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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