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scaffold attachment factor B2; SAF-B2 (SAFB2 KIAA0138)
Function:
- binds to scaffold/matrix attachment region (S/MAR) DNA
- can function as an estrogen receptor corepressor
- can also inhibit cell proliferation
- phosphorylated upon DNA damage, probably by ATM or ATR
- interacts with SAFB/SAFB1 & SCAM1
- interacts with isoform 2 SRPK1 & inhibits its activity
Structure:
- contains 1 RRM domain (RNA recognition motif)
- contains 1 SAP domain
Compartment: cytoplasm. nucleus
Expression:
- expressed at high levels in the CNS
- epessed at low levels in the liver.
- expressed in a wide number of breast cancer cell lines
Related
eukaryotic translation initiation factor 4E (eIF4E, mRNA cap-binding protein)
General
nuclear protein
phosphoprotein
RNA-binding protein
scaffold protein
Properties
SIZE: entity length = 953 aa
MW = 107 kD
COMPARTMENT: cytoplasm
cell nucleus
MOTIF: acetylation site
SITE: N-TERMINUS
EFFECTOR-BOUND: acetyl
SAP {30-64}
MOTIF: Ser phosphorylation site {S31}
Ser phosphorylation site {S109}
Ser phosphorylation site {S195}
Thr phosphorylation site {T201}
Ser phosphorylation site {S207}
Ser phosphorylation site {S234}
Ser phosphorylation site {S287}
Ser phosphorylation site {S331}
Ser phosphorylation site {S343}
RNP motif
NAME: RNP motif
SITE: 407-485
FOR-BINDING-OF: ribonucleic acid
MOTIF: ribonucleoprotein-1 motif
NAME: ribonucleoprotein-1 motif
FOR-BINDING-OF: ribonucleic acid
MOTIF: ribonucleoprotein-1 motif
ribonucleoprotein-2 motif
ribonucleoprotein-2 motif
FOR-BINDING-OF: ribonucleic acid
MOTIF: ribonucleoprotein-1 motif
ribonucleoprotein-2 motif
lysine-rich region {482-545}
MOTIF: lysine residue (SEVERAL)
Ser phosphorylation site {S513}
SAFB1 interaction {600-953}
MOTIF: Ser phosphorylation site {S613}
glutamate-rich region {619-724}
MOTIF: glutamate residue (SEVERAL)
arginine-rich region {621-788}
MOTIF: arginine residue (SEVERAL)
nuclear translocation signal {713-730}
glycine-rich region {792-926}
Database Correlations
OMIM 608066
UniProt Q14151
PFAM correlations
Entrez Gene 9667
Kegg hsa:9667
References
UniProt :accession Q14151