SATB1
entrez
6304
canonical
uniprot
Q01826
canonical
ensembl
ENSG00000182568
resolver
ensp
ENSP00000341024
resolver
ensp
ENSP00000390529
resolver
ensp
ENSP00000399518
resolver
ensp
ENSP00000399708
resolver
ensp
ENSP00000514846
resolver
ensp
ENSP00000514848
resolver
ensp
ENSP00000611527
resolver
ensp
ENSP00000611529
resolver
genesymbol
SATB1
resolver
hgnc
HGNC:10541
resolver
uniprot
B3KXF1
resolver
uniprot
C9JTR6
resolver
uniprot
Q59EQ0
resolver
uniprot_entry
SATB1_HUMAN
resolver
uniprot_sec
B3KXF1
resolver
uniprot_sec
C9JTR6
resolver
uniprot_sec
Q59EQ0
resolver
amino_acid_sequence
MDHLNEATQGKEHSEMSNNVSDPKGPPAKIARLEQNGSPLGRGRLGSTGAKMQGVPLKHSGHLMKTNLRKGTMLPVFCVVEHYENAIEYDCKEEHAEFVLVRKDMLFNQLIEMALLSLGYSHSSAAQAKGLIQVGKWNPVPLSYVTDAPDATVADMLQDVYHVVTLKIQLHSCPKLEDLPPEQWSHTTVRNALKDLLKDMNQSSLAKECPLSQSMISSIVNSTYYANVSAAKCQEFGRWYKHFKKTKDMMVEMDSLSELSQQGANHVNFGQQPVPGNTAEQPPSPAQLSHGSQPSVRTPLPNLHPGLVSTPISPQLVNQQLVMAQLLNQQYAVNRLLAQQSLNQQYLNHPPPVSRSMNKPLEQQVSTNTEVSSEIYQWVRDELKRAGISQAVFARVAFNRTQGLLSEILRKEEDPKTASQSLLVNLRAMQNFLQLPEAERDRIYQDERERSLNAASAMGPAPLISTPPSRPPQVKTATIATERNGKPENNTMNINASIYDEIQQEMKRAKVSQALFAKVAATKSQGWLCELLRWKEDPSPENRTLWENLSMIRRFLSLPQPERDAIYEQESNAVHHHGDRPPHIIHVPAEQIQQQQQQQQQQQQQQQAPPPPQPQQQPQTGPRLPPRQPTVASPAESDEENRQKTRPRTKISVEALGILQSFIQDVGLYPDEEAIQTLSAQLDLPKYTIIKFFQNQRYYLKHHGKLKDNSGLEVDVAEYKEEELLKDLEESVQDKNTNTLFSVKLEEELSVEGNTDINTDLKD
uniprot
proteins
disease_involvement
DISEASE: Den Hoed-de Boer-Voisin syndrome (DHDBV) [MIM:619229]: A disorder characterized by global developmental delay, moderately to severely impaired intellectual development, poor or absent speech, delayed motor skills, and early-onset epilepsy in many patients. Most affected individuals have feeding difficulties, poor overall growth, dysmorphic facial features, and significant dental anomalies resembling amelogenesis imperfecta. More variable features include visual defects, behavioral abnormalities, and non-specific involvement of other organ systems. DHDBV transmission pattern is consistent with autosomal dominant inheritance with incomplete penetrance and variable expressivity. {ECO:0000269|PubMed:33513338}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Developmental delay with dysmorphic facies and dental anomalies (DEFDA) [MIM:619228]: A disorder characterized by mild global developmental delay, impaired intellectual development, walking by 2 to 3 years, and slow language acquisition. The severity of the disorder ranges from moderate cognitive deficits to mild learning difficulties or behavioral abnormalities. Most patients have dysmorphic facial features, abnormal dentition and non-specific visual defects. DEFDA transmission pattern is consistent with autosomal dominant inheritance with incomplete penetrance and variable expressivity. {ECO:0000269|PubMed:33513338}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Crucial silencing factor contributing to the initiation of X inactivation mediated by Xist RNA that occurs during embryogenesis and in lymphoma (By similarity). 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 (e.g. PML at the MHC-I locus) 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. 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. Interacts with the unique region (UR) of cytomegalovirus (CMV). Alu-like motifs and SATB1-binding sites provide a unique chromatin context which seems preferentially targeted by the HIV-1 integration machinery. Moreover, HIV-1 Tat may overcome SATB1-mediated repression of IL2 and IL2RA (interleukin) in T-cells by binding to the same domain as HDAC1. Delineates specific epigenetic modifications at target gene loci, directly up-regulating metastasis-associated genes while down-regulating tumor-suppressor genes. Reprograms chromatin organization and the transcription profiles of breast tumors to promote growth and metastasis. Promotes neuronal differentiation of neural stem/progenitor cells in the adult subventricular zone, possibly by positively regulating the expression of NEUROD1 (By similarity). {ECO:0000250|UniProtKB:Q60611, ECO:0000269|PubMed:10595394, ECO:0000269|PubMed:11463840, ECO:0000269|PubMed:12374985, ECO:0000269|PubMed:12692553, ECO:0000269|PubMed:1505028, ECO:0000269|PubMed:15618465, ECO:0000269|PubMed:15713622, ECO:0000269|PubMed:16377216, ECO:0000269|PubMed:16630892, ECO:0000269|PubMed:17173041, ECO:0000269|PubMed:17376900, ECO:0000269|PubMed:18337816, ECO:0000269|PubMed:19103759, ECO:0000269|PubMed:19247486, ECO:0000269|PubMed:19332023, ECO:0000269|PubMed:19430959, ECO:0000269|PubMed:33513338, ECO:0000269|PubMed:9111059, ECO:0000269|PubMed:9548713}.
uniprot
proteins
mass_dalton
85957
uniprot
proteins
mutagenesis
MUTAGEN 29; /note="K->A: Loss of nuclear localization, cytoplasmic."; /evidence="ECO:0000269|PubMed:15970696"; MUTAGEN 32; /note="R->A: Loss of nuclear localization, cytoplasmic."; /evidence="ECO:0000269|PubMed:15970696"; MUTAGEN 34; /note="E->A: Normal nuclear localization."; /evidence="ECO:0000269|PubMed:15970696"; MUTAGEN 36; /note="N->A: Normal nuclear localization."; /evidence="ECO:0000269|PubMed:15970696"; MUTAGEN 136; /note="K->A,Q,R: No acetylation."; /evidence="ECO:0000269|PubMed:16630892, ECO:0000269|PubMed:19103759"; MUTAGEN 185; /note="S->A: No phosphorylation."; /evidence="ECO:0000269|PubMed:16630892"; MUTAGEN 254; /note="D->A: CASP6-resistant."; /evidence="ECO:0000269|PubMed:11463840"; MUTAGEN 373; /note="S->A: Slightly reduced MAR-DNA-binding."; /evidence="ECO:0000269|PubMed:16371359"; MUTAGEN 380; /note="R->N: Reduced MAR-DNA-binding."; /evidence="ECO:0000269|PubMed:16371359"; MUTAGEN 384; /note="K->N: Impaired MAR-DNA-binding."; /evidence="ECO:0000269|PubMed:16371359"; MUTAGEN 395; /note="R->N: Reduced MAR-DNA-binding."; /evidence="ECO:0000269|PubMed:16371359"; MUTAGEN 402; /note="Q->A: Impaired MAR-DNA-binding."; /evidence="ECO:0000269|PubMed:17652321"; MUTAGEN 403; /note="G->A: Impaired MAR-DNA-binding."; /evidence="ECO:0000269|PubMed:17652321"; MUTAGEN 406; /note="S->A: Impaired MAR-DNA-binding."; /evidence="ECO:0000269|PubMed:16371359"; MUTAGEN 410; /note="R->N: Impaired MAR-DNA-binding."; /evidence="ECO:0000269|PubMed:16371359"; MUTAGEN 411; /note="K->R: Normal sumoylation."; /evidence="ECO:0000269|PubMed:18408014"; MUTAGEN 416; /note="K->N: Impaired MAR-DNA-binding."; /evidence="ECO:0000269|PubMed:16371359"; MUTAGEN 427; /note="R->N: Reduced MAR-DNA-binding."; /evidence="ECO:0000269|PubMed:16371359"; MUTAGEN 442; /note="R->N: Reduced MAR-DNA-binding."; /evidence="ECO:0000269|PubMed:16371359"; MUTAGEN 451; /note="S->A: Slightly reduced MAR-DNA-binding."; /evidence="ECO:0000269|PubMed:16371359"; MUTAGEN 475; /note="K->N: Reduced MAR-DNA-binding."; /evidence="ECO:0000269|PubMed:16371359"; MUTAGEN 486; /note="K->R: Normal sumoylation."; /evidence="ECO:0000269|PubMed:18408014"; MUTAGEN 646; /note="R->A: Reduced interaction with matrix attachment region (MAR) DNA; when associated with A-648."; /evidence="ECO:0000269|PubMed:9111059"; MUTAGEN 648; /note="R->A: Reduced interaction with matrix attachment region (MAR) DNA; when associated with A-646."; /evidence="ECO:0000269|PubMed:9111059"; MUTAGEN 693..695; /note="FQN->AAA: Reduced interaction with matrix attachment region (MAR) DNA."; /evidence="ECO:0000269|PubMed:9111059"; MUTAGEN 720; /note="K->R: Normal sumoylation."; /evidence="ECO:0000269|PubMed:18408014"; MUTAGEN 744; /note="K->R: Loss of sumoylation."; /evidence="ECO:0000269|PubMed:18408014
uniprot
proteins
post_translational_modification
PTM: Sumoylated. Sumoylation promotes cleavage by caspases. {ECO:0000269|PubMed:15561718, ECO:0000269|PubMed:18408014}.; 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. {ECO:0000269|PubMed:16630892}.; 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:15561718, ECO:0000269|PubMed:18408014}.
uniprot
proteins
protein_family
CUT homeobox family
uniprot
proteins
pubmed
10595394
uniprot
proteins
pubmed
10800076
uniprot
proteins
pubmed
11463840
uniprot
proteins
pubmed
12036295
uniprot
proteins
pubmed
12374985
uniprot
proteins
pubmed
12692553
uniprot
proteins
pubmed
14605447
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1505028
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15561718
uniprot
proteins
pubmed
15618465
uniprot
proteins
pubmed
15713622
uniprot
proteins
pubmed
15851481
uniprot
proteins
pubmed
15970696
uniprot
proteins
pubmed
16079286
uniprot
proteins
pubmed
16371359
uniprot
proteins
pubmed
16377216
uniprot
proteins
pubmed
16630892
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17173041
uniprot
proteins
pubmed
17376900
uniprot
proteins
pubmed
17512569
uniprot
proteins
pubmed
17652321
uniprot
proteins
pubmed
18187506
uniprot
proteins
pubmed
18337816
uniprot
proteins
pubmed
18408014
uniprot
proteins
pubmed
19103759
uniprot
proteins
pubmed
19247486
uniprot
proteins
pubmed
19332023
uniprot
proteins
pubmed
19430959
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
33513338
uniprot
proteins
pubmed
9111059
uniprot
proteins
pubmed
9548713
uniprot
proteins
sequence_length
763
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:10800076, ECO:0000269|PubMed:18408014}. Nucleus, PML body {ECO:0000269|PubMed:18408014}. Note=Organized into a cage-like network anchoring loops of heterochromatin and tethering specialized DNA sequences (PubMed:12692553). When sumoylated, localized in promyelocytic leukemia nuclear bodies (PML NBs) (PubMed:18408014). {ECO:0000269|PubMed:12692553, ECO:0000269|PubMed:18408014}.
uniprot
proteins