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O75446 (SAP30_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase complex subunit SAP30
Alternative name(s):
30 kDa Sin3-associated polypeptide
Sin3 corepressor complex subunit SAP30
Sin3-associated polypeptide p30
Gene names
Name:SAP30
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 UniProtKB O88574

Subunit structure

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. Ref.1 Ref.5

Subcellular location

Nucleus Ref.2.

Tissue specificity

Expressed in all tissues tested with highest levels in pancreas, ovary, PBL, spleen and thymus; lowest levels in brain, placenta, lung and kidney. Ref.2

Sequence similarities

Belongs to the SAP30 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 220220Histone deacetylase complex subunit SAP30
PRO_0000097582

Regions

Zinc finger67 – 11549Atypical
Region1 – 129129Interaction with NCOR1 By similarity
Region130 – 22091Interaction with SIN3A By similarity
Compositional bias15 – 5945Ala-rich

Amino acid modifications

Modified residue1311Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Modified residue1381Phosphoserine Ref.6 Ref.7 Ref.8 Ref.10
Modified residue1451Phosphothreonine Ref.7

Experimental info

Mutagenesis671C → A: Abolishes zinc-binding. Ref.12
Mutagenesis681C → A: Retains zinc-binding. Ref.12
Mutagenesis1081H → A: Retains zinc-binding. Ref.12
Mutagenesis1121C → A: Abolishes zinc-binding. Ref.12

Secondary structure

............. 220
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75446 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: FF84E06B17AFCAC2

FASTA22023,306
        10         20         30         40         50         60 
MNGFTPDEMS RGGDAAAAVA AVVAAAAAAA SAGNGTGAGT GAEVPGAGAV SAAGPPGAAG 

        70         80         90        100        110        120 
PGPGQLCCLR EDGERCGRAA GNASFSKRIQ KSISQKKVKI ELDKSARHLY ICDYHKNLIQ 

       130        140        150        160        170        180 
SVRNRRKRKG SDDDGGDSPV QDIDTPEVDL YQLQVNTLRR YKRHFKLPTR PGLNKAQLVE 

       190        200        210        220 
IVGCHFRSIP VNEKDTLTYF IYSVKNDKNK SDLKVDSGVH 

« Hide

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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: Brain.
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF055993 mRNA. Translation: AAC33316.1.
CH471056 Genomic DNA. Translation: EAX04755.1.
CH471056 Genomic DNA. Translation: EAX04756.1.
BC016757 mRNA. Translation: AAH16757.1.
CCDSCCDS3817.1.
RefSeqNP_003855.1. NM_003864.3.
UniGeneHs.591715.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KDPNMR-A64-131[»]
ProteinModelPortalO75446.
SMRO75446. Positions 64-220.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114346. 33 interactions.
IntActO75446. 8 interactions.
MINTMINT-133479.
STRING9606.ENSP00000296504.

PTM databases

PhosphoSiteO75446.

Proteomic databases

MaxQBO75446.
PaxDbO75446.
PeptideAtlasO75446.
PRIDEO75446.

Protocols and materials databases

DNASU8819.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296504; ENSP00000296504; ENSG00000164105.
GeneID8819.
KEGGhsa:8819.
UCSCuc003itd.3. human.

Organism-specific databases

CTD8819.
GeneCardsGC04P174292.
HGNCHGNC:10532. SAP30.
MIM603378. gene.
neXtProtNX_O75446.
PharmGKBPA34941.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG81414.
HOGENOMHOG000007811.
HOVERGENHBG057907.
InParanoidO75446.
OMAKIDSGVH.
OrthoDBEOG7P5T35.
PhylomeDBO75446.
TreeFamTF324135.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

BgeeO75446.
CleanExHS_SAP30.
GenevestigatorO75446.

Family and domain databases

InterProIPR024145. His_deAcase_SAP30/SAP30L.
IPR025718. SAP30_Sin3-bd.
IPR025717. SAP30_zn-finger.
[Graphical view]
PANTHERPTHR13286. PTHR13286. 1 hit.
PfamPF13867. SAP30_Sin3_bdg. 1 hit.
PF13866. zf-SAP30. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75446.
GeneWikiSAP30.
GenomeRNAi8819.
NextBio33082.
PROO75446.
SOURCESearch...

Entry information

Entry nameSAP30_HUMAN
AccessionPrimary (citable) accession number: O75446
Secondary accession number(s): D3DP38
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM