Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9UKV0

- HDAC9_HUMAN

UniProt

Q9UKV0 - HDAC9_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histone deacetylase 9

Gene

HDAC9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.
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.

Catalytic activityi

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

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi646 – 6461ZincBy similarity
Metal bindingi648 – 6481ZincBy similarity
Metal bindingi654 – 6541ZincBy similarity
Metal bindingi731 – 7311ZincBy similarity
Active sitei783 – 7831By similarity

GO - Molecular functioni

  1. histone deacetylase activity Source: BHF-UCL
  2. histone deacetylase binding Source: BHF-UCL
  3. metal ion binding Source: UniProtKB-KW
  4. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  5. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
  6. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
  7. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
  8. protein deacetylase activity Source: BHF-UCL
  9. protein kinase C binding Source: UniProtKB
  10. repressing transcription factor binding Source: BHF-UCL
  11. transcription corepressor activity Source: BHF-UCL
  12. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. B cell activation Source: UniProtKB
  2. B cell differentiation Source: UniProtKB
  3. cellular response to insulin stimulus Source: BHF-UCL
  4. heart development Source: BHF-UCL
  5. histone deacetylation Source: BHF-UCL
  6. histone H3 deacetylation Source: BHF-UCL
  7. histone H4 deacetylation Source: BHF-UCL
  8. inflammatory response Source: UniProtKB
  9. negative regulation of transcription, DNA-templated Source: BHF-UCL
  10. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  11. Notch signaling pathway Source: Reactome
  12. peptidyl-lysine deacetylation Source: BHF-UCL
  13. positive regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
  14. regulation of skeletal muscle fiber development Source: UniProtKB
  15. regulation of striated muscle cell differentiation Source: UniProtKB
  16. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.1.98. 2681.
ReactomeiREACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 9 (EC:3.5.1.98)
Short name:
HD9
Alternative name(s):
Histone deacetylase 7B
Short name:
HD7
Short name:
HD7b
Histone deacetylase-related protein
MEF2-interacting transcription repressor MITR
Gene namesi
Name:HDAC9
Synonyms:HDAC7, HDAC7B, HDRP, KIAA0744, MITR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:14065. HDAC9.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. histone deacetylase complex Source: UniProtKB
  3. histone methyltransferase complex Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
  6. transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Organism-specific databases

Orphaneti708. Peters anomaly.
PharmGKBiPA38377.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10111011Histone deacetylase 9PRO_0000114710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221Phosphoserine1 Publication
Modified residuei220 – 2201PhosphoserineBy similarity
Modified residuei240 – 2401PhosphoserineBy similarity
Modified residuei451 – 4511PhosphoserineBy similarity

Post-translational modificationi

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.By similarity2 Publications
Sumoylated.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UKV0.
PaxDbiQ9UKV0.
PRIDEiQ9UKV0.

PTM databases

PhosphoSiteiQ9UKV0.

Expressioni

Tissue specificityi

Broadly expressed, with highest levels in brain, heart, muscle and testis. Isoform 3 is present in human bladder carcinoma cells (at protein level).4 Publications

Gene expression databases

BgeeiQ9UKV0.
CleanExiHS_HDAC7.
HS_HDAC9.
ExpressionAtlasiQ9UKV0. baseline and differential.
GenevestigatoriQ9UKV0.

Organism-specific databases

HPAiHPA028926.

Interactioni

Subunit structurei

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.By similarity5 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi115083. 99 interactions.
DIPiDIP-39904N.
IntActiQ9UKV0. 29 interactions.
MINTiMINT-205121.
STRINGi9606.ENSP00000408617.

Structurei

3D structure databases

ProteinModelPortaliQ9UKV0.
SMRiQ9UKV0. Positions 629-1005.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 275Interaction with CTBP1By similarity
Regioni136 – 15419Interaction with MEF2By similarityAdd
BLAST
Regioni175 – 343169Interaction with MAPK10By similarityAdd
BLAST
Regioni218 – 26144Interaction with ETV6Add
BLAST
Regioni631 – 978348Histone deacetylaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0123.
GeneTreeiENSGT00530000062809.
HOGENOMiHOG000232065.
HOVERGENiHBG057100.
InParanoidiQ9UKV0.
KOiK11409.
OMAiVEYLEAF.
OrthoDBiEOG7RFTH5.
PhylomeDBiQ9UKV0.
TreeFamiTF106174.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR024643. Hist_deacetylase_Gln_rich_N.
IPR017320. Histone_deAcase_II_euk.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF12203. HDAC4_Gln. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037911. HDAC_II_euk. 1 hit.
PRINTSiPR01270. HDASUPER.

Sequences (11)i

Sequence statusi: Complete.

