SubmitCancel

Skip Header

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

Q96DB2

- HDA11_HUMAN

UniProt

Q96DB2 - HDA11_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 11

Gene
HDAC11
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. Histone deacetylases act via the formation of large multiprotein complexes.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei143 – 1431 By similarity

GO - Molecular functioni

  1. histone deacetylase activity Source: UniProtKB
  2. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  3. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
  4. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
  5. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
  6. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. chromatin modification Source: UniProtKB
  2. histone deacetylation Source: UniProtKB
  3. oligodendrocyte development Source: Ensembl
  4. regulation of transcription, DNA-templated Source: UniProtKB-KW
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

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 11 (EC:3.5.1.98)
Short name:
HD11
Gene namesi
Name:HDAC11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:19086. HDAC11.

Subcellular locationi

Nucleus
Note: Predominantly nuclear.

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. histone deacetylase complex Source: UniProtKB
  3. nucleus Source: UniProtKB
  4. plasma membrane Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38793.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 347347Histone deacetylase 11PRO_0000114715Add
BLAST

Proteomic databases

PaxDbiQ96DB2.
PRIDEiQ96DB2.

PTM databases

PhosphoSiteiQ96DB2.

Expressioni

Tissue specificityi

Weakly expressed in most tissues. Strongly expressed in brain, heart, skeletal muscle, kidney and testis.

Gene expression databases

ArrayExpressiQ96DB2.
BgeeiQ96DB2.
CleanExiHS_HDAC11.
GenevestigatoriQ96DB2.

Interactioni

Subunit structurei

Interacts with HDAC6.1 Publication

Protein-protein interaction databases

BioGridi122970. 134 interactions.
IntActiQ96DB2. 129 interactions.
MINTiMINT-1411829.
STRINGi9606.ENSP00000295757.

Structurei

3D structure databases

ProteinModelPortaliQ96DB2.
SMRiQ96DB2. Positions 19-333.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 326313Histone deacetylaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0123.
HOGENOMiHOG000280018.
HOVERGENiHBG051893.
InParanoidiQ96DB2.
KOiK11418.
OMAiDIIVYNA.
PhylomeDBiQ96DB2.
TreeFamiTF106176.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PRINTSiPR01270. HDASUPER.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96DB2-1) [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

MLHTTQLYQH VPETRWPIVY SPRYNITFMG LEKLHPFDAG KWGKVINFLK    50
EEKLLSDSML VEAREASEED LLVVHTRRYL NELKWSFAVA TITEIPPVIF 100
LPNFLVQRKV LRPLRTQTGG TIMAGKLAVE RGWAINVGGG FHHCSSDRGG 150
GFCAYADITL AIKFLFERVE GISRATIIDL DAHQGNGHER DFMDDKRVYI 200
MDVYNRHIYP GDRFAKQAIR RKVELEWGTE DDEYLDKVER NIKKSLQEHL 250
PDVVVYNAGT DILEGDRLGG LSISPAGIVK RDELVFRMVR GRRVPILMVT 300
SGGYQKRTAR IIADSILNLF GLGLIGPESP SVSAQNSDTP LLPPAVP 347
Length:347
Mass (Da):39,183
Last modified:December 1, 2001 - v1
Checksum:i0D976CAF6EAC7A15
GO
Isoform 2 (identifier: Q96DB2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.
     85-107: Missing.

Note: No experimental confirmation available.

Show »
Length:296
Mass (Da):33,124
Checksum:i60C0E21BA00DF261
GO

Sequence cautioni

The sequence CAB70712.1 differs from that shown. Reason: Frameshift at positions 177, 198 and 200.
The sequence BAB15127.1 differs from that shown. Reason: Erroneous termination at position 107. Translated as Gln.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform 2. VSP_043082Add
BLAST
Alternative sequencei85 – 10723Missing in isoform 2. VSP_043083Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151R → P in BAB15272. 1 Publication
Sequence conflicti113 – 1131P → A in CAB70712. 1 Publication
Sequence conflicti212 – 2121D → Y in CAB70712. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK025426 mRNA. Translation: BAB15127.1. Sequence problems.
AK025890 mRNA. Translation: BAB15272.1.
AK293223 mRNA. Translation: BAG56762.1.
AC027124 Genomic DNA. No translation available.
BC009676 mRNA. Translation: AAH09676.1.
AL137362 mRNA. Translation: CAB70712.1. Frameshift.
CCDSiCCDS2615.1. [Q96DB2-1]
CCDS46760.1. [Q96DB2-2]
RefSeqiNP_001129513.1. NM_001136041.2. [Q96DB2-2]
NP_079103.2. NM_024827.3. [Q96DB2-1]
UniGeneiHs.744132.

Genome annotation databases

EnsembliENST00000295757; ENSP00000295757; ENSG00000163517. [Q96DB2-1]
ENST00000522202; ENSP00000429794; ENSG00000163517. [Q96DB2-2]
GeneIDi79885.
KEGGihsa:79885.
UCSCiuc003bxy.3. human. [Q96DB2-1]
uc011auy.2. human. [Q96DB2-2]

Polymorphism databases

DMDMi26394832.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK025426 mRNA. Translation: BAB15127.1 . Sequence problems.
AK025890 mRNA. Translation: BAB15272.1 .
AK293223 mRNA. Translation: BAG56762.1 .
AC027124 Genomic DNA. No translation available.
BC009676 mRNA. Translation: AAH09676.1 .
AL137362 mRNA. Translation: CAB70712.1 . Frameshift.
CCDSi CCDS2615.1. [Q96DB2-1 ]
CCDS46760.1. [Q96DB2-2 ]
RefSeqi NP_001129513.1. NM_001136041.2. [Q96DB2-2 ]
NP_079103.2. NM_024827.3. [Q96DB2-1 ]
UniGenei Hs.744132.

3D structure databases

ProteinModelPortali Q96DB2.
SMRi Q96DB2. Positions 19-333.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122970. 134 interactions.
IntActi Q96DB2. 129 interactions.
MINTi MINT-1411829.
STRINGi 9606.ENSP00000295757.

Chemistry

BindingDBi Q96DB2.
ChEMBLi CHEMBL2093865.
GuidetoPHARMACOLOGYi 2615.

PTM databases

PhosphoSitei Q96DB2.

Polymorphism databases

DMDMi 26394832.

Proteomic databases

PaxDbi Q96DB2.
PRIDEi Q96DB2.

Protocols and materials databases

DNASUi 79885.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295757 ; ENSP00000295757 ; ENSG00000163517 . [Q96DB2-1 ]
ENST00000522202 ; ENSP00000429794 ; ENSG00000163517 . [Q96DB2-2 ]
GeneIDi 79885.
KEGGi hsa:79885.
UCSCi uc003bxy.3. human. [Q96DB2-1 ]
uc011auy.2. human. [Q96DB2-2 ]

Organism-specific databases

CTDi 79885.
GeneCardsi GC03P013496.
HGNCi HGNC:19086. HDAC11.
MIMi 607226. gene.
neXtProti NX_Q96DB2.
PharmGKBi PA38793.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0123.
HOGENOMi HOG000280018.
HOVERGENi HBG051893.
InParanoidi Q96DB2.
KOi K11418.
OMAi DIIVYNA.
PhylomeDBi Q96DB2.
TreeFami TF106176.

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 HDAC11.
GenomeRNAii 79885.
NextBioi 69691.
PROi Q96DB2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96DB2.
Bgeei Q96DB2.
CleanExi HS_HDAC11.
Genevestigatori Q96DB2.

Family and domain databases

Gene3Di 3.40.800.20. 1 hit.
InterProi IPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
[Graphical view ]
PANTHERi PTHR10625. PTHR10625. 1 hit.
Pfami PF00850. Hist_deacetyl. 1 hit.
[Graphical view ]
PRINTSi PR01270. HDASUPER.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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 1 AND 2).
    Tissue: Colon mucosa.
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 1).
    Tissue: Uterus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 113-347 (ISOFORM 1).
    Tissue: Testis.
  5. "Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family."
    Gao L., Cueto M.A., Asselbergs F., Atadja P.
    J. Biol. Chem. 277:25748-25755(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, FUNCTION, INTERACTION WITH HDAC6.

Entry informationi

Entry nameiHDA11_HUMAN
AccessioniPrimary (citable) accession number: Q96DB2
Secondary accession number(s): B4DDK1
, Q9H6I7, Q9H6X3, Q9NTC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: December 1, 2001
Last modified: September 3, 2014
This is version 124 of the entry and version 1 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

Miscellaneous

Its activity is inhibited by trapoxin, a known histone deacetylase inhibitor.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi