SAP18_HUMAN
ID SAP18_HUMAN Reviewed; 153 AA.
AC O00422; B2R494; Q2TTR4; Q6IAW9; Q8N606; Q9UF14; X6RAL5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Histone deacetylase complex subunit SAP18;
DE AltName: Full=18 kDa Sin3-associated polypeptide;
DE AltName: Full=2HOR0202;
DE AltName: Full=Cell growth-inhibiting gene 38 protein;
DE AltName: Full=Sin3-associated polypeptide p18;
GN Name=SAP18; ORFNames=GIG38;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP SIN3A AND HDAC1.
RX PubMed=9150135; DOI=10.1016/s0092-8674(00)80216-0;
RA Zhang Y., Iratni R., Erdjument-Bromage H., Tempst P., Reinberg D.;
RT "Histone deacetylases and SAP18, a novel polypeptide, are components of a
RT human Sin3 complex.";
RL Cell 89:357-364(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Kawasaki H., Housman D.E., Graybiel A.M.;
RT "Characterization of proteins interacting with CAMPGEF.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hair follicle dermal papilla;
RA Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Chung H.J., Sohn M.Y., Hwang S.Y.,
RA Im S.U., Jung E.J., Lee H.D., Kim J.C.;
RT "A catalogue of genes in the human dermal papilla cells as identified by
RT expressed sequence tags.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kim J.W.;
RT "Identification of a human cell growth inhibiting gene.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain cortex;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP IDENTIFICATION IN THE ASAP COMPLEX, AND FUNCTION OF THE ASAP COMPLEX.
RX PubMed=12665594; DOI=10.1128/mcb.23.8.2981-2990.2003;
RA Schwerk C., Prasad J., Degenhardt K., Erdjument-Bromage H., White E.,
RA Tempst P., Kidd V.J., Manley J.L., Lahti J.M., Reinberg D.;
RT "ASAP, a novel protein complex involved in RNA processing and apoptosis.";
RL Mol. Cell. Biol. 23:2981-2990(2003).
RN [11]
RP IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX,
RP IDENTIFICATION IN THE ASAP COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16314458; DOI=10.1261/rna.2155905;
RA Tange T.O., Shibuya T., Jurica M.S., Moore M.J.;
RT "Biochemical analysis of the EJC reveals two new factors and a stable
RT tetrameric protein core.";
RL RNA 11:1869-1883(2005).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RNPS1 AND ACIN1, AND
RP MUTAGENESIS OF ASP-118; THR-121 AND LYS-126.
RX PubMed=20966198; DOI=10.1261/rna.2304410;
RA Singh K.K., Erkelenz S., Rattay S., Dehof A.K., Hildebrandt A.,
RA Schulze-Osthoff K., Schaal H., Schwerk C.;
RT "Human SAP18 mediates assembly of a splicing regulatory multiprotein
RT complex via its ubiquitin-like fold.";
RL RNA 16:2442-2454(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP FUNCTION.
RX PubMed=22203037; DOI=10.1128/mcb.06130-11;
RA Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M.,
RA Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R.,
RA Elela S.A., Prinos P., Chabot B.;
RT "Proteins associated with the exon junction complex also control the
RT alternative splicing of apoptotic regulators.";
RL Mol. Cell. Biol. 32:954-967(2012).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
RP STRUCTURE BY NMR OF 6-149, AND INTERACTION WITH SUFU.
RX PubMed=17002296; DOI=10.1021/bi060687l;
RA McCallum S.A., Bazan J.F., Merchant M., Yin J., Pan B., de Sauvage F.J.,
RA Fairbrother W.J.;
RT "Structure of SAP18: a ubiquitin fold in histone deacetylase complex
RT assembly.";
RL Biochemistry 45:11974-11982(2006).
CC -!- FUNCTION: Component of the SIN3-repressing complex. Enhances the
CC ability of SIN3-HDAC1-mediated transcriptional repression. When
CC tethered to the promoter, it can direct the formation of a repressive
CC complex to core histone proteins. Auxiliary component of the splicing-
CC dependent multiprotein exon junction complex (EJC) deposited at splice
CC junction on mRNAs. The EJC is a dynamic structure consisting of core
CC proteins and several peripheral nuclear and cytoplasmic associated
CC factors that join the complex only transiently either during EJC
CC assembly or during subsequent mRNA metabolism. Component of the ASAP
CC and PSAP complexes which bind RNA in a sequence-independent manner and
CC are proposed to be recruited to the EJC prior to or during the splicing
CC process and to regulate specific excision of introns in specific
CC transcription subsets. The ASAP complex can inhibit mRNA processing
CC during in vitro splicing reactions. The ASAP complex promotes apoptosis
CC and is disassembled after induction of apoptosis. Involved in the
CC splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic
CC genes); specifically inhibits the formation of proapoptotic isoforms
CC such as Bcl-X(S); the activity is different from the established EJC
CC assembly and function. {ECO:0000269|PubMed:12665594,
CC ECO:0000269|PubMed:20966198, ECO:0000269|PubMed:22203037,
CC ECO:0000269|PubMed:9150135}.
CC -!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex
CC (EJC). Component of the heterotrimeric ASAP (apoptosis- and splicing-
CC associated protein) and PSAP complexes consisting of RNPS1, SAP18 and
CC either ACIN1 or PNN, respectively; the ASAP and PSAP complexes probably
CC are formed mutually exclusive. For the ASAP complex, the association of
CC SAP18 seems to require a preformed RNPS1:ACIN1 complex. Forms a complex
CC with SIN3A and HDAC1. Interacts with SUFU.
CC {ECO:0000269|PubMed:12665594, ECO:0000269|PubMed:16314458,
CC ECO:0000269|PubMed:17002296, ECO:0000269|PubMed:20966198,
CC ECO:0000269|PubMed:9150135}.
CC -!- INTERACTION:
CC O00422; Q9H4E7: DEF6; NbExp=3; IntAct=EBI-1044156, EBI-745369;
CC O00422; Q13547: HDAC1; NbExp=2; IntAct=EBI-1044156, EBI-301834;
CC O00422; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1044156, EBI-6509505;
CC O00422; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-1044156, EBI-741158;
CC O00422; Q9H307: PNN; NbExp=2; IntAct=EBI-1044156, EBI-681904;
CC O00422; Q14498: RBM39; NbExp=9; IntAct=EBI-1044156, EBI-395290;
CC O00422; Q14498-3: RBM39; NbExp=3; IntAct=EBI-1044156, EBI-6654703;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16314458}. Cytoplasm
CC {ECO:0000269|PubMed:16314458}. Nucleus speckle
CC {ECO:0000269|PubMed:20966198}. Note=Shuttles between the nucleus and
CC the cytoplasm (PubMed:16314458). Colocalizes with ACIN1 and SRSF2 in
CC nuclear speckles (PubMed:20966198). {ECO:0000269|PubMed:16314458,
CC ECO:0000269|PubMed:20966198}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=O00422-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00422-2; Sequence=VSP_060066;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the SAP18 family. {ECO:0000305}.
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DR EMBL; U96915; AAC51322.1; -; mRNA.
DR EMBL; U78303; AAF21220.1; -; mRNA.
DR EMBL; AF153608; AAD41090.1; -; mRNA.
DR EMBL; AY550970; AAT52216.1; -; mRNA.
DR EMBL; CR457035; CAG33316.1; -; mRNA.
DR EMBL; AK311748; BAG34691.1; -; mRNA.
DR EMBL; AL158032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08291.1; -; Genomic_DNA.
DR EMBL; BC030836; AAH30836.1; -; mRNA.
DR CCDS; CCDS9295.2; -. [O00422-2]
DR RefSeq; NP_005861.2; NM_005870.4. [O00422-2]
DR PDB; 2HDE; NMR; -; A=6-149.
DR PDBsum; 2HDE; -.
DR AlphaFoldDB; O00422; -.
DR BMRB; O00422; -.
DR SMR; O00422; -.
DR BioGRID; 115573; 236.
DR CORUM; O00422; -.
DR DIP; DIP-33590N; -.
DR IntAct; O00422; 50.
DR MINT; O00422; -.
DR STRING; 9606.ENSP00000481842; -.
DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
DR GlyGen; O00422; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00422; -.
DR PhosphoSitePlus; O00422; -.
DR SwissPalm; O00422; -.
DR BioMuta; SAP18; -.
DR EPD; O00422; -.
DR jPOST; O00422; -.
DR MassIVE; O00422; -.
DR MaxQB; O00422; -.
DR PaxDb; O00422; -.
DR PeptideAtlas; O00422; -.
DR PRIDE; O00422; -.
DR ProteomicsDB; 47879; -.
DR Antibodypedia; 1801; 171 antibodies from 25 providers.
DR DNASU; 10284; -.
DR Ensembl; ENST00000382533.8; ENSP00000371973.4; ENSG00000150459.12. [O00422-2]
DR Ensembl; ENST00000607003.5; ENSP00000475925.1; ENSG00000150459.12. [O00422-1]
DR Ensembl; ENST00000621421.4; ENSP00000481842.1; ENSG00000150459.12. [O00422-2]
DR GeneID; 10284; -.
DR KEGG; hsa:10284; -.
DR MANE-Select; ENST00000382533.9; ENSP00000371973.4; NM_005870.5; NP_005861.2. [O00422-2]
DR UCSC; uc001uns.4; human.
DR UCSC; uc058vux.1; human. [O00422-1]
DR CTD; 10284; -.
DR GeneCards; SAP18; -.
DR HGNC; HGNC:10530; SAP18.
DR HPA; ENSG00000150459; Low tissue specificity.
DR MIM; 602949; gene.
DR neXtProt; NX_O00422; -.
DR OpenTargets; ENSG00000150459; -.
DR PharmGKB; PA34940; -.
DR VEuPathDB; HostDB:ENSG00000150459; -.
DR eggNOG; KOG3391; Eukaryota.
DR GeneTree; ENSGT00390000003152; -.
DR HOGENOM; CLU_108681_0_1_1; -.
DR InParanoid; O00422; -.
DR OMA; VYPNFRN; -.
DR OrthoDB; 1622057at2759; -.
DR PhylomeDB; O00422; -.
DR TreeFam; TF313032; -.
DR PathwayCommons; O00422; -.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; O00422; -.
DR SIGNOR; O00422; -.
DR BioGRID-ORCS; 10284; 726 hits in 1086 CRISPR screens.
DR ChiTaRS; SAP18; human.
DR EvolutionaryTrace; O00422; -.
DR GeneWiki; SAP18; -.
DR GenomeRNAi; 10284; -.
DR Pharos; O00422; Tbio.
DR PRO; PR:O00422; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; O00422; protein.
DR Bgee; ENSG00000150459; Expressed in adult organism and 214 other tissues.
DR ExpressionAtlas; O00422; baseline and differential.
DR Genevisible; O00422; HS.
DR GO; GO:0061574; C:ASAP complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000118; C:histone deacetylase complex; TAS:ProtInc.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.10.20.550; -; 1.
DR InterPro; IPR017250; Hist_deAcase_cplx_SAP18.
DR InterPro; IPR010516; SAP18.
DR InterPro; IPR042534; SAP18_sf.
DR PANTHER; PTHR13082; PTHR13082; 1.
DR Pfam; PF06487; SAP18; 1.
DR PIRSF; PIRSF037637; HDAC_SAP18; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Cytoplasm;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..153
FT /note="Histone deacetylase complex subunit SAP18"
FT /id="PRO_0000220975"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..153
FT /note="Involved in splicing regulation activity"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CROSSLNK 13
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MLAAGVGGQGERLAGRRRKM (in isoform 2)"
FT /id="VSP_060066"
FT MUTAGEN 118
FT /note="D->A: Abolishes splicing regulation activity and
FT interaction with RNPS1 and ACIN1; when associated with A-
FT 121."
FT /evidence="ECO:0000269|PubMed:20966198"
FT MUTAGEN 121
FT /note="T->A: Abolishes splicing regulation activity and
FT interaction with RNPS1 and ACIN1; when associated with A-
FT 118."
FT /evidence="ECO:0000269|PubMed:20966198"
FT MUTAGEN 126
FT /note="K->A: No effect on splicing regulation activity."
FT /evidence="ECO:0000269|PubMed:20966198"
FT CONFLICT 114
FT /note="K -> E (in Ref. 2; AAF21220)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="P -> T (in Ref. 9; AAH30836)"
FT /evidence="ECO:0000305"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:2HDE"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:2HDE"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2HDE"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:2HDE"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:2HDE"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:2HDE"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:2HDE"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:2HDE"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2HDE"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:2HDE"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:2HDE"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:2HDE"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:2HDE"
SQ SEQUENCE 153 AA; 17561 MW; C7E479FFE9CA5774 CRC64;
MAVESRVTQE EIKKEPEKPI DREKTCPLLL RVFTTNNGRH HRMDEFSRGN VPSSELQIYT
WMDATLKELT SLVKEVYPEA RKKGTHFNFA IVFTDVKRPG YRVKEIGSTM SGRKGTDDSM
TLQSQKFQIG DYLDIAITPP NRAPPPSGRM RPY
