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O00422 (SAP18_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase complex subunit SAP18
Alternative name(s):
18 kDa Sin3-associated polypeptide
2HOR0202
Cell growth-inhibiting gene 38 protein
Sin3-associated polypeptide p18
Gene names
Name:SAP18
ORF Names:GIG38
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.10 Ref.13 Ref.15

Subunit structure

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. Ref.1 Ref.10 Ref.11 Ref.13 Ref.16

Subcellular location

Nucleus. Cytoplasm. Nucleus speckle. Note: Shuttles between the nucleus and the cytoplasm. Colocalizes with ACIN1 and SRSF2 in nuclear speckles. Ref.11 Ref.13

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the SAP18 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HDAC1Q135472EBI-1044156,EBI-301834

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 153152Histone deacetylase complex subunit SAP18
PRO_0000220975

Regions

Region93 – 15361Involved in splicing regulation activity

Amino acid modifications

Modified residue21N-acetylalanine Ref.12

Experimental info

Mutagenesis1181D → A: Abolishes splicing regulation activity and interaction with RNPS1 and ACIN1; when associated with A-121. Ref.13
Mutagenesis1211T → A: Abolishes splicing regulation activity and interaction with RNPS1 and ACIN1; when associated with A-118. Ref.13
Mutagenesis1261K → A: No effect on splicing regulation activity. Ref.13
Sequence conflict1141K → E in AAF21220. Ref.2
Sequence conflict1461P → T in AAH30836. Ref.9

Secondary structure

.......................... 153
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O00422 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: C7E479FFE9CA5774

FASTA15317,561
        10         20         30         40         50         60 
MAVESRVTQE EIKKEPEKPI DREKTCPLLL RVFTTNNGRH HRMDEFSRGN VPSSELQIYT 

        70         80         90        100        110        120 
WMDATLKELT SLVKEVYPEA RKKGTHFNFA IVFTDVKRPG YRVKEIGSTM SGRKGTDDSM 

       130        140        150 
TLQSQKFQIG DYLDIAITPP NRAPPPSGRM RPY 

« Hide

References

« Hide 'large scale' references
[1]"Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex."
Zhang Y., Iratni R., Erdjument-Bromage H., Tempst P., Reinberg D.
Cell 89:357-364(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SIN3A AND HDAC1.
[2]"Characterization of proteins interacting with CAMPGEF."
Kawasaki H., Housman D.E., Graybiel A.M.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"A catalogue of genes in the human dermal papilla cells as identified by expressed sequence tags."
Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Chung H.J., Sohn M.Y., Hwang S.Y., Im S.U., Jung E.J., Lee H.D., Kim J.C.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hair follicle dermal papilla.
[4]"Identification of a human cell growth inhibiting gene."
Kim J.W.
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.
[7]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: Hypothalamus.
[10]"ASAP, a novel protein complex involved in RNA processing and apoptosis."
Schwerk C., Prasad J., Degenhardt K., Erdjument-Bromage H., White E., Tempst P., Kidd V.J., Manley J.L., Lahti J.M., Reinberg D.
Mol. Cell. Biol. 23:2981-2990(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE ASAP COMPLEX, FUNCTION OF THE ASAP COMPLEX.
[11]"Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core."
Tange T.O., Shibuya T., Jurica M.S., Moore M.J.
RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, IDENTIFICATION IN THE ASAP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[13]"Human SAP18 mediates assembly of a splicing regulatory multiprotein complex via its ubiquitin-like fold."
Singh K.K., Erkelenz S., Rattay S., Dehof A.K., Hildebrandt A., Schulze-Osthoff K., Schaal H., Schwerk C.
RNA 16:2442-2454(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RNPS1 AND ACIN1, MUTAGENESIS OF ASP-118; THR-121 AND LYS-126.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Proteins associated with the exon junction complex also control the alternative splicing of apoptotic regulators."
Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M., Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R., Elela S.A., Prinos P., Chabot B.
Mol. Cell. Biol. 32:954-967(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Structure of SAP18: a ubiquitin fold in histone deacetylase complex assembly."
McCallum S.A., Bazan J.F., Merchant M., Yin J., Pan B., de Sauvage F.J., Fairbrother W.J.
Biochemistry 45:11974-11982(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 6-149, INTERACTION WITH SUFU.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U96915 mRNA. Translation: AAC51322.1.
U78303 mRNA. Translation: AAF21220.1.
AF153608 mRNA. Translation: AAD41090.1.
AY550970 mRNA. Translation: AAT52216.1.
CR457035 mRNA. Translation: CAG33316.1.
AK311748 mRNA. Translation: BAG34691.1.
AL158032 Genomic DNA. Translation: CAH69949.1.
CH471075 Genomic DNA. Translation: EAX08291.1.
BC030836 mRNA. Translation: AAH30836.1.
RefSeqNP_005861.2. NM_005870.4.
UniGeneHs.524899.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HDENMR-A6-149[»]
ProteinModelPortalO00422.
SMRO00422. Positions 6-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115573. 92 interactions.
DIPDIP-33590N.
IntActO00422. 12 interactions.
MINTMINT-5002140.
STRING9606.ENSP00000371973.

Protein family/group databases

TCDB3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSiteO00422.

Proteomic databases

PaxDbO00422.
PeptideAtlasO00422.
PRIDEO00422.

Protocols and materials databases

DNASU10284.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000607003; ENSP00000475925; ENSG00000150459.
GeneID10284.
KEGGhsa:10284.
UCSCuc001uns.3. human.

Organism-specific databases

CTD10284.
GeneCardsGC13P021714.
H-InvDBHIX0011163.
HGNCHGNC:10530. SAP18.
HPACAB012273.
HPA011352.
MIM602949. gene.
neXtProtNX_O00422.
PharmGKBPA34940.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249491.
HOGENOMHOG000238745.
HOVERGENHBG003465.
InParanoidO00422.
KOK14324.
OrthoDBEOG79SDZS.
PhylomeDBO00422.
TreeFamTF313032.

Enzyme and pathway databases

SignaLinkO00422.

Gene expression databases

BgeeO00422.
CleanExHS_SAP18.
GenevestigatorO00422.

Family and domain databases

InterProIPR017250. Hist_deAcase_cplx_SAP18.
IPR010516. SAP18.
[Graphical view]
PANTHERPTHR13082. PTHR13082. 1 hit.
PfamPF06487. SAP18. 1 hit.
[Graphical view]
PIRSFPIRSF037637. HDAC_SAP18. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSAP18. human.
EvolutionaryTraceO00422.
GeneWikiSAP18.
GenomeRNAi10284.
NextBio38964.
PROO00422.
SOURCESearch...

Entry information

Entry nameSAP18_HUMAN
AccessionPrimary (citable) accession number: O00422
Secondary accession number(s): B2R494 expand/collapse secondary AC list , Q2TTR4, Q6IAW9, Q8N606, Q9UF14
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 127 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 13

Human chromosome 13: entries, gene names and cross-references to MIM