SANBR_MOUSE
ID SANBR_MOUSE Reviewed; 718 AA.
AC Q68FF0; A2AF87; A2AF88; A2AF89; A2AF91; A2AF92; Q3UQL0; Q6GQU5; Q6ZPH2;
AC Q8BPK6; Q9CWA7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=SANT and BTB domain regulator of class switch recombination {ECO:0000250|UniProtKB:Q6NSI8};
DE Short=SANT and BTB domain regulator of CSR;
GN Name=Sanbr {ECO:0000250|UniProtKB:Q6NSI8}; Synonyms=Kiaa1841;
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 MRNA] (ISOFORM 1).
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-335 AND 536-718 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Eye, Heart, and Kidney;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [6]
RP FUNCTION, SUBUNIT, DOMAIN, AND INTERACTION WITH HDAC1 AND NCOR2.
RX PubMed=33831416; DOI=10.1016/j.jbc.2021.100625;
RA Zheng S., Matthews A.J., Rahman N., Herrick-Reynolds K., Sible E.,
RA Choi J.E., Wishnie A., Ng Y.K., Rhodes D., Elledge S.J., Vuong B.Q.;
RT "The uncharacterized SANT and BTB domain-containing protein SANBR inhibits
RT class switch recombination.";
RL J. Biol. Chem. 296:100625-100625(2021).
CC -!- FUNCTION: Negatively regulates class switch recombination or isotype
CC switching in splenic B-cells. {ECO:0000269|PubMed:33831416}.
CC -!- SUBUNIT: Homodimer (PubMed:33831416). Interacts (via the BTB domain)
CC with HDAC1 and NCOR2 (PubMed:33831416). {ECO:0000269|PubMed:33831416}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q68FF0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68FF0-2; Sequence=VSP_032303;
CC -!- DOMAIN: The BTB domain is important for homodimerization and for its
CC function in negative regulation of class switch recombination.
CC {ECO:0000269|PubMed:33831416}.
CC -!- SIMILARITY: Belongs to the KIAA1841 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH72622.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC98264.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAM16941.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM16943.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM16946.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK129454; BAC98264.1; ALT_INIT; mRNA.
DR EMBL; AL672049; CAM16941.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL672049; CAM16942.1; -; Genomic_DNA.
DR EMBL; AL672049; CAM16943.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL672049; CAM16945.1; -; Genomic_DNA.
DR EMBL; AL672049; CAM16946.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC072622; AAH72622.1; ALT_FRAME; mRNA.
DR EMBL; BC079876; AAH79876.1; -; mRNA.
DR EMBL; AK002465; BAB22119.1; -; mRNA.
DR EMBL; AK053838; BAC35550.1; -; mRNA.
DR EMBL; AK142320; BAE25029.1; -; mRNA.
DR CCDS; CCDS36119.1; -. [Q68FF0-1]
DR CCDS; CCDS88137.1; -. [Q68FF0-2]
DR RefSeq; NP_001334171.1; NM_001347242.1. [Q68FF0-2]
DR RefSeq; NP_082136.2; NM_027860.3. [Q68FF0-1]
DR RefSeq; XP_006514870.1; XM_006514807.3.
DR RefSeq; XP_006514871.1; XM_006514808.3. [Q68FF0-1]
DR RefSeq; XP_011242051.1; XM_011243749.1. [Q68FF0-1]
DR RefSeq; XP_017170257.1; XM_017314768.1. [Q68FF0-1]
DR RefSeq; XP_017170259.1; XM_017314770.1.
DR AlphaFoldDB; Q68FF0; -.
DR SMR; Q68FF0; -.
DR STRING; 10090.ENSMUSP00000044265; -.
DR iPTMnet; Q68FF0; -.
DR PhosphoSitePlus; Q68FF0; -.
DR MaxQB; Q68FF0; -.
DR PaxDb; Q68FF0; -.
DR PRIDE; Q68FF0; -.
DR ProteomicsDB; 269132; -. [Q68FF0-1]
DR ProteomicsDB; 269133; -. [Q68FF0-2]
DR Antibodypedia; 30587; 58 antibodies from 13 providers.
DR Ensembl; ENSMUST00000043356; ENSMUSP00000044265; ENSMUSG00000042208. [Q68FF0-1]
DR Ensembl; ENSMUST00000093267; ENSMUSP00000090955; ENSMUSG00000042208. [Q68FF0-2]
DR Ensembl; ENSMUST00000109532; ENSMUSP00000105158; ENSMUSG00000042208. [Q68FF0-1]
DR Ensembl; ENSMUST00000180260; ENSMUSP00000136118; ENSMUSG00000042208. [Q68FF0-1]
DR GeneID; 71675; -.
DR KEGG; mmu:71675; -.
DR UCSC; uc007ifh.1; mouse. [Q68FF0-1]
DR CTD; 84542; -.
DR MGI; MGI:1918925; 0610010F05Rik.
DR VEuPathDB; HostDB:ENSMUSG00000042208; -.
DR eggNOG; ENOG502QRE4; Eukaryota.
DR GeneTree; ENSGT00390000008178; -.
DR HOGENOM; CLU_016494_0_0_1; -.
DR InParanoid; Q68FF0; -.
DR OMA; ECAKRFE; -.
DR OrthoDB; 904755at2759; -.
DR PhylomeDB; Q68FF0; -.
DR TreeFam; TF324503; -.
DR BioGRID-ORCS; 71675; 3 hits in 72 CRISPR screens.
DR ChiTaRS; 0610010F05Rik; mouse.
DR PRO; PR:Q68FF0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q68FF0; protein.
DR Bgee; ENSMUSG00000042208; Expressed in trigeminal ganglion and 234 other tissues.
DR ExpressionAtlas; Q68FF0; baseline and differential.
DR Genevisible; Q68FF0; MM.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0045190; P:isotype switching; IDA:UniProtKB.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR045902; SANBR-like.
DR InterPro; IPR021777; SANBR_BTB.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR20946; PTHR20946; 1.
DR Pfam; PF11822; DUF3342; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Reference proteome.
FT CHAIN 1..718
FT /note="SANT and BTB domain regulator of class switch
FT recombination"
FT /id="PRO_0000324599"
FT DOMAIN 21..59
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 147..255
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 555..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..146
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032303"
FT CONFLICT 149
FT /note="I -> V (in Ref. 4; BAC35550)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="I -> L (in Ref. 3; AAH79876)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 718 AA; 81996 MW; F8730D777D57C272 CRC64;
MSRGYPENNN FLNNNNQMVL DMILYPLIGI PQTINWETVA RLVPGLTPKE CVKRFDELKS
CGSSPVDNQY NPLMATGEGP VETLATYIKS SLLDTQGDFQ ETPVDQDTVS KAGRHSIATT
RNCSSESENC TARNAGEETG ESEGPNMVIH VCDEAKSLKE DFICPRDLLI SEMKYFAEYL
SMDAQRWEEV DISVHCDVHI FNWLIKYVKR NTKESKDCEI PALEPGNVIS ILISSEFLKM
DSLVEQCIQY CHKNMNAIVA APCNMNCINA NLLTRIADLF THNEIDDLKD KKDKFRSKLF
CKKIERLFDP EYSNPDSRNN AATLYRCCLC KKLLTRETER RIPCIPGKIN VDRHGNIIYI
HIRDKTWDVH EYLNSLFEEL KSWRDVYWRL WGTVNWLTCS RCYQAFLCIE FSHCQYHSEV
VVYSSTVNSL NTVGTGIYPC CNQKVLRFDP TQLTKGCKVR DHMVVLHDQG ENDDSPSCPP
AKILDDLHKH KDVIAVPFLK DAVSDPGVGS CDEKGLEYEI LLEPNTPWGS KTGELNAFLS
LKNWTLQLKQ QSLFSEEEEY TTGSEVTEDE VGDEEEIAKK QRKKEKPKKF TKPPKKQLSS
PCSQKKEKTL EKSTSRDVSP FVVSMQKNKW DASRSLRFNQ DAQREDDQRR MSEITGHLIK
MRLGDLDRVK AKESKEFAGG IYSRLEAQVR ASVPVTARQN SSDKNQRSKS RFGQGRPA
