SATB2_MOUSE
ID SATB2_MOUSE Reviewed; 733 AA.
AC Q8VI24;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=DNA-binding protein SATB2;
DE AltName: Full=Special AT-rich sequence-binding protein 2;
GN Name=Satb2; Synonyms=Kiaa1034;
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 1), AND DEVELOPMENTAL STAGE.
RX PubMed=12915443; DOI=10.1093/hmg/ddg248;
RA FitzPatrick D.R., Carr I.M., McLaren L., Leek J.P., Wightman P.,
RA Williamson K., Gautier P., McGill N., Hayward C., Firth H., Markham A.F.,
RA Fantes J.A., Bonthron D.T.;
RT "Identification of SATB2 as the cleft palate gene on 2q32-q33.";
RL Hum. Mol. Genet. 12:2491-2501(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
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 [3]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ATF4 AND RUNX2, AND TISSUE
RP SPECIFICITY.
RX PubMed=16751105; DOI=10.1016/j.cell.2006.05.012;
RA Dobreva G., Chahrour M., Dautzenberg M., Chirivella L., Kanzler B.,
RA Farinas I., Karsenty G., Grosschedl R.;
RT "SATB2 is a multifunctional determinant of craniofacial patterning and
RT osteoblast differentiation.";
RL Cell 125:971-986(2006).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18255030; DOI=10.1016/j.neuron.2007.12.012;
RA Alcamo E.A., Chirivella L., Dautzenberg M., Dobreva G., Farinas I.,
RA Grosschedl R., McConnell S.K.;
RT "Satb2 regulates callosal projection neuron identity in the developing
RT cerebral cortex.";
RL Neuron 57:364-377(2008).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18255031; DOI=10.1016/j.neuron.2007.12.028;
RA Britanova O., de Juan Romero C., Cheung A., Kwan K.Y., Schwark M.,
RA Gyorgy A., Vogel T., Akopov S., Mitkovski M., Agoston D., Sestan N.,
RA Molnar Z., Tarabykin V.;
RT "Satb2 is a postmitotic determinant for upper-layer neuron specification in
RT the neocortex.";
RL Neuron 57:378-392(2008).
RN [6]
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).
CC -!- FUNCTION: Binds to DNA, at nuclear matrix- or scaffold-associated
CC regions. Thought to recognize the sugar-phosphate structure of double-
CC stranded DNA. Transcription factor controlling nuclear gene expression,
CC by binding to matrix attachment regions (MARs) of DNA and inducing a
CC local chromatin-loop remodeling. Acts as a docking site for several
CC chromatin remodeling enzymes and also by recruiting corepressors
CC (HDACs) or coactivators (HATs) directly to promoters and enhancers.
CC Required for the initiation of the upper-layer neurons (UL1) specific
CC genetic program and for the inactivation of deep-layer neurons (DL) and
CC UL2 specific genes, probably by modulating Bcl11b expression. Repressor
CC of Ctip2 and regulatory determinant of corticocortical connections in
CC the developing cerebral cortex. May play an important role in palate
CC formation. Acts as a molecular node in a transcriptional network
CC regulating skeletal development and osteoblast differentiation.
CC {ECO:0000269|PubMed:16751105, ECO:0000269|PubMed:18255030,
CC ECO:0000269|PubMed:18255031}.
CC -!- SUBUNIT: Interacts with PIAS1 (By similarity). Interacts with ATF4 and
CC RUNX2; resulting in enhanced DNA binding and transactivation by these
CC transcription factors. {ECO:0000250, ECO:0000269|PubMed:16751105}.
CC -!- INTERACTION:
CC Q8VI24; P53564: Cux1; NbExp=3; IntAct=EBI-5737999, EBI-642309;
CC Q8VI24; O09106: Hdac1; NbExp=4; IntAct=EBI-5737999, EBI-301912;
CC Q8VI24; Q9R190: Mta2; NbExp=2; IntAct=EBI-5737999, EBI-904134;
CC Q8VI24; Q60698: Ski; NbExp=3; IntAct=EBI-5737999, EBI-15969860;
CC Q8VI24; P12755: SKI; Xeno; NbExp=2; IntAct=EBI-5737999, EBI-347281;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000255|PROSITE-
CC ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00374}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VI24-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VI24-2; Sequence=VSP_008967;
CC -!- TISSUE SPECIFICITY: Expressed in cortical neurons that extend axons
CC across the corpus callosum. Also expressed in branchial arches and in
CC cells of the osteoblast lineage, but not in chondrocytes and
CC osteoclasts. {ECO:0000269|PubMed:16751105,
CC ECO:0000269|PubMed:18255030}.
