SAP25_MOUSE
ID SAP25_MOUSE Reviewed; 186 AA.
AC Q1EHW4;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Histone deacetylase complex subunit SAP25;
DE AltName: Full=25 kDa Sin3-associated polypeptide;
DE AltName: Full=Sin3 corepressor complex subunit SAP25;
DE AltName: Full=mSin3A-binding protein;
GN Name=Sap25;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH SIN3A AND HDAC2.
RX PubMed=16449650; DOI=10.1128/mcb.26.4.1386-1397.2006;
RA Shiio Y., Rose D.W., Aur R., Donohoe S., Aebersold R., Eisenman R.N.;
RT "Identification and characterization of SAP25, a novel component of the
RT mSin3 corepressor complex.";
RL Mol. Cell. Biol. 26:1386-1397(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP STRUCTURE BY NMR OF 126-186 IN COMPLEX WITH SIN3A.
RX PubMed=18089292; DOI=10.1016/j.jmb.2007.11.079;
RA Sahu S.C., Swanson K.A., Kang R.S., Huang K., Brubaker K., Ratcliff K.,
RA Radhakrishnan I.;
RT "Conserved themes in target recognition by the PAH1 and PAH2 domains of the
RT Sin3 transcriptional corepressor.";
RL J. Mol. Biol. 375:1444-1456(2008).
CC -!- FUNCTION: Involved in the transcriptional repression mediated by the
CC mSIN3A but not the N-CoR corepressor complex.
CC {ECO:0000269|PubMed:16449650}.
CC -!- SUBUNIT: May be a component of the mSIN3A corepressor complex.
CC Interacts with SIN3A and HDAC2. {ECO:0000269|PubMed:16449650,
CC ECO:0000269|PubMed:18089292}.
CC -!- INTERACTION:
CC Q1EHW4; Q60520: Sin3a; NbExp=4; IntAct=EBI-937195, EBI-349034;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16449650}. Cytoplasm
CC {ECO:0000269|PubMed:16449650}. Note=Shuttles between the nucleus and
CC the cytoplasm.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16449650}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK164339; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AM275337; CAK36853.1; -; mRNA.
DR EMBL; AK164339; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK158025; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001075431.2; NM_001081962.2.
DR PDB; 2RMS; NMR; -; B=126-186.
DR PDBsum; 2RMS; -.
DR AlphaFoldDB; Q1EHW4; -.
DR BMRB; Q1EHW4; -.
DR SMR; Q1EHW4; -.
DR CORUM; Q1EHW4; -.
DR IntAct; Q1EHW4; 31.
DR STRING; 10090.ENSMUSP00000127076; -.
DR PhosphoSitePlus; Q1EHW4; -.
DR PaxDb; Q1EHW4; -.
DR PRIDE; Q1EHW4; -.
DR ProteomicsDB; 256700; -.
DR DNASU; 751865; -.
DR GeneID; 751865; -.
DR KEGG; mmu:751865; -.
DR CTD; 100316904; -.
DR MGI; MGI:3802945; Sap25.
DR eggNOG; ENOG502SWKH; Eukaryota.
DR InParanoid; Q1EHW4; -.
DR OrthoDB; 1577943at2759; -.
DR PhylomeDB; Q1EHW4; -.
DR BioGRID-ORCS; 751865; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Sap25; mouse.
DR EvolutionaryTrace; Q1EHW4; -.
DR PRO; PR:Q1EHW4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q1EHW4; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR IDEAL; IID50088; -.
DR InterPro; IPR029163; SAP25.
DR PANTHER; PTHR39231; PTHR39231; 1.
DR Pfam; PF15476; SAP25; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..186
FT /note="Histone deacetylase complex subunit SAP25"
FT /id="PRO_0000350874"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:2RMS"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:2RMS"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:2RMS"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2RMS"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2RMS"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2RMS"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2RMS"
SQ SEQUENCE 186 AA; 19845 MW; CAAACACC24E15246 CRC64;
MSPLPLRDPS HQANAGPRLV EPSCGPGVSL SNRTLCHPSW PMYDNWGRSP TTSERPEEEQ
VVSKDTGVPV RNYEDVFLLD PLLPCGQRVP LILTKPPQQA MDSRKLLLPP PIMSPSVHPS
SSQACSSTWL SEAEMIALAG LLQMSQGEQT PNCVASSLPS TSCPDPVSVS EDPGPSGDQS
CSGTDT
