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Q9UKV0 (HDAC9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 118. 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
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)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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.9 Ref.10 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.9 Ref.10 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.9 Ref.10 Ref.11

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.10

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.13 Ref.15 Ref.16

Sumoylated. Ref.3 Ref.12

Involvement in disease

Note=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
   Molecular functionChromatin regulator
Hydrolase
Repressor
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processB cell differentiation

Traceable author statement. Source: UniProtKB

cellular response to insulin stimulus

Inferred from direct assay. 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

inflammatory response

Traceable author statement. 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-dependent

Inferred from direct assay Ref.10Ref.1. 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. Source: BHF-UCL

regulation of skeletal muscle fiber development

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from direct assay Ref.16. Source: UniProtKB

histone deacetylase complex

Traceable author statement. Source: UniProtKB

histone methyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor complex

Inferred from direct assay. Source: BHF-UCL

   Molecular functionNAD-dependent histone deacetylase activity (H3-K14 specific)

Inferred from electronic annotation. Source: EC

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

Inferred from electronic annotation. Source: EC

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

Inferred from electronic annotation. Source: EC

histone deacetylase activity (H3-K16 specific)

Inferred from electronic annotation. Source: EC

histone deacetylase binding

Inferred from physical interaction Ref.3. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.3. Source: IntAct

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

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BCL6P411822EBI-765444,EBI-765407
ETV6P412123EBI-765476,EBI-1372759
Ncor1Q609742EBI-765476,EBI-349004From a different organism.

Alternative products

This entry describes 7 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: Phosphorylated on Tyr-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: Phosphorylated on Tyr-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
Note: Phosphorylated on Tyr-1010.

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

Amino acid modifications

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

Natural variations

Alternative sequence881K → KLQQ in isoform 6 and isoform 7.
VSP_023766
Alternative sequence218 – 26144Missing in isoform 6.
VSP_023767
Alternative sequence487 – 57488Missing in isoform 2.
VSP_002082
Alternative sequence575 – 59016PFLEP…SVRQA → VIGKDLAPGFVIKVII in isoform 3.
VSP_002083
Alternative sequence591 – 1011421Missing in isoform 3.
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 conflict991L → I in AAF04254. Ref.8
Sequence conflict4371T → P in AAF04254. Ref.8
Sequence conflict644 – 6474HQCV → KPNS in AAF04254. Ref.8
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

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: 11535832] [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: 12706107] [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: 12590135] [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: 9872452] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[5]"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: 12853948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[7]"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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1011 (ISOFORM 6).
[8]"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: 10523670] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 99-650 (ISOFORM 2).
Tissue: Brain.
[9]"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: 10487760] [Abstract]
Cited for: IDENTIFICATION (ISOFORM 3), INTERACTION WITH HDAC1, FUNCTION.
[10]"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: 10655483] [Abstract]
Cited for: IDENTIFICATION (ISOFORM 3), TISSUE SPECIFICITY, INTERACTION WITH HDAC1 AND HDAC3, FUNCTION.
[11]"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: 10487761] [Abstract]
Cited for: INTERACTION WITH MEF2.
[12]"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: 12032081] [Abstract]
Cited for: SUMOYLATION.
[13]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1010 (ISOFORM 7), MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[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: 16611996] [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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, MASS SPECTROMETRY.
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: 20188095] [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: 21248752] [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.
AC004994 Genomic DNA. Translation: AAC78618.2.
CH471073 Genomic DNA. Translation: EAW93702.1.
BC111735 mRNA. Translation: AAI11736.1. Frameshift.
BC150328 mRNA. Translation: AAI50329.1.
BC152405 mRNA. Translation: AAI52406.1.
AF124924 mRNA. Translation: AAF04254.1.
IPIIPI00215728.
IPI00215729.
IPI00215730.
IPI00232519.
IPI00328781.
IPI00829837.
IPI00829883.
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...

Protein-protein interaction databases

IntActQ9UKV0. 24 interactions.
STRINGQ9UKV0.

PTM databases

PhosphoSiteQ9UKV0.

Polymorphism databases

DMDM19865267.

Proteomic databases

PRIDEQ9UKV0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000432645; ENSP00000410337; ENSG00000048052.
GeneID9734.
KEGGhsa:9734.
UCSCuc003sue.1. human.
uc003sug.1. human.
uc003suh.1. human.
uc003sui.1. human.
uc003suj.1. human.

Organism-specific databases

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

Phylogenomic databases

eggNOGprNOG19380.
HOVERGENHBG057100.
InParanoidQ9UKV0.
OMAAAFMQQP.
PhylomeDBQ9UKV0.

Enzyme and pathway databases

BRENDA3.5.1.98. 2681.
Pathway_Interaction_DBhdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.

Gene expression databases

ArrayExpressQ9UKV0.
BgeeQ9UKV0.
CleanExHS_HDAC7.
HS_HDAC9.
GenevestigatorQ9UKV0.
GermOnlineENSG00000048052. Homo sapiens.

Family and domain databases

InterProIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR024643. Hist_deacetylase_Gln_rich_N.
IPR017320. Histone_deAcase_II_euk.
[Graphical view]
Gene3DG3DSA:3.40.800.20. His_deacetylse. 1 hit.
KOK11409.
PANTHERPTHR10625. His_deacetylse. 1 hit.
PfamPF12203. HDAC4_Gln. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037911. HDAC_II_euk. 1 hit.
PRINTSPR01270. HDASUPER.
ProtoNetSearch...

Other

DrugBankDB00313. Valproic Acid.
NextBio36620.
SOURCESearch...

Entry information

Entry nameHDAC9_HUMAN
AccessionPrimary (citable) accession number: Q9UKV0
Secondary accession number(s): A7E2F3 expand/collapse secondary AC list , O94845, O95028, Q2M2R6, Q86SL1, Q86US3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 18, 2001
Last modified: December 14, 2011
This is version 118 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

Human chromosome 7

Human chromosome 7: 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

SIMILARITY comments

Index of protein domains and families

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