CC -!- DEVELOPMENTAL STAGE: Expression first detected at 10.5 dpc in the
CC maxillary component of the first pharyngeal arch and the lateral aspect
CC of the frontonasal process in the regions that will subsequently fuse
CC to form the primary palate. At 11 - 11.5 dpc, the expression pattern
CC demarcates the region of the medial aspect of the maxillary process
CC within the primitive oral cavity, which will form the palate shelf. By
CC 12.5 dpc, symmetrical expression is seen in the medial edges of the
CC developing palate shelves and this continues until 13.5 dpc when the
CC strongest expression is in the mesenchyme underlying the medial edge
CC epithelia. By the time of palatal shelf fusion at 14.5 dpc the
CC expression is dramatically down-regulated. No expression detected
CC elsewhere in the embryo at any stage examined.
CC {ECO:0000269|PubMed:12915443}.
CC -!- PTM: Sumoylated by PIAS1. Sumoylation promotes nuclear localization,
CC but represses transcription factor activity (By similarity).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Malformations in 2 of the major axonal tracts
CC interconnecting the cortical hemispheres: the corpus callosum (c.c) and
CC the anterior commissure (a.c). Misrouted afferent and efferent cortical
CC axon connections. Impaired migration of upper-layer neurons. Ectopic
CC expression of Ctip2. Craniofacial abnormalities and defects in
CC osteoblast differentiation and function. {ECO:0000269|PubMed:16751105,
CC ECO:0000269|PubMed:18255030, ECO:0000269|PubMed:18255031}.
CC -!- SIMILARITY: Belongs to the CUT homeobox family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98080.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF319623; AAL37172.1; -; mRNA.
DR EMBL; AK129270; BAC98080.1; ALT_INIT; mRNA.
DR CCDS; CCDS14965.1; -. [Q8VI24-1]
DR RefSeq; NP_631885.1; NM_139146.2. [Q8VI24-1]
DR RefSeq; XP_017175119.1; XM_017319630.1.
DR RefSeq; XP_017175120.1; XM_017319631.1.
DR AlphaFoldDB; Q8VI24; -.
DR SMR; Q8VI24; -.
DR BioGRID; 229351; 6.
DR DIP; DIP-60021N; -.
DR IntAct; Q8VI24; 93.
DR MINT; Q8VI24; -.
DR STRING; 10090.ENSMUSP00000110057; -.
DR iPTMnet; Q8VI24; -.
DR PhosphoSitePlus; Q8VI24; -.
DR MaxQB; Q8VI24; -.
DR PaxDb; Q8VI24; -.
DR PRIDE; Q8VI24; -.
DR ProteomicsDB; 255459; -. [Q8VI24-1]
DR ProteomicsDB; 255460; -. [Q8VI24-2]
DR Antibodypedia; 19915; 321 antibodies from 41 providers.
DR DNASU; 212712; -.
DR Ensembl; ENSMUST00000042857; ENSMUSP00000046067; ENSMUSG00000038331. [Q8VI24-2]
DR Ensembl; ENSMUST00000114415; ENSMUSP00000110057; ENSMUSG00000038331. [Q8VI24-1]
DR GeneID; 212712; -.
DR KEGG; mmu:212712; -.
DR UCSC; uc007bas.1; mouse. [Q8VI24-1]
DR UCSC; uc011wlc.1; mouse. [Q8VI24-2]
DR CTD; 23314; -.
DR MGI; MGI:2679336; Satb2.
DR VEuPathDB; HostDB:ENSMUSG00000038331; -.
DR eggNOG; KOG3755; Eukaryota.
DR GeneTree; ENSGT00390000008096; -.
DR HOGENOM; CLU_012559_1_0_1; -.
DR InParanoid; Q8VI24; -.
DR OMA; KXGLLSE; -.
DR OrthoDB; 204499at2759; -.
DR PhylomeDB; Q8VI24; -.
