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 02-OCT-2024, entry version 204. 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=4; IntAct=EBI-1044156, EBI-681904; CC O00422; Q14498: RBM39; NbExp=12; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 314. DR ComplexPortal; CPX-2256; ASAP splicing-associated complex. DR ComplexPortal; CPX-2257; PSAP splicing-associated complex. DR CORUM; O00422; -. DR DIP; DIP-33590N; -. DR IntAct; O00422; 135. DR MINT; O00422; -. DR STRING; 9606.ENSP00000481842; -. DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family. DR GlyGen; O00422; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; O00422; -. DR PhosphoSitePlus; O00422; -. DR SwissPalm; O00422; -. DR BioMuta; SAP18; -. DR jPOST; O00422; -. DR MassIVE; O00422; -. DR PaxDb; 9606-ENSP00000481842; -. DR PeptideAtlas; O00422; -. DR ProteomicsDB; 47879; -. DR Pumba; O00422; -. DR Antibodypedia; 1801; 197 antibodies from 26 providers. DR DNASU; 10284; -. DR Ensembl; ENST00000382533.9; ENSP00000371973.4; ENSG00000150459.13. [O00422-2] DR Ensembl; ENST00000607003.5; ENSP00000475925.1; ENSG00000150459.13. [O00422-1] DR Ensembl; ENST00000621421.4; ENSP00000481842.1; ENSG00000150459.13. [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 AGR; HGNC:10530; -. DR CTD; 10284; -. DR DisGeNET; 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; 2727794at2759; -. 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-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-9679191; Potential therapeutics for SARS. DR SignaLink; O00422; -. DR SIGNOR; O00422; -. DR BioGRID-ORCS; 10284; 758 hits in 1165 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 216 other cell types or tissues. DR ExpressionAtlas; O00422; baseline and differential. 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:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB. 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; ASAP complex, SAP18 subunit; 1. DR InterPro; IPR017250; Hist_deAcase_cplx_SAP18. DR InterPro; IPR010516; SAP18. DR InterPro; IPR042534; SAP18_sf. DR PANTHER; PTHR13082:SF0; HISTONE DEACETYLASE COMPLEX SUBUNIT SAP18; 1. DR PANTHER; PTHR13082; SAP18; 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 Proteomics identification; Reference proteome; Repressor; Transcription; KW Transcription regulation; 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 //