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Protein

Histone deacetylase complex subunit SAP30

Gene

SAP30

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

Functioni

Involved in the functional recruitment of the Sin3-histone deacetylase complex (HDAC) to a specific subset of N-CoR corepressor complexes. Capable of transcription repression by N-CoR. Active in deacetylating core histone octamers (when in a complex) but inactive in deacetylating nucleosomal histones.By similarity1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri67 – 115AtypicalAdd BLAST49

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000164105-MONOMER.
ReactomeiR-HSA-3214815. HDACs deacetylate histones.
R-HSA-427413. NoRC negatively regulates rRNA expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase complex subunit SAP30
Alternative name(s):
30 kDa Sin3-associated polypeptide
Sin3 corepressor complex subunit SAP30
Sin3-associated polypeptide p30
Gene namesi
Name:SAP30Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:10532. SAP30.

Subcellular locationi

GO - Cellular componenti

  • histone deacetylase complex Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi67C → A: Abolishes zinc-binding. 1 Publication1
Mutagenesisi68C → A: Retains zinc-binding. 1 Publication1
Mutagenesisi108H → A: Retains zinc-binding. 1 Publication1
Mutagenesisi112C → A: Abolishes zinc-binding. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000164105.
PharmGKBiPA34941.

Polymorphism and mutation databases

BioMutaiSAP30.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000975821 – 220Histone deacetylase complex subunit SAP30Add BLAST220

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5PhosphothreonineCombined sources1
Modified residuei131PhosphoserineCombined sources1
Modified residuei138PhosphoserineCombined sources1
Modified residuei145PhosphothreonineCombined sources1
Cross-linki214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO75446.
MaxQBiO75446.
PaxDbiO75446.
PeptideAtlasiO75446.
PRIDEiO75446.

PTM databases

iPTMnetiO75446.
PhosphoSitePlusiO75446.
UniCarbKBiO75446.

Expressioni

Tissue specificityi

Expressed in all tissues tested with highest levels in pancreas, ovary, PBL, spleen and thymus; lowest levels in brain, placenta, lung and kidney.1 Publication

Gene expression databases

BgeeiENSG00000164105.
CleanExiHS_SAP30.
GenevisibleiO75446. HS.

Organism-specific databases

HPAiCAB022627.
HPA059012.

Interactioni

Subunit structurei

Interacts with SIN3A, SIN3B, HDAC2 and NCOR1. Interacts with SAMS1 (By similarity). Component of the histone deacetylase complex that includes at least SIN3A, HDAC1 and HDAC2. Interacts with HDAC1 and HCFC1.By similarity2 Publications

Protein-protein interaction databases

BioGridi114346. 55 interactors.
IntActiO75446. 35 interactors.
MINTiMINT-133479.
STRINGi9606.ENSP00000296504.

Structurei

Secondary structure

1220
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi64 – 66Combined sources3
Beta strandi69 – 71Combined sources3
Helixi87 – 96Combined sources10
Beta strandi99 – 102Combined sources4
Helixi113 – 120Combined sources8
Beta strandi123 – 125Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KDPNMR-A64-131[»]
ProteinModelPortaliO75446.
SMRiO75446.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75446.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 129Interaction with NCOR1By similarityAdd BLAST129
Regioni130 – 220Interaction with SIN3ABy similarityAdd BLAST91

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi15 – 59Ala-richSequence analysisAdd BLAST45

Sequence similaritiesi

Belongs to the SAP30 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri67 – 115AtypicalAdd BLAST49

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IHMG. Eukaryota.
ENOG4111GVC. LUCA.
GeneTreeiENSGT00390000006633.
HOGENOMiHOG000007811.
HOVERGENiHBG057907.
InParanoidiO75446.
KOiK19202.
OMAiKIDSGVH.
OrthoDBiEOG091G0PSQ.
PhylomeDBiO75446.
TreeFamiTF324135.

Family and domain databases

InterProiIPR024145. His_deAcase_SAP30/SAP30L.
IPR025718. SAP30_Sin3-bd.
IPR025717. SAP30_zn-finger.
[Graphical view]
PANTHERiPTHR13286. PTHR13286. 1 hit.
PfamiPF13867. SAP30_Sin3_bdg. 1 hit.
PF13866. zf-SAP30. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75446-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGFTPDEMS RGGDAAAAVA AVVAAAAAAA SAGNGTGAGT GAEVPGAGAV
60 70 80 90 100
SAAGPPGAAG PGPGQLCCLR EDGERCGRAA GNASFSKRIQ KSISQKKVKI
110 120 130 140 150
ELDKSARHLY ICDYHKNLIQ SVRNRRKRKG SDDDGGDSPV QDIDTPEVDL
160 170 180 190 200
YQLQVNTLRR YKRHFKLPTR PGLNKAQLVE IVGCHFRSIP VNEKDTLTYF
210 220
IYSVKNDKNK SDLKVDSGVH
Length:220
Mass (Da):23,306
Last modified:November 1, 1998 - v1
Checksum:iFF84E06B17AFCAC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055993 mRNA. Translation: AAC33316.1.
CH471056 Genomic DNA. Translation: EAX04755.1.
CH471056 Genomic DNA. Translation: EAX04756.1.
BC016757 mRNA. Translation: AAH16757.1.
CCDSiCCDS3817.1.
RefSeqiNP_003855.1. NM_003864.3.
UniGeneiHs.591715.

Genome annotation databases

EnsembliENST00000296504; ENSP00000296504; ENSG00000164105.
GeneIDi8819.
KEGGihsa:8819.
UCSCiuc003itd.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055993 mRNA. Translation: AAC33316.1.
CH471056 Genomic DNA. Translation: EAX04755.1.
CH471056 Genomic DNA. Translation: EAX04756.1.
BC016757 mRNA. Translation: AAH16757.1.
CCDSiCCDS3817.1.
RefSeqiNP_003855.1. NM_003864.3.
UniGeneiHs.591715.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KDPNMR-A64-131[»]
ProteinModelPortaliO75446.
SMRiO75446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114346. 55 interactors.
IntActiO75446. 35 interactors.
MINTiMINT-133479.
STRINGi9606.ENSP00000296504.

PTM databases

iPTMnetiO75446.
PhosphoSitePlusiO75446.
UniCarbKBiO75446.

Polymorphism and mutation databases

BioMutaiSAP30.

Proteomic databases

EPDiO75446.
MaxQBiO75446.
PaxDbiO75446.
PeptideAtlasiO75446.
PRIDEiO75446.

Protocols and materials databases

DNASUi8819.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296504; ENSP00000296504; ENSG00000164105.
GeneIDi8819.
KEGGihsa:8819.
UCSCiuc003itd.4. human.

Organism-specific databases

CTDi8819.
GeneCardsiSAP30.
HGNCiHGNC:10532. SAP30.
HPAiCAB022627.
HPA059012.
MIMi603378. gene.
neXtProtiNX_O75446.
OpenTargetsiENSG00000164105.
PharmGKBiPA34941.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHMG. Eukaryota.
ENOG4111GVC. LUCA.
GeneTreeiENSGT00390000006633.
HOGENOMiHOG000007811.
HOVERGENiHBG057907.
InParanoidiO75446.
KOiK19202.
OMAiKIDSGVH.
OrthoDBiEOG091G0PSQ.
PhylomeDBiO75446.
TreeFamiTF324135.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000164105-MONOMER.
ReactomeiR-HSA-3214815. HDACs deacetylate histones.
R-HSA-427413. NoRC negatively regulates rRNA expression.

Miscellaneous databases

EvolutionaryTraceiO75446.
GeneWikiiSAP30.
GenomeRNAii8819.
PROiO75446.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000164105.
CleanExiHS_SAP30.
GenevisibleiO75446. HS.

Family and domain databases

InterProiIPR024145. His_deAcase_SAP30/SAP30L.
IPR025718. SAP30_Sin3-bd.
IPR025717. SAP30_zn-finger.
[Graphical view]
PANTHERiPTHR13286. PTHR13286. 1 hit.
PfamiPF13867. SAP30_Sin3_bdg. 1 hit.
PF13866. zf-SAP30. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSAP30_HUMAN
AccessioniPrimary (citable) accession number: O75446
Secondary accession number(s): D3DP38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: November 1, 1998
Last modified: November 30, 2016
This is version 133 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 4
    Human chromosome 4: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.