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Reviewed, UniProtKB/Swiss-Prot Q8WUI4 (HDAC7_HUMAN)

Last modified February 9, 2010. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete 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. Ref.10 Ref.11 Ref.13 Ref.15

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 may be due to its phosphorylation. Ref.10

Domain

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

Post-translational modification

May be phosphorylated by CaMK1 By similarity.

Miscellaneous

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

Sequence similarities

Belongs to the histone deacetylase family. Type 2 subfamily.

Sequence caution

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

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

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

Amino acid modifications

Modified residue1091Phosphoserine Ref.17
Modified residue1141Phosphotyrosine Ref.16
Modified residue2831Phosphoserine Ref.17
Modified residue2861Phosphothreonine Ref.17
Modified residue3581Phosphoserine By similarity
Modified residue4861Phosphoserine Ref.17 Ref.18 Ref.19
Modified residue4871Phosphoserine Ref.14

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.20
VAR_036043

Experimental info

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.

Checksum: 0276ABAAAB3DC052
Show »

FASTA48051,829
Isoform 3.

Checksum: E828F548BB42ABDC
Show »

FASTA91599,093
Isoform 4.

Checksum: 398316C4225621DA
Show »

FASTA92299,755
Isoform 5.

Checksum: 3493E377594FFC18
Show »

FASTA991106,740
Isoform 6.

Checksum: 86EA1E69F1CEF667
Show »

FASTA974105,111
Isoform 7.

Checksum: A5DDAB73E16AD10D
Show »

FASTA954102,906
Isoform 8.

Checksum: 77630923616F2890
Show »

FASTA1,014108,937
Isoform 9.

Checksum: F9EACA7D416CD74E
Show »

FASTA42546,041
Isoform 10.

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: 14702039] [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: 16541075] [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: 15489334] [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: 17974005] [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: 11262386] [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: 11466315] [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: 12239305] [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: 12551922] [Abstract]
Cited for: INTERACTION WITH KAT5.
[14]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, MASS SPECTROMETRY.
Tissue: Epithelium.
[15]"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: 17373667] [Abstract]
Cited for: INTERACTION WITH KDM5B.
[16]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-114, MASS SPECTROMETRY.
[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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-283; THR-286 AND SER-486, MASS SPECTROMETRY.
[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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, MASS SPECTROMETRY.
[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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, MASS SPECTROMETRY.
Tissue: T-cell.
[20]"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: 16959974] [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.
IPIIPI00306189.
IPI00386808.
IPI00743474.
IPI00909569.
IPI00916348.
IPI00916470.
IPI00916810.
IPI00917034.
IPI00944518.
IPI00944634.
PIRT17245.
RefSeqNP_001091886.1.
NP_056216.2.
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[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29860N.
IntActQ8WUI4. 2 interactions.
STRINGQ8WUI4.

PTM databases

PhosphoSiteQ8WUI4.

Proteomic databases

PRIDEQ8WUI4.

Genome annotation databases

EnsemblENST00000080059; ENSP00000080059; ENSG00000061273; Homo sapiens. [Genome view]
ENST00000310824; ENSP00000309766; ENSG00000061273; Homo sapiens. [Genome view]
ENST00000354334; ENSP00000351326; ENSG00000061273; Homo sapiens. [Genome view]
ENST00000380610; ENSP00000369984; ENSG00000061273; Homo sapiens. [Genome view]
ENST00000419356; ENSP00000396436; ENSG00000061273; Homo sapiens. [Genome view]
GeneID51564.
KEGGhsa:51564.
UCSCuc001rqe.1. human.
uc001rqi.2. human.
uc001rqj.2. human.

Organism-specific databases

CTD51564.
GeneCardsGC12M046463.
H-InvDBHIX0010580.
HIX0026420.
HGNCHGNC:14067. HDAC7.
HPAHPA004775.
MIM606542. gene.
PharmGKBPA29232.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ8WUI4.
InParanoidQ8WUI4.
OrthoDBEOG9RBT49.
PhylomeDBQ8WUI4.

Enzyme and pathway databases

Pathway_Interaction_DBhif1_tfpathway. HIF-1-alpha transcription factor network.
ar_tf_pathway. Regulation of Androgen receptor activity.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.

Gene expression databases

ArrayExpressQ8WUI4.
BgeeQ8WUI4.
CleanExHS_HDAC7.
GenevestigatorQ8WUI4.
GermOnlineENSG00000061273. Homo sapiens.

Family and domain databases

InterProIPR000286. His_deacetylse.
IPR017320. Histone_deAcase_II_euk.
[Graphical view]
Gene3DG3DSA:3.40.800.20. His_deacetylse. 1 hit.
PANTHERPTHR10625. His_deacetylse. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037911. HDAC_II_euk. 1 hit.
PRINTSPR01270. HDASUPER.
ProtoNetSearch...

Other Resources

PMAP-CutDBQ8WUI4.
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: February 9, 2010
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 12

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents