Q01826 (SATB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-binding protein SATB1

Alternative name(s):
Special AT-rich sequence-binding protein 1

Gene names

Name:

SATB1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	763 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 than HDAC1. Delineates specific epigenetic modifications at target gene loci, directly upregulating metastasis-associated genes while downregulating tumor-suppressor genes. Reprograms chromatin organization and the transcription profiles of breast tumors to promote growth and metastasis. Ref.1 Ref.7 Ref.8 Ref.9 Ref.11 Ref.13 Ref.15 Ref.16 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.28 Ref.31 Ref.32 Ref.33 Ref.34
Subunit structure	Interacts (via DNA-binding domains) with CUX1; leading to inhibit the attachment to DNA By similarity. Homodimer. Part of the nuclear protein complex gamma-globin promoter and enhancer binding factor (gamma-PE) composed at least by SATB1 and HOXB2. Interaction with CtBP1 when not acetylated stabalizes attachment to DNA and promotes transcription repression. Interacts with PCAF. Interacts with sumoylated PML, HDAC1 and HIV-1 Tat via the PDZ-like dimerization domain. Interacts also with DYNLT3 and POLR2J2. Binds to EP300. Ref.11 Ref.12 Ref.14 Ref.20 Ref.21 Ref.23 Ref.25 Ref.26 Ref.29 Ref.33
Subcellular location	Nucleus matrix. 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). Ref.1 Ref.10 Ref.15 Ref.17 Ref.19 Ref.20 Ref.27
Tissue specificity	Expressed predominantly in thymus. Ref.1
Post-translational modification	Sumoylated. Sumoylation promotes cleavage by caspases. Ref.18 Ref.27 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. Ref.23 Cleaved at Asp-254 by caspase-3 and caspase-6 during T-cell apoptosis in thymus and during B-cell stimulation. The cleaved forms can not dimerize and lose transcription regulation function because of impaired DNA and chromatin association. Ref.10 Ref.11 Ref.22 Ref.27
Sequence similarities	Belongs to the CUT homeobox family. Contains 2 CUT DNA-binding domains. Contains 1 homeobox DNA-binding domain.
Sequence caution	The sequence BAD92998.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Domain	Homeobox Repeat
Ligand	DNA-binding
Molecular function	Chromatin regulator Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular component disassembly involved in apoptosis Traceable author statement. Source: Reactome interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.19. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	PML body Inferred from direct assay Ref.27. Source: UniProtKB nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	double-stranded DNA binding Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction Ref.27. Source: IntAct sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CASP6	P55212	2	EBI-743747,EBI-718729
SUMO1	P63165	2	EBI-743747,EBI-80140

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q01826-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q01826-2)

The sequence of this isoform differs from the canonical sequence as follows:
     592-592: I → IQSPSPTTLGKGESRGVFLPGLPTPAPWLGAAP

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 763

763

DNA-binding protein SATB1

PRO_0000202398

Regions

DNA binding

361 – 448

88

CUT 1

DNA binding

484 – 571

88

CUT 2

DNA binding

645 – 704

60

Homeobox

Region

90 – 204

115

PDZ-like dimerization domain

Region

224 – 278

55

Nuclear matrix targeting sequence (NMTS)

Region

400 – 410

11

Matrix attachment region (MAR) DNA-binding

Motif

20 – 40

21

Nuclear localization signal Ref.17

Motif

139 – 143

5

Protein interaction

Compositional bias

591 – 607

17

Poly-Gln

Compositional bias

609 – 614

6

Poly-Pro

Sites

Binding site

390

1

Matrix attachment region (MAR) DNA

Binding site

425

1

Matrix attachment region (MAR) DNA

Site

254 – 255

2

Cleavage; by caspases

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.30

Modified residue

136

1

N6-acetyllysine Ref.23

Modified residue

185

1

Phosphoserine Ref.23

Cross-link

744

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.27

Natural variations

Alternative sequence

592

1

I → IQSPSPTTLGKGESRGVFLP GLPTPAPWLGAAP in isoform 2.

VSP_038296

Experimental info

Mutagenesis

29

1

K → A: Loss of nuclear localization, cytoplasmic. Ref.17

Mutagenesis

32

1

R → A: Loss of nuclear localization, cytoplasmic. Ref.17

Mutagenesis

34

1

E → A: Normal nuclear localization. Ref.17

Mutagenesis

36

1

N → A: Normal nuclear localization. Ref.17

Mutagenesis

136

1

K → A, Q or R: No acetylation. Ref.23 Ref.33

Mutagenesis

185

1

S → A: No phosphorylation. Ref.23

Mutagenesis

254

1

D → A: CASP6-resistant. Ref.11

Mutagenesis

373

1

S → A: Slightly reduced MAR-DNA-binding. Ref.35

Mutagenesis

380

1

R → N: Reduced MAR-DNA-binding. Ref.35

Mutagenesis

384

1

K → N: Impaired MAR-DNA-binding. Ref.35

Mutagenesis

395

1

R → N: Reduced MAR-DNA-binding. Ref.35

Mutagenesis

402

1

Q → A: Impaired MAR-DNA-binding. Ref.36

Mutagenesis

403

1

G → A: Impaired MAR-DNA-binding. Ref.36

Mutagenesis

406

1

S → A: Impaired MAR-DNA-binding. Ref.35

Mutagenesis

410

1

R → N: Impaired MAR-DNA-binding. Ref.35

Mutagenesis

411

1

K → R: Normal sumoylation. Ref.27

Mutagenesis

416

1

K → N: Impaired MAR-DNA-binding. Ref.35

Mutagenesis

427

1

R → N: Reduced MAR-DNA-binding. Ref.35

Mutagenesis

442

1

R → N: Reduced MAR-DNA-binding. Ref.35

Mutagenesis

451

1

S → A: Slightly reduced MAR-DNA-binding. Ref.35

Mutagenesis

475

1

K → N: Reduced MAR-DNA-binding. Ref.35

Mutagenesis

486

1

K → R: Normal sumoylation. Ref.27

Mutagenesis

646

1

R → A: Reduced interaction with matrix attachment region (MAR) DNA; when associated with A-648. Ref.7

Mutagenesis

648

1

R → A: Reduced interaction with matrix attachment region (MAR) DNA; when associated with A-646. Ref.7

Mutagenesis

693 – 695

3

FQN → AAA: Reduced interaction with matrix attachment region (MAR) DNA. Ref.7

Mutagenesis

720

1

K → R: Normal sumoylation. Ref.27

Mutagenesis

744

1

K → R: Loss of sumoylation. Ref.27

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

763

Helix Strand Turn

Details...

Helix

375 – 386

12

Helix

390 – 398

9

Helix

402 – 411

10

Helix

415 – 417

3

Helix

420 – 433

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: D4FE09B09FB7683B	FASTA	763	85,957
	10 20 30 40 50 60 MDHLNEATQG KEHSEMSNNV SDPKGPPAKI ARLEQNGSPL GRGRLGSTGA KMQGVPLKHS 70 80 90 100 110 120 GHLMKTNLRK GTMLPVFCVV EHYENAIEYD CKEEHAEFVL VRKDMLFNQL IEMALLSLGY 130 140 150 160 170 180 SHSSAAQAKG LIQVGKWNPV PLSYVTDAPD ATVADMLQDV YHVVTLKIQL HSCPKLEDLP 190 200 210 220 230 240 PEQWSHTTVR NALKDLLKDM NQSSLAKECP LSQSMISSIV NSTYYANVSA AKCQEFGRWY 250 260 270 280 290 300 KHFKKTKDMM VEMDSLSELS QQGANHVNFG QQPVPGNTAE QPPSPAQLSH GSQPSVRTPL 310 320 330 340 350 360 PNLHPGLVST PISPQLVNQQ LVMAQLLNQQ YAVNRLLAQQ SLNQQYLNHP PPVSRSMNKP 370 380 390 400 410 420 LEQQVSTNTE VSSEIYQWVR DELKRAGISQ AVFARVAFNR TQGLLSEILR KEEDPKTASQ 430 440 450 460 470 480 SLLVNLRAMQ NFLQLPEAER DRIYQDERER SLNAASAMGP APLISTPPSR PPQVKTATIA 490 500 510 520 530 540 TERNGKPENN TMNINASIYD EIQQEMKRAK VSQALFAKVA ATKSQGWLCE LLRWKEDPSP 550 560 570 580 590 600 ENRTLWENLS MIRRFLSLPQ PERDAIYEQE SNAVHHHGDR PPHIIHVPAE QIQQQQQQQQ 610 620 630 640 650 660 QQQQQQQAPP PPQPQQQPQT GPRLPPRQPT VASPAESDEE NRQKTRPRTK ISVEALGILQ 670 680 690 700 710 720 SFIQDVGLYP DEEAIQTLSA QLDLPKYTII KFFQNQRYYL KHHGKLKDNS GLEVDVAEYK 730 740 750 760 EEELLKDLEE SVQDKNTNTL FSVKLEEELS VEGNTDINTD LKD
	Isoform 2 [UniParc]. Checksum: 4883C06CCD96D9FF	FASTA	795	89,127
	10 20 30 40 50 60 MDHLNEATQG KEHSEMSNNV SDPKGPPAKI ARLEQNGSPL GRGRLGSTGA KMQGVPLKHS 70 80 90 100 110 120 GHLMKTNLRK GTMLPVFCVV EHYENAIEYD CKEEHAEFVL VRKDMLFNQL IEMALLSLGY 130 140 150 160 170 180 SHSSAAQAKG LIQVGKWNPV PLSYVTDAPD ATVADMLQDV YHVVTLKIQL HSCPKLEDLP 190 200 210 220 230 240 PEQWSHTTVR NALKDLLKDM NQSSLAKECP LSQSMISSIV NSTYYANVSA AKCQEFGRWY 250 260 270 280 290 300 KHFKKTKDMM VEMDSLSELS QQGANHVNFG QQPVPGNTAE QPPSPAQLSH GSQPSVRTPL 310 320 330 340 350 360 PNLHPGLVST PISPQLVNQQ LVMAQLLNQQ YAVNRLLAQQ SLNQQYLNHP PPVSRSMNKP 370 380 390 400 410 420 LEQQVSTNTE VSSEIYQWVR DELKRAGISQ AVFARVAFNR TQGLLSEILR KEEDPKTASQ 430 440 450 460 470 480 SLLVNLRAMQ NFLQLPEAER DRIYQDERER SLNAASAMGP APLISTPPSR PPQVKTATIA 490 500 510 520 530 540 TERNGKPENN TMNINASIYD EIQQEMKRAK VSQALFAKVA ATKSQGWLCE LLRWKEDPSP 550 560 570 580 590 600 ENRTLWENLS MIRRFLSLPQ PERDAIYEQE SNAVHHHGDR PPHIIHVPAE QIQSPSPTTL 610 620 630 640 650 660 GKGESRGVFL PGLPTPAPWL GAAPQQQQQQ QQQQQQQQQA PPPPQPQQQP QTGPRLPPRQ 670 680 690 700 710 720 PTVASPAESD EENRQKTRPR TKISVEALGI LQSFIQDVGL YPDEEAIQTL SAQLDLPKYT 730 740 750 760 770 780 IIKFFQNQRY YLKHHGKLKD NSGLEVDVAE YKEEELLKDL EESVQDKNTN TLFSVKLEEE 790 LSVEGNTDIN TDLKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A tissue-specific MAR/SAR DNA-binding protein with unusual binding site recognition." Dickinson L.A., Joh T., Kohwi Y., Kohwi-Shigematsu T. Cell 70:631-645(1992) [PubMed: 1505028] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Hippocampus.
[3]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno F.R. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[4]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed: 16641997] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung.
[7]	"An atypical homeodomain in SATB1 promotes specific recognition of the key structural element in a matrix attachment region." Dickinson L.A., Dickinson C.D., Kohwi-Shigematsu T. J. Biol. Chem. 272:11463-11470(1997) [PubMed: 9111059] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ARG-646; ARG-648 AND 693-PHE--ASN-695.
[8]	"The genomic sequences bound to special AT-rich sequence-binding protein 1 (SATB1) in vivo in Jurkat T cells are tightly associated with the nuclear matrix at the bases of the chromatin loops." de Belle I., Cai S., Kohwi-Shigematsu T. J. Cell Biol. 141:335-348(1998) [PubMed: 9548713] [Abstract] Cited for: FUNCTION.
[9]	"The gammaPE complex contains both SATB1 and HOXB2 and has positive and negative roles in human gamma-globin gene regulation." Case S.S., Huber P., Lloyd J.A. DNA Cell Biol. 18:805-817(1999) [PubMed: 10595394] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE GAMMA-GLOBIN PROMOTER COMPLEX, IDENTIFICATION IN THE ENHANCER BINDING FACTOR COMPLEX.
[10]	"The fate of the nuclear matrix-associated-region-binding protein SATB1 during apoptosis." Gotzmann J., Meissner M., Gerner C. Cell Death Differ. 7:425-438(2000) [PubMed: 10800076] [Abstract] Cited for: CLEAVAGE BY CASPASES, SUBCELLULAR LOCATION.
[11]	"SATB1 cleavage by caspase 6 disrupts PDZ domain-mediated dimerization, causing detachment from chromatin early in T-cell apoptosis." Galande S., Dickinson L.A., Mian I.S., Sikorska M., Kohwi-Shigematsu T. Mol. Cell. Biol. 21:5591-5604(2001) [PubMed: 11463840] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-254, SUBUNIT, CLEAVAGE BY CASPASE-6.
[12]	"The thymocyte-specific MAR binding protein, SATB1, interacts in vitro with a novel variant of DNA-directed RNA polymerase II, subunit 11." Durrin L.K., Krontiris T.G. Genomics 79:809-817(2002) [PubMed: 12036295] [Abstract] Cited for: INTERACTION WITH POLR2J2.
[13]	"SATB1 targets chromatin remodelling to regulate genes over long distances." Yasui D., Miyano M., Cai S., Varga-Weisz P., Kohwi-Shigematsu T. Nature 419:641-645(2002) [PubMed: 12374985] [Abstract] Cited for: FUNCTION.
[14]	"SATB1 makes a complex with p300 and represses gp91(phox) promoter activity." Fujii Y., Kumatori A., Nakamura M. Microbiol. Immunol. 47:803-811(2003) [PubMed: 14605447] [Abstract] Cited for: INTERACTION WITH EP300.
[15]	"Tissue-specific nuclear architecture and gene expression regulated by SATB1." Cai S., Han H.-J., Kohwi-Shigematsu T. Nat. Genet. 34:42-51(2003) [PubMed: 12692553] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]	"SATB1 family protein expressed during early erythroid differentiation modifies globin gene expression." Wen J., Huang S., Rogers H., Dickinson L.A., Kohwi-Shigematsu T., Noguchi C.T. Blood 105:3330-3339(2005) [PubMed: 15618465] [Abstract] Cited for: FUNCTION.
[17]	"A nuclear targeting determinant for SATB1, a genome organizer in the T cell lineage." Nakayama Y., Mian I.S., Kohwi-Shigematsu T., Ogawa T. Cell Cycle 4:1099-1106(2005) [PubMed: 15970696] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-29; ARG-32; GLU-34 AND ASN-36, NUCLEAR LOCALIZATION SIGNAL.
[18]	"Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates." Gocke C.B., Yu H., Kang J. J. Biol. Chem. 280:5004-5012(2005) [PubMed: 15561718] [Abstract] Cited for: SUMOYLATION.
[19]	"Nuclear matrix binding regulates SATB1-mediated transcriptional repression." Seo J., Lozano M.M., Dudley J.P. J. Biol. Chem. 280:24600-24609(2005) [PubMed: 15851481] [Abstract] Cited for: SUBCELLULAR LOCATION, NUCLEAR MATRIX TARGETING SEQUENCE.
[20]	"Dynein light chain rp3 acts as a nuclear matrix-associated transcriptional modulator in a dynein-independent pathway." Yeh T.-Y., Chuang J.-Z., Sung C.-H. J. Cell Sci. 118:3431-3443(2005) [PubMed: 16079286] [Abstract] Cited for: INTERACTION WITH DYNLT3, SUBCELLULAR LOCATION.
[21]	"Displacement of SATB1-bound histone deacetylase 1 corepressor by the human immunodeficiency virus type 1 transactivator induces expression of interleukin-2 and its receptor in T cells." Kumar P.P., Purbey P.K., Ravi D.S., Mitra D., Galande S. Mol. Cell. Biol. 25:1620-1633(2005) [PubMed: 15713622] [Abstract] Cited for: FUNCTION, INTERACTION WITH HIV-1 TAT AND HDAC1.
[22]	"The behavior of SATB1, a MAR-binding protein, in response to apoptosis stimulation." Sun Y., Wang T., Su Y., Yin Y., Xu S., Ma C., Han X. Cell Biol. Int. 30:244-247(2006) [PubMed: 16377216] [Abstract] Cited for: FUNCTION, CLEAVAGE BY CASPASE-3.
[23]	"Phosphorylation of SATB1, a global gene regulator, acts as a molecular switch regulating its transcriptional activity in vivo." Kumar P.P., Purbey P.K., Sinha C.K., Notani D., Limaye A., Jayani R.S., Galande S. Mol. Cell 22:231-243(2006) [PubMed: 16630892] [Abstract] Cited for: FUNCTION, MASS SPECTROMETRY, INTERACTION WITH HDAC1 AND PCAF, MUTAGENESIS OF LYS-136 AND SER-185, ACETYLATION AT LYS-136, PHOSPHORYLATION AT SER-185.
[24]	"SATB1-binding sequences and Alu-like motifs define a unique chromatin context in the vicinity of human immunodeficiency virus type 1 integration sites." Kumar P.P., Mehta S., Purbey P.K., Notani D., Jayani R.S., Purohit H.J., Raje D.V., Ravi D.S., Bhonde R.R., Mitra D., Galande S. J. Virol. 81:5617-5627(2007) [PubMed: 17376900] [Abstract] Cited for: FUNCTION.
[25]	"Functional interaction between PML and SATB1 regulates chromatin-loop architecture and transcription of the MHC class I locus." Kumar P.P., Bischof O., Purbey P.K., Notani D., Urlaub H., Dejean A., Galande S. Nat. Cell Biol. 9:45-56(2007) [PubMed: 17173041] [Abstract] Cited for: FUNCTION, INTERACTION WITH PML.
[26]	"Cellular homeoproteins, SATB1 and CDP, bind to the unique region between the human cytomegalovirus UL127 and major immediate-early genes." Lee J., Klase Z., Gao X., Caldwell J.S., Stinski M.F., Kashanchi F., Chao S.-H. Virology 366:117-125(2007) [PubMed: 17512569] [Abstract] Cited for: INTERACTION WITH CYTOMEGALOVIRUS UNIQUE REGION.
[27]	"SUMO conjugation to the matrix attachment region-binding protein, special AT-rich sequence-binding protein-1 (SATB1), targets SATB1 to promyelocytic nuclear bodies where it undergoes caspase cleavage." Tan J.-A.T., Sun Y., Song J., Chen Y., Krontiris T.G., Durrin L.K. J. Biol. Chem. 283:18124-18134(2008) [PubMed: 18408014] [Abstract] Cited for: SUMOYLATION AT LYS-744, MUTAGENESIS OF LYS-411; LYS-486; LYS-720 AND LYS-744, SUBCELLULAR LOCATION, CLEAVAGE BY CASPASE-6.
[28]	"SATB1 reprogrammes gene expression to promote breast tumour growth and metastasis." Han H.-J., Russo J., Kohwi Y., Kohwi-Shigematsu T. Nature 452:187-193(2008) [PubMed: 18337816] [Abstract] Cited for: FUNCTION, ROLE IN BREAST TUMOR GROWTH AND METASTASIS.
[29]	"PDZ domain-mediated dimerization and homeodomain-directed specificity are required for high-affinity DNA binding by SATB1." Purbey P.K., Singh S., Kumar P.P., Mehta S., Ganesh K.N., Mitra D., Galande S. Nucleic Acids Res. 36:2107-2122(2008) [PubMed: 18187506] [Abstract] Cited for: SUBUNIT, INTERACTION WITH DNA AND NUCLEAR MATRIX.
[30]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[31]	"SATB1 regulates beta-like globin genes through matrix related nuclear relocation of the cluster." Gong H., Wang Z., Zhao G.-W., Lv X., Wei G.-H., Wang L., Liu D.-P., Liang C.-C. Biochem. Biophys. Res. Commun. 383:11-15(2009) [PubMed: 19332023] [Abstract] Cited for: FUNCTION.
[32]	"SATB1 binds an intronic MAR sequence in human PI3kgamma in vitro." Cai R., Xu W., Dai B., Cai X., Xu R., Lu J. Mol. Biol. Rep. 37:1461-1465(2010) [PubMed: 19430959] [Abstract] Cited for: FUNCTION.
[33]	"Acetylation-dependent interaction of SATB1 and CtBP1 mediates transcriptional repression by SATB1." Purbey P.K., Singh S., Notani D., Kumar P.P., Limaye A.S., Galande S. Mol. Cell. Biol. 29:1321-1337(2009) [PubMed: 19103759] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LYS-136, INTERACTION WITH CTBP1.
[34]	"Inter-MAR association contributes to transcriptionally active looping events in human beta-globin gene cluster." Wang L., Di L.-J., Lv X., Zheng W., Xue Z., Guo Z.-C., Liu D.-P., Liang C.-C. PLoS ONE 4:E4629-E4629(2009) [PubMed: 19247486] [Abstract] Cited for: FUNCTION.
[35]	"Solution structure and DNA-binding mode of the matrix attachment region-binding domain of the transcription factor SATB1 that regulates the T-cell maturation." Yamaguchi H., Tateno M., Yamasaki K. J. Biol. Chem. 281:5319-5327(2006) [PubMed: 16371359] [Abstract] Cited for: STRUCTURE BY NMR OF 353-490 IN COMPLEX WITH MAR DNA, MUTAGENESIS OF SER-373; ARG-380; LYS-384; ARG-395; SER-406; ARG-410; LYS-416; ARG-427; ARG-442; SER-451 AND LYS-475.
[36]	"Structural basis for recognition of the matrix attachment region of DNA by transcription factor SATB1." Yamasaki K., Akiba T., Yamasaki T., Harata K. Nucleic Acids Res. 35:5073-5084(2007) [PubMed: 17652321] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 368-452 IN COMPLEX WITH MAR DNA, MUTAGENESIS OF GLN-402 AND GLY-403.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M97287 mRNA. Translation: AAA60304.1.
AK127242 mRNA. Translation: BAG54463.1.
AB209761 mRNA. Translation: BAD92998.1. Different initiation.
AC139618 Genomic DNA. No translation available.
AC144521 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64291.1.
BC001744 mRNA. Translation: AAH01744.1.

IPI

IPI00009804.
IPI00555719.

PIR

A43314.

RefSeq

NP_001124482.1. NM_001131010.2.
NP_001182399.1. NM_001195470.1.
NP_002962.1. NM_002971.4.

UniGene

Hs.517717.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YSE	NMR	-	A	353-490	[»]
2L1P	NMR	-	A	179-250	[»]
2O49	X-ray	2.00	A	368-452	[»]
2O4A	X-ray	1.75	A	368-452	[»]
3NZL	X-ray	1.20	A	179-250	[»]

ProteinModelPortal

Q01826.

SMR

Q01826. Positions 179-250, 370-452, 486-573, 646-704.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48757N.

IntAct

Q01826. 9 interactions.

MINT

MINT-1478608.

STRING

Q01826.

PTM databases

PhosphoSite

Q01826.

Polymorphism databases

DMDM

417747.

Proteomic databases

PRIDE

Q01826.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000332610; ENSP00000333367; ENSG00000182568.
ENST00000338745; ENSP00000341024; ENSG00000182568.
ENST00000454909; ENSP00000399708; ENSG00000182568.

GeneID

6304.

KEGG

hsa:6304.

UCSC

uc003cbh.1. human.

Organism-specific databases

CTD

6304.

GeneCards

GC03M018364.

H-InvDB

HIX0017285.

HGNC

HGNC:10541. SATB1.

HPA

CAB023814.

MIM

602075. gene.

neXtProt

NX_Q01826.

PharmGKB

PA34951.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17957.

GeneTree

ENSGT00390000008096.

HOVERGEN

HBG054240.

OrthoDB

EOG4BVRT9.

PhylomeDB

Q01826.

Enzyme and pathway databases

Pathway_Interaction_DB

caspase_pathway. Caspase cascade in apoptosis.

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

Q01826.

Bgee

Q01826.

CleanEx

HS_SATB1.

Genevestigator

Q01826.

GermOnline

ENSG00000182568. Homo sapiens.

Family and domain databases

InterPro

IPR003350. Hmoeo_CUT.
IPR001356. Homeobox.
IPR009057. Homeodomain-like.
IPR012287. Homeodomain-rel.
IPR010982. Lambda_DNA-bd.
[Graphical view]

Gene3D

G3DSA:1.10.260.40. G3DSA:1.10.260.40. 2 hits.
G3DSA:1.10.10.60. Homeodomain-rel. 1 hit.

Pfam

PF02376. CUT. 2 hits.
PF00046. Homeobox. 1 hit.
[Graphical view]

SMART

SM00389. HOX. 1 hit.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 1 hit.
SSF47413. Lambda_like_DNA. 2 hits.

PROSITE

PS51042. CUT. 2 hits.
PS00027. HOMEOBOX_1. False negative.
PS50071. HOMEOBOX_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

24475.

PMAP-CutDB

Q01826.

SOURCE

Search...

Entry information

Entry name

SATB1_HUMAN

Accession

Primary (citable) accession number: Q01826
Secondary accession number(s): B3KXF1, C9JTR6, Q59EQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	January 25, 2012
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.