This entry describes 11 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9UKV0-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MHSMISSVDV KSEVPVGLEP ISPLDLRTDL RMMMPVVDPV VREKQLQQEL
60 70 80 90 100
LLIQQQQQIQ KQLLIAEFQK QHENLTRQHQ AQLQEHIKEL LAIKQQQELL
110 120 130 140 150
EKEQKLEQQR QEQEVERHRR EQQLPPLRGK DRGRERAVAS TEVKQKLQEF
160 170 180 190 200
LLSKSATKDT PTNGKNHSVS RHPKLWYTAA HHTSLDQSSP PLSGTSPSYK
210 220 230 240 250
YTLPGAQDAK DDFPLRKTAS EPNLKVRSRL KQKVAERRSS PLLRRKDGNV
260 270 280 290 300
VTSFKKRMFE VTESSVSSSS PGSGPSSPNN GPTGSVTENE TSVLPPTPHA
310 320 330 340 350
EQMVSQQRIL IHEDSMNLLS LYTSPSLPNI TLGLPAVPSQ LNASNSLKEK
360 370 380 390 400
QKCETQTLRQ GVPLPGQYGG SIPASSSHPH VTLEGKPPNS SHQALLQHLL
410 420 430 440 450
LKEQMRQQKL LVAGGVPLHP QSPLATKERI SPGIRGTHKL PRHRPLNRTQ
460 470 480 490 500
SAPLPQSTLA QLVIQQQHQQ FLEKQKQYQQ QIHMNKLLSK SIEQLKQPGS
510 520 530 540 550
HLEEAEEELQ GDQAMQEDRA PSSGNSTRSD SSACVDDTLG QVGAVKVKEE
560 570 580 590 600
PVDSDEDAQI QEMESGEQAA FMQQPFLEPT HTRALSVRQA PLAAVGMDGL
610 620 630 640 650
EKHRLVSRTH SSPAASVLPH PAMDRPLQPG SATGIAYDPL MLKHQCVCGN
660 670 680 690 700
STTHPEHAGR IQSIWSRLQE TGLLNKCERI QGRKASLEEI QLVHSEHHSL
710 720 730 740 750
LYGTNPLDGQ KLDPRILLGD DSQKFFSSLP CGGLGVDSDT IWNELHSSGA
760 770 780 790 800
ARMAVGCVIE LASKVASGEL KNGFAVVRPP GHHAEESTAM GFCFFNSVAI
810 820 830 840 850
TAKYLRDQLN ISKILIVDLD VHHGNGTQQA FYADPSILYI SLHRYDEGNF
860 870 880 890 900
FPGSGAPNEV GTGLGEGYNI NIAWTGGLDP PMGDVEYLEA FRTIVKPVAK
910 920 930 940 950
EFDPDMVLVS AGFDALEGHT PPLGGYKVTA KCFGHLTKQL MTLADGRVVL
960 970 980 990 1000
ALEGGHDLTA ICDASEACVN ALLGNELEPL AEDILHQSPN MNAVISLQKI
1010
IEIQSMSLKF S
Length:1,011
Mass (Da):111,297
Last modified:October 18, 2001 - v2
Checksum:i43ED2785E73CD924
GO
Isoform 2 (identifier: Q9UKV0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     487-574: Missing.

Show »
Length:923
Mass (Da):101,805
Checksum:i095F634F623A684F
GO
Isoform 3 (identifier: Q9UKV0-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:590
Mass (Da):65,887
Checksum:i02931057CF0E4C25
GO
Isoform 4 (identifier: Q9UKV0-4) [UniParc]FASTAAdd to Basket

Also known as: HDAC9a

The sequence of this isoform differs from the canonical sequence as follows:
     861-879: GTGLGEGYNINIAWTGGLD → RFISLEPHFYLYLSGNCIA
     880-1011: Missing.

Show »
Length:879
Mass (Da):97,471
Checksum:iD3BFC3CE99E817DB
GO
Isoform 5 (identifier: Q9UKV0-5) [UniParc]FASTAAdd to Basket

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.Curated

Show »
Length:1,066
Mass (Da):117,208
Checksum:iEE7D908DF45D20CB
GO
Isoform 6 (identifier: Q9UKV0-6) [UniParc]FASTAAdd to Basket

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..Curated

Show »
Length:1,025
Mass (Da):112,451
Checksum:i3BEFD662BF24E677
GO
Isoform 7 (identifier: Q9UKV0-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     88-88: K → KLQQ
     1006-1011: MSLKFS → KYWKSVRMVAVPRGCALAGAQLQEETETVSALASLTVDVEQPFAQEDSRTAGEPMEEEPAL

Show »
Length:1,069
Mass (Da):117,577
Checksum:i5DFBB8DD4C6547C5
GO
Isoform 8 (identifier: Q9UKV0-8) [UniParc]FASTAAdd to Basket

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.

Show »
Length:588
Mass (Da):65,508
Checksum:iE58854328ED1B5BE
GO
Isoform 9 (identifier: Q9UKV0-9) [UniParc]FASTAAdd to Basket

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

Show »
Length:546
Mass (Da):60,761
Checksum:iCFC8BA27CFD1AA31
GO
Isoform 10 (identifier: Q9UKV0-10) [UniParc]FASTAAdd to Basket

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.

Show »
Length:562
Mass (Da):62,852
Checksum:i6557FECB5FFF1A5A
GO
Isoform 11 (identifier: Q9UKV0-11) [UniParc]FASTAAdd to Basket

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.

Show »
Length:513
Mass (Da):57,092
Checksum:i3868A8C73426BCC2
GO

Sequence cautioni

Isoform 6 : The sequence AAI11736.1 differs from that shown. Reason: Frameshift at position 1021.
The sequence BAA34464.2 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161V → A in BAH12570. (PubMed:14702039)Curated
Sequence conflicti99 – 991L → I in AAF04254. (PubMed:10523670)Curated
Sequence conflicti153 – 1531S → I in BAH14164. (PubMed:14702039)Curated
Sequence conflicti315 – 3151S → F in BAH14176. (PubMed:14702039)Curated
Sequence conflicti332 – 3321L → M in BAH14164. (PubMed:14702039)Curated
Sequence conflicti416 – 4161V → F in BAH14164. (PubMed:14702039)Curated
Sequence conflicti437 – 4371T → P in AAF04254. (PubMed:10523670)Curated
Sequence conflicti644 – 6474HQCV → KPNS in AAF04254. (PubMed:10523670)Curated
Sequence conflicti746 – 7461H → R in AAO27363. (PubMed:12590135)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti921 – 9211P → T Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
VAR_064719

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3131Missing in isoform 10 and isoform 11. 1 PublicationVSP_046827Add
BLAST
Alternative sequencei1 – 11M → MMSSPAQPDLMWNLVPWVLF CGCCRIFPDGVAGREQLLAQ QRM in isoform 8. 1 PublicationVSP_043428
Alternative sequencei88 – 881K → KLQQ in isoform 6, isoform 7 and isoform 10. 3 PublicationsVSP_023766
Alternative sequencei177 – 1782Missing in isoform 11. 1 PublicationVSP_046828
Alternative sequencei218 – 26144Missing in isoform 6, isoform 8, isoform 9 and isoform 11. 2 PublicationsVSP_023767Add
BLAST
Alternative sequencei487 – 57488Missing in isoform 2. 1 PublicationVSP_002082Add
BLAST
Alternative sequencei575 – 59016PFLEP…SVRQA → VIGKDLAPGFVIKVII in isoform 3, isoform 8, isoform 9, isoform 10 and isoform 11. 3 PublicationsVSP_002083Add
BLAST
Alternative sequencei591 – 1011421Missing in isoform 3, isoform 8, isoform 9, isoform 10 and isoform 11. 3 PublicationsVSP_002084Add
BLAST
Alternative sequencei861 – 87919GTGLG…TGGLD → RFISLEPHFYLYLSGNCIA in isoform 4. 1 PublicationVSP_002085Add
BLAST
Alternative sequencei880 – 1011132Missing in isoform 4. 1 PublicationVSP_002086Add
BLAST
Alternative sequencei1006 – 10116MSLKFS → KYWKSVRMVAVPRGCALAGA QLQEETETVSALASLTVDVE QPFAQEDSRTAGEPMEEEPA L in isoform 5, isoform 6 and isoform 7. 3 PublicationsVSP_023768

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS47553.1. [Q9UKV0-7]
CCDS47554.1. [Q9UKV0-5]
CCDS47555.1. [Q9UKV0-1]
CCDS47557.1. [Q9UKV0-3]
CCDS56465.1. [Q9UKV0-8]
CCDS56466.1. [Q9UKV0-9]
CCDS56467.1. [Q9UKV0-10]
CCDS56468.1. [Q9UKV0-11]
RefSeqiNP_001191073.1. NM_001204144.1. [Q9UKV0-8]
NP_001191074.1. NM_001204145.1. [Q9UKV0-9]
NP_001191075.1. NM_001204146.1.
NP_001191076.1. NM_001204147.1. [Q9UKV0-11]
NP_001191077.1. NM_001204148.1. [Q9UKV0-10]
NP_055522.1. NM_014707.1. [Q9UKV0-3]
NP_478056.1. NM_058176.2. [Q9UKV0-1]
NP_848510.1. NM_178423.1. [Q9UKV0-5]
NP_848512.1. NM_178425.2. [Q9UKV0-7]
UniGeneiHs.196054.

Genome annotation databases

EnsembliENST00000401921; 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]
GeneIDi9734.
KEGGihsa:9734.
UCSCiuc003sua.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]
uc011jye.2. human.

Polymorphism databases

DMDMi19865267.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS47553.1. [Q9UKV0-7 ]
CCDS47554.1. [Q9UKV0-5 ]
CCDS47555.1. [Q9UKV0-1 ]
CCDS47557.1. [Q9UKV0-3 ]
CCDS56465.1. [Q9UKV0-8 ]
CCDS56466.1. [Q9UKV0-9 ]
CCDS56467.1. [Q9UKV0-10 ]
CCDS56468.1. [Q9UKV0-11 ]
RefSeqi NP_001191073.1. NM_001204144.1. [Q9UKV0-8 ]
NP_001191074.1. NM_001204145.1. [Q9UKV0-9 ]
NP_001191075.1. NM_001204146.1.
NP_001191076.1. NM_001204147.1. [Q9UKV0-11 ]
NP_001191077.1. NM_001204148.1. [Q9UKV0-10 ]
NP_055522.1. NM_014707.1. [Q9UKV0-3 ]
NP_478056.1. NM_058176.2. [Q9UKV0-1 ]
NP_848510.1. NM_178423.1. [Q9UKV0-5 ]
NP_848512.1. NM_178425.2. [Q9UKV0-7 ]
UniGenei Hs.196054.

3D structure databases

ProteinModelPortali Q9UKV0.
SMRi Q9UKV0. Positions 629-1005.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115083. 99 interactions.
DIPi DIP-39904N.
IntActi Q9UKV0. 29 interactions.
MINTi MINT-205121.
STRINGi 9606.ENSP00000408617.

Chemistry

BindingDBi Q9UKV0.
ChEMBLi CHEMBL4145.
DrugBanki DB00313. Valproic Acid.
GuidetoPHARMACOLOGYi 2620.

PTM databases

PhosphoSitei Q9UKV0.

Polymorphism databases

DMDMi 19865267.

Proteomic databases

MaxQBi Q9UKV0.
PaxDbi Q9UKV0.
PRIDEi Q9UKV0.

Protocols and materials databases

DNASUi 9734.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000401921 ; 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 ]
GeneIDi 9734.
KEGGi hsa:9734.
UCSCi uc003sua.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 ]
uc011jye.2. human.

Organism-specific databases

CTDi 9734.
GeneCardsi GC07P018179.
HGNCi HGNC:14065. HDAC9.
HPAi HPA028926.
MIMi 606543. gene.
neXtProti NX_Q9UKV0.
Orphaneti 708. Peters anomaly.
PharmGKBi PA38377.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0123.
GeneTreei ENSGT00530000062809.
HOGENOMi HOG000232065.
HOVERGENi HBG057100.
InParanoidi Q9UKV0.
KOi K11409.
OMAi VEYLEAF.
OrthoDBi EOG7RFTH5.
PhylomeDBi Q9UKV0.
TreeFami TF106174.

Enzyme and pathway databases

BRENDAi 3.5.1.98. 2681.
Reactomei REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.

Miscellaneous databases

GeneWikii HDAC9.
GenomeRNAii 9734.
NextBioi 36620.
PROi Q9UKV0.
SOURCEi Search...

Gene expression databases

Bgeei Q9UKV0.
CleanExi HS_HDAC7.
HS_HDAC9.
ExpressionAtlasi Q9UKV0. baseline and differential.
Genevestigatori Q9UKV0.

Family and domain databases

Gene3Di 3.40.800.20. 1 hit.
InterProi IPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR024643. Hist_deacetylase_Gln_rich_N.
IPR017320. Histone_deAcase_II_euk.
[Graphical view ]
PANTHERi PTHR10625. PTHR10625. 1 hit.
Pfami PF12203. HDAC4_Gln. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view ]
PIRSFi PIRSF037911. HDAC_II_euk. 1 hit.
PRINTSi PR01270. HDASUPER.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. Cited for: SUMOYLATION.
  14. 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. Cited for: VARIANT THR-921.

Entry informationi

Entry nameiHDAC9_HUMAN
AccessioniPrimary (citable) accession number: Q9UKV0
Secondary accession number(s): A7E2F3
, B7Z4I4, B7Z917, B7Z928, B7Z940, C9JS87, E7EX34, F8W9E0, O94845, O95028, Q2M2R6, Q86SL1, Q86US3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 18, 2001
Last modified: October 29, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3