Satb1
entrez
20230
canonical
uniprot
Q60611
canonical
ensembl
ENSMUSG00000023927
resolver
ensp
ENSMUSP00000116006
resolver
ensp
ENSMUSP00000116020
resolver
ensp
ENSMUSP00000118839
resolver
ensp
ENSMUSP00000119842
resolver
ensp
ENSMUSP00000120536
resolver
ensp
ENSMUSP00000128841
resolver
ensp
ENSMUSP00000134957
resolver
ensp
ENSMUSP00000199932
resolver
ensp
ENSMUSP00000199934
resolver
ensp
ENSMUSP00000199938
resolver
ensp
ENSMUSP00000199941
resolver
ensp
ENSMUSP00000199942
resolver
ensp
ENSMUSP00000199946
resolver
ensp
ENSMUSP00000199947
resolver
ensp
ENSMUSP00000199948
resolver
enst
ENSMUST00000129667
resolver
enst
ENSMUST00000133574
resolver
enst
ENSMUST00000140979
resolver
enst
ENSMUST00000144331
resolver
enst
ENSMUST00000152830
resolver
enst
ENSMUST00000169480
resolver
enst
ENSMUST00000176669
resolver
genesymbol
Satb1
resolver
uniprot
E9PVB7
resolver
uniprot
Q91XB1
resolver
uniprot_entry
E9PVB7_MOUSE
resolver
uniprot_entry
SATB1_MOUSE
resolver
uniprot_sec
Q91XB1
resolver
amino_acid_sequence
MDHLNEATQGKEHSEMSNNVSDPKGPPAKIARLEQNGSPLGRGRLGSTGGKMQGVPLKHSGHLMKTNLRKGTMLPVFCVVEHYENAIEYDCKEEHAEFVLVRKDMLFNQLIEMALLSLGYSHSSAAQAKGLIQVGKWNPVPLSYVTDAPDATVADMLQDVYHVVTLKIQLHSCPKLEDLPPEQWSHTTVRNALKDLLKDMNQSSLAKECPLSQSMISSIVNSTYYANVSAAKCQEFGRWYKHFKKTKDMMVEMDSLSELSQQGANHVNFGQQPVPGNTAEQPPSPAQLSHGSQPSVRTPLPNLHPGLVSTPISPQLVNQQLVMAQLLNQQYAVNRLLAQQSLNQQYLNHPPPVSRSMNKPLEQQVSTNTEVSSEIYQWVRDELKRAGISQAVFARVAFNRTQGLLSEILRKEEDPKTASQSLLVNLRAMQNFLQLPEAERDRIYQDERERSLNAASAMGPAPLLSTPPSRPPQVKTATLATERNGKPENNTMNINASIYDEIQQEMKRAKVSQALFAKVAATKSQGWLCELLRWKEDPSPENRTLWENLSMIRRFLSLPQPERDAIYEQESNAVHHHGDRPPHIIHVPAEQIQQQQQQQQQQQQQQQPPPPPPQPQPQPQAGPRLPPRQPTVASSAESDEENRQKTRPRTKISVEALGILQSFIQDVGLYPDEEAIQTLSAQLDLPKYTIIKFFQNQRYYLKHHGKLKDNSGLEVDVAEYKDEELLKDLEESVQDKNANTLFSVKLEEELSVEGSTDVNADLKD
uniprot
proteins
function
FUNCTION: Required for the switching of fetal globin species, and beta- and gamma-globin genes regulation during erythroid differentiation. Plays a role in chromatin organization and nuclear architecture during apoptosis (By similarity). Crucial silencing factor contributing to the initiation of X inactivation mediated by Xist RNA that occurs during embryogenesis and in lymphoma. Binds to DNA at special AT-rich sequences, the consensus SATB1-binding sequence (CSBS), at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcriptional repressor controlling nuclear and viral gene expression in a phosphorylated and acetylated status-dependent manner, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Modulates genes that are essential in the maturation of the immune T-cell CD8SP from thymocytes. Promotes neuronal differentiation of neural stem/progenitor cells in the adult subventricular zone, possibly by positively regulating the expression of NEUROD1 (PubMed:26305964). {ECO:0000250, ECO:0000269|PubMed:10716941, ECO:0000269|PubMed:11463840, ECO:0000269|PubMed:12692553, ECO:0000269|PubMed:15814699, ECO:0000269|PubMed:17057718, ECO:0000269|PubMed:18722016, ECO:0000269|PubMed:19103759, ECO:0000269|PubMed:19386260, ECO:0000269|PubMed:26305964, ECO:0000269|PubMed:9271405}.
uniprot
proteins
mass_dalton
85880
uniprot
proteins
post_translational_modification
PTM: Sumoylated. Sumoylation promotes cleavage by caspases. {ECO:0000250}.; PTM: Phosphorylated by PKC. Acetylated by PCAF. Phosphorylated form interacts with HDAC1, but unphosphorylated form interacts with PCAF. DNA binding properties are activated by phosphorylation and inactivated by acetylation. In opposition, gene expression is down-regulated by phosphorylation but up-regulated by acetylation (By similarity). {ECO:0000250}.; PTM: Cleaved at Asp-254 by caspase-3 and caspase-6 during T-cell apoptosis in thymus and during B-cell stimulation. The cleaved forms cannot dimerize and lose transcription regulation function because of impaired DNA and chromatin association. {ECO:0000269|PubMed:11463840}.
uniprot
proteins
protein_family
CUT homeobox family
uniprot
proteins
pubmed
10373541
uniprot
proteins
pubmed
10716941
uniprot
proteins
pubmed
11463840
uniprot
proteins
pubmed
12692553
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15814699
uniprot
proteins
pubmed
15851481
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17057718
uniprot
proteins
pubmed
18722016
uniprot
proteins
pubmed
19103759
uniprot
proteins
pubmed
19386260
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
26305964
uniprot
proteins
pubmed
8114718
uniprot
proteins
pubmed
9271405
uniprot
proteins
sequence_length
764
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Note=Organized into a cage-like network anchoring loops of heterochromatin and tethering specialized DNA sequences. When sumoylated, localized in promyelocytic leukemia nuclear bodies (PML NBs) (By similarity). {ECO:0000250}.
uniprot
proteins