SBNO2_HUMAN
ID SBNO2_HUMAN Reviewed; 1366 AA.
AC Q9Y2G9; A8K8P2; B3KWJ1; O75257; Q3KQX0; Q8TEM0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein strawberry notch homolog 2;
GN Name=SBNO2; Synonyms=KIAA0963;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 102-1366 (ISOFORM 1).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 898-1366 (ISOFORM 1).
RC TISSUE=Skin;
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 [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [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. Inhibits the DCSTAMP-repressive
CC activity of TAL1, hence enhancing the access of the transcription
CC factor MITF to the DC-STAMP promoter in osteoclast. Plays a role in
CC bone homeostasis; required as a positive regulator in TNFSF11//RANKL-
CC mediated osteoclast fusion via a DCSTAMP-dependent pathway. May also be
CC required in the regulation of osteoblast differentiation (By
CC similarity). Involved in the transcriptional corepression of NF-kappaB
CC in macrophages (PubMed:18025162). Plays a role as a regulator in the
CC pro-inflammatory cascade (PubMed:18025162).
CC {ECO:0000250|UniProtKB:Q7TNB8, ECO:0000269|PubMed:18025162}.
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.
CC {ECO:0000250|UniProtKB:Q7TNB8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2G9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2G9-3; Sequence=VSP_041216;
CC -!- TISSUE SPECIFICITY: Detected in macrophages. IL10 regulates expression
CC in a STAT3-dependent way. {ECO:0000269|PubMed:18025162}.
CC -!- INDUCTION: Up-regulated by interleukin IL6 and soluble interleukin
CC receptor IL6R in astrocytes (PubMed:25903009).
CC {ECO:0000269|PubMed:25903009}.
CC -!- SIMILARITY: Belongs to the SBNO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC28919.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA76807.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB84928.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB023180; BAA76807.2; ALT_INIT; mRNA.
DR EMBL; AK125139; BAG54153.1; -; mRNA.
DR EMBL; AK292407; BAF85096.1; -; mRNA.
DR EMBL; AC005390; AAC28919.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK074102; BAB84928.1; ALT_FRAME; mRNA.
DR EMBL; BC106021; AAI06022.1; -; mRNA.
DR CCDS; CCDS45894.1; -. [Q9Y2G9-1]
DR CCDS; CCDS45895.1; -. [Q9Y2G9-3]
DR PIR; T02748; T02748.
DR RefSeq; NP_001093592.1; NM_001100122.1. [Q9Y2G9-3]
DR RefSeq; NP_055778.2; NM_014963.2. [Q9Y2G9-1]
DR AlphaFoldDB; Q9Y2G9; -.
DR BioGRID; 116568; 6.
DR IntAct; Q9Y2G9; 3.
DR STRING; 9606.ENSP00000354733; -.
DR iPTMnet; Q9Y2G9; -.
DR PhosphoSitePlus; Q9Y2G9; -.
DR BioMuta; SBNO2; -.
DR DMDM; 166233537; -.
DR EPD; Q9Y2G9; -.
DR jPOST; Q9Y2G9; -.
DR MassIVE; Q9Y2G9; -.
DR MaxQB; Q9Y2G9; -.
DR PaxDb; Q9Y2G9; -.
DR PeptideAtlas; Q9Y2G9; -.
DR PRIDE; Q9Y2G9; -.
DR ProteomicsDB; 85775; -. [Q9Y2G9-1]
DR ProteomicsDB; 85776; -. [Q9Y2G9-3]
DR Antibodypedia; 63340; 42 antibodies from 10 providers.
DR DNASU; 22904; -.
DR Ensembl; ENST00000361757.8; ENSP00000354733.2; ENSG00000064932.16. [Q9Y2G9-1]
DR Ensembl; ENST00000438103.6; ENSP00000400762.1; ENSG00000064932.16. [Q9Y2G9-3]
DR Ensembl; ENST00000612198.3; ENSP00000477651.1; ENSG00000278788.4. [Q9Y2G9-1]
DR Ensembl; ENST00000622719.2; ENSP00000482802.1; ENSG00000278788.4. [Q9Y2G9-3]
DR Ensembl; ENST00000631948.1; ENSP00000488808.1; ENSG00000278788.4. [Q9Y2G9-1]
DR GeneID; 22904; -.
DR KEGG; hsa:22904; -.
DR MANE-Select; ENST00000361757.8; ENSP00000354733.2; NM_014963.3; NP_055778.2.
DR UCSC; uc002lrj.5; human. [Q9Y2G9-1]
DR CTD; 22904; -.
DR DisGeNET; 22904; -.
DR GeneCards; SBNO2; -.
DR HGNC; HGNC:29158; SBNO2.
DR HPA; ENSG00000064932; Low tissue specificity.
DR MIM; 615729; gene.
DR neXtProt; NX_Q9Y2G9; -.
DR OpenTargets; ENSG00000064932; -.
DR PharmGKB; PA162402390; -.
DR VEuPathDB; HostDB:ENSG00000064932; -.
DR eggNOG; KOG1513; Eukaryota.
DR GeneTree; ENSGT00940000159946; -.
DR InParanoid; Q9Y2G9; -.
DR OMA; ARHSHKR; -.
DR OrthoDB; 141580at2759; -.
DR PhylomeDB; Q9Y2G9; -.
DR TreeFam; TF313526; -.
DR PathwayCommons; Q9Y2G9; -.
DR SignaLink; Q9Y2G9; -.
DR BioGRID-ORCS; 22904; 31 hits in 1083 CRISPR screens.
DR ChiTaRS; SBNO2; human.
DR GenomeRNAi; 22904; -.
DR Pharos; Q9Y2G9; Tbio.
DR PRO; PR:Q9Y2G9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9Y2G9; protein.
DR Bgee; ENSG00000064932; Expressed in blood and 94 other tissues.
DR ExpressionAtlas; Q9Y2G9; baseline and differential.
DR Genevisible; Q9Y2G9; HS.
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; IEA:Ensembl.
DR GO; GO:0061430; P:bone trabecula morphogenesis; IEA:Ensembl.
DR GO; GO:0071348; P:cellular response to interleukin-11; ISS:UniProtKB.
DR GO; GO:0071354; P:cellular response to interleukin-6; IDA:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0002281; P:macrophage activation involved in immune response; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0030316; P:osteoclast differentiation; IBA:GO_Central.
DR GO; GO:0072675; P:osteoclast fusion; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Activator; Alternative splicing; Differentiation; Osteogenesis;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1366
FT /note="Protein strawberry notch homolog 2"
FT /id="PRO_0000314560"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1324..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..197
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..636
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..93
FT /note="MLAVGPAMDRDYPQHEPPPAGSLLYSPPPLQSAMLHCPYWNTFSLPPYPAFS
FT SDSRPFMSSASFLGSQPCPDTSYAPVATASSLPPKTCDFAQ -> MREPLPGSASWGTP
FT GPPSAGTMSQLQLWLQFEALNK (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041216"
FT CONFLICT 545
FT /note="K -> R (in Ref. 2; BAF85096)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="S -> F (in Ref. 2; BAG54153)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="P -> S (in Ref. 1; BAA76807 and 4; BAB84928)"
FT /evidence="ECO:0000305"
FT CONFLICT 724
FT /note="R -> Q (in Ref. 4; BAB84928)"
FT /evidence="ECO:0000305"
FT CONFLICT 1343
FT /note="A -> G (in Ref. 4; BAB84928)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1366 AA; 150275 MW; 6AE084F984DDEC2E CRC64;
MLAVGPAMDR DYPQHEPPPA GSLLYSPPPL QSAMLHCPYW NTFSLPPYPA FSSDSRPFMS
SASFLGSQPC PDTSYAPVAT ASSLPPKTCD FAQDSSYFED FSNISIFSSS VDSLSDIVDT
PDFLPADSLN QVSTIWDDNP APSTHDKLFQ LSRPFAGFED FLPSHSTPLL VSYQEQSVQS
QPEEEDEAEE EEAEELGHTE TYADYVPSKS KIGKQHPDRV VETSTLSSVP PPDITYTLAL
PSDSGALSAL QLEAITYACQ QHEVLLPSGQ RAGFLIGDGA GVGKGRTVAG VILENHLRGR
KKALWFSVSN DLKYDAERDL RDIEATGIAV HALSKIKYGD TTTSEGVLFA TYSALIGESQ
AGGQHRTRLR QILDWCGEAF EGVIVFDECH KAKNAGSTKM GKAVLDLQNK LPLARVVYAS
ATGASEPRNM IYMSRLGIWG EGTPFRNFEE FLHAIEKRGV GAMEIVAMDM KVSGMYIARQ
LSFSGVTFRI EEIPLAPAFE CVYNRAALLW AEALNVFQQA ADWIGLESRK SLWGQFWSAH
QRFFKYLCIA AKVRRLVELA REELARDKCV VIGLQSTGEA RTREVLGEND GHLNCFVSAA
EGVFLSLIQK HFPSTKRKRD RGAGSKRKRR PRGRGAKAPR LACETAGVIR ISDDSSTESD
PGLDSDFNSS PESLVDDDVV IVDAVGLPSD DRGPLCLLQR DPHGPGVLER VERLKQDLLD
KVRRLGRELP VNTLDELIDQ LGGPQRVAEM TGRKGRVVSR PDGTVAFESR AEQGLSIDHV
NLREKQRFMS GEKLVAIISE ASSSGVSLQA DRRVQNQRRR VHMTLELPWS ADRAIQQFGR
THRSNQVSAP EYVFLISELA GERRFASIVA KRLESLGALT HGDRRATESR DLSKYNFENK
YGTRALHCVL TTILSQTENK VPVPQGYPGG VPTFFRDMKQ GLLSVGIGGR ESRNGCLDVE
KDCSITKFLN RILGLEVHKQ NALFQYFSDT FDHLIEMDKR EGKYDMGILD LAPGIEEIYE
ESQQVFLAPG HPQDGQVVFY KISVDRGLKW EDAFAKSLAL TGPYDGFYLS YKVRGNKPSC
LLAEQNRGQF FTVYKPNIGR QSQLEALDSL RRKFHRVTAE EAKEPWESGY ALSLTHCSHS
AWNRHCRLAQ EGKDCLQGLR LRHHYMLCGA LLRVWGRIAA VMADVSSSSY LQIVRLKTKD
RKKQVGIKIP EGCVRRVLQE LRLMDADVKR RQAPALGCPA PPAPRPLALP CGPGEVLDLT
YSPPAEAFPP PPHFSFPAPL SLDAGPGVVP LGTPDAQADP AALAHQGCDI NFKEVLEDML
RSLHAGPPSE GALGEGAGAG GAAGGGPERQ SVIQFSPPFP GAQAPL