DR TreeFam; TF332714; -.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR BioGRID-ORCS; 212712; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Satb2; mouse.
DR PRO; PR:Q8VI24; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8VI24; protein.
DR Bgee; ENSMUSG00000038331; Expressed in facial bone and 153 other tissues.
DR ExpressionAtlas; Q8VI24; baseline and differential.
DR Genevisible; Q8VI24; MM.
DR GO; GO:0000785; C:chromatin; IC:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:MGI.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IC:NTNU_SB.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IGI:MGI.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IDA:MGI.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0002076; P:osteoblast development; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR CDD; cd00086; homeodomain; 1.
DR CDD; cd11585; SATB1_N; 1.
DR Gene3D; 1.10.260.40; -; 2.
DR Gene3D; 1.10.260.70; -; 1.
DR Gene3D; 3.10.20.710; -; 1.
DR InterPro; IPR003350; CUT_dom.
DR InterPro; IPR032355; CUTL.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR039673; SATB1/SATB2.
DR InterPro; IPR038216; SATB_CUTL_sf.
DR InterPro; IPR038224; SATB_ULD_sf.
DR InterPro; IPR032392; ULD.
DR PANTHER; PTHR15116; PTHR15116; 1.
DR Pfam; PF02376; CUT; 2.
DR Pfam; PF16557; CUTL; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF16534; ULD; 1.
DR SMART; SM01109; CUT; 2.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 2.
DR PROSITE; PS51042; CUT; 2.
DR PROSITE; PS51983; CUTL; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS51982; ULD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Chromosomal rearrangement;
KW Developmental protein; DNA-binding; Homeobox; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..733
FT /note="DNA-binding protein SATB2"
FT /id="PRO_0000202401"
FT DOMAIN 57..158
FT /note="ULD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01326"
FT DOMAIN 161..234
FT /note="CUTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01327"
FT DNA_BIND 350..437
FT /note="CUT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 473..560
FT /note="CUT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 615..674
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..610
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..712
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPW6"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPW6"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPW6"
FT MOD_RES 467
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPW6"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPW6"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPW6"
FT CROSSLNK 30
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPW6"
FT CROSSLNK 161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPW6"
FT CROSSLNK 233
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UPW6"
FT CROSSLNK 475
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPW6"
FT CROSSLNK 724
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPW6"
FT VAR_SEQ 58..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_008967"
SQ SEQUENCE 733 AA; 82559 MW; 153CFD1CC3491F25 CRC64;
MERRSESPCL RDSPDRRSGS PDVKGPPPVK VARLEQNGSP MGARGRPNGA VAKAVGGLMI
PVFCVVEQLD GSLEYDNREE HAEFVLVRKD VLFSQLVETA LLALGYSHSS AAQAQGIIKL
GRWNPLPLSY VTDAPDATVA DMLQDVYHVV TLKIQLQSCS KLEDLPAEQW NHATVRNALK
ELLKEMNQST LAKECPLSQS MISSIVNSTY YANVSATKCQ EFGRWYKKYK KIKVERVERE
NLSDYCVLGQ RPMHLPNMNQ LASLGKTNEQ SPHSQIHHST PIRNQVPALQ PIMSPGLLSP
QLSPQLVRQQ IAMAHLINQQ IAVSRLLAHQ HPQAINQQFL NHPPIPRAVK PEPTNSSVEV
SPDIYQQVRD ELKRASVSQA VFARVAFNRT QGLLSEILRK EEDPRTASQS LLVNLRAMQN
FLNLPEVERD RIYQDERERS MNPNVSMVSS ASSSPSSSRT PQAKTSTPTT DLPIKVDGAN
VNITAAIYDE IQQEMKRAKV SQALFAKVAA NKSQGWLCEL LRWKENPSPE NRTLWENLCT
IRRFLNLPQH ERDVIYEEES RHHHSERMQH VVQLPPEPVQ VLHRQQSQPT KESSPPREEA
PPPPPPTEDS CAKKPRSRTK ISLEALGILQ SFIHDVGLYP DQEAIHTLSA QLDLPKHTII
KFFQNQRYHV KHHGKLKEHL GSAVDVAEYK DEELLTESEE NDSEEGSEEM YKVEAEEENA
DKSKAAPAET DQR
