SP30L_HUMAN
ID SP30L_HUMAN Reviewed; 183 AA.
AC Q9HAJ7; E9PAU7; E9PAY2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Histone deacetylase complex subunit SAP30L;
DE AltName: Full=HCV non-structural protein 4A-transactivated protein 2;
DE AltName: Full=Sin3 corepressor complex subunit SAP30L;
DE AltName: Full=Sin3-associated protein p30-like;
GN Name=SAP30L; Synonyms=NS4ATP2;
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), SUBCELLULAR LOCATION, MUTAGENESIS
RP OF 88-ARG-LYS-89, INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=14680513; DOI=10.1186/1471-2164-4-53;
RA Lindfors K., Viiri K.M., Niittynen M., Heinonen T.Y., Maki M.,
RA Kainulainen H.;
RT "TGF-beta induces the expression of SAP30L, a novel nuclear protein.";
RL BMC Genomics 4:53-53(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Liu Y., Yang Y., Cheng J., Ji D., Li L., Zhang L., Chen J.;
RT "Homo sapiens gene 2 transactivated by nonstructural protein 4A of
RT hepatitis C virus (NS4ATP2) mRNA.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-135 (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-137 (ISOFORM 3).
RC TISSUE=Chronic myeloid leukemia cell, and Oligodendroglioma;
RG The Cancer Genome Anatomy Project (CGAP) at the National Cancer Institute;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INTERACTION WITH FEZ1.
RX PubMed=16484223; DOI=10.1074/jbc.m513280200;
RA Assmann E.M., Alborghetti M.R., Camargo M.E.R., Kobarg J.;
RT "FEZ1 dimerization and interaction with transcription regulatory proteins
RT involves its coiled-coil region.";
RL J. Biol. Chem. 281:9869-9881(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SIN3A; HDAC1 AND HDAC2,
RP AND MUTAGENESIS OF 120-ARG--LYS-127.
RX PubMed=16820529; DOI=10.1093/nar/gkl401;
RA Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K.,
RA Peterson P., Maeki M., Kainulainen H., Lohi O.;
RT "SAP30L interacts with members of the Sin3A corepressor complex and targets
RT Sin3A to the nucleolus.";
RL Nucleic Acids Res. 34:3288-3298(2006).
RN [10]
RP ALTERNATIVE SPLICING, IDENTIFICATION OF ISOFORMS 1; 2 AND 3, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 109-VAL--GLN-113.
RX PubMed=18070604; DOI=10.1016/j.febslet.2007.11.084;
RA Korkeamaeki H., Viiri K., Kukkonen M.K., Maeki M., Lohi O.;
RT "Alternative mRNA splicing of SAP30L regulates its transcriptional
RT repression activity.";
RL FEBS Lett. 582:379-384(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-92 AND SER-99, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP FUNCTION, LIPID-BINDING, DNA-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF 88-ARG--ARG-90.
RX PubMed=19015240; DOI=10.1128/mcb.01213-08;
RA Viiri K.M., Jaenis J., Siggers T., Heinonen T.Y., Valjakka J., Bulyk M.L.,
RA Maeki M., Lohi O.;
RT "DNA-binding and -bending activities of SAP30L and SAP30 are mediated by a
RT zinc-dependent module and monophosphoinositides.";
RL Mol. Cell. Biol. 29:342-356(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP STRUCTURE BY NMR OF 25-92 IN COMPLEX WITH ZINC IONS, FUNCTION, ZINC-FINGER
RP DOMAIN, LIPID-BINDING, DNA-BINDING, AND DISULFIDE BONDS.
RX PubMed=26609676; DOI=10.1002/pro.2849;
RA Laitaoja M., Tossavainen H., Pihlajamaa T., Valjakka J., Viiri K., Lohi O.,
RA Permi P., Janis J.;
RT "Redox-dependent disulfide bond formation in SAP30L corepressor protein:
RT Implications for structure and function.";
RL Protein Sci. 25:572-586(2016).
CC -!- FUNCTION: [Isoform 1]: Functions as transcription repressor, probably
CC via its interaction with histone deacetylase complexes
CC (PubMed:16820529, PubMed:18070604). Involved in the functional
CC recruitment of the class 1 Sin3-histone deacetylase complex (HDAC) to
CC the nucleolus (PubMed:16820529). Binds DNA, apparently without
CC sequence-specificity, and bends bound double-stranded DNA
CC (PubMed:19015240). Binds phosphoinositol phosphates (phosphoinositol 3-
CC phosphate, phosphoinositol 4-phosphate and phosphoinositol 5-phosphate)
CC via the same basic sequence motif that mediates DNA binding and nuclear
CC import (PubMed:19015240, PubMed:26609676).
CC {ECO:0000269|PubMed:16820529, ECO:0000269|PubMed:18070604,
CC ECO:0000269|PubMed:19015240, ECO:0000269|PubMed:26609676}.
CC -!- FUNCTION: [Isoform 2]: Functions as transcription repressor; isoform 2
CC has lower transcription repressor activity than isoform 1 and isoform
CC 3. {ECO:0000269|PubMed:18070604}.
CC -!- FUNCTION: [Isoform 3]: Functions as transcription repressor; its
CC activity is marginally lower than that of isoform 1.
CC {ECO:0000269|PubMed:18070604}.
CC -!- SUBUNIT: Interacts with components of the histone deacetylase complex
CC SIN3A, HDAC1 and HDAC2 (PubMed:16820529). Binds histones and
CC nucleosomes (PubMed:19015240). Interacts with FEZ1 (PubMed:16484223).
CC {ECO:0000269|PubMed:16484223, ECO:0000269|PubMed:16820529,
CC ECO:0000269|PubMed:19015240}.
CC -!- INTERACTION:
CC Q9HAJ7; Q92997: DVL3; NbExp=3; IntAct=EBI-2340040, EBI-739789;
CC Q9HAJ7; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-2340040, EBI-2549423;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleolus
CC {ECO:0000269|PubMed:14680513, ECO:0000269|PubMed:16820529,
CC ECO:0000269|PubMed:18070604, ECO:0000269|PubMed:19015240}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleolus
CC {ECO:0000269|PubMed:18070604}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, nucleolus
CC {ECO:0000269|PubMed:18070604}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9HAJ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HAJ7-2; Sequence=VSP_046221;
CC Name=3;
CC IsoId=Q9HAJ7-3; Sequence=VSP_046860;
CC -!- TISSUE SPECIFICITY: Detected in brain and ovary, and at lower levels in
CC heart, small intestine, lung, kidney, skeletal muscle, stomach and
CC spleen (at protein level) (PubMed:18070604). Ubiquitous; expressed in
CC all tissues tested with highest levels in testis (PubMed:14680513).
CC {ECO:0000269|PubMed:14680513, ECO:0000269|PubMed:18070604}.
CC -!- INDUCTION: Up-regulated by TGFB1. {ECO:0000269|PubMed:14680513}.
CC -!- DOMAIN: The zinc-finger domain mediates direct interaction with DNA and
CC phosphoinositol phosphates (phosphoinositol 3-phosphate,
CC phosphoinositol 4-phosphate and phosphoinositol 5-phosphate)
CC (PubMed:26609676). In vitro oxydation causes reversible disulfide bond
CC formation between Cys residues in the zinc-finger domain and reversible
CC loss of zinc ion binding (PubMed:26609676).
CC {ECO:0000269|PubMed:26609676}.
CC -!- SIMILARITY: Belongs to the SAP30 family. {ECO:0000305}.
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DR EMBL; AY341060; AAQ16562.1; -; mRNA.
DR EMBL; AY846876; AAX54477.1; -; mRNA.
DR EMBL; AK021588; BAB13848.1; -; mRNA.
DR EMBL; AC008625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61637.1; -; Genomic_DNA.
DR EMBL; BC009829; AAH09829.1; -; mRNA.
DR EMBL; AI199517; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AI436556; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS4326.1; -. [Q9HAJ7-1]
DR CCDS; CCDS47321.1; -. [Q9HAJ7-3]
DR CCDS; CCDS47322.1; -. [Q9HAJ7-2]
DR RefSeq; NP_001124534.1; NM_001131062.1. [Q9HAJ7-3]
DR RefSeq; NP_001124535.1; NM_001131063.1. [Q9HAJ7-2]
DR RefSeq; NP_078908.1; NM_024632.5. [Q9HAJ7-1]
DR PDB; 2N1U; NMR; -; A=25-92.
DR PDBsum; 2N1U; -.
DR AlphaFoldDB; Q9HAJ7; -.
DR SMR; Q9HAJ7; -.
DR BioGRID; 122808; 31.
DR ComplexPortal; CPX-3321; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3322; SIN3B histone deacetylase complex.
DR ComplexPortal; CPX-3323; SIN3A histone deacetylase complex, ES cell-specific variant.
DR IntAct; Q9HAJ7; 14.
DR MINT; Q9HAJ7; -.
DR STRING; 9606.ENSP00000297109; -.
DR iPTMnet; Q9HAJ7; -.
DR PhosphoSitePlus; Q9HAJ7; -.
DR BioMuta; SAP30L; -.
DR DMDM; 74734226; -.
DR EPD; Q9HAJ7; -.
DR jPOST; Q9HAJ7; -.
DR MassIVE; Q9HAJ7; -.
DR MaxQB; Q9HAJ7; -.
DR PaxDb; Q9HAJ7; -.
DR PeptideAtlas; Q9HAJ7; -.
DR PRIDE; Q9HAJ7; -.
DR ProteomicsDB; 19082; -.
DR ProteomicsDB; 19103; -.
DR ProteomicsDB; 81408; -. [Q9HAJ7-1]
DR Antibodypedia; 16444; 112 antibodies from 25 providers.
DR DNASU; 79685; -.
DR Ensembl; ENST00000297109.11; ENSP00000297109.5; ENSG00000164576.12. [Q9HAJ7-1]
DR Ensembl; ENST00000426761.2; ENSP00000416393.2; ENSG00000164576.12. [Q9HAJ7-2]
DR Ensembl; ENST00000440364.6; ENSP00000390927.2; ENSG00000164576.12. [Q9HAJ7-3]
DR GeneID; 79685; -.
DR KEGG; hsa:79685; -.
DR MANE-Select; ENST00000297109.11; ENSP00000297109.5; NM_024632.6; NP_078908.1.
DR UCSC; uc003lvk.4; human. [Q9HAJ7-1]
DR CTD; 79685; -.
DR DisGeNET; 79685; -.
DR GeneCards; SAP30L; -.
DR HGNC; HGNC:25663; SAP30L.
DR HPA; ENSG00000164576; Low tissue specificity.
DR MIM; 610398; gene.
DR neXtProt; NX_Q9HAJ7; -.
DR OpenTargets; ENSG00000164576; -.
DR PharmGKB; PA144596386; -.
DR VEuPathDB; HostDB:ENSG00000164576; -.
DR eggNOG; ENOG502QWFH; Eukaryota.
DR GeneTree; ENSGT00390000006633; -.
DR HOGENOM; CLU_097961_1_0_1; -.
DR InParanoid; Q9HAJ7; -.
DR OMA; QCARTKR; -.
DR OrthoDB; 1520155at2759; -.
DR PhylomeDB; Q9HAJ7; -.
DR TreeFam; TF324135; -.
DR PathwayCommons; Q9HAJ7; -.
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; Q9HAJ7; -.
DR BioGRID-ORCS; 79685; 10 hits in 1082 CRISPR screens.
DR ChiTaRS; SAP30L; human.
DR GenomeRNAi; 79685; -.
DR Pharos; Q9HAJ7; Tbio.
DR PRO; PR:Q9HAJ7; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9HAJ7; protein.
DR Bgee; ENSG00000164576; Expressed in right testis and 181 other tissues.
DR Genevisible; Q9HAJ7; HS.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0016580; C:Sin3 complex; IC:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0044378; F:non-sequence-specific DNA binding, bending; IDA:UniProtKB.
DR GO; GO:0031491; F:nucleosome binding; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 6.10.160.20; -; 1.
DR InterPro; IPR024145; His_deAcase_SAP30/SAP30L.
DR InterPro; IPR038291; SAP30_C_sf.
DR InterPro; IPR025718; SAP30_Sin3-bd.
DR InterPro; IPR025717; SAP30_zn-finger.
DR PANTHER; PTHR13286; PTHR13286; 1.
DR Pfam; PF13867; SAP30_Sin3_bdg; 1.
DR Pfam; PF13866; zf-SAP30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Disulfide bond;
KW DNA-binding; Isopeptide bond; Lipid-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..183
FT /note="Histone deacetylase complex subunit SAP30L"
FT /id="PRO_0000309500"
FT ZN_FING 29..77
FT /note="Atypical"
FT /evidence="ECO:0000305|PubMed:26609676"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..90
FT /note="Important for DNA and phosphoinositide binding"
FT /evidence="ECO:0000269|PubMed:19015240"
FT MOTIF 86..91
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000305|PubMed:14680513"
FT COMPBIAS 87..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SQF8"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT DISULFID 29..30
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:26609676"
FT DISULFID 38..74
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:26609676"
FT CROSSLNK 49
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75446"
FT CROSSLNK 155
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75446"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75446"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75446"
FT VAR_SEQ 68..113
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.7, ECO:0000305|PubMed:18070604"
FT /id="VSP_046221"
FT VAR_SEQ 68..108
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.7, ECO:0000305|PubMed:18070604"
FT /id="VSP_046860"
FT MUTAGEN 88..90
FT /note="RKR->AAA: Strongly reduces affinity for DNA and for
FT phosphoinositides."
FT /evidence="ECO:0000269|PubMed:19015240"
FT MUTAGEN 88..89
FT /note="RK->KS: Impairs nuclear localization."
FT /evidence="ECO:0000269|PubMed:14680513"
FT MUTAGEN 109..113
FT /note="Missing: Reduces transcriptional repressor activity,
FT reduces localization in nucleoli, but has no effect on
FT association with histone deacylase complexes."
FT /evidence="ECO:0000269|PubMed:18070604"
FT MUTAGEN 120..127
FT /note="RRYKRHYK->AAAAAAAA: Abolishes nucleolar
FT localization."
FT /evidence="ECO:0000269|PubMed:16820529"
FT CONFLICT 31
FT /note="L -> R (in Ref. 7; AI199517)"
FT /evidence="ECO:0000305"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2N1U"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:2N1U"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:2N1U"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2N1U"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:2N1U"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2N1U"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:2N1U"
SQ SEQUENCE 183 AA; 20877 MW; EB19E448C6A1FA45 CRC64;
MNGFSTEEDS REGPPAAPAA AAPGYGQSCC LIEDGERCVR PAGNASFSKR VQKSISQKKL
KLDIDKSVRH LYICDFHKNF IQSVRNKRKR KTSDDGGDSP EHDTDIPEVD LFQLQVNTLR
RYKRHYKLQT RPGFNKAQLA ETVSRHFRNI PVNEKETLAY FIYMVKSNKS RLDQKSEGGK
QLE
