SAFB

From Wikipedia, the free encyclopedia

Scaffold attachment factor B

Identifiers

SAFB; HET; HAP; DKFZp779C1727; SAFB1

External IDs

OMIM: 602895 MGI: 2146974 HomoloGene: 2229

Gene ontology
Molecular Function:	• nucleotide binding • nucleic acid binding • DNA binding • double-stranded DNA binding • RNA binding • protein binding
Cellular Component:	• nucleus
Biological Process:	• establishment and/or maintenance of chromatin architecture • transcription • regulation of transcription, DNA-dependent

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_002967 (mRNA)
NP_002958 (protein)

XM_001002609 (mRNA)
XP_001002609 (protein)

Location

Chr 19: 5.57 - 5.62 Mb

Chr 17: 56.27 - 56.29 Mb

Pubmed search

[1]

[2]

Scaffold attachment factor B, also known as SAFB, is a human gene.^[1]

This gene encodes a DNA-binding protein that has high specificity for scaffold or matrix attachment region DNA elements (S/MAR DNA). This protein is thought to be involved in attaching the base of chromatin loops to the nuclear matrix but there is conflicting evidence as to whether this protein is a component of chromatin or a nuclear matrix protein. Scaffold attachment factors are a specific subset of nuclear matrix proteins (NMP) that specifically bind to S/MAR. This encoded protein is thought to serve as a molecular base to assemble a 'transcriptosome complex' in the vicinity of actively transcribed genes. It is involved in the regulation of the heat shock protein 27 transcription and also can act as an estrogen receptor corepressor. This gene is a candidate gene for breast tumorigenesis.^[1]

[edit] References

^ ^a ^b Entrez Gene: SAFB scaffold attachment factor B.

[edit] Further reading

Oesterreich S (2004). "Scaffold attachment factors SAFB1 and SAFB2: Innocent bystanders or critical players in breast tumorigenesis?". J. Cell. Biochem. 90 (4): 653–61. doi:10.1002/jcb.10685. PMID 14587024.
Romig H, Fackelmayer FO, Renz A, et al. (1992). "Characterization of SAF-A, a novel nuclear DNA binding protein from HeLa cells with high affinity for nuclear matrix/scaffold attachment DNA elements.". EMBO J. 11 (9): 3431–40. PMID 1324173.
Renz A, Fackelmayer FO (1996). "Purification and molecular cloning of the scaffold attachment factor B (SAF-B), a novel human nuclear protein that specifically binds to S/MAR-DNA.". Nucleic Acids Res. 24 (5): 843–9. PMID 8600450.
Oesterreich S, Lee AV, Sullivan TM, et al. (1997). "Novel nuclear matrix protein HET binds to and influences activity of the HSP27 promoter in human breast cancer cells.". J. Cell. Biochem. 67 (2): 275–86. PMID 9328833.
DuPont BR, Garcia DK, Sullivan TM, et al. (1998). "Assignment of SAFB encoding Hsp27 ERE-TATA binding protein (HET)/scaffold attachment factor B (SAF-B) to human chromosome 19 band p13.". Cytogenet. Cell Genet. 79 (3-4): 284–5. PMID 9605873.
Nayler O, Strätling W, Bourquin JP, et al. (1998). "SAF-B protein couples transcription and pre-mRNA splicing to SAR/MAR elements.". Nucleic Acids Res. 26 (15): 3542–9. PMID 9671816.
Weighardt F, Cobianchi F, Cartegni L, et al. (1999). "A novel hnRNP protein (HAP/SAF-B) enters a subset of hnRNP complexes and relocates in nuclear granules in response to heat shock.". J. Cell. Sci. 112 ( Pt 10): 1465–76. PMID 10212141.
Oesterreich S, Zhang Q, Hopp T, et al. (2000). "Tamoxifen-bound estrogen receptor (ER) strongly interacts with the nuclear matrix protein HET/SAF-B, a novel inhibitor of ER-mediated transactivation.". Mol. Endocrinol. 14 (3): 369–81. PMID 10707955.
Shnyreva M, Schullery DS, Suzuki H, et al. (2000). "Interaction of two multifunctional proteins. Heterogeneous nuclear ribonucleoprotein K and Y-box-binding protein.". J. Biol. Chem. 275 (20): 15498–503. PMID 10809782.
Arao Y, Kuriyama R, Kayama F, Kato S (2000). "A nuclear matrix-associated factor, SAF-B, interacts with specific isoforms of AUF1/hnRNP D.". Arch. Biochem. Biophys. 380 (2): 228–36. doi:10.1006/abbi.2000.1938. PMID 10933876.
Stoss O, Olbrich M, Hartmann AM, et al. (2001). "The STAR/GSG family protein rSLM-2 regulates the selection of alternative splice sites.". J. Biol. Chem. 276 (12): 8665–73. doi:10.1074/jbc.M006851200. PMID 11118435.
Oesterreich S, Allredl DC, Mohsin SK, et al. (2001). "High rates of loss of heterozygosity on chromosome 19p13 in human breast cancer.". Br. J. Cancer 84 (4): 493–8. doi:10.1054/bjoc.2000.1606. PMID 11207044.
Nikolakaki E, Kohen R, Hartmann AM, et al. (2001). "Cloning and characterization of an alternatively spliced form of SR protein kinase 1 that interacts specifically with scaffold attachment factor-B.". J. Biol. Chem. 276 (43): 40175–82. doi:10.1074/jbc.M104755200. PMID 11509566.
Paul C, Manero F, Gonin S, et al. (2002). "Hsp27 as a negative regulator of cytochrome C release.". Mol. Cell. Biol. 22 (3): 816–34. PMID 11784858.
Traweger A, Fuchs R, Krizbai IA, et al. (2003). "The tight junction protein ZO-2 localizes to the nucleus and interacts with the heterogeneous nuclear ribonucleoprotein scaffold attachment factor-B.". J. Biol. Chem. 278 (4): 2692–700. doi:10.1074/jbc.M206821200. PMID 12403786.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Townson SM, Dobrzycka KM, Lee AV, et al. (2003). "SAFB2, a new scaffold attachment factor homolog and estrogen receptor corepressor.". J. Biol. Chem. 278 (22): 20059–68. doi:10.1074/jbc.M212988200. PMID 12660241.
van den IJssel P, Wheelock R, Prescott A, et al. (2003). "Nuclear speckle localisation of the small heat shock protein alpha B-crystallin and its inhibition by the R120G cardiomyopathy-linked mutation.". Exp. Cell Res. 287 (2): 249–61. PMID 12837281.
Tai HH, Geisterfer M, Bell JC, et al. (2003). "CHD1 associates with NCoR and histone deacetylase as well as with RNA splicing proteins.". Biochem. Biophys. Res. Commun. 308 (1): 170–6. PMID 12890497.
Li J, Hawkins IC, Harvey CD, et al. (2003). "Regulation of alternative splicing by SRrp86 and its interacting proteins.". Mol. Cell. Biol. 23 (21): 7437–47. PMID 14559993.