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Q9UKV0 (HDAC9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 9

Short name=HD9
EC=3.5.1.98
Alternative name(s):
Histone deacetylase 7B
Short name=HD7
Short name=HD7b
Histone deacetylase-related protein
MEF2-interacting transcription repressor MITR
Gene names
Name:HDAC9
Synonyms:HDAC7, HDAC7B, HDRP, KIAA0744, MITR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1011 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. Represses MEF2-dependent transcription. Ref.1 Ref.3 Ref.10 Ref.11 Ref.14

Isoform 3 lacks active site residues and therefore is catalytically inactive. Represses MEF2-dependent transcription by recruiting HDAC1 and/or HDAC3. Seems to inhibit skeletal myogenesis and to be involved in heart development. Protects neurons from apoptosis, both by inhibiting JUN phosphorylation by MAPK10 and by repressing JUN transcription via HDAC1 recruitment to JUN promoter. Ref.1 Ref.3 Ref.10 Ref.11 Ref.14

Catalytic activity

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

Enzyme regulation

Inhibited by Trichostatin A (TSA) and suberoylanilide hydroxamic acid. Ref.1

Subunit structure

Homodimer. Interacts with CTBP1. The phosphorylated form interacts with 14-3-3 By similarity. Interacts with HDAC1 and HDAC3, and probably with HDAC4 and HDAC5. Interacts with MEF2, MAPK10, ETV6, NCOR1 and BCL6. Ref.1 Ref.3 Ref.10 Ref.11 Ref.12

Subcellular location

Nucleus By similarity Ref.3.

Tissue specificity

Broadly expressed, with highest levels in brain, heart, muscle and testis. Isoform 3 is present in human bladder carcinoma cells (at protein level). Ref.1 Ref.2 Ref.3 Ref.11

Post-translational modification

Phosphorylated on Ser-220 and Ser-450; which promotes 14-3-3-binding, impairs interaction with MEF2, and antagonizes antimyogenic activity. Phosphorylated on Ser-240; which impairs nuclear accumulation By similarity. Isoform 7 is phosphorylated on Tyr-1010. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Ref.16

Sumoylated. Ref.3 Ref.13

Involvement in disease

A chromosomal aberration involving HDAC9 is found in a family with Peters anomaly. Translocation t(1;7)(q41;p21) with TGFB2 resulting in lack of HDAC9 protein.

Sequence similarities

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

Sequence caution

The sequence BAA34464.2 differs from that shown. Reason: Erroneous initiation.

Isoform 6: The sequence AAI11736.1 differs from that shown. Reason: Frameshift at position 1021.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Hydrolase
Repressor
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell activation

Traceable author statement PubMed 12711221. Source: UniProtKB

B cell differentiation

Traceable author statement PubMed 12711221. Source: UniProtKB

Notch signaling pathway

Traceable author statement. Source: Reactome

cellular response to insulin stimulus

Inferred from direct assay PubMed 19303849. Source: BHF-UCL

heart development

Inferred from sequence or structural similarity. Source: BHF-UCL

histone H3 deacetylation

Inferred from direct assay Ref.3. Source: BHF-UCL

histone H4 deacetylation

Inferred from direct assay Ref.3. Source: BHF-UCL

histone deacetylation

Inferred from direct assay Ref.1. Source: BHF-UCL

inflammatory response

Traceable author statement PubMed 12711221. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.1Ref.11. Source: BHF-UCL

peptidyl-lysine deacetylation

Inferred from direct assay Ref.1. Source: BHF-UCL

positive regulation of cell migration involved in sprouting angiogenesis

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

regulation of skeletal muscle fiber development

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of striated muscle cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.16. Source: UniProtKB

histone deacetylase complex

Traceable author statement PubMed 12711221. Source: UniProtKB

histone methyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

transcription factor complex

Inferred from direct assay PubMed 15567413PubMed 19303849. Source: BHF-UCL

   Molecular_functionNAD-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

histone deacetylase activity

Inferred from direct assay Ref.1. Source: BHF-UCL

histone deacetylase binding

Inferred from direct assay Ref.11. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein deacetylase activity

Inferred from direct assay Ref.1. Source: BHF-UCL

protein kinase C binding

Inferred from physical interaction Ref.16. Source: UniProtKB

repressing transcription factor binding

Inferred from direct assay Ref.3. Source: BHF-UCL

transcription corepressor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

transcription factor binding

Inferred from physical interaction PubMed 10748098. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BCL6P411822EBI-765444,EBI-765407
ETV6P412123EBI-765476,EBI-1372759
Ncor1Q609743EBI-1372717,EBI-349004From a different organism.

Alternative products

This entry describes 11 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q9UKV0-1)

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: Q9UKV0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     487-574: Missing.
Isoform 3 (identifier: Q9UKV0-3)

Also known as: HDRP; MITR;

The sequence of this isoform differs from the canonical sequence as follows:
     575-590: PFLEPTHTRALSVRQA → VIGKDLAPGFVIKVII
     591-1011: Missing.
Note: Major form in most tissues. Inactive due to lack of active site residues.
Isoform 4 (identifier: Q9UKV0-4)

Also known as: HDAC9a;

The sequence of this isoform differs from the canonical sequence as follows:
     861-879: GTGLGEGYNINIAWTGGLD → RFISLEPHFYLYLSGNCIA
     880-1011: Missing.
Isoform 5 (identifier: Q9UKV0-5)

Also known as: HDAC9b; HDAC9fl;

The sequence of this isoform differs from the canonical sequence as follows:
     1006-1011: MSLKFS → KYWKSVRMVAVPRGCALAGAQLQEETETVSALASLTVDVEQPFAQEDSRTAGEPMEEEPAL
Note: Contains a phosphotyrosine at position 1007 (Probable).
Isoform 6 (identifier: Q9UKV0-6)

The sequence of this isoform differs from the canonical sequence as follows:
     88-88: K → KLQQ
     218-261: Missing.
     1006-1011: MSLKFS → KYWKSVRMVAVPRGCALAGAQLQEETETVSALASLTVDVEQPFAQEDSRTAGEPMEEEPAL
Note: Contains a phosphotyrosine at position 966 (Probable). Excluded from the nucleus. Does not interact with ETV6..
Isoform 7 (identifier: Q9UKV0-7)

The sequence of this isoform differs from the canonical sequence as follows:
     88-88: K → KLQQ
     1006-1011: MSLKFS → KYWKSVRMVAVPRGCALAGAQLQEETETVSALASLTVDVEQPFAQEDSRTAGEPMEEEPAL
Isoform 8 (identifier: Q9UKV0-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MMSSPAQPDLMWNLVPWVLFCGCCRIFPDGVAGREQLLAQQRM
     218-261: Missing.
     575-590: PFLEPTHTRALSVRQA → VIGKDLAPGFVIKVII
     591-1011: Missing.
Note: No experimental confirmation available.
Isoform 9 (identifier: Q9UKV0-9)

The sequence of this isoform differs from the canonical sequence as follows:
     218-261: Missing.
     575-590: PFLEPTHTRALSVRQA → VIGKDLAPGFVIKVII
     591-1011: Missing.
Isoform 10 (identifier: Q9UKV0-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.
     88-88: K → KLQQ
     575-590: PFLEPTHTRALSVRQA → VIGKDLAPGFVIKVII
     591-1011: Missing.
Isoform 11 (identifier: Q9UKV0-11)

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.
     177-178: Missing.
     218-261: Missing.
     575-590: PFLEPTHTRALSVRQA → VIGKDLAPGFVIKVII
     591-1011: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10111011Histone deacetylase 9
PRO_0000114710

Regions

Region23 – 275Interaction with CTBP1 By similarity
Region136 – 15419Interaction with MEF2 By similarity
Region175 – 343169Interaction with MAPK10 By similarity
Region218 – 26144Interaction with ETV6
Region631 – 978348Histone deacetylase

Sites

Active site7831 By similarity
Metal binding6461Zinc By similarity
Metal binding6481Zinc By similarity
Metal binding6541Zinc By similarity
Metal binding7311Zinc By similarity

Amino acid modifications

Modified residue221Phosphoserine Ref.15
Modified residue2201Phosphoserine By similarity
Modified residue2401Phosphoserine By similarity
Modified residue4511Phosphoserine By similarity

Natural variations

Alternative sequence1 – 3131Missing in isoform 10 and isoform 11.
VSP_046827
Alternative sequence11M → MMSSPAQPDLMWNLVPWVLF CGCCRIFPDGVAGREQLLAQ QRM in isoform 8.
VSP_043428
Alternative sequence881K → KLQQ in isoform 6, isoform 7 and isoform 10.
VSP_023766
Alternative sequence177 – 1782Missing in isoform 11.
VSP_046828
Alternative sequence218 – 26144Missing in isoform 6, isoform 8, isoform 9 and isoform 11.
VSP_023767
Alternative sequence487 – 57488Missing in isoform 2.
VSP_002082
Alternative sequence575 – 59016PFLEP…SVRQA → VIGKDLAPGFVIKVII in isoform 3, isoform 8, isoform 9, isoform 10 and isoform 11.
VSP_002083
Alternative sequence591 – 1011421Missing in isoform 3, isoform 8, isoform 9, isoform 10 and isoform 11.
VSP_002084
Alternative sequence861 – 87919GTGLG…TGGLD → RFISLEPHFYLYLSGNCIA in isoform 4.
VSP_002085
Alternative sequence880 – 1011132Missing in isoform 4.
VSP_002086
Alternative sequence1006 – 10116MSLKFS → KYWKSVRMVAVPRGCALAGA QLQEETETVSALASLTVDVE QPFAQEDSRTAGEPMEEEPA L in isoform 5, isoform 6 and isoform 7.
VSP_023768
Natural variant9211P → T Found in a renal cell carcinoma sample; somatic mutation. Ref.17
VAR_064719

Experimental info

Sequence conflict161V → A in BAH12570. Ref.5
Sequence conflict991L → I in AAF04254. Ref.9
Sequence conflict1531S → I in BAH14164. Ref.5
Sequence conflict3151S → F in BAH14176. Ref.5
Sequence conflict3321L → M in BAH14164. Ref.5
Sequence conflict4161V → F in BAH14164. Ref.5
Sequence conflict4371T → P in AAF04254. Ref.9
Sequence conflict644 – 6474HQCV → KPNS in AAF04254. Ref.9
Sequence conflict7461H → R in AAO27363. Ref.3

Sequences

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

Last modified October 18, 2001. Version 2.
Checksum: 43ED2785E73CD924

FASTA1,011111,297
        10         20         30         40         50         60 
MHSMISSVDV KSEVPVGLEP ISPLDLRTDL RMMMPVVDPV VREKQLQQEL LLIQQQQQIQ 

        70         80         90        100        110        120 
KQLLIAEFQK QHENLTRQHQ AQLQEHIKEL LAIKQQQELL EKEQKLEQQR QEQEVERHRR 

       130        140        150        160        170        180 
EQQLPPLRGK DRGRERAVAS TEVKQKLQEF LLSKSATKDT PTNGKNHSVS RHPKLWYTAA 

       190        200        210        220        230        240 
HHTSLDQSSP PLSGTSPSYK YTLPGAQDAK DDFPLRKTAS EPNLKVRSRL KQKVAERRSS 

       250        260        270        280        290        300 
PLLRRKDGNV VTSFKKRMFE VTESSVSSSS PGSGPSSPNN GPTGSVTENE TSVLPPTPHA 

       310        320        330        340        350        360 
EQMVSQQRIL IHEDSMNLLS LYTSPSLPNI TLGLPAVPSQ LNASNSLKEK QKCETQTLRQ 

       370        380        390        400        410        420 
GVPLPGQYGG SIPASSSHPH VTLEGKPPNS SHQALLQHLL LKEQMRQQKL LVAGGVPLHP 

       430        440        450        460        470        480 
QSPLATKERI SPGIRGTHKL PRHRPLNRTQ SAPLPQSTLA QLVIQQQHQQ FLEKQKQYQQ 

       490        500        510        520        530        540 
QIHMNKLLSK SIEQLKQPGS HLEEAEEELQ GDQAMQEDRA PSSGNSTRSD SSACVDDTLG 

       550        560        570        580        590        600 
QVGAVKVKEE PVDSDEDAQI QEMESGEQAA FMQQPFLEPT HTRALSVRQA PLAAVGMDGL 

       610        620        630        640        650        660 
EKHRLVSRTH SSPAASVLPH PAMDRPLQPG SATGIAYDPL MLKHQCVCGN STTHPEHAGR 

       670        680        690        700        710        720 
IQSIWSRLQE TGLLNKCERI QGRKASLEEI QLVHSEHHSL LYGTNPLDGQ KLDPRILLGD 

       730        740        750        760        770        780 
DSQKFFSSLP CGGLGVDSDT IWNELHSSGA ARMAVGCVIE LASKVASGEL KNGFAVVRPP 

       790        800        810        820        830        840 
GHHAEESTAM GFCFFNSVAI TAKYLRDQLN ISKILIVDLD VHHGNGTQQA FYADPSILYI 

       850        860        870        880        890        900 
SLHRYDEGNF FPGSGAPNEV GTGLGEGYNI NIAWTGGLDP PMGDVEYLEA FRTIVKPVAK 

       910        920        930        940        950        960 
EFDPDMVLVS AGFDALEGHT PPLGGYKVTA KCFGHLTKQL MTLADGRVVL ALEGGHDLTA 

       970        980        990       1000       1010 
ICDASEACVN ALLGNELEPL AEDILHQSPN MNAVISLQKI IEIQSMSLKF S 

« Hide

Isoform 2 [UniParc].

Checksum: 095F634F623A684F
Show »

FASTA923101,805
Isoform 3 (HDRP) (MITR) [UniParc].

Checksum: 02931057CF0E4C25
Show »

FASTA59065,887
Isoform 4 (HDAC9a) [UniParc].

Checksum: D3BFC3CE99E817DB
Show »

FASTA87997,471
Isoform 5 (HDAC9b) (HDAC9fl) [UniParc].

Checksum: EE7D908DF45D20CB
Show »

FASTA1,066117,208
Isoform 6 [UniParc].

Checksum: 3BEFD662BF24E677
Show »

FASTA1,025112,451
Isoform 7 [UniParc].

Checksum: 5DFBB8DD4C6547C5
Show »

FASTA1,069117,577
Isoform 8 [UniParc].

Checksum: E58854328ED1B5BE
Show »

FASTA58865,508
Isoform 9 [UniParc].

Checksum: CFC8BA27CFD1AA31
Show »

FASTA54660,761
Isoform 10 [UniParc].

Checksum: 6557FECB5FFF1A5A
Show »

FASTA56262,852
Isoform 11 [UniParc].

Checksum: 3868A8C73426BCC2
Show »

FASTA51357,092

References

« Hide 'large scale' references
[1]"Cloning and characterization of a histone deacetylase, HDAC9."
Zhou X., Marks P.A., Rifkind R.A., Richon V.M.
Proc. Natl. Acad. Sci. U.S.A. 98:10572-10577(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), TISSUE SPECIFICITY, INTERACTION WITH MEF2, FUNCTION, ENZYME REGULATION.
Tissue: Brain.
[2]"Molecular characterization of a familial translocation implicates disruption of HDAC9 and possible position effect on TGFbeta2 in the pathogenesis of Peters' anomaly."
David D., Cardoso J., Marques B., Marques R., Silva E.D., Santos H., Boavida M.G.
Genomics 81:489-503(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION WITH TGFB2.
Tissue: Lens.
[3]"The histone deacetylase 9 gene encodes multiple protein isoforms."
Petrie K., Guidez F., Howell L., Healy L., Waxman S., Greaves M., Zelent A.
J. Biol. Chem. 278:16059-16072(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORMS 3; 6 AND 7), INTERACTION WITH ETV6; NCOR1 AND BCL6, FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION.
Tissue: Brain.
[4]"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[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 8; 9; 10 AND 11).
Tissue: Brain and Trachea.
[6]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1011 (ISOFORM 6).
[9]"HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor."
Wang A.H., Bertos N.R., Vezmar M., Pelletier N., Crosato M., Heng H.H., Th'ng J., Han J., Yang X.-J.
Mol. Cell. Biol. 19:7816-7827(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 99-650 (ISOFORM 2).
Tissue: Brain.
[10]"MEF-2 function is modified by a novel co-repressor, MITR."
Sparrow D.B., Miska E.A., Langley E., Reynaud-Deonauth S., Kotecha S., Towers N., Spohr G., Kouzarides T., Mohun T.J.
EMBO J. 18:5085-5098(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION (ISOFORM 3), INTERACTION WITH HDAC1, FUNCTION.
[11]"Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5."
Zhou X., Richon V.M., Rifkind R.A., Marks P.A.
Proc. Natl. Acad. Sci. U.S.A. 97:1056-1061(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION (ISOFORM 3), TISSUE SPECIFICITY, INTERACTION WITH HDAC1 AND HDAC3, FUNCTION.
[12]"HDAC4 deacetylase associates with and represses the MEF2 transcription factor."
Miska E.A., Karlsson C., Langley E., Nielsen S.J., Pines J., Kouzarides T.
EMBO J. 18:5099-5107(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MEF2.
[13]"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase."
Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E., Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.
EMBO J. 21:2682-2691(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION.
[14]"Neuroprotection by histone deacetylase-related protein."
Morrison B.E., Majdzadeh N., Zhang X., Lyles A., Bassel-Duby R., Olson E.N., D'Mello S.R.
Mol. Cell. Biol. 26:3550-3564(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"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-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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.
[17]"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma."
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. expand/collapse author list , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-921.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY032737 mRNA. Translation: AAK66821.1.
AY032738 mRNA. Translation: AAK66822.1.
AJ459808 mRNA. Translation: CAD30851.1.
AY197371 mRNA. Translation: AAO27363.1.
AB018287 mRNA. Translation: BAA34464.2. Different initiation.
AK297404 mRNA. Translation: BAH12570.1.
AK304298 mRNA. Translation: BAH14153.1.
AK304343 mRNA. Translation: BAH14164.1.
AK304410 mRNA. Translation: BAH14176.1.
AC002088 Genomic DNA. No translation available.
AC002124 Genomic DNA. No translation available.
AC002410 Genomic DNA. No translation available.
AC002433 Genomic DNA. No translation available.
AC004744 Genomic DNA. No translation available.
AC004994 Genomic DNA. No translation available.
AC005249 Genomic DNA. No translation available.
AC010082 Genomic DNA. No translation available.
AC074193 Genomic DNA. No translation available.
AC091697 Genomic DNA. No translation available.
CH471073 Genomic DNA. Translation: EAW93702.1.
CH471073 Genomic DNA. Translation: EAW93703.1.
BC111735 mRNA. Translation: AAI11736.1. Frameshift.
BC150328 mRNA. Translation: AAI50329.1.
BC152405 mRNA. Translation: AAI52406.1.
AF124924 mRNA. Translation: AAF04254.1.
RefSeqNP_001191073.1. NM_001204144.1.
NP_001191074.1. NM_001204145.1.
NP_001191075.1. NM_001204146.1.
NP_001191076.1. NM_001204147.1.
NP_001191077.1. NM_001204148.1.
NP_055522.1. NM_014707.1.
NP_478056.1. NM_058176.2.
NP_848510.1. NM_178423.1.
NP_848512.1. NM_178425.2.
UniGeneHs.196054.

3D structure databases

ProteinModelPortalQ9UKV0.
SMRQ9UKV0. Positions 37-101, 629-1005.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115083. 99 interactions.
IntActQ9UKV0. 28 interactions.
MINTMINT-205121.
STRING9606.ENSP00000408617.

Chemistry

BindingDBQ9UKV0.
ChEMBLCHEMBL4145.
DrugBankDB00313. Valproic Acid.
GuidetoPHARMACOLOGY2620.

PTM databases

PhosphoSiteQ9UKV0.

Polymorphism databases

DMDM19865267.

Proteomic databases

PaxDbQ9UKV0.
PRIDEQ9UKV0.

Protocols and materials databases

DNASU9734.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000401921; ENSP00000383912; ENSG00000048052. [Q9UKV0-6]
ENST00000405010; ENSP00000384382; ENSG00000048052. [Q9UKV0-3]
ENST00000406451; ENSP00000384657; ENSG00000048052. [Q9UKV0-5]
ENST00000417496; ENSP00000401669; ENSG00000048052. [Q9UKV0-8]
ENST00000428307; ENSP00000395655; ENSG00000048052. [Q9UKV0-9]
ENST00000432645; ENSP00000410337; ENSG00000048052. [Q9UKV0-1]
ENST00000441542; ENSP00000408617; ENSG00000048052. [Q9UKV0-7]
ENST00000456174; ENSP00000388568; ENSG00000048052. [Q9UKV0-10]
ENST00000524023; ENSP00000430036; ENSG00000048052. [Q9UKV0-11]
GeneID9734.
KEGGhsa:9734.
UCSCuc003sua.1. human. [Q9UKV0-6]
uc003sud.2. human. [Q9UKV0-3]
uc003sue.3. human. [Q9UKV0-5]
uc003suf.2. human. [Q9UKV0-7]
uc003suh.3. human. [Q9UKV0-1]
uc011jya.2. human. [Q9UKV0-8]
uc011jyd.2. human. [Q9UKV0-4]

Organism-specific databases

CTD9734.
GeneCardsGC07P018179.
HGNCHGNC:14065. HDAC9.
HPAHPA028926.
MIM606543. gene.
neXtProtNX_Q9UKV0.
Orphanet708. Peters anomaly.
PharmGKBPA38377.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000232065.
HOVERGENHBG057100.
InParanoidQ9UKV0.
KOK11409.
OMAVEYLEAF.
OrthoDBEOG7RFTH5.
PhylomeDBQ9UKV0.
TreeFamTF106174.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressQ9UKV0.
BgeeQ9UKV0.
CleanExHS_HDAC7.
HS_HDAC9.
GenevestigatorQ9UKV0.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR024643. Hist_deacetylase_Gln_rich_N.
IPR017320. Histone_deAcase_II_euk.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF12203. HDAC4_Gln. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037911. HDAC_II_euk. 1 hit.
PRINTSPR01270. HDASUPER.
ProtoNetSearch...

Other

GeneWikiHDAC9.
GenomeRNAi9734.
NextBio36620.
PROQ9UKV0.
SOURCESearch...

Entry information

Entry nameHDAC9_HUMAN
AccessionPrimary (citable) accession number: Q9UKV0
Secondary accession number(s): A7E2F3 expand/collapse secondary AC list , B7Z4I4, B7Z917, B7Z928, B7Z940, C9JS87, E7EX34, F8W9E0, O94845, O95028, Q2M2R6, Q86SL1, Q86US3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 18, 2001
Last modified: April 16, 2014
This is version 143 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

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 7

Human chromosome 7: entries, gene names and cross-references to MIM