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Q8WUI4 (HDAC7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase 7

Short name=HD7
EC=3.5.1.98
Alternative name(s):
Histone deacetylase 7A
Short name=HD7a
Gene names
Name:HDAC7
Synonyms:HDAC7A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length952 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors By similarity. May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene. Ref.12

Catalytic activity

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

Subunit structure

Interacts with HDAC1, HDAC2, HDAC3, HDAC4, HDAC5, NCOR1, NCOR2, SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1, SAP30 and MBD3. Interacts with the 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C By similarity. Interacts with KAT5 and EDNRA. Interacts with KDM5B. Interacts with ZMYND15 By similarity. Interacts with PML (isoform PML-4) Ref.10 Ref.11 Ref.13 Ref.16 Ref.23

Subcellular location

Nucleus. Cytoplasm. Note: In the nucleus, it associates with distinct subnuclear dot-like structures. Shuttles between the nucleus and the cytoplasm. Treatment with EDN1 results in shuttling from the nucleus to the perinuclear region. The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation. Ref.10 Ref.14

Domain

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

Post-translational modification

May be phosphorylated by CaMK1. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylation at Ser-155 by MARK2, MARK3 and PRKD1 promotes interaction with 14-3-3 proteins and export from the nucleus. Phosphorylation at Ser-155 is a prerequisite for phosphorylation at Ser-181. Ref.14 Ref.15 Ref.20

Miscellaneous

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

Sequence similarities

Belongs to the histone deacetylase family. HD type 2 subfamily.

Sequence caution

The sequence AAF63491.1 differs from that shown. Reason: Frameshift at position 877.

The sequence BAA91474.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA91545.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB15759.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB55363.1 differs from that shown. Reason: Erroneous initiation.

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Hydrolase
Repressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Traceable author statement. Source: Reactome

cell-cell junction assembly

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-2 production

Inferred from direct assay PubMed 17360565. Source: BHF-UCL

negative regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 17997710. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration involved in sprouting angiogenesis

Inferred from mutant phenotype PubMed 19351956. Source: BHF-UCL

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

vasculogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay Ref.14PubMed 17997710. Source: UniProtKB

histone deacetylase complex

Inferred from electronic annotation. Source: InterPro

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.14PubMed 17997710. Source: UniProtKB

   Molecular_function14-3-3 protein binding

Inferred from direct assay Ref.14. Source: UniProtKB

NAD-dependent histone deacetylase activity (H3-K14 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K18 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K9 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H4-K16 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

activating transcription factor binding

Inferred from physical interaction PubMed 20590529. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase C binding

Inferred from physical interaction Ref.20. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.14. Source: UniProtKB

repressing transcription factor binding

Inferred from physical interaction PubMed 17360565. Source: BHF-UCL

transcription corepressor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 10 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WUI4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8WUI4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-472: Missing.
     473-520: LAQGGHRPLS...TPARTLPFTT → MQACVGVRGV...WVPALTLAPA
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8WUI4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     227-263: Missing.
Isoform 4 (identifier: Q8WUI4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     227-256: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q8WUI4-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHSPGADGTQVSPGAHYCSPTGAGCPRPCADTPGPQPQPM
Isoform 6 (identifier: Q8WUI4-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHSPGAGCPRPCADTPGPQPQPM
Isoform 7 (identifier: Q8WUI4-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHSPGADGTQVSPGAHYCSPTGAGCPRPCADTPGPQPQPM
     227-263: Missing.
Isoform 8 (identifier: Q8WUI4-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSDLRKRELGALFTSRGTGGVEWDGTQVSPGAHYCSPTGAGCPRPCADTPGPQPQPM
     892-952: SKYWGCMQRL...LVEEEEPMNL → MGALTLSQIP...QGLTKKKWRQ
Isoform 9 (identifier: Q8WUI4-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-527: Missing.
Isoform 10 (identifier: Q8WUI4-10)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 952952Histone deacetylase 7
PRO_0000114705

