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Q8WUI4

- HDAC7_HUMAN

UniProt

Q8WUI4 - HDAC7_HUMAN

Protein

Histone deacetylase 7

Gene

HDAC7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (16 May 2003)
      Previous versions | rss
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    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.By similarity1 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 – 6701By 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

    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.

    GO - Cellular componenti

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

    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 – 1091Phosphoserine2 Publications
    Modified residuei155 – 1551Phosphoserine; by MARK2, MARK3 and PKD/PRKD12 Publications
    Modified residuei181 – 1811Phosphoserine; by PKD/PRKD25 Publications
    Modified residuei283 – 2831Phosphoserine3 Publications
    Modified residuei286 – 2861Phosphothreonine3 Publications
    Modified residuei358 – 3581Phosphoserine; by PKD/PRKD1By similarity
    Modified residuei486 – 4861Phosphoserine4 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-181.7 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).By similarity5 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8WUI4.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 268268Transcription repression 1By similarityAdd
    BLAST
    Regioni1 – 9898Interaction with MEF2CBy similarityAdd
    BLAST
    Regioni49 – 149101Interaction with MEF2ABy similarityAdd
    BLAST
    Regioni218 – 546329Transcription repression 2By similarityAdd
    BLAST
    Regioni518 – 865348Histone deacetylaseAdd
    BLAST
    Regioni877 – 95276Interaction with SIN3ABy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi918 – 95235Nuclear export signalBy 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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti50 – 501M → T in BAG64517. (PubMed:14702039)Curated
    Sequence conflicti225 – 26440Missing in AAF63491. 1 PublicationCuratedAdd
    BLAST
    Sequence conflicti276 – 2761P → L in BAA91545. (PubMed:14702039)Curated
    Sequence conflicti561 – 5611R → L in BAA91545. (PubMed:14702039)Curated
    Sequence conflicti614 – 6141V → E in AAF63491. 1 PublicationCurated
    Sequence conflicti644 – 6441S → R in BAB15759. (PubMed:14702039)Curated
    Sequence conflicti665 – 6651R → W in BAA91474. (PubMed:14702039)Curated
    Sequence conflicti700 – 7001K → KASK in AAF63491. 1 PublicationCurated
    Sequence conflicti750 – 7501G → S in BAA91545. (PubMed:14702039)Curated
    Sequence conflicti777 – 7771A → T in BAB55363. (PubMed:14702039)Curated
    Sequence conflicti825 – 8251Q → H in BAA91474. (PubMed:14702039)Curated

    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. 1 PublicationVSP_038102Add
    BLAST
    Alternative sequencei1 – 472472Missing in isoform 2. 1 PublicationVSP_007429Add
    BLAST
    Alternative sequencei1 – 338338Missing in isoform 10. 1 PublicationVSP_038103Add
    BLAST
    Alternative sequencei1 – 11M → MHSPGADGTQVSPGAHYCSP TGAGCPRPCADTPGPQPQPM in isoform 5 and isoform 7. 2 PublicationsVSP_038104
    Alternative sequencei1 – 11M → MHSPGAGCPRPCADTPGPQP QPM in isoform 6. 1 PublicationVSP_038105
    Alternative sequencei1 – 11M → MSDLRKRELGALFTSRGTGG VEWDGTQVSPGAHYCSPTGA GCPRPCADTPGPQPQPM in isoform 8. 1 PublicationVSP_038106
    Alternative sequencei227 – 26337Missing in isoform 3 and isoform 7. 3 PublicationsVSP_008772Add
    BLAST
    Alternative sequencei227 – 25630Missing in isoform 4. CuratedVSP_007430Add
    BLAST
    Alternative sequencei473 – 52048LAQGG…LPFTT → MQACVGVRGVYPPGSMWVPA VAVLACSLQPRPWGVRTPWV PALTLAPA in isoform 2. 1 PublicationVSP_007431Add
    BLAST
    Alternative sequencei892 – 95261SKYWG…EPMNL → MGALTLSQIPGHGSSQQQAG GAFSRPGHPCRAAVVMVNTG AACSAWPPVQTPGCLECQGL TKKKWRQ in isoform 8. 1 PublicationVSP_038107Add
    BLAST

    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

    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: October 1, 2014
    This is version 144 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