SBNO2_MOUSE
ID SBNO2_MOUSE Reviewed; 1349 AA.
AC Q7TNB8; Q3UE14; Q6P3A3; Q70X02;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein strawberry notch homolog 2;
GN Name=Sbno2; Synonyms=Sno, Stno;
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] (ISOFORM 2).
RC STRAIN=PRM/Alf; TISSUE=Skin;
RA Da Silva N.R., Aubin-Houzelstein G., Bernex F., Salaun P., Panthier J.J.;
RT "Strawberry notch operates in the niche of melanocyte stem cells.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Dendritic cell;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Thymus;
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 TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18025162; DOI=10.4049/jimmunol.179.11.7215;
RA El Kasmi K.C., Smith A.M., Williams L., Neale G., Panopolous A.,
RA Watowich S.S., Hacker H., Foxwell B.M., Murray P.J.;
RT "A transcriptional repressor and corepressor induced by the STAT3-regulated
RT anti-inflammatory signaling pathway.";
RL J. Immunol. 179:7215-7219(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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, INTERACTION WITH TAL1, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=23980096; DOI=10.1084/jem.20130512;
RA Maruyama K., Uematsu S., Kondo T., Takeuchi O., Martino M.M., Kawasaki T.,
RA Akira S.;
RT "Strawberry notch homologue 2 regulates osteoclast fusion by enhancing the
RT expression of DC-STAMP.";
RL J. Exp. Med. 210:1947-1960(2013).
RN [7]
RP INDUCTION.
RX PubMed=25903009; DOI=10.1002/glia.22841;
RA Grill M., Syme T.E., Nocon A.L., Lu A.Z., Hancock D., Rose-John S.,
RA Campbell I.L.;
RT "Strawberry notch homolog 2 is a novel inflammatory response factor
RT predominantly but not exclusively expressed by astrocytes in the central
RT nervous system.";
RL Glia 63:1738-1752(2015).
CC -!- FUNCTION: Acts as a transcriptional coregulator, that can have both
CC coactivator and corepressor functions (PubMed:18025162,
CC PubMed:23980096). Inhibits the DCSTAMP-repressive activity of TAL1,
CC hence enhancing the access of the transcription factor MITF to the DC-
CC STAMP promoter in osteoclast (PubMed:23980096). Plays a role in bone
CC homeostasis; required as a positive regulator in TNFSF11//RANKL-
CC mediated osteoclast fusion via a DCSTAMP-dependent pathway
CC (PubMed:23980096). May also be required in the regulation of osteoblast
CC differentiation (PubMed:23980096). Involved in the transcriptional
CC corepression of NF-kappaB in macrophages. Plays a role as a regulator
CC in the pro-inflammatory cascade (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y2G9, ECO:0000269|PubMed:23980096}.
CC -!- SUBUNIT: Interacts with TAL1; this interaction inhibits TAL1 occupancy
CC of the DCSTAMP promoter, leading to the activation of the DCSTAMP
CC promoter by the transcription factor MITF (PubMed:23980096).
CC {ECO:0000269|PubMed:23980096}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7TNB8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TNB8-2; Sequence=VSP_030309;
CC Name=3;
CC IsoId=Q7TNB8-3; Sequence=VSP_030305, VSP_030306, VSP_030307,
CC VSP_030308;
CC -!- TISSUE SPECIFICITY: Expressed in the spleen and bone marrow, and to a
CC lesser extent in the kidney, liver, brain, skin, heart and muscle
CC (PubMed:23980096). Expressed predominantly in osteoclasts, and to a
CC lesser extent in T-cells, B-cells and osteoblasts (PubMed:23980096).
CC Expressed in macrophages (PubMed:18025162).
CC {ECO:0000269|PubMed:18025162, ECO:0000269|PubMed:23980096}.
CC -!- INDUCTION: Up-regulated by interleukin IL6 together with soluble
CC interleukin receptor IL6R in astrocytes (PubMed:25903009). Up-regulated
CC by interleukins such as IL1B or tumor necrosis factor TNF in astrocytes
CC (at protein level) (PubMed:25903009). Up-regulated by interleukin IL6
CC together with soluble interleukin receptor IL6R in astrocytes
CC (PubMed:25903009). Up-regulated also by other cytokines such as
CC interleukin IL11, oncostatin M (OSM) and leukemia inhibitory factor
CC (LIF) (PubMed:25903009). Up-regulated by interleukin such as IL1B or
CC tumor necrosis factor TNF in astrocytes (PubMed:25903009). Up-regulated
CC by lipopolysaccharide (LPS) (PubMed:25903009, PubMed:23980096). Up-
CC regulated by interleukin IL10 in a STAT3-dependent manner in bone
CC marrow derived macrophages (PubMed:18025162). Up-regulated by
CC TNFSF11//RANKL in a c-Fos/FOS-dependent manner (PubMed:23980096).
CC {ECO:0000269|PubMed:18025162, ECO:0000269|PubMed:23980096,
CC ECO:0000269|PubMed:25903009}.
CC -!- DISRUPTION PHENOTYPE: Mice display a severe osteopetrotic phenotype
CC characterized with an increased bone mass (PubMed:23980096). Show a
CC reduction in the osteoclast surface/bone surface and eroded
CC surface/bone surface ratio, but the osteoclast number/bone surface
CC ratio is normal (PubMed:23980096). Show also a reduction in
CC nuclei/osteoclast ratio (PubMed:23980096). Exhibit an impairment in
CC TNFSF11//RANKL-mediated osteoclast fusion (PubMed:23980096). Show a
CC slight inhibition of osteoblast differentiation (PubMed:23980096).
CC {ECO:0000269|PubMed:23980096}.
CC -!- SIMILARITY: Belongs to the SBNO 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; AJ512611; CAD54758.1; -; mRNA.
DR EMBL; AK149806; BAE29097.1; -; mRNA.
DR EMBL; AK155674; BAE33382.1; -; mRNA.
DR EMBL; BC056369; AAH56369.1; -; mRNA.
DR EMBL; BC064113; AAH64113.1; -; mRNA.
DR CCDS; CCDS24008.1; -. [Q7TNB8-1]
DR RefSeq; NP_906271.1; NM_183426.1. [Q7TNB8-1]
DR RefSeq; XP_006513555.1; XM_006513492.1. [Q7TNB8-1]
DR RefSeq; XP_006513556.1; XM_006513493.1. [Q7TNB8-1]
DR RefSeq; XP_006513557.1; XM_006513494.1. [Q7TNB8-1]
DR RefSeq; XP_006513558.1; XM_006513495.2. [Q7TNB8-2]
DR RefSeq; XP_006513559.1; XM_006513496.2.
DR AlphaFoldDB; Q7TNB8; -.
DR BioGRID; 229712; 1.
DR IntAct; Q7TNB8; 2.
DR STRING; 10090.ENSMUSP00000041635; -.
DR iPTMnet; Q7TNB8; -.
DR PhosphoSitePlus; Q7TNB8; -.
DR EPD; Q7TNB8; -.
DR MaxQB; Q7TNB8; -.
DR PaxDb; Q7TNB8; -.
DR PeptideAtlas; Q7TNB8; -.
DR PRIDE; Q7TNB8; -.
DR ProteomicsDB; 256840; -. [Q7TNB8-1]
DR ProteomicsDB; 256841; -. [Q7TNB8-2]
DR ProteomicsDB; 256842; -. [Q7TNB8-3]
DR Antibodypedia; 63340; 42 antibodies from 10 providers.
DR DNASU; 216161; -.
DR Ensembl; ENSMUST00000042771; ENSMUSP00000041635; ENSMUSG00000035673. [Q7TNB8-1]
DR Ensembl; ENSMUST00000219260; ENSMUSP00000151590; ENSMUSG00000035673. [Q7TNB8-1]
DR GeneID; 216161; -.
DR KEGG; mmu:216161; -.
DR UCSC; uc007gbm.1; mouse. [Q7TNB8-2]
DR UCSC; uc007gbn.1; mouse. [Q7TNB8-1]
DR UCSC; uc007gbq.1; mouse. [Q7TNB8-3]
DR CTD; 22904; -.
DR MGI; MGI:2448490; Sbno2.
DR VEuPathDB; HostDB:ENSMUSG00000035673; -.
DR eggNOG; KOG1513; Eukaryota.
DR GeneTree; ENSGT00940000159946; -.
DR HOGENOM; CLU_000212_0_0_1; -.
DR InParanoid; Q7TNB8; -.
DR OMA; ARHSHKR; -.
DR OrthoDB; 141580at2759; -.
DR PhylomeDB; Q7TNB8; -.
DR TreeFam; TF313526; -.
DR BioGRID-ORCS; 216161; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Sbno2; mouse.
DR PRO; PR:Q7TNB8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q7TNB8; protein.
DR Bgee; ENSMUSG00000035673; Expressed in granulocyte and 216 other tissues.
DR ExpressionAtlas; Q7TNB8; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR GO; GO:0061430; P:bone trabecula morphogenesis; IMP:MGI.
DR GO; GO:0071348; P:cellular response to interleukin-11; IDA:UniProtKB.
DR GO; GO:0071354; P:cellular response to interleukin-6; IDA:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IDA:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR GO; GO:0002281; P:macrophage activation involved in immune response; IMP:UniProtKB.
DR GO; GO:0072674; P:multinuclear osteoclast differentiation; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0030316; P:osteoclast differentiation; IMP:MGI.
DR GO; GO:0072675; P:osteoclast fusion; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR030410; SBNO2.
DR InterPro; IPR026937; SBNO_Helicase_C_dom.
DR InterPro; IPR026741; SNO.
DR InterPro; IPR039187; SNO_AAA.
DR PANTHER; PTHR12706; PTHR12706; 1.
DR PANTHER; PTHR12706:SF5; PTHR12706:SF5; 1.
DR Pfam; PF13872; AAA_34; 1.
DR Pfam; PF13871; Helicase_C_4; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Differentiation; Osteogenesis;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1349
FT /note="Protein strawberry notch homolog 2"
FT /id="PRO_0000314561"
FT REGION 170..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..191
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..630
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..74
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030305"
FT VAR_SEQ 75..89
FT /note="ATVPSFFSKSSDFPQ -> MSQLRFWLQFAALNK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030306"
FT VAR_SEQ 688..729
FT /note="SLYPLQRDLQGPGVVERVERLKQGLLAKVRALGRELPVNTLD -> EPPSSS
FT QTQGSRHNHMRPIPPNTLVTDGETETHSQGQGYAIK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030307"
FT VAR_SEQ 730..1349
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030308"
FT VAR_SEQ 1036
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_030309"
FT CONFLICT 595
FT /note="A -> G (in Ref. 2; BAE29097)"
FT /evidence="ECO:0000305"
FT CONFLICT 972
FT /note="H -> R (in Ref. 2; BAE29097)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1349 AA; 149294 MW; 0F7F42BA691770DE CRC64;
MLAVEPTMDG DFPPHELPPP GGGIQLQNRL LHCPWWGSFS PSLYPTFSSE NQQFVGSTPF
LGGQSCPETS YPTTATVPSF FSKSSDFPQD PSCLEDLSNA SVFSSSVDSL SDIPDTPDFL
QADSLNEVPT IWDVSTTSTT HDKLFIPSGP FSAPEDPVTS LSSTPLLISY QSHSQPEEEE
GEEEEETEEL GHAETYADYV PSKSKIGKQH PDRVVETSTL SSVPPPDITY TLALPTSDNS
TLSALQLEAI TYACQQHEVL LPSGQRAGFL IGDGAGVGKG RTVAGIIVEN YLRGRKKALW
FSASNDLKYD AERDLRDIEA PGIAVHALSK IKYGDNTTSE GVLFATYSAL IGESQAGGQH
RTRLRQILQW CGEGFDGVIV FDECHKAKNA SSTKMGKAVL DLQSKLPQAR VVYASATGAS
EPRNMIYMSR LGIWGEGTPF RTFEEFLHAI EKRGVGAMEI VAMDMKVSGM YIARQLSFSG
VTFRIEEIPL SPAFQQVYNR AARLWAEALS VFQQAADWIG LESRKSLWGQ FWSAHQRFFK
YLCIAAKVHR LVELAQQELS RDKCVVIGLQ STGEARTREV LDENEGRLDC FVSAAEGVFL
SLIQKHFPST RRRRDRGGGK RKRRPRGRGP KASRLSLEAA GVIRISDGSS TESDAGLDSD
FNSSPESLVD DDVVIVDAPT HPTDDRGSLY PLQRDLQGPG VVERVERLKQ GLLAKVRALG
RELPVNTLDQ LIHQLGGPEC VAEMTGRKGR VVSRPDGTVV FESRAEQGLS IDHVNLREKQ
RFMSGEKLVA IISEASSSGV SLQADRRVQN QRRRVHMTLE LPWSADRAIQ QFGRTHRSNQ
VSAPEYVFLI SELAGERRFA SIVAKRLESL GALTHGDRRA TESRDLSKYN FENKYGARAL
SRVLATIMGQ TDNRVPLPQG YPGGDTAFFR DMKQGLLSVG IGSRESRSGC LDVEKDCSIT
KFLNRILGLE VHKQNALFQY FSDTFDHLIE IDKKEGRYDM GILDLAPGIN EIHEESQQVF
LAPGHPQDGQ VVFYKQISVD RGMKWEEALT RSLELKGPYD GFYLSYKVRG SKMSCLLAEQ
NRGEYFTVYK PNIGRQSQLE TLDSLCRKFH RVTVEEAREP WESSYALSLE HCSHTTWNQR
CRLTQEGKCC AQGLRLRHHY MLCGALLRVW GRIAAVMADV SSSSYLQIVR LKTKDKKKQV
GIKIPEGCVH RVLQELQLMD AEVKRRSTHG LAARPPTPRA ITLPCGPGEV LDLTYSPPAE
AFPTPPRFAF PSLPPPDPSS LMLGARDPAT NPVELAHQSC DINFREVLED MLRSLRAGPT
ETPAPLVGVG GGGTERQSVI HFSPPFPNS
