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Protein

Histone deacetylase 7

Gene

HDAC7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity). May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene. Positively regulates the transcriptional repressor activity of FOXP3 (PubMed:17360565).By similarity2 Publications

Miscellaneous

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

Catalytic activityi

Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi533Zinc1
Metal bindingi535Zinc1
Metal bindingi541Zinc1
Metal bindingi618Zinc1
Active sitei670By similarity1
Sitei843Contributes to catalysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChromatin regulator, Hydrolase, Repressor
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.1.98 2681
ReactomeiR-HSA-2122947 NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants
R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-8943724 Regulation of PTEN gene transcription
SIGNORiQ8WUI4

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 7 (EC:3.5.1.98)
Short name:
HD7
Alternative name(s):
Histone deacetylase 7A
Short name:
HD7a
Gene namesi
Name:HDAC7
Synonyms:HDAC7A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000061273.17
HGNCiHGNC:14067 HDAC7
MIMi606542 gene
neXtProtiNX_Q8WUI4

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi150L → A: Abolishes phosphorylation at S-155. 1 Publication1
Mutagenesisi155S → 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. 1 Publication1
Mutagenesisi181S → A: Abolishes nuclear export; when associated with A-155; A-358 and A-486. 1 Publication1
Mutagenesisi358S → A: Abolishes nuclear export; when associated with A-192; A-1118 and A-486. 1 Publication1
Mutagenesisi486S → A: Abolishes nuclear export; when associated with A-192; A-1118 and A-358. 1 Publication1
Mutagenesisi843H → A: Enhanced deacetylase activity. 1 Publication1
Mutagenesisi843H → F: Enhanced deacetylase activity. 1 Publication1
Mutagenesisi843H → Y: 6000 fold increase in deacetylase activity. 1 Publication1

Organism-specific databases

DisGeNETi51564
OpenTargetsiENSG00000061273
PharmGKBiPA162390579

Chemistry databases

ChEMBLiCHEMBL2716
DrugBankiDB05015 Belinostat
DB06603 Panobinostat
GuidetoPHARMACOLOGYi2661

Polymorphism and mutation databases

BioMutaiHDAC7
DMDMi30913097

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001147051 – 952Histone deacetylase 7Add BLAST952

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei109PhosphoserineCombined sources1
Modified residuei155Phosphoserine; by MARK2, MARK3 and PKD/PRKD11 Publication1
Modified residuei181Phosphoserine; by PKD/PRKD2Combined sources2 Publications1
Modified residuei283PhosphoserineCombined sources1
Modified residuei286PhosphothreonineCombined sources1
Modified residuei358Phosphoserine; by PKD/PRKD1By similarity1
Modified residuei364PhosphoserineCombined sources1
Modified residuei405PhosphoserineCombined sources1
Modified residuei486PhosphoserineCombined sources1
Modified residuei487PhosphoserineCombined sources1
Modified residuei507PhosphoserineCombined sources1
Modified residuei595PhosphoserineCombined sources1

Post-translational modificationi

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-181.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8WUI4
MaxQBiQ8WUI4
PaxDbiQ8WUI4
PeptideAtlasiQ8WUI4
PRIDEiQ8WUI4
ProteomicsDBi74678
74679 [Q8WUI4-10]
74680 [Q8WUI4-2]
74681 [Q8WUI4-3]
74682 [Q8WUI4-4]
74683 [Q8WUI4-5]
74684 [Q8WUI4-6]
74685 [Q8WUI4-7]
74686 [Q8WUI4-8]
74687 [Q8WUI4-9]

PTM databases

iPTMnetiQ8WUI4
PhosphoSitePlusiQ8WUI4

Miscellaneous databases

PMAP-CutDBiQ8WUI4

Expressioni

Gene expression databases

BgeeiENSG00000061273 Expressed in 224 organ(s), highest expression level in left adrenal gland
CleanExiHS_HDAC7
ExpressionAtlasiQ8WUI4 baseline and differential
GenevisibleiQ8WUI4 HS

Organism-specific databases

HPAiHPA004775

Interactioni

Subunit structurei

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). Interacts with FOXP3.By similarity6 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi119613, 95 interactors
CORUMiQ8WUI4
DIPiDIP-29860N
IntActiQ8WUI4, 49 interactors
MINTiQ8WUI4
STRINGi9606.ENSP00000080059

Chemistry databases

BindingDBiQ8WUI4

Structurei

Secondary structure

1952
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ8WUI4
SMRiQ8WUI4
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WUI4

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 268Transcription repression 1By similarityAdd BLAST268
Regioni1 – 98Interaction with MEF2CBy similarityAdd BLAST98
Regioni49 – 149Interaction with MEF2ABy similarityAdd BLAST101
Regioni218 – 546Transcription repression 2By similarityAdd BLAST329
Regioni518 – 865Histone deacetylaseAdd BLAST348
Regioni877 – 952Interaction with SIN3ABy similarityAdd BLAST76

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi918 – 952Nuclear export signalBy similarityAdd BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi197 – 203Poly-Ser7
Compositional biasi368 – 373Poly-Pro6

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1343 Eukaryota
COG0123 LUCA
GeneTreeiENSGT00530000062809
HOVERGENiHBG057100
InParanoidiQ8WUI4
KOiK11408
PhylomeDBiQ8WUI4
TreeFamiTF106174

Family and domain databases

Gene3Di3.40.800.20, 1 hit
InterProiView protein in InterPro
IPR000286 His_deacetylse
IPR023801 His_deacetylse_dom
IPR037138 His_deacetylse_dom_sf
IPR017320 Histone_deAcase_II_euk
IPR023696 Ureohydrolase_dom_sf
PANTHERiPTHR10625 PTHR10625, 4 hits
PfamiView protein in Pfam
PF00850 Hist_deacetyl, 1 hit
PIRSFiPIRSF037911 HDAC_II_euk, 1 hit
PRINTSiPR01270 HDASUPER
SUPFAMiSSF52768 SSF52768, 1 hit

Sequences (10+)i

Sequence statusi: Complete.

This entry describes 10 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 10 described isoforms and 18 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q8WUI4-1) [UniParc]FASTAAdd to basket

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

« Hide
        10         20         30         40         50
MDLRVGQRPP VEPPPEPTLL ALQRPQRLHH HLFLAGLQQQ RSVEPMRLSM
60 70 80 90 100
DTPMPELQVG PQEQELRQLL HKDKSKRSAV ASSVVKQKLA EVILKKQQAA
110 120 130 140 150
LERTVHPNSP GIPYRTLEPL ETEGATRSML SSFLPPVPSL PSDPPEHFPL
160 170 180 190 200
RKTVSEPNLK LRYKPKKSLE RRKNPLLRKE SAPPSLRRRP AETLGDSSPS
210 220 230 240 250
SSSTPASGCS SPNDSEHGPN PILGSEALLG QRLRLQETSV APFALPTVSL
260 270 280 290 300
LPAITLGLPA PARADSDRRT HPTLGPRGPI LGSPHTPLFL PHGLEPEAGG
310 320 330 340 350
TLPSRLQPIL LLDPSGSHAP LLTVPGLGPL PFHFAQSLMT TERLSGSGLH
360 370 380 390 400
WPLSRTRSEP LPPSATAPPP PGPMQPRLEQ LKTHVQVIKR SAKPSEKPRL
410 420 430 440 450
RQIPSAEDLE TDGGGPGQVV DDGLEHRELG HGQPEARGPA PLQQHPQVLL
460 470 480 490 500
WEQQRLAGRL PRGSTGDTVL LPLAQGGHRP LSRAQSSPAA PASLSAPEPA
510 520 530 540 550
SQARVLSSSE TPARTLPFTT GLIYDSVMLK HQCSCGDNSR HPEHAGRIQS
560 570 580 590 600
IWSRLQERGL RSQCECLRGR KASLEELQSV HSERHVLLYG TNPLSRLKLD
610 620 630 640 650
NGKLAGLLAQ RMFVMLPCGG VGVDTDTIWN ELHSSNAARW AAGSVTDLAF
660 670 680 690 700
KVASRELKNG FAVVRPPGHH ADHSTAMGFC FFNSVAIACR QLQQQSKASK
710 720 730 740 750
ILIVDWDVHH GNGTQQTFYQ DPSVLYISLH RHDDGNFFPG SGAVDEVGAG
760 770 780 790 800
SGEGFNVNVA WAGGLDPPMG DPEYLAAFRI VVMPIAREFS PDLVLVSAGF
810 820 830 840 850
DAAEGHPAPL GGYHVSAKCF GYMTQQLMNL AGGAVVLALE GGHDLTAICD
860 870 880 890 900
ASEACVAALL GNRVDPLSEE GWKQKPNLNA IRSLEAVIRV HSKYWGCMQR
910 920 930 940 950
LASCPDSWVP RVPGADKEEV EAVTALASLS VGILAEDRPS EQLVEEEEPM

NL
Length:952
Mass (Da):102,927
Last modified:May 16, 2003 - v2
Checksum:i786785B084667731
GO
Isoform 2 (identifier: Q8WUI4-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:480
Mass (Da):51,829
Checksum:i0276ABAAAB3DC052
GO
Isoform 3 (identifier: Q8WUI4-3) [UniParc]FASTAAdd to basket

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

Show »
Length:915
Mass (Da):99,093
Checksum:iE828F548BB42ABDC
GO
Isoform 4 (identifier: Q8WUI4-4) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:922
Mass (Da):99,755
Checksum:i398316C4225621DA
GO
Isoform 5 (identifier: Q8WUI4-5) [UniParc]FASTAAdd to basket

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

Show »
Length:991
Mass (Da):106,740
Checksum:i3493E377594FFC18
GO
Isoform 6 (identifier: Q8WUI4-6) [UniParc]FASTAAdd to basket

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

Show »
Length:974
Mass (Da):105,111
Checksum:i86EA1E69F1CEF667
GO
Isoform 7 (identifier: Q8WUI4-7) [UniParc]FASTAAdd to basket

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

Show »
Length:954
Mass (Da):102,906
Checksum:iA5DDAB73E16AD10D
GO
Isoform 8 (identifier: Q8WUI4-8) [UniParc]FASTAAdd to basket

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

Show »
Length:1,014
Mass (Da):108,937
Checksum:i77630923616F2890
GO
Isoform 9 (identifier: Q8WUI4-9) [UniParc]FASTAAdd to basket

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

Show »
Length:425
Mass (Da):46,041
Checksum:iF9EACA7D416CD74E
GO
Isoform 10 (identifier: Q8WUI4-10) [UniParc]FASTAAdd to basket

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

Show »
Length:614
Mass (Da):66,187
Checksum:i2B638DD8C866B502
GO

Computationally mapped potential isoform sequencesi

There are 18 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3KPH8J3KPH8_HUMAN
Histone deacetylase
HDAC7
1,014Annotation score:
C9JEB6C9JEB6_HUMAN
Histone deacetylase 7
HDAC7
274Annotation score:
C9JNI4C9JNI4_HUMAN
Histone deacetylase 7
HDAC7
153Annotation score:
H0YH91H0YH91_HUMAN
Histone deacetylase 7
HDAC7
384Annotation score:
H0YHJ5H0YHJ5_HUMAN
Histone deacetylase 7
HDAC7
110Annotation score:
A0A087WYQ4A0A087WYQ4_HUMAN
Histone deacetylase 7
HDAC7
205Annotation score:
C9JVZ1C9JVZ1_HUMAN
Histone deacetylase 7
HDAC7
133Annotation score:
C9J102C9J102_HUMAN
Histone deacetylase 7
HDAC7
138Annotation score:
C9JGF5C9JGF5_HUMAN
Histone deacetylase 7
HDAC7
88Annotation score:
C9JZ79C9JZ79_HUMAN
Histone deacetylase 7
HDAC7
78Annotation score:
There are more potential isoformsShow all

Sequence cautioni

The sequence AAF63491 differs from that shown. Reason: Frameshift at position 877.Curated
The sequence BAA91474 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA91545 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAB15759 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAB55363 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAC56929 differs from that shown. Intron retention.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti50M → T in BAG64517 (PubMed:14702039).Curated1
Sequence conflicti225 – 264Missing in AAF63491 (Ref. 1) CuratedAdd BLAST40
Sequence conflicti276P → L in BAA91545 (PubMed:14702039).Curated1
Sequence conflicti561R → L in BAA91545 (PubMed:14702039).Curated1
Sequence conflicti614V → E in AAF63491 (Ref. 1) Curated1
Sequence conflicti644S → R in BAB15759 (PubMed:14702039).Curated1
Sequence conflicti665R → W in BAA91474 (PubMed:14702039).Curated1
Sequence conflicti700K → KASK in AAF63491 (Ref. 1) Curated1
Sequence conflicti750G → S in BAA91545 (PubMed:14702039).Curated1
Sequence conflicti777A → T in BAB55363 (PubMed:14702039).Curated1
Sequence conflicti825Q → H in BAA91474 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03604343V → M in a breast cancer sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0381021 – 527Missing in isoform 9. 1 PublicationAdd BLAST527
Alternative sequenceiVSP_0074291 – 472Missing in isoform 2. 1 PublicationAdd BLAST472
Alternative sequenceiVSP_0381031 – 338Missing in isoform 10. 1 PublicationAdd BLAST338
Alternative sequenceiVSP_0381041M → MHSPGADGTQVSPGAHYCSP TGAGCPRPCADTPGPQPQPM in isoform 5 and isoform 7. 2 Publications1
Alternative sequenceiVSP_0381051M → MHSPGAGCPRPCADTPGPQP QPM in isoform 6. 1 Publication1
Alternative sequenceiVSP_0381061M → MSDLRKRELGALFTSRGTGG VEWDGTQVSPGAHYCSPTGA GCPRPCADTPGPQPQPM in isoform 8. 1 Publication1
Alternative sequenceiVSP_008772227 – 263Missing in isoform 3 and isoform 7. 3 PublicationsAdd BLAST37
Alternative sequenceiVSP_007430227 – 256Missing in isoform 4. CuratedAdd BLAST30
Alternative sequenceiVSP_007431473 – 520LAQGG…LPFTT → MQACVGVRGVYPPGSMWVPA VAVLACSLQPRPWGVRTPWV PALTLAPA in isoform 2. 1 PublicationAdd BLAST48
Alternative sequenceiVSP_038107892 – 952SKYWG…EPMNL → MGALTLSQIPGHGSSQQQAG GAFSRPGHPCRAAVVMVNTG AACSAWPPVQTPGCLECQGL TKKKWRQ in isoform 8. 1 PublicationAdd BLAST61

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS41776.1 [Q8WUI4-7]
CCDS81685.1 [Q8WUI4-6]
CCDS8756.2 [Q8WUI4-5]
PIRiT17245
RefSeqiNP_001091886.1, NM_001098416.3 [Q8WUI4-7]
NP_001295019.1, NM_001308090.1 [Q8WUI4-6]
NP_056216.2, NM_015401.4 [Q8WUI4-5]
XP_011536783.1, XM_011538481.1 [Q8WUI4-1]
XP_011536784.1, XM_011538482.1 [Q8WUI4-1]
UniGeneiHs.200063

Genome annotation databases

EnsembliENST00000080059; ENSP00000080059; ENSG00000061273 [Q8WUI4-5]
ENST00000354334; ENSP00000351326; ENSG00000061273 [Q8WUI4-7]
ENST00000427332; ENSP00000404394; ENSG00000061273 [Q8WUI4-1]
ENST00000552960; ENSP00000448532; ENSG00000061273 [Q8WUI4-6]
GeneIDi51564
KEGGihsa:51564
UCSCiuc001rqj.5 human [Q8WUI4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS41776.1 [Q8WUI4-7]
CCDS81685.1 [Q8WUI4-6]
CCDS8756.2 [Q8WUI4-5]
PIRiT17245
RefSeqiNP_001091886.1, NM_001098416.3 [Q8WUI4-7]
NP_001295019.1, NM_001308090.1 [Q8WUI4-6]
NP_056216.2, NM_015401.4 [Q8WUI4-5]
XP_011536783.1, XM_011538481.1 [Q8WUI4-1]
XP_011536784.1, XM_011538482.1 [Q8WUI4-1]
UniGeneiHs.200063

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C0YX-ray2.10A/B/C482-903[»]
3C0ZX-ray2.10A/B/C482-903[»]
3C10X-ray2.00A/B/C482-903[»]
3ZNRX-ray2.40A/B/C482-903[»]
3ZNSX-ray2.45A/B/C482-903[»]
ProteinModelPortaliQ8WUI4
SMRiQ8WUI4
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119613, 95 interactors
CORUMiQ8WUI4
DIPiDIP-29860N
IntActiQ8WUI4, 49 interactors
MINTiQ8WUI4
STRINGi9606.ENSP00000080059

Chemistry databases

BindingDBiQ8WUI4
ChEMBLiCHEMBL2716
DrugBankiDB05015 Belinostat
DB06603 Panobinostat
GuidetoPHARMACOLOGYi2661

PTM databases

iPTMnetiQ8WUI4
PhosphoSitePlusiQ8WUI4

Polymorphism and mutation databases

BioMutaiHDAC7
DMDMi30913097

Proteomic databases

EPDiQ8WUI4
MaxQBiQ8WUI4
PaxDbiQ8WUI4
PeptideAtlasiQ8WUI4
PRIDEiQ8WUI4
ProteomicsDBi74678
74679 [Q8WUI4-10]
74680 [Q8WUI4-2]
74681 [Q8WUI4-3]
74682 [Q8WUI4-4]
74683 [Q8WUI4-5]
74684 [Q8WUI4-6]
74685 [Q8WUI4-7]
74686 [Q8WUI4-8]
74687 [Q8WUI4-9]

Protocols and materials databases

DNASUi51564
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000080059; ENSP00000080059; ENSG00000061273 [Q8WUI4-5]
ENST00000354334; ENSP00000351326; ENSG00000061273 [Q8WUI4-7]
ENST00000427332; ENSP00000404394; ENSG00000061273 [Q8WUI4-1]
ENST00000552960; ENSP00000448532; ENSG00000061273 [Q8WUI4-6]
GeneIDi51564
KEGGihsa:51564
UCSCiuc001rqj.5 human [Q8WUI4-1]

Organism-specific databases

CTDi51564
DisGeNETi51564
EuPathDBiHostDB:ENSG00000061273.17
GeneCardsiHDAC7
H-InvDBiHIX0129669
HGNCiHGNC:14067 HDAC7
HPAiHPA004775
MIMi606542 gene
neXtProtiNX_Q8WUI4
OpenTargetsiENSG00000061273
PharmGKBiPA162390579
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1343 Eukaryota
COG0123 LUCA
GeneTreeiENSGT00530000062809
HOVERGENiHBG057100
InParanoidiQ8WUI4
KOiK11408
PhylomeDBiQ8WUI4
TreeFamiTF106174

Enzyme and pathway databases

BRENDAi3.5.1.98 2681
ReactomeiR-HSA-2122947 NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants
R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-8943724 Regulation of PTEN gene transcription
SIGNORiQ8WUI4

Miscellaneous databases

ChiTaRSiHDAC7 human
EvolutionaryTraceiQ8WUI4
GeneWikiiHDAC7
GenomeRNAii51564
PMAP-CutDBiQ8WUI4
PROiPR:Q8WUI4
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000061273 Expressed in 224 organ(s), highest expression level in left adrenal gland
CleanExiHS_HDAC7
ExpressionAtlasiQ8WUI4 baseline and differential
GenevisibleiQ8WUI4 HS

Family and domain databases

Gene3Di3.40.800.20, 1 hit
InterProiView protein in InterPro
IPR000286 His_deacetylse
IPR023801 His_deacetylse_dom
IPR037138 His_deacetylse_dom_sf
IPR017320 Histone_deAcase_II_euk
IPR023696 Ureohydrolase_dom_sf
PANTHERiPTHR10625 PTHR10625, 4 hits
PfamiView protein in Pfam
PF00850 Hist_deacetyl, 1 hit
PIRSFiPIRSF037911 HDAC_II_euk, 1 hit
PRINTSiPR01270 HDASUPER
SUPFAMiSSF52768 SSF52768, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiHDAC7_HUMAN
AccessioniPrimary (citable) accession number: Q8WUI4
Secondary accession number(s): B3KY08
, B4DWI0, B4E0Q5, Q6P1W9, Q6W9G7, Q7Z4K2, Q7Z5I1, Q96K01, Q9BR73, Q9H7L0, Q9NW41, Q9NWA9, Q9NYK9, Q9UFU7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 16, 2003
Last modified: November 7, 2018
This is version 181 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
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