Regions

Region1 – 268268Transcription repression 1 By similarity
Region1 – 9898Interaction with MEF2C By similarity
Region49 – 149101Interaction with MEF2A By similarity
Region218 – 546329Transcription repression 2 By similarity
Region518 – 865348Histone deacetylase
Region877 – 95276Interaction with SIN3A By similarity
Motif918 – 95235Nuclear export signal By similarity
Compositional bias197 – 2037Poly-Ser
Compositional bias368 – 3736Poly-Pro

Sites

Active site6701 By similarity
Metal binding5331Zinc
Metal binding5351Zinc
Metal binding5411Zinc
Metal binding6181Zinc
Site8431Contributes to catalysis

Amino acid modifications

Modified residue1091Phosphoserine Ref.17
Modified residue1551Phosphoserine; by MARK2, MARK3 and PKD/PRKD1 Probable
Modified residue1811Phosphoserine; by PKD/PRKD2 Ref.14 Ref.15 Ref.21 Ref.22
Modified residue2831Phosphoserine Ref.17 Ref.21
Modified residue2861Phosphothreonine Ref.17 Ref.21
Modified residue3581Phosphoserine; by PKD/PRKD1 By similarity
Modified residue4861Phosphoserine Ref.17 Ref.19 Ref.22

Natural variations

Alternative sequence1 – 527527Missing in isoform 9.
VSP_038102
Alternative sequence1 – 472472Missing in isoform 2.
VSP_007429
Alternative sequence1 – 338338Missing in isoform 10.
VSP_038103
Alternative sequence11M → MHSPGADGTQVSPGAHYCSP TGAGCPRPCADTPGPQPQPM in isoform 5 and isoform 7.
VSP_038104
Alternative sequence11M → MHSPGAGCPRPCADTPGPQP QPM in isoform 6.
VSP_038105
Alternative sequence11M → MSDLRKRELGALFTSRGTGG VEWDGTQVSPGAHYCSPTGA GCPRPCADTPGPQPQPM in isoform 8.
VSP_038106
Alternative sequence227 – 26337Missing in isoform 3 and isoform 7.
VSP_008772
Alternative sequence227 – 25630Missing in isoform 4.
VSP_007430
Alternative sequence473 – 52048LAQGG…LPFTT → MQACVGVRGVYPPGSMWVPA VAVLACSLQPRPWGVRTPWV PALTLAPA in isoform 2.
VSP_007431
Alternative sequence892 – 95261SKYWG…EPMNL → MGALTLSQIPGHGSSQQQAG GAFSRPGHPCRAAVVMVNTG AACSAWPPVQTPGCLECQGL TKKKWRQ in isoform 8.
VSP_038107
Natural variant431V → M in a breast cancer sample; somatic mutation. Ref.26
VAR_036043

Experimental info

Mutagenesis1501L → A: Abolishes phosphorylation at S-155. Ref.14
Mutagenesis1551S → A: Abolishes nuclear export; when associated with A-181; A-358 and A-486. Abolishes phosphorylation by MARK2 and MARK3, interaction with 14-3-3 and localization to the cytoplasm. Ref.14
Mutagenesis1811S → A: Abolishes nuclear export; when associated with A-155; A-358 and A-486. Ref.14
Mutagenesis3581S → A: Abolishes nuclear export; when associated with A-192; A-1118 and A-486. Ref.14
Mutagenesis4861S → A: Abolishes nuclear export; when associated with A-192; A-1118 and A-358. Ref.14
Mutagenesis8431H → A: Enhanced deacetylase activity. Ref.25
Mutagenesis8431H → F: Enhanced deacetylase activity. Ref.25
Mutagenesis8431H → Y: 6000 fold increase in deacetylase activity. Ref.25
Sequence conflict501M → T in BAG64517. Ref.5
Sequence conflict225 – 26440Missing in AAF63491. Ref.1
Sequence conflict2761P → L in BAA91545. Ref.5
Sequence conflict5611R → L in BAA91545. Ref.5
Sequence conflict6141V → E in AAF63491. Ref.1
Sequence conflict6441S → R in BAB15759. Ref.5
Sequence conflict6651R → W in BAA91474. Ref.5
Sequence conflict7001K → KASK in AAF63491. Ref.1
Sequence conflict7501G → S in BAA91545. Ref.5
Sequence conflict7771A → T in BAB55363. Ref.5
Sequence conflict8251Q → H in BAA91474. Ref.5

