helix

871 – 873

3

Helix

878 – 891

14

Turn

892 – 894

3

Helix

896 – 898

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 16, 2003. Version 2. Checksum: 786785B084667731	FASTA	952	102,927
	10 20 30 40 50 60 MDLRVGQRPP VEPPPEPTLL ALQRPQRLHH HLFLAGLQQQ RSVEPMRLSM DTPMPELQVG 70 80 90 100 110 120 PQEQELRQLL HKDKSKRSAV ASSVVKQKLA EVILKKQQAA LERTVHPNSP GIPYRTLEPL 130 140 150 160 170 180 ETEGATRSML SSFLPPVPSL PSDPPEHFPL RKTVSEPNLK LRYKPKKSLE RRKNPLLRKE 190 200 210 220 230 240 SAPPSLRRRP AETLGDSSPS SSSTPASGCS SPNDSEHGPN PILGSEALLG QRLRLQETSV 250 260 270 280 290 300 APFALPTVSL LPAITLGLPA PARADSDRRT HPTLGPRGPI LGSPHTPLFL PHGLEPEAGG 310 320 330 340 350 360 TLPSRLQPIL LLDPSGSHAP LLTVPGLGPL PFHFAQSLMT TERLSGSGLH WPLSRTRSEP 370 380 390 400 410 420 LPPSATAPPP PGPMQPRLEQ LKTHVQVIKR SAKPSEKPRL RQIPSAEDLE TDGGGPGQVV 430 440 450 460 470 480 DDGLEHRELG HGQPEARGPA PLQQHPQVLL WEQQRLAGRL PRGSTGDTVL LPLAQGGHRP 490 500 510 520 530 540 LSRAQSSPAA PASLSAPEPA SQARVLSSSE TPARTLPFTT GLIYDSVMLK HQCSCGDNSR 550 560 570 580 590 600 HPEHAGRIQS IWSRLQERGL RSQCECLRGR KASLEELQSV HSERHVLLYG TNPLSRLKLD 610 620 630 640 650 660 NGKLAGLLAQ RMFVMLPCGG VGVDTDTIWN ELHSSNAARW AAGSVTDLAF KVASRELKNG 670 680 690 700 710 720 FAVVRPPGHH ADHSTAMGFC FFNSVAIACR QLQQQSKASK ILIVDWDVHH GNGTQQTFYQ 730 740 750 760 770 780 DPSVLYISLH RHDDGNFFPG SGAVDEVGAG SGEGFNVNVA WAGGLDPPMG DPEYLAAFRI 790 800 810 820 830 840 VVMPIAREFS PDLVLVSAGF DAAEGHPAPL GGYHVSAKCF GYMTQQLMNL AGGAVVLALE 850 860 870 880 890 900 GGHDLTAICD ASEACVAALL GNRVDPLSEE GWKQKPNLNA IRSLEAVIRV HSKYWGCMQR 910 920 930 940 950 LASCPDSWVP RVPGADKEEV EAVTALASLS VGILAEDRPS EQLVEEEEPM NL
	Isoform 2 [UniParc]. Checksum: 0276ABAAAB3DC052	FASTA	480	51,829
	10 20 30 40 50 60 MQACVGVRGV YPPGSMWVPA VAVLACSLQP RPWGVRTPWV PALTLAPAGL IYDSVMLKHQ 70 80 90 100 110 120 CSCGDNSRHP EHAGRIQSIW SRLQERGLRS QCECLRGRKA SLEELQSVHS ERHVLLYGTN 130 140 150 160 170 180 PLSRLKLDNG KLAGLLAQRM FVMLPCGGVG VDTDTIWNEL HSSNAARWAA GSVTDLAFKV 190 200 210 220 230 240 ASRELKNGFA VVRPPGHHAD HSTAMGFCFF NSVAIACRQL QQQSKASKIL IVDWDVHHGN 250 260 270 280 290 300 GTQQTFYQDP SVLYISLHRH DDGNFFPGSG AVDEVGAGSG EGFNVNVAWA GGLDPPMGDP 310 320 330 340 350 360 EYLAAFRIVV MPIAREFSPD LVLVSAGFDA AEGHPAPLGG YHVSAKCFGY MTQQLMNLAG 370 380 390 400 410 420 GAVVLALEGG HDLTAICDAS EACVAALLGN RVDPLSEEGW KQKPNLNAIR SLEAVIRVHS 430 440 450 460 470 480 KYWGCMQRLA SCPDSWVPRV PGADKEEVEA VTALASLSVG ILAEDRPSEQ LVEEEEPMNL
	Isoform 3 [UniParc]. Checksum: E828F548BB42ABDC	FASTA	915	99,093
	10 20 30 40 50 60 MDLRVGQRPP VEPPPEPTLL ALQRPQRLHH HLFLAGLQQQ RSVEPMRLSM DTPMPELQVG 70 80 90 100 110 120 PQEQELRQLL HKDKSKRSAV ASSVVKQKLA EVILKKQQAA LERTVHPNSP GIPYRTLEPL 130 140 150 160 170 180 ETEGATRSML SSFLPPVPSL PSDPPEHFPL RKTVSEPNLK LRYKPKKSLE RRKNPLLRKE 190 200 210 220 230 240 SAPPSLRRRP AETLGDSSPS SSSTPASGCS SPNDSEHGPN PILGSEADSD RRTHPTLGPR 250 260 270 280 290 300 GPILGSPHTP LFLPHGLEPE AGGTLPSRLQ PILLLDPSGS HAPLLTVPGL GPLPFHFAQS 310 320 330 340 350 360 LMTTERLSGS GLHWPLSRTR SEPLPPSATA PPPPGPMQPR LEQLKTHVQV IKRSAKPSEK 370 380 390 400 410 420 PRLRQIPSAE DLETDGGGPG QVVDDGLEHR ELGHGQPEAR GPAPLQQHPQ VLLWEQQRLA 430 440 450 460 470 480 GRLPRGSTGD TVLLPLAQGG HRPLSRAQSS PAAPASLSAP EPASQARVLS SSETPARTLP 490 500 510 520 530 540 FTTGLIYDSV MLKHQCSCGD NSRHPEHAGR IQSIWSRLQE RGLRSQCECL RGRKASLEEL 550 560 570 580 590 600 QSVHSERHVL LYGTNPLSRL KLDNGKLAGL LAQRMFVMLP CGGVGVDTDT IWNELHSSNA 610 620 630 640 650 660 ARWAAGSVTD LAFKVASREL KNGFAVVRPP GHHADHSTAM GFCFFNSVAI ACRQLQQQSK 670 680 690 700 710 720 ASKILIVDWD VHHGNGTQQT FYQDPSVLYI SLHRHDDGNF FPGSGAVDEV GAGSGEGFNV 730 740 750 760 770 780 NVAWAGGLDP PMGDPEYLAA FRIVVMPIAR EFSPDLVLVS AGFDAAEGHP APLGGYHVSA 790 800 810 820 830 840 KCFGYMTQQL MNLAGGAVVL ALEGGHDLTA ICDASEACVA ALLGNRVDPL SEEGWKQKPN 850 860 870 880 890 900 LNAIRSLEAV IRVHSKYWGC MQRLASCPDS WVPRVPGADK EEVEAVTALA SLSVGILAED 910 RPSEQLVEEE EPMNL
	Isoform 4 [UniParc]. Checksum: 398316C4225621DA	FASTA	922	99,755
	10 20 30 40 50 60 MDLRVGQRPP VEPPPEPTLL ALQRPQRLHH HLFLAGLQQQ RSVEPMRLSM DTPMPELQVG 70 80 90 100 110 120 PQEQELRQLL HKDKSKRSAV ASSVVKQKLA EVILKKQQAA LERTVHPNSP GIPYRTLEPL 130 140 150 160 170 180 ETEGATRSML SSFLPPVPSL PSDPPEHFPL RKTVSEPNLK LRYKPKKSLE RRKNPLLRKE 190 200 210 220 230 240 SAPPSLRRRP AETLGDSSPS SSSTPASGCS SPNDSEHGPN PILGSEGLPA PARADSDRRT 250 260 270 280 290 300 HPTLGPRGPI LGSPHTPLFL PHGLEPEAGG TLPSRLQPIL LLDPSGSHAP LLTVPGLGPL 310 320 330 340 350 360 PFHFAQSLMT TERLSGSGLH WPLSRTRSEP LPPSATAPPP PGPMQPRLEQ LKTHVQVIKR 370 380 390 400 410 420 SAKPSEKPRL RQIPSAEDLE TDGGGPGQVV DDGLEHRELG HGQPEARGPA PLQQHPQVLL 430 440 450 460 470 480 WEQQRLAGRL PRGSTGDTVL LPLAQGGHRP LSRAQSSPAA PASLSAPEPA SQARVLSSSE 490 500 510 520 530 540 TPARTLPFTT GLIYDSVMLK HQCSCGDNSR HPEHAGRIQS IWSRLQERGL RSQCECLRGR 550 560 570 580 590 600 KASLEELQSV HSERHVLLYG TNPLSRLKLD NGKLAGLLAQ RMFVMLPCGG VGVDTDTIWN 610 620 630 640 650 660 ELHSSNAARW AAGSVTDLAF KVASRELKNG FAVVRPPGHH ADHSTAMGFC FFNSVAIACR 670 680 690 700 710 720 QLQQQSKASK ILIVDWDVHH GNGTQQTFYQ DPSVLYISLH RHDDGNFFPG SGAVDEVGAG 730 740 750 760 770 780 SGEGFNVNVA WAGGLDPPMG DPEYLAAFRI VVMPIAREFS PDLVLVSAGF DAAEGHPAPL 790 800 810 820 830 840 GGYHVSAKCF GYMTQQLMNL AGGAVVLALE GGHDLTAICD ASEACVAALL GNRVDPLSEE 850 860 870 880 890 900 GWKQKPNLNA IRSLEAVIRV HSKYWGCMQR LASCPDSWVP RVPGADKEEV EAVTALASLS 910 920 VGILAEDRPS EQLVEEEEPM NL
	Isoform 5 [UniParc]. Checksum: 3493E377594FFC18	FASTA	991	106,740
	10 20 30 40 50 60 MHSPGADGTQ VSPGAHYCSP TGAGCPRPCA DTPGPQPQPM DLRVGQRPPV EPPPEPTLLA 70 80 90 100 110 120 LQRPQRLHHH LFLAGLQQQR SVEPMRLSMD TPMPELQVGP QEQELRQLLH KDKSKRSAVA 130 140 150 160 170 180 SSVVKQKLAE VILKKQQAAL ERTVHPNSPG IPYRTLEPLE TEGATRSMLS SFLPPVPSLP 190 200 210 220 230 240 SDPPEHFPLR KTVSEPNLKL RYKPKKSLER RKNPLLRKES APPSLRRRPA ETLGDSSPSS 250 260 270 280 290 300 SSTPASGCSS PNDSEHGPNP ILGSEALLGQ RLRLQETSVA PFALPTVSLL PAITLGLPAP 310 320 330 340 350 360 ARADSDRRTH PTLGPRGPIL GSPHTPLFLP HGLEPEAGGT LPSRLQPILL LDPSGSHAPL 370 380 390 400 410 420 LTVPGLGPLP FHFAQSLMTT ERLSGSGLHW PLSRTRSEPL PPSATAPPPP GPMQPRLEQL 430 440 450 460 470 480 KTHVQVIKRS AKPSEKPRLR QIPSAEDLET DGGGPGQVVD DGLEHRELGH GQPEARGPAP 490 500 510 520 530 540 LQQHPQVLLW EQQRLAGRLP RGSTGDTVLL PLAQGGHRPL SRAQSSPAAP ASLSAPEPAS 550 560 570 580 590 600 QARVLSSSET PARTLPFTTG LIYDSVMLKH QCSCGDNSRH PEHAGRIQSI WSRLQERGLR 610 620 630 640 650 660 SQCECLRGRK ASLEELQSVH SERHVLLYGT NPLSRLKLDN GKLAGLLAQR MFVMLPCGGV 670 680 690 700 710 720 GVDTDTIWNE LHSSNAARWA AGSVTDLAFK VASRELKNGF AVVRPPGHHA DHSTAMGFCF 730 740 750 760 770 780 FNSVAIACRQ LQQQSKASKI LIVDWDVHHG NGTQQTFYQD PSVLYISLHR HDDGNFFPGS 790 800 810 820 830 840 GAVDEVGAGS GEGFNVNVAW AGGLDPPMGD PEYLAAFRIV VMPIAREFSP DLVLVSAGFD 850 860 870 880 890 900 AAEGHPAPLG GYHVSAKCFG YMTQQLMNLA GGAVVLALEG GHDLTAICDA SEACVAALLG 910 920 930 940 950 960 NRVDPLSEEG WKQKPNLNAI RSLEAVIRVH SKYWGCMQRL ASCPDSWVPR VPGADKEEVE 970 980 990 AVTALASLSV GILAEDRPSE QLVEEEEPMN L
	Isoform 6 [UniParc]. Checksum: 86EA1E69F1CEF667	FASTA	974	105,111
	10 20 30 40 50 60 MHSPGAGCPR PCADTPGPQP QPMDLRVGQR PPVEPPPEPT LLALQRPQRL HHHLFLAGLQ 70 80 90 100 110 120 QQRSVEPMRL SMDTPMPELQ VGPQEQELRQ LLHKDKSKRS AVASSVVKQK LAEVILKKQQ 130 140 150 160 170 180 AALERTVHPN SPGIPYRTLE PLETEGATRS MLSSFLPPVP SLPSDPPEHF PLRKTVSEPN 190 200 210 220 230 240 LKLRYKPKKS LERRKNPLLR KESAPPSLRR RPAETLGDSS PSSSSTPASG CSSPNDSEHG 250 260 270 280 290 300 PNPILGSEAL LGQRLRLQET SVAPFALPTV SLLPAITLGL PAPARADSDR RTHPTLGPRG 310 320 330 340 350 360 PILGSPHTPL FLPHGLEPEA GGTLPSRLQP ILLLDPSGSH APLLTVPGLG PLPFHFAQSL 370 380 390 400 410 420 MTTERLSGSG LHWPLSRTRS EPLPPSATAP PPPGPMQPRL EQLKTHVQVI KRSAKPSEKP 430 440 450 460 470 480 RLRQIPSAED LETDGGGPGQ VVDDGLEHRE LGHGQPEARG PAPLQQHPQV LLWEQQRLAG 490 500 510 520 530 540 RLPRGSTGDT VLLPLAQGGH RPLSRAQSSP AAPASLSAPE PASQARVLSS SETPARTLPF 550 560 570 580 590 600 TTGLIYDSVM LKHQCSCGDN SRHPEHAGRI QSIWSRLQER GLRSQCECLR GRKASLEELQ 610 620 630 640 650 660 SVHSERHVLL YGTNPLSRLK LDNGKLAGLL AQRMFVMLPC GGVGVDTDTI WNELHSSNAA 670 680 690 700 710 720 RWAAGSVTDL AFKVASRELK NGFAVVRPPG HHADHSTAMG FCFFNSVAIA CRQLQQQSKA 730 740 750 760 770 780 SKILIVDWDV HHGNGTQQTF YQDPSVLYIS LHRHDDGNFF PGSGAVDEVG AGSGEGFNVN 790 800 810 820 830 840 VAWAGGLDPP MGDPEYLAAF RIVVMPIARE FSPDLVLVSA GFDAAEGHPA PLGGYHVSAK 850 860 870 880 890 900 CFGYMTQQLM NLAGGAVVLA LEGGHDLTAI CDASEACVAA LLGNRVDPLS EEGWKQKPNL 910 920 930 940 950 960 NAIRSLEAVI RVHSKYWGCM QRLASCPDSW VPRVPGADKE EVEAVTALAS LSVGILAEDR 970 PSEQLVEEEE PMNL
	Isoform 7 [UniParc]. Checksum: A5DDAB73E16AD10D	FASTA	954	102,906
	10 20 30 40 50 60 MHSPGADGTQ VSPGAHYCSP TGAGCPRPCA DTPGPQPQPM DLRVGQRPPV EPPPEPTLLA 70 80 90 100 110 120 LQRPQRLHHH LFLAGLQQQR SVEPMRLSMD TPMPELQVGP QEQELRQLLH KDKSKRSAVA 130 140 150 160 170 180 SSVVKQKLAE VILKKQQAAL ERTVHPNSPG IPYRTLEPLE TEGATRSMLS SFLPPVPSLP 190 200 210 220 230 240 SDPPEHFPLR KTVSEPNLKL RYKPKKSLER RKNPLLRKES APPSLRRRPA ETLGDSSPSS 250 260 270 280 290 300 SSTPASGCSS PNDSEHGPNP ILGSEADSDR RTHPTLGPRG PILGSPHTPL FLPHGLEPEA 310 320 330 340 350 360 GGTLPSRLQP ILLLDPSGSH APLLTVPGLG PLPFHFAQSL MTTERLSGSG LHWPLSRTRS 370 380 390 400 410 420 EPLPPSATAP PPPGPMQPRL EQLKTHVQVI KRSAKPSEKP RLRQIPSAED LETDGGGPGQ 430 440 450 460 470 480 VVDDGLEHRE LGHGQPEARG PAPLQQHPQV LLWEQQRLAG RLPRGSTGDT VLLPLAQGGH 490 500 510 520 530 540 RPLSRAQSSP AAPASLSAPE PASQARVLSS SETPARTLPF TTGLIYDSVM LKHQCSCGDN 550 560 570 580 590 600 SRHPEHAGRI QSIWSRLQER GLRSQCECLR GRKASLEELQ SVHSERHVLL YGTNPLSRLK 610 620 630 640 650 660 LDNGKLAGLL AQRMFVMLPC GGVGVDTDTI WNELHSSNAA RWAAGSVTDL AFKVASRELK 670 680 690 700 710 720 NGFAVVRPPG HHADHSTAMG FCFFNSVAIA CRQLQQQSKA SKILIVDWDV HHGNGTQQTF 730 740 750 760 770 780 YQDPSVLYIS LHRHDDGNFF PGSGAVDEVG AGSGEGFNVN VAWAGGLDPP MGDPEYLAAF 790 800 810 820 830 840 RIVVMPIARE FSPDLVLVSA GFDAAEGHPA PLGGYHVSAK CFGYMTQQLM NLAGGAVVLA 850 860 870 880 890 900 LEGGHDLTAI CDASEACVAA LLGNRVDPLS EEGWKQKPNL NAIRSLEAVI RVHSKYWGCM 910 920 930 940 950 QRLASCPDSW VPRVPGADKE EVEAVTALAS LSVGILAEDR PSEQLVEEEE PMNL
	Isoform 8 [UniParc]. Checksum: 77630923616F2890	FASTA	1,014	108,937
	10 20 30 40 50 60 MSDLRKRELG ALFTSRGTGG VEWDGTQVSP GAHYCSPTGA GCPRPCADTP GPQPQPMDLR 70 80 90 100 110 120 VGQRPPVEPP PEPTLLALQR PQRLHHHLFL AGLQQQRSVE PMRLSMDTPM PELQVGPQEQ 130 140 150 160 170 180 ELRQLLHKDK SKRSAVASSV VKQKLAEVIL KKQQAALERT VHPNSPGIPY RTLEPLETEG 190 200 210 220 230 240 ATRSMLSSFL PPVPSLPSDP PEHFPLRKTV SEPNLKLRYK PKKSLERRKN PLLRKESAPP 250 260 270 280 290 300 SLRRRPAETL GDSSPSSSST PASGCSSPND SEHGPNPILG SEALLGQRLR LQETSVAPFA 310 320 330 340 350 360 LPTVSLLPAI