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.

Q13547

- HDAC1_HUMAN

UniProt

Q13547 - HDAC1_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 1
Gene
HDAC1, RPD3L1
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. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation.7 Publications

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 sitei141 – 1411

GO - Molecular functioni

  1. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  2. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
  3. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
  4. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
  5. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  6. RNA polymerase II transcription corepressor activity Source: BHF-UCL
  7. activating transcription factor binding Source: UniProtKB
  8. core promoter binding Source: UniProtKB
  9. deacetylase activity Source: UniProtKB
  10. enzyme binding Source: UniProtKB
  11. histone deacetylase activity Source: UniProtKB
  12. histone deacetylase binding Source: BHF-UCL
  13. protein binding Source: UniProtKB
  14. protein deacetylase activity Source: UniProtKB
  15. sequence-specific DNA binding transcription factor activity Source: ProtInc
  16. transcription factor binding Source: UniProtKB
  17. transcription regulatory region sequence-specific DNA binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. ATP-dependent chromatin remodeling Source: UniProt
  2. Notch signaling pathway Source: Reactome
  3. blood coagulation Source: Reactome
  4. chromatin modification Source: UniProtKB
  5. chromatin remodeling Source: BHF-UCL
  6. circadian regulation of gene expression Source: UniProtKB
  7. embryonic digit morphogenesis Source: BHF-UCL
  8. epidermal cell differentiation Source: BHF-UCL
  9. eyelid development in camera-type eye Source: BHF-UCL
  10. fungiform papilla formation Source: BHF-UCL
  11. gene expression Source: Reactome
  12. hair follicle placode formation Source: BHF-UCL
  13. histone H3 deacetylation Source: BHF-UCL
  14. histone H4 deacetylation Source: BHF-UCL
  15. histone deacetylation Source: UniProtKB
  16. mitotic cell cycle Source: Reactome
  17. negative regulation by host of viral transcription Source: UniProtKB
  18. negative regulation of androgen receptor signaling pathway Source: BHF-UCL
  19. negative regulation of apoptotic process Source: BHF-UCL
  20. negative regulation of cell cycle Source: Reactome
  21. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  22. negative regulation of transcription, DNA-templated Source: UniProtKB
  23. neurotrophin TRK receptor signaling pathway Source: Reactome
  24. odontogenesis of dentin-containing tooth Source: BHF-UCL
  25. positive regulation of cell proliferation Source: BHF-UCL
  26. positive regulation of receptor biosynthetic process Source: BHF-UCL
  27. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  28. positive regulation of transcription, DNA-templated Source: BHF-UCL
  29. protein deacetylation Source: UniProtKB
  30. transcription initiation from RNA polymerase II promoter Source: Reactome
  31. transcription, DNA-templated Source: Reactome
  32. transforming growth factor beta receptor signaling pathway Source: Reactome
  33. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Biological rhythms, Host-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_111214. G0 and Early G1.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_13695. p75NTR negatively regulates cell cycle via SC1.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_200731. deactivation of the beta-catenin transactivating complex.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_953. RNA Polymerase I Transcription Initiation.
SABIO-RKQ13547.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 1 (EC:3.5.1.98)
Short name:
HD1
Gene namesi
Name:HDAC1
Synonyms:RPD3L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:4852. HDAC1.

Subcellular locationi

GO - Cellular componenti

  1. NuRD complex Source: UniProtKB
  2. Sin3 complex Source: BHF-UCL
  3. cytoplasm Source: UniProtKB
  4. cytosol Source: UniProtKB
  5. histone deacetylase complex Source: UniProtKB
  6. nuclear chromatin Source: BHF-UCL
  7. nucleoplasm Source: BHF-UCL
  8. nucleus Source: UniProtKB
  9. protein complex Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi141 – 1411H → A: Abolishes histone deacetylase activity. 1 Publication
Mutagenesisi287 – 2871F → Y: Abolishes interaction with CHFR; when associated with I-297. 1 Publication
Mutagenesisi297 – 2971M → I: Abolishes interaction with CHFR; when associated with Y-287. 1 Publication
Mutagenesisi391 – 48292Missing: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes.
Add
BLAST
Mutagenesisi421 – 4211S → A: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes. 1 Publication
Mutagenesisi421 – 4211S → D or E: Slightly decreases deacetylase activity. 1 Publication
Mutagenesisi423 – 4231S → A: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes. 1 Publication
Mutagenesisi423 – 4231S → D or E: Decreases deacetylase activity. 1 Publication
Mutagenesisi424 – 4241E → A: Slightly decreases deacetylase activity, no effect on interaction with NuRD and SIN3 complexes.
Mutagenesisi425 – 4251E → A: No effect on deacetylase activity, no effect on interaction with NuRD and SIN3 complexes.
Mutagenesisi426 – 4261E → A: Decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes.

Organism-specific databases

PharmGKBiPA29226.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482Histone deacetylase 1
PRO_0000114687Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741N6-acetyllysine1 Publication
Modified residuei220 – 2201N6-acetyllysine1 Publication
Modified residuei393 – 3931Phosphoserine6 Publications
Modified residuei421 – 4211Phosphoserine; by CK26 Publications
Modified residuei423 – 4231Phosphoserine; by CK26 Publications
Modified residuei432 – 4321N6-methylated lysine; by EHMT21 Publication
Cross-linki444 – 444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki476 – 476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Post-translational modificationi

Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1.3 Publications
Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5.1 Publication
Ubiquitinated by CHFR, leading to its degradation by the proteasome By similarity. Ubiquitinated by KCTD11, leading to proteasomal degradation.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ13547.
PaxDbiQ13547.
PeptideAtlasiQ13547.
PRIDEiQ13547.

PTM databases

PhosphoSiteiQ13547.

Expressioni

Tissue specificityi

Ubiquitous, with higher levels in heart, pancreas and testis, and lower levels in kidney and brain.

Gene expression databases

ArrayExpressiQ13547.
BgeeiQ13547.
CleanExiHS_HDAC1.
GenevestigatoriQ13547.

Organism-specific databases

HPAiCAB005017.
HPA029693.

Interactioni

Subunit structurei

Part of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylation (NuRD) complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex. Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Found in a trimeric complex with APBB1 and TSHZ3; the interaction between HDAC1 and APBB1 is mediated by TSHZ3. Component of a RCOR/GFI/KDM1A/HDAC complex. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A. Associates with the 9-1-1 complex; interacts with HUS1. Found in a complex with DNMT3A and HDAC7. Interacts with the non-histone region of H2AFY. Interacts with TRIM28; the interaction recruits HDAC1 to E2F1 and inhibits its acetylation. Interacts with SP1; the interaction deacetylates SP1 and regulates its transcriptional activity. Interacts with SP3; the interaction deacetylates SP3 and regulates its transcriptional activity. In vitro, C(18) ceramides increase this interaction and the subsequent SP3 deacetylation and SP3-mediated repression of the TERT promoter. Interacts with TSHZ3 (via N-terminus); the interaction is direct. Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Interacts with C10orf90/FATS (via its N-terminal); the interaction prevents binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization of CDKN1A/p21. Interacts with CDKN1A/p21. Interacts with CDK5 complexed to CDK5R1 (p25). Interacts directly with GFI1 and GFI1B. Interacts with NR1D2 (via C-terminus). Interacts with TSC22D3 isoform 1; this interaction affects HDAC1 activity on MYOG promoter and thus inhibits MYOD1 transcriptional activity. Interacts with BAZ2A/TIP5, BANP, BCL6, BCOR, BHLHE40/DEC1, BRMS1, BRMS1L, CBFA2T3, CHFR, CIART, CRY1, DAXX, DDIT3/CHOP, DDX5, DNMT1, E4F1, EP300, HCFC1, HDAC9, INSM1, NFE4, NR4A2/NURR1, MIER1, KDM4A, KDM5B, KLF1, MINT, NRIP1, PCAF, PHB2, PRDM6, PRDM16, RB1, RERE, SAMSN1, SAP30L, SETDB1, SMAD3, SMARCA4/BRG1, SMYD2, SUV39H1, TGIF, TGIF2, TRAF6, UHRF1, UHRF2, ZMYND15, ZNF431 and ZNF541.

Binary interactionsi

WithEntry#Exp.IntActNotes
ARID5BQ148654EBI-301834,EBI-1210388
BCL11BQ9C0K03EBI-301834,EBI-6597578
BRMS1Q9HCU94EBI-301834,EBI-714781
C16orf87Q6PH813EBI-301834,EBI-6598617
CHD4Q148396EBI-301834,EBI-372916
CSNK2A1P684002EBI-301834,EBI-347804
DAXXQ9UER72EBI-301834,EBI-77321
DDX17Q92841-43EBI-301834,EBI-5280703
DDX5P178444EBI-301834,EBI-351962
DHX30Q7L2E33EBI-301834,EBI-1211456
DNMT3LQ9UJW33EBI-301834,EBI-740967
E4F1Q66K893EBI-301834,EBI-1227043
EHMT2Q96KQ73EBI-301834,EBI-744366
EID3Q8N1402EBI-301834,EBI-744483
FAM60AQ9NP504EBI-301834,EBI-741906
GFI1Q996844EBI-301834,EBI-949368
HCFC1P516102EBI-301834,EBI-396176
HDAC2Q927699EBI-301834,EBI-301821
HIST2H4BP628052EBI-301834,EBI-302023
MAGEA1P433552EBI-301834,EBI-740978
MBD1Q9UIS92EBI-301834,EBI-867196
MIER1Q8N1087EBI-301834,EBI-3504940
MTA1Q133304EBI-301834,EBI-714236
NCOR2Q9Y6182EBI-301834,EBI-80830
NFKB1P198384EBI-301834,EBI-300010
NPM1P067482EBI-301834,EBI-78579
NR2E3Q9Y5X42EBI-301834,EBI-7216962
PRDM5Q9NQX13EBI-301834,EBI-4292031
PWWP2AQ96N644EBI-301834,EBI-6597774
RB1P064004EBI-301834,EBI-491274
RBBP4Q090286EBI-301834,EBI-620823
RBBP7Q165765EBI-301834,EBI-352227
RELAQ042065EBI-301834,EBI-73886
SAP18O004222EBI-301834,EBI-1044156
SUV39H1O434633EBI-301834,EBI-349968
TP53P046376EBI-301834,EBI-366083

Protein-protein interaction databases

BioGridi109315. 541 interactions.
DIPiDIP-24184N.
IntActiQ13547. 166 interactions.
MINTiMINT-90475.
STRINGi9606.ENSP00000362649.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 144
Helixi19 – 213
Helixi33 – 4412
Helixi48 – 503
Beta strandi51 – 566
Helixi61 – 644
Turni65 – 673
Helixi70 – 789
Turni83 – 864
Helixi88 – 947
Turni97 – 993
Helixi106 – 12520
Beta strandi130 – 1367
Beta strandi151 – 1533
Helixi155 – 1639
Turni164 – 1663
Beta strandi170 – 1745
Beta strandi176 – 1783
Helixi181 – 1866
Turni187 – 1893
Beta strandi191 – 20010
Beta strandi205 – 2073
Helixi217 – 2193
Beta strandi223 – 2286
Helixi234 – 25219
Beta strandi255 – 2606
Helixi263 – 2653
Helixi278 – 28912
Beta strandi295 – 2984
Helixi305 – 31915
Helixi334 – 3363
Turni338 – 3403
Helixi356 – 37116

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TYImodel-A1-482[»]
4BKXX-ray3.00B1-482[»]
ProteinModelPortaliQ13547.
SMRiQ13547. Positions 8-376.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 321313Histone deacetylase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0123.
HOGENOMiHOG000225180.
HOVERGENiHBG057112.
InParanoidiQ13547.
KOiK06067.
OMAiLTQGTKR.
OrthoDBiEOG7DNNTW.
PhylomeDBiQ13547.
TreeFamiTF106171.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSiPR01270. HDASUPER.
PR01271. HISDACETLASE.

Sequencei

Sequence statusi: Complete.

Q13547-1 [UniParc]FASTAAdd to Basket

« Hide

MAQTQGTRRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK    50
MEIYRPHKAN AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC 100
PVFDGLFEFC QLSTGGSVAS AVKLNKQQTD IAVNWAGGLH HAKKSEASGF 150
CYVNDIVLAI LELLKYHQRV LYIDIDIHHG DGVEEAFYTT DRVMTVSFHK 200
YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI FKPVMSKVME 250
MFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG 300
GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM 350
TNQNTNEYLE KIKQRLFENL RMLPHAPGVQ MQAIPEDAIP EESGDEDEDD 400
PDKRISICSS DKRIACEEEF SDSEEEGEGG RKNSSNFKKA KRVKTEDEKE 450
KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK LA 482
Length:482
Mass (Da):55,103
Last modified:November 1, 1997 - v1
Checksum:i4D35B7C1ED7838D6
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti312 – 3121W → R in BAA08909. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U50079 mRNA. Translation: AAC50475.1.
D50405 mRNA. Translation: BAA08909.1.
BC000301 mRNA. Translation: AAH00301.1.
CCDSiCCDS360.1.
RefSeqiNP_004955.2. NM_004964.2.
UniGeneiHs.88556.

Genome annotation databases

EnsembliENST00000373548; ENSP00000362649; ENSG00000116478.
GeneIDi3065.
KEGGihsa:3065.
UCSCiuc001bvb.1. human.

Polymorphism databases

DMDMi2498443.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U50079 mRNA. Translation: AAC50475.1 .
D50405 mRNA. Translation: BAA08909.1 .
BC000301 mRNA. Translation: AAH00301.1 .
CCDSi CCDS360.1.
RefSeqi NP_004955.2. NM_004964.2.
UniGenei Hs.88556.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TYI model - A 1-482 [» ]
4BKX X-ray 3.00 B 1-482 [» ]
ProteinModelPortali Q13547.
SMRi Q13547. Positions 8-376.
ModBasei Search...

Protein-protein interaction databases

BioGridi 109315. 541 interactions.
DIPi DIP-24184N.
IntActi Q13547. 166 interactions.
MINTi MINT-90475.
STRINGi 9606.ENSP00000362649.

Chemistry

BindingDBi Q13547.
ChEMBLi CHEMBL2111429.
DrugBanki DB02546. Vorinostat.
GuidetoPHARMACOLOGYi 2658.

PTM databases

PhosphoSitei Q13547.

Polymorphism databases

DMDMi 2498443.

Proteomic databases

MaxQBi Q13547.
PaxDbi Q13547.
PeptideAtlasi Q13547.
PRIDEi Q13547.

Protocols and materials databases

DNASUi 3065.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373548 ; ENSP00000362649 ; ENSG00000116478 .
GeneIDi 3065.
KEGGi hsa:3065.
UCSCi uc001bvb.1. human.

Organism-specific databases

CTDi 3065.
GeneCardsi GC01P032757.
HGNCi HGNC:4852. HDAC1.
HPAi CAB005017.
HPA029693.
MIMi 601241. gene.
neXtProti NX_Q13547.
PharmGKBi PA29226.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0123.
HOGENOMi HOG000225180.
HOVERGENi HBG057112.
InParanoidi Q13547.
KOi K06067.
OMAi LTQGTKR.
OrthoDBi EOG7DNNTW.
PhylomeDBi Q13547.
TreeFami TF106171.

Enzyme and pathway databases

Reactomei REACT_111214. G0 and Early G1.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_13695. p75NTR negatively regulates cell cycle via SC1.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_200731. deactivation of the beta-catenin transactivating complex.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_953. RNA Polymerase I Transcription Initiation.
SABIO-RK Q13547.

Miscellaneous databases

ChiTaRSi HDAC1. human.
GeneWikii HDAC1.
GenomeRNAii 3065.
NextBioi 12125.
PROi Q13547.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13547.
Bgeei Q13547.
CleanExi HS_HDAC1.
Genevestigatori Q13547.

Family and domain databases

Gene3Di 3.40.800.20. 1 hit.
InterProi IPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view ]
PANTHERi PTHR10625. PTHR10625. 1 hit.
Pfami PF00850. Hist_deacetyl. 1 hit.
[Graphical view ]
PIRSFi PIRSF037913. His_deacetylse_1. 1 hit.
PRINTSi PR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p."
    Taunton J., Hassig C.A., Schreiber S.L.
    Science 272:408-411(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: T-cell.
  2. "Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3, a transcription factor in Saccharomyces cerevisiae."
    Furukawa Y., Kawakami T., Sudo K., Inazawa J., Matsumine A., Akiyama T., Nakamura Y.
    Cytogenet. Cell Genet. 73:130-133(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal lung.
  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].
    Tissue: Lung.
  4. Cited for: INTERACTION WITH HDAC9.
  5. "BCoR, a novel corepressor involved in BCL-6 repression."
    Huynh K.D., Fischle W., Verdin E., Bardwell V.J.
    Genes Dev. 14:1810-1823(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCOR.
  6. "HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins."
    Cai R.L., Yan-Neale Y., Cueto M.A., Xu H., Cohen D.
    J. Biol. Chem. 275:27909-27916(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE 9-1-1 COMPLEX AND HUS1.
  7. "Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing."
    Wei L.-N., Hu X., Chandra D., Seto E., Farooqui M.
    J. Biol. Chem. 275:40782-40787(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NRIP1.
  8. "Sequestration and inhibition of Daxx-mediated transcriptional repression by PML."
    Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D.
    Mol. Cell. Biol. 20:1784-1796(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAXX.
  9. "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: INTERACTION WITH HDAC9.
  10. "Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation."
    Pflum M.K.H., Tong J.K., Lane W.S., Schreiber S.L.
    J. Biol. Chem. 276:47733-47741(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-421 AND SER-423, MUTAGENESIS OF SER-421 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "Sharp, an inducible cofactor that integrates nuclear receptor repression and activation."
    Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M.
    Genes Dev. 15:1140-1151(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MINT.
  12. "Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1."
    Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y., Howard B.H.
    J. Biol. Chem. 276:6817-6824(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MBD2 AND MBD3.
  13. "TGIF2 interacts with histone deacetylase 1 and represses transcription."
    Melhuish T.A., Gallo C.M., Wotton D.
    J. Biol. Chem. 276:32109-32114(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGIF2.
  14. "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain."
    Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N., Downing J.R., Meyers S., Hiebert S.W.
    Mol. Cell. Biol. 21:6470-6483(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBFA2T3.
  15. Cited for: SUMOYLATION.
  16. "SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities."
    David G., Neptune M.A., DePinho R.A.
    J. Biol. Chem. 277:23658-23663(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-444 AND LYS-476.
  17. "Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the parathyroid hormone gene."
    Bhakat K.K., Izumi T., Yang S.H., Hazra T.K., Mitra S.
    EMBO J. 22:6299-6309(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APEX1.
  18. "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1."
    Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.
    Genes Dev. 17:896-911(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCFC1.
  19. "A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes."
    Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.
    J. Biol. Chem. 278:7234-7239(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BHC COMPLEX WITH PHF21A; HDAC2; HMG20B; KDM1A; RCOR1; ZMYM2; ZNF217; ZMYM3; KIAA0182 AND GTF2I.
  20. Cited for: INTERACTION WITH SP3, FUNCTION.
  21. "Human MI-ER1 alpha and beta function as transcriptional repressors by recruitment of histone deacetylase 1 to their conserved ELM2 domain."
    Ding Z., Gillespie L.L., Paterno G.D.
    Mol. Cell. Biol. 23:250-258(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MIER1.
  22. "Identification and characterization of three new components of the mSin3A corepressor complex."
    Fleischer T.C., Yun U.J., Ayer D.E.
    Mol. Cell. Biol. 23:3456-3467(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2.
  23. "Modulation of p120E4F transcriptional activity by the Gam1 adenoviral early protein."
    Colombo R., Draetta G.F., Chiocca S.
    Oncogene 22:2541-2547(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH E4F1.
  24. "Identification of a novel BRMS1-homologue protein p40 as a component of the mSin3A/p33(ING1b)/HDAC1 deacetylase complex."
    Nikolaev A.Y., Papanikolaou N.A., Li M., Qin J., Gu W.
    Biochem. Biophys. Res. Commun. 323:1216-1222(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRMS1L.
  25. "MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation."
    Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R., Boss J.M., Wade P.A.
    Cell 119:75-86(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCL6, IDENTIFICATION IN THE NURD COMPLEX.
  26. "Site-specific acetylation of the fetal globin activator NF-E4 prevents its ubiquitination and regulates its interaction with the histone deacetylase, HDAC1."
    Zhao Q., Cumming H., Cerruti L., Cunningham J.M., Jane S.M.
    J. Biol. Chem. 279:41477-41486(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFE4.
  27. "SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1."
    Cheng J., Wang D., Wang Z., Yeh E.T.H.
    Mol. Cell. Biol. 24:6021-6028(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DESUMOYLATION BY SENP1.
  28. "ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain."
    Unoki M., Nishidate T., Nakamura Y.
    Oncogene 23:7601-7610(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UHRF1 AND UHRF2.
  29. "NuRD and SIN3 histone deacetylase complexes in development."
    Ahringer J.
    Trends Genet. 16:351-356(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON DEACETYLASE COMPLEXES.
  30. "Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein."
    Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.
    J. Biol. Chem. 280:28507-28518(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KDM4A.
  31. "Tumor suppressor SMAR1 mediates cyclin D1 repression by recruitment of the SIN3/histone deacetylase 1 complex."
    Rampalli S., Pavithra L., Bhatt A., Kundu T.K., Chattopadhyay S.
    Mol. Cell. Biol. 25:8415-8429(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BANP.
  32. "INSM1 functions as a transcriptional repressor of the neuroD/beta2 gene through the recruitment of cyclin D1 and histone deacetylases."
    Liu W.D., Wang H.W., Muguira M., Breslin M.B., Lan M.S.
    Biochem. J. 397:169-177(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INSM1.
  33. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  34. "Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription."
    Hung J.J., Wang Y.T., Chang W.C.
    Mol. Cell. Biol. 26:1770-1785(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SP1, FUNCTION.
  35. "Breast cancer metastasis suppressor 1 functions as a corepressor by enhancing histone deacetylase 1-mediated deacetylation of RelA/p65 and promoting apoptosis."
    Liu Y., Smith P.W., Jones D.R.
    Mol. Cell. Biol. 26:8683-8696(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BRMS1.
  36. "SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus."
    Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K., Peterson P., Maeki M., Kainulainen H., Lohi O.
    Nucleic Acids Res. 34:3288-3298(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SAP30L.
  37. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  38. "Mechanisms of ceramide-mediated repression of the human telomerase reverse transcriptase promoter via deacetylation of Sp3 by histone deacetylase 1."
    Wooten-Blanks L.G., Song P., Senkal C.E., Ogretmen B.
    FASEB J. 21:3386-3397(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SP3.
  39. "Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases."
    Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K., Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P., Taylor-Papadimitriou J.
    Int. J. Cancer 121:265-275(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KDM5B.
  40. "Regulation of E2F1 function by the nuclear corepressor KAP1."
    Wang C., Rauscher F.J. III, Cress W.D., Chen J.
    J. Biol. Chem. 282:29902-29909(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM28, FUNCTION.
  41. "Critical and functional regulation of CHOP (C/EBP homologous protein) through the N-terminal portion."
    Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.
    J. Biol. Chem. 282:35687-35694(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDIT3.
  42. "Involvement of chromatin and histone deacetylation in SV40 T antigen transcription regulation."
    Valls E., Blanco-Garcia N., Aquizu N., Piedra D., Estaras C., de la Cruz X., Martinez-Balbas M.A.
    Nucleic Acids Res. 35:1958-1968(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN.
  43. "SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1."
    Jacobs A.M., Nicol S.M., Hislop R.G., Jaffray E.G., Hay R.T., Fuller-Pace F.V.
    Oncogene 26:5866-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX5.
  44. "The orphan nuclear receptor Rev-erbbeta recruits Tip60 and HDAC1 to regulate apolipoprotein CIII promoter."
    Wang J., Liu N., Liu Z., Li Y., Song C., Yuan H., Li Y.Y., Zhao X., Lu H.
    Biochim. Biophys. Acta 1783:224-236(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NR1D2.
  45. "Nuclear tumor necrosis factor receptor-associated factor 6 in lymphoid cells negatively regulates c-Myb-mediated transactivation through small ubiquitin-related modifier-1 modification."
    Pham L.V., Zhou H.J., Lin-Lee Y.C., Tamayo A.T., Yoshimura L.C., Fu L., Darnay B.G., Ford R.J.
    J. Biol. Chem. 283:5081-5089(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF6.
  46. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  47. "CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation."
    Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.
    Mol. Cell 32:718-726(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH CDYL; MIER1; MIER2 AND HDAC2.
  48. Cited for: METHYLATION AT LYS-432.
  49. "A calcium-dependent switch in a CREST-BRG1 complex regulates activity-dependent gene expression."
    Qiu Z., Ghosh A.
    Neuron 60:775-787(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RB1 AND SMARCA4/BRG1.
  50. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  51. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  52. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  53. Cited for: INTERACTION WITH PRDM16 AND SMAD3.
  54. Cited for: FUNCTION, INTERACTION WITH TSHZ3, IDENTIFICATION IN A TRIMERIC COMPLEX WITH APBB1 AND TSHZ3.
  55. "Chfr is linked to tumour metastasis through the downregulation of HDAC1."
    Oh Y.M., Kwon Y.E., Kim J.M., Bae S.J., Lee B.K., Yoo S.J., Chung C.H., Deshaies R.J., Seol J.H.
    Nat. Cell Biol. 11:295-302(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH CHFR, MUTAGENESIS OF HIS-141; PHE-287 AND MET-297.
  56. "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-393; SER-421 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  57. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74 AND LYS-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  58. Cited for: UBIQUITINATION BY KCTD11.
  59. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  60. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  61. "Maintenance of silent chromatin through replication requires SWI/SNF-like chromatin remodeler SMARCAD1."
    Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., Mermoud J.E.
    Mol. Cell 42:285-296(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMARCAD1.
  62. "SUMOylation of DEC1 protein regulates its transcriptional activity and enhances its stability."
    Hong Y., Xing X., Li S., Bi H., Yang C., Zhao F., Liu Y., Ao X., Chang A.K., Wu H.
    PLoS ONE 6:E23046-E23046(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BHLHE40.
  63. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHDAC1_HUMAN
AccessioniPrimary (citable) accession number: Q13547
Secondary accession number(s): Q92534
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 175 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi