SP30L_MOUSE
ID SP30L_MOUSE Reviewed; 182 AA.
AC Q5SQF8; Q504M9; Q9CUZ7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Histone deacetylase complex subunit SAP30L;
DE AltName: Full=Sin3 corepressor complex subunit SAP30L;
DE AltName: Full=Sin3-associated protein p30-like;
GN Name=Sap30l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Pancreas;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-182.
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-98, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-98, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Functions as transcription repressor, probably via its
CC interaction with histone deacetylase complexes. Involved in the
CC functional recruitment of the class 1 Sin3-histone deacetylase complex
CC (HDAC) to the nucleolus. Binds DNA, apparently without sequence-
CC specificity, and bends bound double-stranded DNA. Binds phosphoinositol
CC phosphates (phosphoinositol 3-phosphate, phosphoinositol 4-phosphate
CC and phosphoinositol 5-phosphate) via the same basic sequence motif that
CC mediates DNA binding and nuclear import.
CC {ECO:0000250|UniProtKB:Q9HAJ7}.
CC -!- SUBUNIT: Interacts with components of the histone deacetylase complex
CC SIN3A, HDAC1 and HDAC2. Binds histones and nucleosomes. Interacts with
CC FEZ1. {ECO:0000250|UniProtKB:Q9HAJ7}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9HAJ7}.
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). In vitro
CC oxydation causes reversible disulfide bond formation between Cys
CC residues in the zinc-finger domain and reversible loss of zinc ion
CC binding. {ECO:0000250|UniProtKB:Q9HAJ7}.
CC -!- SIMILARITY: Belongs to the SAP30 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH94930.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL732587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051686; AAH51686.1; -; mRNA.
DR EMBL; BC094930; AAH94930.1; ALT_INIT; mRNA.
DR EMBL; BC117029; AAI17030.1; -; mRNA.
DR EMBL; BC117031; AAI17032.1; -; mRNA.
DR EMBL; AK010234; BAB26785.1; -; mRNA.
DR CCDS; CCDS36160.1; -.
DR RefSeq; NP_001074637.1; NM_001081168.1.
DR AlphaFoldDB; Q5SQF8; -.
DR SMR; Q5SQF8; -.
DR ComplexPortal; CPX-3441; SIN3A histone deacetylase complex, ES cell-specific variant.
DR ComplexPortal; CPX-3443; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3444; SIN3B histone deacetylase complex.
DR STRING; 10090.ENSMUSP00000020826; -.
DR iPTMnet; Q5SQF8; -.
DR PhosphoSitePlus; Q5SQF8; -.
DR EPD; Q5SQF8; -.
DR MaxQB; Q5SQF8; -.
DR PaxDb; Q5SQF8; -.
DR PeptideAtlas; Q5SQF8; -.
DR PRIDE; Q5SQF8; -.
DR ProteomicsDB; 257549; -.
DR Antibodypedia; 16444; 112 antibodies from 25 providers.
DR Ensembl; ENSMUST00000020826; ENSMUSP00000020826; ENSMUSG00000020519.
DR GeneID; 50724; -.
DR KEGG; mmu:50724; -.
DR UCSC; uc007jae.1; mouse.
DR CTD; 79685; -.
DR MGI; MGI:1354709; Sap30l.
DR VEuPathDB; HostDB:ENSMUSG00000020519; -.
DR eggNOG; ENOG502QWFH; Eukaryota.
DR GeneTree; ENSGT00390000006633; -.
DR HOGENOM; CLU_097961_1_0_1; -.
DR InParanoid; Q5SQF8; -.
DR OMA; QCARTKR; -.
DR OrthoDB; 1520155at2759; -.
DR PhylomeDB; Q5SQF8; -.
DR TreeFam; TF324135; -.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR BioGRID-ORCS; 50724; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Sap30l; mouse.
DR PRO; PR:Q5SQF8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SQF8; protein.
DR Bgee; ENSMUSG00000020519; Expressed in cleaving embryo and 262 other tissues.
DR Genevisible; Q5SQF8; MM.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0016580; C:Sin3 complex; IC:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0044378; F:non-sequence-specific DNA binding, bending; ISS:UniProtKB.
DR GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISS: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; ISS: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 Acetylation; Disulfide bond; DNA-binding; Isopeptide bond; Lipid-binding;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..182
FT /note="Histone deacetylase complex subunit SAP30L"
FT /id="PRO_0000309501"
FT ZN_FING 28..76
FT /note="Atypical"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..89
FT /note="Important for DNA and phosphoinositide binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HAJ7"
FT MOTIF 85..90
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000250|UniProtKB:Q9HAJ7"
FT COMPBIAS 86..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAJ7"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT DISULFID 28..29
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 37..73
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75446"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75446"
FT CROSSLNK 165
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75446"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75446"
SQ SEQUENCE 182 AA; 20745 MW; 0F3378B3EDC06E8C CRC64;
MNGFSTEEDS REGPPAAPAA APGYGQSCCL IADGERCVRP AGNASFSKRV QKSISQKKLK
LDIDKSVRHL YICDFHKNFI QSVRNKRKRK ASDDGGDSPE HDADIPEVDL FQLQVNTLRR
YKRHYKLQTR PGFNKAQLAE TVSRHFRNIP VNEKETLAYF IYMVKSNRSR LDQKSEGSKQ
LE