TLGLPAPARA DSDRRTHPTL GPRGPILGSP HTPLFLPHGL EPEAGGTLPS 370 380 390 400 410 420 RLQPILLLDP SGSHAPLLTV PGLGPLPFHF AQSLMTTERL SGSGLHWPLS RTRSEPLPPS 430 440 450 460 470 480 ATAPPPPGPM QPRLEQLKTH VQVIKRSAKP SEKPRLRQIP SAEDLETDGG GPGQVVDDGL 490 500 510 520 530 540 EHRELGHGQP EARGPAPLQQ HPQVLLWEQQ RLAGRLPRGS TGDTVLLPLA QGGHRPLSRA 550 560 570 580 590 600 QSSPAAPASL SAPEPASQAR VLSSSETPAR TLPFTTGLIY DSVMLKHQCS CGDNSRHPEH 610 620 630 640 650 660 AGRIQSIWSR LQERGLRSQC ECLRGRKASL EELQSVHSER HVLLYGTNPL SRLKLDNGKL 670 680 690 700 710 720 AGLLAQRMFV MLPCGGVGVD TDTIWNELHS SNAARWAAGS VTDLAFKVAS RELKNGFAVV 730 740 750 760 770 780 RPPGHHADHS TAMGFCFFNS VAIACRQLQQ QSKASKILIV DWDVHHGNGT QQTFYQDPSV 790 800 810 820 830 840 LYISLHRHDD GNFFPGSGAV DEVGAGSGEG FNVNVAWAGG LDPPMGDPEY LAAFRIVVMP 850 860 870 880 890 900 IAREFSPDLV LVSAGFDAAE GHPAPLGGYH VSAKCFGYMT QQLMNLAGGA VVLALEGGHD 910 920 930 940 950 960 LTAICDASEA CVAALLGNRV DPLSEEGWKQ KPNLNAIRSL EAVIRVHMGA LTLSQIPGHG 970 980 990 1000 1010 SSQQQAGGAF SRPGHPCRAA VVMVNTGAAC SAWPPVQTPG CLECQGLTKK KWRQ
	Isoform 9 [UniParc]. Checksum: F9EACA7D416CD74E	FASTA	425	46,041
	10 20 30 40 50 60 MLKHQCSCGD NSRHPEHAGR IQSIWSRLQE RGLRSQCECL RGRKASLEEL QSVHSERHVL 70 80 90 100 110 120 LYGTNPLSRL KLDNGKLAGL LAQRMFVMLP CGGVGVDTDT IWNELHSSNA ARWAAGSVTD 130 140 150 160 170 180 LAFKVASREL KNGFAVVRPP GHHADHSTAM GFCFFNSVAI ACRQLQQQSK ASKILIVDWD 190 200 210 220 230 240 VHHGNGTQQT FYQDPSVLYI SLHRHDDGNF FPGSGAVDEV GAGSGEGFNV NVAWAGGLDP 250 260 270 280 290 300 PMGDPEYLAA FRIVVMPIAR EFSPDLVLVS AGFDAAEGHP APLGGYHVSA KCFGYMTQQL 310 320 330 340 350 360 MNLAGGAVVL ALEGGHDLTA ICDASEACVA ALLGNRVDPL SEEGWKQKPN LNAIRSLEAV 370 380 390 400 410 420 IRVHSKYWGC MQRLASCPDS WVPRVPGADK EEVEAVTALA SLSVGILAED RPSEQLVEEE EPMNL
	Isoform 10 [UniParc]. Checksum: 2B638DD8C866B502	FASTA	614	66,187
	10 20 30 40 50 60 MTTERLSGSG LHWPLSRTRS EPLPPSATAP PPPGPMQPRL EQLKTHVQVI KRSAKPSEKP 70 80 90 100 110 120 RLRQIPSAED LETDGGGPGQ VVDDGLEHRE LGHGQPEARG PAPLQQHPQV LLWEQQRLAG 130 140 150 160 170 180 RLPRGSTGDT VLLPLAQGGH RPLSRAQSSP AAPASLSAPE PASQARVLSS SETPARTLPF 190 200 210 220 230 240 TTGLIYDSVM LKHQCSCGDN SRHPEHAGRI QSIWSRLQER GLRSQCECLR GRKASLEELQ 250 260 270 280 290 300 SVHSERHVLL YGTNPLSRLK LDNGKLAGLL AQRMFVMLPC GGVGVDTDTI WNELHSSNAA 310 320 330 340 350 360 RWAAGSVTDL AFKVASRELK NGFAVVRPPG HHADHSTAMG FCFFNSVAIA CRQLQQQSKA 370 380 390 400 410 420 SKILIVDWDV HHGNGTQQTF YQDPSVLYIS LHRHDDGNFF PGSGAVDEVG AGSGEGFNVN 430 440 450 460 470 480 VAWAGGLDPP MGDPEYLAAF RIVVMPIARE FSPDLVLVSA GFDAAEGHPA PLGGYHVSAK 490 500 510 520 530 540 CFGYMTQQLM NLAGGAVVLA LEGGHDLTAI CDASEACVAA LLGNRVDPLS EEGWKQKPNL 550 560 570 580 590 600 NAIRSLEAVI RVHSKYWGCM QRLASCPDSW VPRVPGADKE EVEAVTALAS LSVGILAEDR 610 PSEQLVEEEE PMNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel class II HDAC is associated with the transcriptional homeodomain repressor CCAAT displacement protein." Li S., Fischle W., Verdin E., Walsh M.J. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Cervix carcinoma.
[2]	"Genomic organization of the human histone deacetylase 7 gene." Petrie K., Zelent A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 5).
[3]	"Homo sapiens histone deacetylase 7A (HDAC7A), transcript variant 3." Zhi Y., Su E.W. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 5; 6; 8 AND 9), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-952 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 651-952. Tissue: Embryo, Mammary gland, Placenta, Spleen, Teratocarcinoma and Thymus.
[6]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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 7), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 242-952 (ISOFORM 1). Tissue: B-cell, Colon and PNS.
[9]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-952 (ISOFORM 1). Tissue: Uterus.
[10]	"Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling." Lee H.-J., Chun M., Kandror K.V. J. Biol. Chem. 276:16597-16600(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EDNRA.
[11]	"Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo." Fischle W., Dequiedt F., Fillion M., Hendzel M.J., Voelter W., Verdin E. J. Biol. Chem. 276:35826-35835(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HDAC3.
[12]	"Signal transduction and transcription factor modification during reactivation of Epstein-Barr virus from latency." Bryant H., Farrell P.J. J. Virol. 76:10290-10298(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Tip60 is a co-repressor for STAT3." Xiao H., Chung J., Kao H.-Y., Yang Y.-C. J. Biol. Chem. 278:11197-11204(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KAT5.
[14]	"New role for hPar-1 kinases EMK and C-TAK1 in regulating localization and activity of class IIa histone deacetylases." Dequiedt F., Martin M., Von Blume J., Vertommen D., Lecomte E., Mari N., Heinen M.F., Bachmann M., Twizere J.C., Huang M.C., Rider M.H., Piwnica-Worms H., Seufferlein T., Kettmann R. Mol. Cell. Biol. 26:7086-7102(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-155 AND SER-181, MUTAGENESIS OF LEU-150; SER-155; SER-181; SER-358 AND SER-486.
[15]	"Phosphorylation at Ser244 by CK1 determines nuclear localization and substrate targeting of PKD2." von Blume J., Knippschild U., Dequiedt F., Giamas G., Beck A., Auer A., Van Lint J., Adler G., Seufferlein T. EMBO J. 26:4619-4633(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-181.
[16]	"Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases." Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K., Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P., Taylor-Papadimitriou J. Int. J. Cancer 121:265-275(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KDM5B.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-283; THR-286 AND SER-486, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases." Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B., McKinsey T.A. FEBS Lett. 584:1103-1110(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[20]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-283 AND THR-286, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-486, MASS SPECTROMETRY.
[22]	"Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor function in colorectal cancer cells." Satow R., Shitashige M., Jigami T., Fukami K., Honda K., Kitabayashi I., Yamada T. Gastroenterology 142:572-581(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PML.
[23]	"Human HDAC7 harbors a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity." Schuetz A., Min J., Allali-Hassani A., Schapira M., Shuen M., Loppnau P., Mazitschek R., Kwiatkowski N.P., Lewis T.A., Maglathin R.L., McLean T.H., Bochkarev A., Plotnikov A.N., Vedadi M., Arrowsmith C.H. J. Biol. Chem. 283:11355-11363(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 482-903, ZINC-BINDING SITES, MUTAGENESIS OF HIS-843.
[24]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-43.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF239243 mRNA. Translation: AAF63491.1. Frameshift.
AY302468 mRNA. Translation: AAQ18232.1.
AY321367 mRNA. Translation: AAP84704.1.
BT009771 mRNA. Translation: AAP88773.1.
AK001032 mRNA. Translation: BAA91474.1. Different initiation.
AK001190 mRNA. Translation: BAA91545.1. Different initiation.
AK024469 mRNA. Translation: BAB15759.1. Different initiation.
AK027781 mRNA. Translation: BAB55363.1. Different initiation.
AK122588 mRNA. Translation: BAC56929.1. Sequence problems.
AK128383 mRNA. Translation: BAG54670.1.
AK299292 mRNA. Translation: BAG61307.1.
AK301545 mRNA. Translation: BAG63042.1.
AK303481 mRNA. Translation: BAG64517.1.
AC004466 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW57957.1.
BC006453 mRNA. Translation: AAH06453.2.
BC020505 mRNA. Translation: AAH20505.2.
BC064840 mRNA. Translation: AAH64840.1.
AL117455 mRNA. Translation: CAB55935.1.

IPI

IPI00306189.
IPI00386808.
IPI00743474.
IPI00909569.
IPI00916348.
IPI00916470.
IPI00916810.
IPI00917034.
IPI00944518.
IPI00944634.

PIR

T17245.

RefSeq

NP_001091886.1. NM_001098416.2.
NP_056216.2. NM_015401.3.

UniGene

Hs.200063.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3C0Y	X-ray	2.10	A/B/C	482-903	[»]
3C0Z	X-ray	2.10	A/B/C	482-903	[»]
3C10	X-ray	2.00	A/B/C	482-903	[»]

ProteinModelPortal

Q8WUI4.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29860N.

IntAct

Q8WUI4. 1 interaction.

MINT

MINT-3089050.

PTM databases

PhosphoSite

Q8WUI4.

Polymorphism databases

DMDM

30913097.

Proteomic databases

PaxDb

Q8WUI4.

PRIDE

Q8WUI4.

Protocols and materials databases

DNASU

51564.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000080059; ENSP00000080059; ENSG00000061273.
ENST00000354334; ENSP00000351326; ENSG00000061273.
ENST00000427332; ENSP00000404394; ENSG00000061273.
ENST00000552960; ENSP00000448532; ENSG00000061273.

GeneID

51564.

KEGG

hsa:51564.

UCSC

uc001rqe.3. human.
uc001rqj.4. human.
uc001rqk.4. human.
uc010slo.2. human.

Organism-specific databases

CTD

51564.

GeneCards

GC12M048176.

H-InvDB

HIX0129669.

HGNC

HGNC:14067. HDAC7.

HPA

HPA004775.

MIM

606542. gene.

neXtProt

NX_Q8WUI4.

PharmGKB

PA162390579.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0123.

HOVERGEN

HBG057100.

InParanoid

Q8WUI4.

KO

K11408.

OrthoDB

EOG4NKBV4.

PhylomeDB

Q8WUI4.

Enzyme and pathway databases

BRENDA

3.5.1.98. 2681.

Pathway_Interaction_DB

hif1_tfpathway. HIF-1-alpha transcription factor network.
ar_tf_pathway. Regulation of Androgen receptor activity.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q8WUI4.

Bgee

Q8WUI4.

CleanEx

HS_HDAC7.

Genevestigator

Q8WUI4.

GermOnline

ENSG00000061273. Homo sapiens.

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

Q8WUI4.

ChEMBL

CHEMBL2716.

ChiTaRS

HDAC7. human.

EvolutionaryTrace

Q8WUI4.

GenomeRNAi

51564.

NextBio

55370.

PMAP-CutDB

Q8WUI4.

SOURCE

Search...

Entry information

Entry name

HDAC7_HUMAN

Accession

Primary (citable) accession number: Q8WUI4
Secondary accession number(s): B3KY08 , B4DWI0, B4E0Q5, Q6P1W9, Q6W9G7, Q7Z4K2, Q7Z5I1, Q96K01, Q9BR73, Q9H7L0, Q9NW41, Q9NWA9, Q9NYK9, Q9UFU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2003
Last sequence update:	May 16, 2003
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.