Secondary structure

....................................................................... 952
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 16, 2003. Version 2.
Checksum: 786785B084667731

FASTA952102,927
        10         20         30         40         50         60 
MDLRVGQRPP VEPPPEPTLL ALQRPQRLHH HLFLAGLQQQ RSVEPMRLSM DTPMPELQVG 

        70         80         90        100        110        120 
PQEQELRQLL HKDKSKRSAV ASSVVKQKLA EVILKKQQAA LERTVHPNSP GIPYRTLEPL 

       130        140        150        160        170        180 
ETEGATRSML SSFLPPVPSL PSDPPEHFPL RKTVSEPNLK LRYKPKKSLE RRKNPLLRKE 

       190        200        210        220        230        240 
SAPPSLRRRP AETLGDSSPS SSSTPASGCS SPNDSEHGPN PILGSEALLG QRLRLQETSV 

       250        260        270        280        290        300 
APFALPTVSL LPAITLGLPA PARADSDRRT HPTLGPRGPI LGSPHTPLFL PHGLEPEAGG 

       310        320        330        340        350        360 
TLPSRLQPIL LLDPSGSHAP LLTVPGLGPL PFHFAQSLMT TERLSGSGLH WPLSRTRSEP 

       370        380        390        400        410        420 
LPPSATAPPP PGPMQPRLEQ LKTHVQVIKR SAKPSEKPRL RQIPSAEDLE TDGGGPGQVV 

       430        440        450        460        470        480 
DDGLEHRELG HGQPEARGPA PLQQHPQVLL WEQQRLAGRL PRGSTGDTVL LPLAQGGHRP 

       490        500        510        520        530        540 
LSRAQSSPAA PASLSAPEPA SQARVLSSSE TPARTLPFTT GLIYDSVMLK HQCSCGDNSR 

       550        560        570        580        590        600 
HPEHAGRIQS IWSRLQERGL RSQCECLRGR KASLEELQSV HSERHVLLYG TNPLSRLKLD 

       610        620        630        640        650        660 
NGKLAGLLAQ RMFVMLPCGG VGVDTDTIWN ELHSSNAARW AAGSVTDLAF KVASRELKNG 

       670        680        690        700        710        720 
FAVVRPPGHH ADHSTAMGFC FFNSVAIACR QLQQQSKASK ILIVDWDVHH GNGTQQTFYQ 

       730        740        750        760        770        780 
DPSVLYISLH RHDDGNFFPG SGAVDEVGAG SGEGFNVNVA WAGGLDPPMG DPEYLAAFRI 

       790        800        810        820        830        840 
VVMPIAREFS PDLVLVSAGF DAAEGHPAPL GGYHVSAKCF GYMTQQLMNL AGGAVVLALE 

       850        860        870        880        890        900 
GGHDLTAICD ASEACVAALL GNRVDPLSEE GWKQKPNLNA IRSLEAVIRV HSKYWGCMQR 

       910        920        930        940        950 
LASCPDSWVP RVPGADKEEV EAVTALASLS VGILAEDRPS EQLVEEEEPM NL 

« Hide

Isoform 2 [UniParc].

Checksum: 0276ABAAAB3DC052
Show »

FASTA48051,829
Isoform 3 [UniParc].

Checksum: E828F548BB42ABDC
Show »

FASTA91599,093
Isoform 4 [UniParc].

Checksum: 398316C4225621DA
Show »

FASTA92299,755
Isoform 5 [UniParc].

Checksum: 3493E377594FFC18
Show »

FASTA991106,740
Isoform 6 [UniParc].

Checksum: 86EA1E69F1CEF667
Show »

FASTA974105,111
Isoform 7 [UniParc].

Checksum: A5DDAB73E16AD10D
Show »

FASTA954102,906
Isoform 8 [UniParc].

Checksum: 77630923616F2890
Show »

FASTA1,014108,937
Isoform 9 [UniParc].

Checksum: F9EACA7D416CD74E
Show »

FASTA42546,041
Isoform 10 [UniParc].

Checksum: 2B638DD8C866B502
Show »

FASTA61466,187

References

« Hide 'large scale' references
[1]"A novel class II HDAC is associated with the transcriptional homeodomain repressor CCAAT displacement protein."
Li S., Fischle W., Verdin E., Walsh M.J.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Cervix carcinoma.
[2]"Genomic organization of the human histone deacetylase 7 gene."
Petrie K., Zelent A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 5).
[3]"Homo sapiens histone deacetylase 7A (HDAC7A), transcript variant 3."
Zhi Y., Su E.W.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , 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. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 242-952 (ISOFORM 1).
Tissue: B-cell, Colon and PNS.
[9]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-952 (ISOFORM 1).
Tissue: Uterus.
[10]"Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling."
Lee H.-J., Chun M., Kandror K.V.
J. Biol. Chem. 276:16597-16600(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EDNRA.
[11]"Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo."
Fischle W., Dequiedt F., Fillion M., Hendzel M.J., Voelter W., Verdin E.
J. Biol. Chem. 276:35826-35835(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC3.
[12]"Signal transduction and transcription factor modification during reactivation of Epstein-Barr virus from latency."
Bryant H., Farrell P.J.
J. Virol. 76:10290-10298(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Tip60 is a co-repressor for STAT3."
Xiao H., Chung J., Kao H.-Y., Yang Y.-C.
J. Biol. Chem. 278:11197-11204(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KAT5.
[14]"New role for hPar-1 kinases EMK and C-TAK1 in regulating localization and activity of class IIa histone deacetylases."
Dequiedt F., Martin M., Von Blume J., Vertommen D., Lecomte E., Mari N., Heinen M.F., Bachmann M., Twizere J.C., Huang M.C., Rider M.H., Piwnica-Worms H., Seufferlein T., Kettmann R.
Mol. Cell. Biol. 26:7086-7102(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-155 AND SER-181, MUTAGENESIS OF LEU-150; SER-155; SER-181; SER-358 AND SER-486.
[15]"Phosphorylation at Ser244 by CK1 determines nuclear localization and substrate targeting of PKD2."
von Blume J., Knippschild U., Dequiedt F., Giamas G., Beck A., Auer A., Van Lint J., Adler G., Seufferlein T.
EMBO J. 26:4619-4633(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-181.
[16]"Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases."
Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K., Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P., Taylor-Papadimitriou J.
Int. J. Cancer 121:265-275(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KDM5B.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-283; THR-286 AND SER-486, 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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Human HDAC7 harbors a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity."
Schuetz A., Min J., Allali-Hassani A., Schapira M., Shuen M., Loppnau P., Mazitschek R., Kwiatkowski N.P., Lewis T.A., Maglathin R.L., McLean T.H., Bochkarev A., Plotnikov A.N., Vedadi M., Arrowsmith C.H.
J. Biol. Chem. 283:11355-11363(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 482-903, ZINC-BINDING SITES, MUTAGENESIS OF HIS-843.
[26]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-43.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF239243 mRNA. Translation: AAF63491.1. Frameshift.
AY302468 mRNA. Translation: AAQ18232.1.
AY321367 mRNA. Translation: AAP84704.1.
BT009771 mRNA. Translation: AAP88773.1.
AK001032 mRNA. Translation: BAA91474.1. Different initiation.
AK001190 mRNA. Translation: BAA91545.1. Different initiation.
AK024469 mRNA. Translation: BAB15759.1. Different initiation.
AK027781 mRNA. Translation: BAB55363.1. Different initiation.
AK122588 mRNA. Translation: BAC56929.1. Sequence problems.
AK128383 mRNA. Translation: BAG54670.1.
AK299292 mRNA. Translation: BAG61307.1.
AK301545 mRNA. Translation: BAG63042.1.
AK303481 mRNA. Translation: BAG64517.1.
AC004466 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW57957.1.
BC006453 mRNA. Translation: AAH06453.2.
BC020505 mRNA. Translation: AAH20505.2.
BC064840 mRNA. Translation: AAH64840.1.
AL117455 mRNA. Translation: CAB55935.1.
PIRT17245.
RefSeqNP_001091886.1. NM_001098416.2.
NP_056216.2. NM_015401.3.
XP_005269025.1. XM_005268968.1.
UniGeneHs.200063.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ8WUI4.
SMRQ8WUI4. Positions 515-900.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119613. 112 interactions.
DIPDIP-29860N.
IntActQ8WUI4. 17 interactions.
MINTMINT-3089050.

Chemistry

BindingDBQ8WUI4.
ChEMBLCHEMBL2716.

PTM databases

PhosphoSiteQ8WUI4.

Polymorphism databases

DMDM30913097.

Proteomic databases

PaxDbQ8WUI4.
PRIDEQ8WUI4.

Protocols and materials databases

DNASU51564.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000080059; ENSP00000080059; ENSG00000061273. [Q8WUI4-5]
ENST00000354334; ENSP00000351326; ENSG00000061273. [Q8WUI4-7]
ENST00000427332; ENSP00000404394; ENSG00000061273. [Q8WUI4-1]
ENST00000552960; ENSP00000448532; ENSG00000061273. [Q8WUI4-6]
GeneID51564.
KEGGhsa:51564.
UCSCuc001rqe.3. human. [Q8WUI4-9]
uc001rqj.4. human. [Q8WUI4-7]
uc001rqk.5. human. [Q8WUI4-1]
uc010slo.2. human. [Q8WUI4-5]

Organism-specific databases

CTD51564.
GeneCardsGC12M048176.
H-InvDBHIX0129669.
HGNCHGNC:14067. HDAC7.
HPAHPA004775.
MIM606542. gene.
neXtProtNX_Q8WUI4.
PharmGKBPA162390579.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0123.
HOVERGENHBG057100.
InParanoidQ8WUI4.
KOK11408.
OrthoDBEOG7RFTH5.
PhylomeDBQ8WUI4.
TreeFamTF106174.

Enzyme and pathway databases

BRENDA3.5.1.98. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ8WUI4.
BgeeQ8WUI4.
CleanExHS_HDAC7.
GenevestigatorQ8WUI4.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR017320. Histone_deAcase_II_euk.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037911. HDAC_II_euk. 1 hit.
PRINTSPR01270. HDASUPER.
ProtoNetSearch...

Other

ChiTaRSHDAC7. human.
EvolutionaryTraceQ8WUI4.
GeneWikiHDAC7.
GenomeRNAi51564.
NextBio55370.
PMAP-CutDBQ8WUI4.
PROQ8WUI4.
SOURCESearch...

Entry information

Entry nameHDAC7_HUMAN
AccessionPrimary (citable) accession number: Q8WUI4
Secondary accession number(s): B3KY08 expand/collapse secondary AC list , B4DWI0, B4E0Q5, Q6P1W9, Q6W9G7, Q7Z4K2, Q7Z5I1, Q96K01, Q9BR73, Q9H7L0, Q9NW41, Q9NWA9, Q9NYK9, Q9UFU7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 16, 2003
Last modified: April 16, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM