Reviewed, UniProtKB/Swiss-Prot Q8WUI4 (HDAC7_HUMAN)

Names and origin

Protein names

Recommended name:
    Histone deacetylase 7
      Short name=HD7
    EC=3.5.1.98
Alternative name(s):
    HD7a

Gene names

Name:	HDAC7
Synonyms:	HDAC7A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	952 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
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 HTATIP and EDNRA. Interacts with KDM5B.
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.7
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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: HPA histone deacetylase complex Inferred from electronic annotation. Source: InterPro
Molecular function	histone deacetylase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 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: Q8WUI4-4)

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

Isoform 4 (identifier: Q8WUI4-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 952

952

Histone deacetylase 7

PRO_0000114705

Regions

Region

1 – 268

268

Transcription repression 1 By similarity

Region

1 – 98

98

Interaction with MEF2C By similarity

Region

49 – 149

101

Interaction with MEF2A By similarity

Region

218 – 546

329

Transcription repression 2 By similarity

Region

518 – 865

348

Histone deacetylase

Region

877 – 952

76

Interaction with SIN3A By similarity

Motif

918 – 952

35

Nuclear export signal By similarity

Compositional bias

197 – 203

7

Poly-Ser

Compositional bias

368 – 373

6

Poly-Pro

Sites

Active site

670

1

By similarity

Amino acid modifications

Modified residue

109

1

Phosphoserine Ref.14

Modified residue

114

1

Phosphotyrosine Ref.13

Modified residue

283

1

Phosphoserine Ref.14

Modified residue

286

1

Phosphothreonine Ref.14

Modified residue

358

1

Phosphoserine By similarity

Modified residue

486

1

Phosphoserine Ref.14

Modified residue

487

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

1 – 472

472

Missing in isoform 2.

VSP_007429

Alternative sequence

227 – 263

37

Missing in isoform 3.

VSP_008772

Alternative sequence

227 – 256

30

Missing in isoform 4.

VSP_007430

Alternative sequence

473 – 520

48

LAQGG…LPFTT → MQACVGVRGVYPPGSMWVPA VAVLACSLQPRPWGVRTPWV PALTLAPA in isoform 2.

VSP_007431

Natural variant

43

1

V → M in a breast cancer sample; somatic mutation. Ref.15

VAR_036043

Experimental info

Sequence conflict

225 – 264

40

Missing in AAF63491. Ref.1

Sequence conflict

276

1

P → L in BAA91545. Ref.2

Sequence conflict

561

1

R → L in BAA91545. Ref.2

Sequence conflict

614

1

V → E in AAF63491. Ref.1

Sequence conflict

644

1

S → R in BAB15759. Ref.2

Sequence conflict

665

1

R → W in BAA91474. Ref.2

Sequence conflict

700

1

K → KASK Ref.1

Sequence conflict

750

1

G → S in BAA91545. Ref.2

Sequence conflict

777

1

A → T in BAB55363. Ref.2

Sequence conflict

825

1

Q → H in BAA91474. Ref.2

Secondary structure

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952

Helix Strand Turn

Details...

Beta strand

520 – 523

4

Helix

526 – 530

5

Helix

538 – 540

3

Helix

546 – 557

12

Helix

561 – 563

3

Beta strand

564 – 567

4

Helix

574 – 577

4

Turn

578 – 580

3

Helix

583 – 590

8

Helix

601 – 609

9

Beta strand

619 – 628

10

Turn

631 – 633

3

Helix

634 – 654

21

Beta strand

656 – 662

7

Beta strand

680 – 682

3

Helix

684 – 694

11

Beta strand

701 – 705

5

Beta strand

707 – 709

3

Helix

712 – 718

7

Beta strand

724 – 731

8

Turn

733 – 735

3

Helix

750 – 752

3

Beta strand

756 – 761

6

Helix

771 – 780

10

Helix

782 – 789

8

Beta strand

792 – 798

7

Helix

808 – 810

3

Helix

817 – 828

12

Helix

831 – 833

3

Beta strand

835 – 839

5

Helix

845 – 859

15

Helix

866 – 868

3

Helix

870 – 873

4

Helix

878 – 891

14

Turn

892 – 894

3

Helix

896 – 898

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 16, 2003. Version 2. Checksum: 786785B084667731	FASTA	952	102,927
	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
	Isoform 2. Checksum: 0276ABAAAB3DC052	FASTA	480	51,829
	10 20 30 40 50 60 MQACVGVRGV YPPGSMWVPA VAVLACSLQP RPWGVRTPWV PALTLAPAGL IYDSVMLKHQ 70 80 90 100 110 120 CSCGDNSRHP EHAGRIQSIW SRLQERGLRS QCECLRGRKA SLEELQSVHS ERHVLLYGTN 130 140 150 160 170 180 PLSRLKLDNG KLAGLLAQRM FVMLPCGGVG VDTDTIWNEL HSSNAARWAA GSVTDLAFKV 190 200 210 220 230 240 ASRELKNGFA VVRPPGHHAD HSTAMGFCFF NSVAIACRQL QQQSKASKIL IVDWDVHHGN 250 260 270 280 290 300 GTQQTFYQDP SVLYISLHRH DDGNFFPGSG AVDEVGAGSG EGFNVNVAWA GGLDPPMGDP 310 320 330 340 350 360 EYLAAFRIVV MPIAREFSPD LVLVSAGFDA AEGHPAPLGG YHVSAKCFGY MTQQLMNLAG 370 380 390 400 410 420 GAVVLALEGG HDLTAICDAS EACVAALLGN RVDPLSEEGW KQKPNLNAIR SLEAVIRVHS 430 440 450 460 470 480 KYWGCMQRLA SCPDSWVPRV PGADKEEVEA VTALASLSVG ILAEDRPSEQ LVEEEEPMNL
	Isoform 3. Checksum: E828F548BB42ABDC	FASTA	915	99,093
	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 PILGSEADSD RRTHPTLGPR 250 260 270 280 290 300 GPILGSPHTP LFLPHGLEPE AGGTLPSRLQ PILLLDPSGS HAPLLTVPGL GPLPFHFAQS 310 320 330 340 350 360 LMTTERLSGS GLHWPLSRTR SEPLPPSATA PPPPGPMQPR LEQLKTHVQV IKRSAKPSEK 370 380 390 400 410 420 PRLRQIPSAE DLETDGGGPG QVVDDGLEHR ELGHGQPEAR GPAPLQQHPQ VLLWEQQRLA 430 440 450 460 470 480 GRLPRGSTGD TVLLPLAQGG HRPLSRAQSS PAAPASLSAP EPASQARVLS SSETPARTLP 490 500 510 520 530 540 FTTGLIYDSV MLKHQCSCGD NSRHPEHAGR IQSIWSRLQE RGLRSQCECL RGRKASLEEL 550 560 570 580 590 600 QSVHSERHVL LYGTNPLSRL KLDNGKLAGL LAQRMFVMLP CGGVGVDTDT IWNELHSSNA 610 620 630 640 650 660 ARWAAGSVTD LAFKVASREL KNGFAVVRPP GHHADHSTAM GFCFFNSVAI ACRQLQQQSK 670 680 690 700 710 720 ASKILIVDWD VHHGNGTQQT FYQDPSVLYI SLHRHDDGNF FPGSGAVDEV GAGSGEGFNV 730 740 750 760 770 780 NVAWAGGLDP PMGDPEYLAA FRIVVMPIAR EFSPDLVLVS AGFDAAEGHP APLGGYHVSA 790 800 810 820 830 840 KCFGYMTQQL MNLAGGAVVL ALEGGHDLTA ICDASEACVA ALLGNRVDPL SEEGWKQKPN 850 860 870 880 890 900 LNAIRSLEAV IRVHSKYWGC MQRLASCPDS WVPRVPGADK EEVEAVTALA SLSVGILAED 910 RPSEQLVEEE EPMNL
	Isoform 4. Checksum: 398316C4225621DA	FASTA	922	99,755
	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 PILGSEGLPA PARADSDRRT 250 260 270 280 290 300 HPTLGPRGPI LGSPHTPLFL PHGLEPEAGG TLPSRLQPIL LLDPSGSHAP LLTVPGLGPL 310 320 330 340 350 360 PFHFAQSLMT TERLSGSGLH WPLSRTRSEP LPPSATAPPP PGPMQPRLEQ LKTHVQVIKR 370 380 390 400 410 420 SAKPSEKPRL RQIPSAEDLE TDGGGPGQVV DDGLEHRELG HGQPEARGPA PLQQHPQVLL 430 440 450 460 470 480 WEQQRLAGRL PRGSTGDTVL LPLAQGGHRP LSRAQSSPAA PASLSAPEPA SQARVLSSSE 490 500 510 520 530 540 TPARTLPFTT GLIYDSVMLK HQCSCGDNSR HPEHAGRIQS IWSRLQERGL RSQCECLRGR 550 560 570 580 590 600 KASLEELQSV HSERHVLLYG TNPLSRLKLD NGKLAGLLAQ RMFVMLPCGG VGVDTDTIWN 610 620 630 640 650 660 ELHSSNAARW AAGSVTDLAF KVASRELKNG FAVVRPPGHH ADHSTAMGFC FFNSVAIACR 670 680 690 700 710 720 QLQQQSKASK ILIVDWDVHH GNGTQQTFYQ DPSVLYISLH RHDDGNFFPG SGAVDEVGAG 730 740 750 760 770 780 SGEGFNVNVA WAGGLDPPMG DPEYLAAFRI VVMPIAREFS PDLVLVSAGF DAAEGHPAPL 790 800 810 820 830 840 GGYHVSAKCF GYMTQQLMNL AGGAVVLALE GGHDLTAICD ASEACVAALL GNRVDPLSEE 850 860 870 880 890 900 GWKQKPNLNA IRSLEAVIRV HSKYWGCMQR LASCPDSWVP RVPGADKEEV EAVTALASLS 910 920 VGILAEDRPS EQLVEEEEPM NL

References

	« Hide 'large scale' referencesShow '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]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-952 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 651-952. Tissue: Embryo, Placenta, Spleen and Teratocarcinoma.
[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]	"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: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder 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.
[6]	"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] OF 242-952 (ISOFORM 1). Tissue: B-cell and Colon.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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 HTATIP.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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. , 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

EMBLGenBankDDBJ

AF239243 mRNA. Translation: AAF63491.1. Frameshift.
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.
AY321367 mRNA. Translation: AAP84704.1.
AC004466 Genomic DNA. No translation available.
AL117455 mRNA. Translation: CAB55935.1.
BC006453 mRNA. Translation: AAH06453.1. Different initiation.
BC020505 mRNA. Translation: AAH20505.2.

IPI

IPI00306189.
IPI00386808.
IPI00743474.
IPI00916348.

PIR

T17245.

UniGene

Hs.200063

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8WUI4. 2 interactions.

PTM databases

PhosphoSite

Q8WUI4.

Proteomic databases

PRIDE

Q8WUI4.

Genome annotation databases

Ensembl

ENSG00000061273. Homo sapiens. [Contig view]

Organism-specific databases

GeneCards

GC12M046463.

H-InvDB

HIX0010580.
HIX0026420.

HGNC

HGNC:14067. HDAC7.

HPA

HPA004775.

MIM

606542. gene.

PharmGKB

PA29232.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q8WUI4.

Enzyme and pathway databases

Pathway_Interaction_DB

hif1_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.

Reactome

REACT_71. Gene Expression.

Gene expression databases

Bgee

Q8WUI4.

CleanEx

HS_HDAC7.

GermOnline

ENSG00000061273. Homo sapiens.

Family and domain databases

InterPro

IPR000286. His_deacetylse.
IPR017320. Histone_deAcase_II_euk.
[Graphical view]

Gene3D

G3DSA:3.40.800.20. His_deacetylse. 1 hit.

PANTHER

PTHR10625. His_deacetylse. 1 hit.

Pfam

PF00850. Hist_deacetyl. 1 hit.
[Graphical view]

PIRSF

PIRSF037911. HDAC_II_euk. 1 hit.

PRINTS

PR01270. HDASUPER.

ProtoNet

Search...

Other Resources

PMAP-CutDB

Q8WUI4.

SOURCE

Search...

Entry information

Entry name

HDAC7_HUMAN

Accession

Primary (citable) accession number: Q8WUI4
Secondary accession number(s): 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:	June 16, 2009
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)