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Q8WUI4

- HDAC7_HUMAN

UniProt

Q8WUI4 - HDAC7_HUMAN

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Protein

Histone deacetylase 7

Gene
HDAC7, HDAC7A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors By similarity. May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi533 – 5331Zinc
Metal bindingi535 – 5351Zinc
Metal bindingi541 – 5411Zinc
Metal bindingi618 – 6181Zinc
Active sitei670 – 6701 By similarity
Sitei843 – 8431Contributes to catalysis

GO - Molecular functioni

  1. 14-3-3 protein binding Source: UniProtKB
  2. activating transcription factor binding Source: UniProtKB
  3. chromatin binding Source: Ensembl
  4. metal ion binding Source: UniProtKB-KW
  5. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  6. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
  7. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
  8. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
  9. protein binding Source: UniProtKB
  10. protein kinase binding Source: UniProtKB
  11. protein kinase C binding Source: UniProtKB
  12. repressing transcription factor binding Source: BHF-UCL
  13. transcription corepressor activity Source: Ensembl

GO - Biological processi

  1. cell-cell junction assembly Source: Ensembl
  2. negative regulation of interleukin-2 production Source: BHF-UCL
  3. negative regulation of osteoblast differentiation Source: UniProtKB
  4. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  5. Notch signaling pathway Source: Reactome
  6. positive regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
  7. transcription, DNA-templated Source: UniProtKB-KW
  8. vasculogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.1.98. 2681.
ReactomeiREACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 7 (EC:3.5.1.98)
Short name:
HD7
Alternative name(s):
Histone deacetylase 7A
Short name:
HD7a
Gene namesi
Name:HDAC7
Synonyms:HDAC7A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:14067. HDAC7.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. histone deacetylase complex Source: InterPro
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi150 – 1501L → A: Abolishes phosphorylation at S-155. 1 Publication
Mutagenesisi155 – 1551S → 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 Publication
Mutagenesisi181 – 1811S → A: Abolishes nuclear export; when associated with A-155; A-358 and A-486. 1 Publication
Mutagenesisi358 – 3581S → A: Abolishes nuclear export; when associated with A-192; A-1118 and A-486. 1 Publication
Mutagenesisi486 – 4861S → A: Abolishes nuclear export; when associated with A-192; A-1118 and A-358. 1 Publication
Mutagenesisi843 – 8431H → A: Enhanced deacetylase activity. 1 Publication
Mutagenesisi843 – 8431H → F: Enhanced deacetylase activity. 1 Publication
Mutagenesisi843 – 8431H → Y: 6000 fold increase in deacetylase activity. 1 Publication

Organism-specific databases

PharmGKBiPA162390579.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 952952Histone deacetylase 7PRO_0000114705Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei109 – 1091Phosphoserine1 Publication
Modified residuei155 – 1551Phosphoserine; by MARK2, MARK3 and PKD/PRKD1 Inferred
Modified residuei181 – 1811Phosphoserine; by PKD/PRKD24 Publications
Modified residuei283 – 2831Phosphoserine2 Publications
Modified residuei286 – 2861Phosphothreonine2 Publications
Modified residuei358 – 3581Phosphoserine; by PKD/PRKD1 By similarity
Modified residuei486 – 4861Phosphoserine3 Publications

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

MaxQBiQ8WUI4.
PaxDbiQ8WUI4.
PRIDEiQ8WUI4.

PTM databases

PhosphoSiteiQ8WUI4.

Miscellaneous databases

PMAP-CutDBQ8WUI4.

Expressioni

Gene expression databases

ArrayExpressiQ8WUI4.
BgeeiQ8WUI4.
CleanExiHS_HDAC7.
GenevestigatoriQ8WUI4.

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).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ICP0P083933EBI-1048378,EBI-6148881From a different organism.
PRKD2Q9BZL66EBI-1048378,EBI-1384325
SFNP319473EBI-1048378,EBI-476295
YWHAZP631043EBI-1048378,EBI-347088

Protein-protein interaction databases

BioGridi119613. 112 interactions.
DIPiDIP-29860N.
IntActiQ8WUI4. 17 interactions.
MINTiMINT-3089050.

Structurei

Secondary structure

1
952
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi520 – 5234
Helixi526 – 5305
Helixi538 – 5403
Helixi546 – 55712
Helixi561 – 5633
Beta strandi564 – 5674
Helixi574 – 5774
Turni578 – 5803
Helixi583 – 5908
Helixi601 – 6099
Beta strandi621 – 6266
Turni631 – 6333
Helixi634 – 65320
Beta strandi656 – 6627
Beta strandi680 – 6823
Helixi684 – 69512
Beta strandi701 – 7055
Beta strandi707 – 7093
Helixi712 – 7187
Beta strandi724 – 7318
Turni733 – 7364
Helixi750 – 7523
Beta strandi756 – 7616
Beta strandi765 – 7673
Helixi771 – 78010
Helixi782 – 7898
Beta strandi792 – 7987
Helixi808 – 8103
Helixi817 – 82711
Helixi831 – 8333
Beta strandi835 – 8395
Helixi845 – 86016
Helixi866 – 8683
Helixi871 – 8733
Helixi878 – 89114
Turni892 – 8943
Helixi896 – 8983

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 515-900.

Miscellaneous databases

EvolutionaryTraceiQ8WUI4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 268268Transcription repression 1 By similarityAdd
BLAST
Regioni1 – 9898Interaction with MEF2C By similarityAdd
BLAST
Regioni49 – 149101Interaction with MEF2A By similarityAdd
BLAST
Regioni218 – 546329Transcription repression 2 By similarityAdd
BLAST
Regioni518 – 865348Histone deacetylaseAdd
BLAST
Regioni877 – 95276Interaction with SIN3A By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi918 – 95235Nuclear export signal By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi197 – 2037Poly-Ser
Compositional biasi368 – 3736Poly-Pro

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0123.
HOVERGENiHBG057100.
InParanoidiQ8WUI4.
KOiK11408.
OrthoDBiEOG7RFTH5.
PhylomeDBiQ8WUI4.
TreeFamiTF106174.

Family and domain databases

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

Sequences (10)i

Sequence statusi: Complete.

This entry describes 10 isoformsi produced by alternative splicing. Align

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

MDLRVGQRPP VEPPPEPTLL ALQRPQRLHH HLFLAGLQQQ RSVEPMRLSM    50
DTPMPELQVG PQEQELRQLL HKDKSKRSAV ASSVVKQKLA EVILKKQQAA 100
LERTVHPNSP GIPYRTLEPL ETEGATRSML SSFLPPVPSL PSDPPEHFPL 150
RKTVSEPNLK LRYKPKKSLE RRKNPLLRKE SAPPSLRRRP AETLGDSSPS 200
SSSTPASGCS SPNDSEHGPN PILGSEALLG QRLRLQETSV APFALPTVSL 250
LPAITLGLPA PARADSDRRT HPTLGPRGPI LGSPHTPLFL PHGLEPEAGG 300
TLPSRLQPIL LLDPSGSHAP LLTVPGLGPL PFHFAQSLMT TERLSGSGLH 350
WPLSRTRSEP LPPSATAPPP PGPMQPRLEQ LKTHVQVIKR SAKPSEKPRL 400
RQIPSAEDLE TDGGGPGQVV DDGLEHRELG HGQPEARGPA PLQQHPQVLL 450
WEQQRLAGRL PRGSTGDTVL LPLAQGGHRP LSRAQSSPAA PASLSAPEPA 500
SQARVLSSSE TPARTLPFTT GLIYDSVMLK HQCSCGDNSR HPEHAGRIQS 550
IWSRLQERGL RSQCECLRGR KASLEELQSV HSERHVLLYG TNPLSRLKLD 600
NGKLAGLLAQ RMFVMLPCGG VGVDTDTIWN ELHSSNAARW AAGSVTDLAF 650
KVASRELKNG FAVVRPPGHH ADHSTAMGFC FFNSVAIACR QLQQQSKASK 700
ILIVDWDVHH GNGTQQTFYQ DPSVLYISLH RHDDGNFFPG SGAVDEVGAG 750
SGEGFNVNVA WAGGLDPPMG DPEYLAAFRI VVMPIAREFS PDLVLVSAGF 800
DAAEGHPAPL GGYHVSAKCF GYMTQQLMNL AGGAVVLALE GGHDLTAICD 850
ASEACVAALL GNRVDPLSEE GWKQKPNLNA IRSLEAVIRV HSKYWGCMQR 900
LASCPDSWVP RVPGADKEEV EAVTALASLS VGILAEDRPS EQLVEEEEPM 950
NL 952
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

Sequence cautioni

The sequence BAC56929.1 differs from that shown. Reason: Intron retention.
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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431V → M in a breast cancer sample; somatic mutation. 1 Publication
VAR_036043

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 527527Missing in isoform 9. VSP_038102Add
BLAST
Alternative sequencei1 – 472472Missing in isoform 2. VSP_007429Add
BLAST
Alternative sequencei1 – 338338Missing in isoform 10. VSP_038103Add
BLAST
Alternative sequencei1 – 11M → MHSPGADGTQVSPGAHYCSP TGAGCPRPCADTPGPQPQPM in isoform 5 and isoform 7. VSP_038104
Alternative sequencei1 – 11M → MHSPGAGCPRPCADTPGPQP QPM in isoform 6. VSP_038105
Alternative sequencei1 – 11M → MSDLRKRELGALFTSRGTGG VEWDGTQVSPGAHYCSPTGA GCPRPCADTPGPQPQPM in isoform 8. VSP_038106
Alternative sequencei227 – 26337Missing in isoform 3 and isoform 7. VSP_008772Add
BLAST
Alternative sequencei227 – 25630Missing in isoform 4. VSP_007430Add
BLAST
Alternative sequencei473 – 52048LAQGG…LPFTT → MQACVGVRGVYPPGSMWVPA VAVLACSLQPRPWGVRTPWV PALTLAPA in isoform 2. VSP_007431Add
BLAST
Alternative sequencei892 – 95261SKYWG…EPMNL → MGALTLSQIPGHGSSQQQAG GAFSRPGHPCRAAVVMVNTG AACSAWPPVQTPGCLECQGL TKKKWRQ in isoform 8. VSP_038107Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501M → T in BAG64517. 1 Publication
Sequence conflicti225 – 26440Missing in AAF63491. 1 PublicationAdd
BLAST
Sequence conflicti276 – 2761P → L in BAA91545. 1 Publication
Sequence conflicti561 – 5611R → L in BAA91545. 1 Publication
Sequence conflicti614 – 6141V → E in AAF63491. 1 Publication
Sequence conflicti644 – 6441S → R in BAB15759. 1 Publication
Sequence conflicti665 – 6651R → W in BAA91474. 1 Publication
Sequence conflicti700 – 7001K → KASK in AAF63491. 1 Publication
Sequence conflicti750 – 7501G → S in BAA91545. 1 Publication
Sequence conflicti777 – 7771A → T in BAB55363. 1 Publication
Sequence conflicti825 – 8251Q → H in BAA91474. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
CCDS8756.2. [Q8WUI4-5]
PIRiT17245.
RefSeqiNP_001091886.1. NM_001098416.2. [Q8WUI4-7]
NP_056216.2. NM_015401.3. [Q8WUI4-5]
XP_005269025.1. XM_005268968.1. [Q8WUI4-6]
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.
UCSCiuc001rqe.3. human. [Q8WUI4-9]
uc001rqj.4. human. [Q8WUI4-7]
uc001rqk.5. human. [Q8WUI4-1]
uc010slo.2. human. [Q8WUI4-5]

Polymorphism databases

DMDMi30913097.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS41776.1. [Q8WUI4-7 ]
CCDS8756.2. [Q8WUI4-5 ]
PIRi T17245.
RefSeqi NP_001091886.1. NM_001098416.2. [Q8WUI4-7 ]
NP_056216.2. NM_015401.3. [Q8WUI4-5 ]
XP_005269025.1. XM_005268968.1. [Q8WUI4-6 ]
UniGenei Hs.200063.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
3ZNR X-ray 2.40 A/B/C 482-903 [» ]
3ZNS X-ray 2.45 A/B/C 482-903 [» ]
ProteinModelPortali Q8WUI4.
SMRi Q8WUI4. Positions 515-900.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119613. 112 interactions.
DIPi DIP-29860N.
IntActi Q8WUI4. 17 interactions.
MINTi MINT-3089050.

Chemistry

BindingDBi Q8WUI4.
ChEMBLi CHEMBL2716.
GuidetoPHARMACOLOGYi 2661.

PTM databases

PhosphoSitei Q8WUI4.

Polymorphism databases

DMDMi 30913097.

Proteomic databases

MaxQBi Q8WUI4.
PaxDbi Q8WUI4.
PRIDEi Q8WUI4.

Protocols and materials databases

DNASUi 51564.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000080059 ; ENSP00000080059 ; ENSG00000061273 . [Q8WUI4-5 ]
ENST00000354334 ; ENSP00000351326 ; ENSG00000061273 . [Q8WUI4-7 ]
ENST00000427332 ; ENSP00000404394 ; ENSG00000061273 . [Q8WUI4-1 ]
ENST00000552960 ; ENSP00000448532 ; ENSG00000061273 . [Q8WUI4-6 ]
GeneIDi 51564.
KEGGi hsa:51564.
UCSCi uc001rqe.3. human. [Q8WUI4-9 ]
uc001rqj.4. human. [Q8WUI4-7 ]
uc001rqk.5. human. [Q8WUI4-1 ]
uc010slo.2. human. [Q8WUI4-5 ]

Organism-specific databases

CTDi 51564.
GeneCardsi GC12M048176.
H-InvDB HIX0129669.
HGNCi HGNC:14067. HDAC7.
HPAi HPA004775.
MIMi 606542. gene.
neXtProti NX_Q8WUI4.
PharmGKBi PA162390579.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0123.
HOVERGENi HBG057100.
InParanoidi Q8WUI4.
KOi K11408.
OrthoDBi EOG7RFTH5.
PhylomeDBi Q8WUI4.
TreeFami TF106174.

Enzyme and pathway databases

BRENDAi 3.5.1.98. 2681.
Reactomei REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.

Miscellaneous databases

ChiTaRSi HDAC7. human.
EvolutionaryTracei Q8WUI4.
GeneWikii HDAC7.
GenomeRNAii 51564.
NextBioi 55370.
PMAP-CutDB Q8WUI4.
PROi Q8WUI4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8WUI4.
Bgeei Q8WUI4.
CleanExi HS_HDAC7.
Genevestigatori Q8WUI4.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "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. 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. 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-283; THR-286 AND SER-486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. "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.
  21. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 482-903, ZINC-BINDING SITES, MUTAGENESIS OF HIS-843.
  26. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-43.

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 historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 16, 2003
Last modified: September 3, 2014
This is version 143 of the entry and version 2 of the sequence. [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

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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