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Protein

Histone deacetylase complex subunit SAP18

Gene

Sap18

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit mRNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits the formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function (By similarity).By similarity1 Publication

GO - Biological processi

Keywordsi

Molecular functionRepressor
Biological processmRNA processing, mRNA splicing, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase complex subunit SAP18
Alternative name(s):
18 kDa Sin3-associated polypeptide
Sin3-associated polypeptide p18
Gene namesi
Name:Sap18
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1277978 Sap18

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi26C → R: Impairs interactions with RNPS1, ACIN1 and PNN; reduces ASAP and PSAP complex assemblies. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002209762 – 153Histone deacetylase complex subunit SAP18Add BLAST152

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Cross-linki13Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiO55128
MaxQBiO55128
PaxDbiO55128
PeptideAtlasiO55128
PRIDEiO55128

PTM databases

iPTMnetiO55128
PhosphoSitePlusiO55128

Expressioni

Tissue specificityi

Expressed in all tissues tested; highest levels in the brain, kidney and muscle; lowest levels in lung spleen, liver, intestine and testis, and moderate levels in salivary gland and heart.1 Publication

Gene expression databases

CleanExiMM_SAP18

Interactioni

Subunit structurei

Found in a mRNA splicing-dependent exon junction complex (EJC). Component of the heterotrimeric ASAP (apoptosis- and splicing-associated protein) and PSAP complexes consisting of RNPS1, SAP18 and either ACIN1 or PNN, respectively; the ASAP and PSAP complexes probably are formed mutually exclusive. For the ASAP complex, the association of SAP18 seems to require a preformed RNPS1:ACIN1 complex. Forms a complex with SIN3A and HDAC1. Interacts with SUFU.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SufuQ9Z0P76EBI-3508332,EBI-3508336

Protein-protein interaction databases

BioGridi203070, 9 interactors
DIPiDIP-59924N
IntActiO55128, 8 interactors
MINTiO55128
STRINGi10090.ENSMUSP00000120071

Structurei

Secondary structure

1153
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 11Combined sources3
Helixi22 – 24Combined sources3
Beta strandi28 – 39Combined sources12
Helixi43 – 46Combined sources4
Helixi47 – 49Combined sources3
Beta strandi56 – 60Combined sources5
Helixi66 – 76Combined sources11
Helixi78 – 81Combined sources4
Beta strandi86 – 94Combined sources9
Beta strandi96 – 110Combined sources15
Turni116 – 119Combined sources4
Helixi123 – 125Combined sources3
Beta strandi132 – 138Combined sources7
Helixi140 – 142Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4A6QX-ray1.50A6-143[»]
4A8XX-ray1.90C14-143[»]
4A90X-ray1.90A/B1-143[»]
ProteinModelPortaliO55128
SMRiO55128
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni93 – 153Involved in splicing regulation activityBy similarityAdd BLAST61

Sequence similaritiesi

Belongs to the SAP18 family.Curated

Phylogenomic databases

eggNOGiKOG3391 Eukaryota
ENOG4111FBB LUCA
HOGENOMiHOG000238745
HOVERGENiHBG003465
InParanoidiO55128
KOiK14324
PhylomeDBiO55128

Family and domain databases

InterProiView protein in InterPro
IPR017250 Hist_deAcase_cplx_SAP18
IPR010516 SAP18
PANTHERiPTHR13082 PTHR13082, 1 hit
PfamiView protein in Pfam
PF06487 SAP18, 1 hit
PIRSFiPIRSF037637 HDAC_SAP18, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O55128-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVESRVTQE EIKKEPEKPI DREKTCPLLL RVFTTNNGRH HRMDEFSRGN
60 70 80 90 100
VPSSELQIYT WMDATLKELT SLVKEVYPEA RKKGTHFNFA IVFMDLKRPG
110 120 130 140 150
YRVKEIGSTM SGRKGTDDSM TLQSQKFQIG DYLDIAITPP NRAPPSSGRM

RPY
Length:153
Mass (Da):17,595
Last modified:June 1, 1998 - v1
Checksum:i68FE63E6EAD04E6F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97062 mRNA Translation: CAB09797.1
AK005189 mRNA Translation: BAB23871.1
AK006647 mRNA Translation: BAB24687.1
AK085992 mRNA Translation: BAC39588.1
BC006625 mRNA Translation: AAH06625.1
RefSeqiNP_033145.2, NM_009119.3
UniGeneiMm.30173
Mm.344671

Genome annotation databases

GeneIDi20220
KEGGimmu:20220

Similar proteinsi

Entry informationi

Entry nameiSAP18_MOUSE
AccessioniPrimary (citable) accession number: O55128
Secondary accession number(s): Q545L4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: May 23, 2018
This is version 141 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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