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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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri67 – 11549AtypicalAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • transcription corepressor activity Source: UniProtKB

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

ReactomeiREACT_263923. HDACs deacetylate histones.
REACT_263965. 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
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:10532. SAP30.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671C → A: Abolishes zinc-binding. 1 Publication
Mutagenesisi68 – 681C → A: Retains zinc-binding. 1 Publication
Mutagenesisi108 – 1081H → A: Retains zinc-binding. 1 Publication
Mutagenesisi112 – 1121C → A: Abolishes zinc-binding. 1 Publication

Organism-specific databases

PharmGKBiPA34941.

Polymorphism and mutation databases

BioMutaiSAP30.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 220220Histone deacetylase complex subunit SAP30PRO_0000097582Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311Phosphoserine5 Publications
Modified residuei138 – 1381Phosphoserine4 Publications
Modified residuei145 – 1451Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75446.
PaxDbiO75446.
PeptideAtlasiO75446.
PRIDEiO75446.

PTM databases

PhosphoSiteiO75446.

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

BgeeiO75446.
CleanExiHS_SAP30.
GenevisibleiO75446. HS.

Organism-specific databases

HPAiCAB022627.

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. 33 interactions.
IntActiO75446. 8 interactions.
MINTiMINT-133479.
STRINGi9606.ENSP00000296504.

Structurei

Secondary structure

1
220
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi64 – 663Combined sources
Beta strandi69 – 713Combined sources
Helixi87 – 9610Combined sources
Beta strandi99 – 1024Combined sources
Helixi113 – 1208Combined sources
Beta strandi123 – 1253Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KDPNMR-A64-131[»]
ProteinModelPortaliO75446.
SMRiO75446. Positions 64-220.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75446.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 129129Interaction with NCOR1By similarityAdd
BLAST
Regioni130 – 22091Interaction with SIN3ABy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi15 – 5945Ala-richSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the SAP30 family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri67 – 11549AtypicalAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG81414.
GeneTreeiENSGT00390000006633.
HOGENOMiHOG000007811.
HOVERGENiHBG057907.
InParanoidiO75446.
KOiK19202.
OMAiKIDSGVH.
OrthoDBiEOG7P5T35.
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.3. 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
EntryMethodResolution (Å)ChainPositionsPDBsum
2KDPNMR-A64-131[»]
ProteinModelPortaliO75446.
SMRiO75446. Positions 64-220.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114346. 33 interactions.
IntActiO75446. 8 interactions.
MINTiMINT-133479.
STRINGi9606.ENSP00000296504.

PTM databases

PhosphoSiteiO75446.

Polymorphism and mutation databases

BioMutaiSAP30.

Proteomic databases

MaxQBiO75446.
PaxDbiO75446.
PeptideAtlasiO75446.
PRIDEiO75446.

Protocols and materials databases

DNASUi8819.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296504; ENSP00000296504; ENSG00000164105.
GeneIDi8819.
KEGGihsa:8819.
UCSCiuc003itd.3. human.

Organism-specific databases

CTDi8819.
GeneCardsiGC04P174292.
HGNCiHGNC:10532. SAP30.
HPAiCAB022627.
MIMi603378. gene.
neXtProtiNX_O75446.
PharmGKBiPA34941.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG81414.
GeneTreeiENSGT00390000006633.
HOGENOMiHOG000007811.
HOVERGENiHBG057907.
InParanoidiO75446.
KOiK19202.
OMAiKIDSGVH.
OrthoDBiEOG7P5T35.
PhylomeDBiO75446.
TreeFamiTF324135.

Enzyme and pathway databases

ReactomeiREACT_263923. HDACs deacetylate histones.
REACT_263965. NoRC negatively regulates rRNA expression.

Miscellaneous databases

EvolutionaryTraceiO75446.
GeneWikiiSAP30.
GenomeRNAii8819.
NextBioi33082.
PROiO75446.
SOURCEiSearch...

Gene expression databases

BgeeiO75446.
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...

Publicationsi

« Hide 'large scale' publications
  1. "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex."
    Zhang Y., Sun Z.-W., Iratni R., Erdjument-Bromage H., Tempst P., Hampsey M., Reinberg D.
    Mol. Cell 1:1021-1031(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HDAC1.
    Tissue: Cervix carcinoma.
  2. "SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors."
    Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C., Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G., Ayer D.E., Eisenman R.N.
    Mol. Cell 2:33-42(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: BrainImported.
  5. "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.
  6. "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-131 AND SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-138 AND THR-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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-131 AND SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-131 AND SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "Solution structure of a novel zinc finger motif in the SAP30 polypeptide of the Sin3 corepressor complex and its potential role in nucleic acid recognition."
    He Y., Imhoff R., Sahu A., Radhakrishnan I.
    Nucleic Acids Res. 37:2142-2152(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 64-131, DNA-BINDING, ZINC-FINGER, MUTAGENESIS OF CYS-67; CYS-68; HIS-108 AND CYS-112.

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: July 22, 2015
This is version 119 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

External Data

Dasty 3

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 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.