SAFB2_MOUSE
ID SAFB2_MOUSE Reviewed; 991 AA.
AC Q80YR5; Q8K153;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Scaffold attachment factor B2;
DE Short=SAF-B2;
GN Name=Safb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-939, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Binds to scaffold/matrix attachment region (S/MAR) DNA. Can
CC function as an estrogen receptor corepressor and can also inhibit cell
CC proliferation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SAFB/SAFB1 and SCAM1. Interacts with SRPK1 and
CC inhibits its activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50855.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC050855; AAH50855.1; ALT_INIT; mRNA.
DR EMBL; BC028827; AAH28827.1; -; mRNA.
DR CCDS; CCDS28907.2; -.
DR RefSeq; NP_001025150.2; NM_001029979.2.
DR AlphaFoldDB; Q80YR5; -.
DR SMR; Q80YR5; -.
DR BioGRID; 230337; 6.
DR IntAct; Q80YR5; 1.
DR STRING; 10090.ENSMUSP00000074953; -.
DR iPTMnet; Q80YR5; -.
DR PhosphoSitePlus; Q80YR5; -.
DR EPD; Q80YR5; -.
DR jPOST; Q80YR5; -.
DR MaxQB; Q80YR5; -.
DR PaxDb; Q80YR5; -.
DR PeptideAtlas; Q80YR5; -.
DR PRIDE; Q80YR5; -.
DR ProteomicsDB; 256915; -.
DR Antibodypedia; 23844; 223 antibodies from 28 providers.
DR DNASU; 224902; -.
DR Ensembl; ENSMUST00000075510; ENSMUSP00000074953; ENSMUSG00000042625.
DR GeneID; 224902; -.
DR KEGG; mmu:224902; -.
DR UCSC; uc008dcg.1; mouse.
DR CTD; 9667; -.
DR MGI; MGI:2146808; Safb2.
DR VEuPathDB; HostDB:ENSMUSG00000042625; -.
DR eggNOG; KOG4661; Eukaryota.
DR GeneTree; ENSGT00940000161482; -.
DR HOGENOM; CLU_015021_0_0_1; -.
DR InParanoid; Q80YR5; -.
DR OMA; MHSNNSW; -.
DR OrthoDB; 803886at2759; -.
DR PhylomeDB; Q80YR5; -.
DR TreeFam; TF325240; -.
DR BioGRID-ORCS; 224902; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Safb2; mouse.
DR PRO; PR:Q80YR5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q80YR5; protein.
DR Bgee; ENSMUSG00000042625; Expressed in retinal neural layer and 252 other tissues.
DR ExpressionAtlas; Q80YR5; baseline and differential.
DR Genevisible; Q80YR5; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IDA:MGI.
DR GO; GO:0050684; P:regulation of mRNA processing; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060008; P:Sertoli cell differentiation; IMP:MGI.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034782; SAFB2.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR PANTHER; PTHR15683:SF4; PTHR15683:SF4; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; DNA-binding; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CHAIN 2..991
FT /note="Scaffold attachment factor B2"
FT /id="PRO_0000081908"
FT DOMAIN 25..59
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 451..529
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 755..772
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 84..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..281
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT MOD_RES 658
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT MOD_RES 939
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 60
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 60
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 183
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 194
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 310
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 429
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 435
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 439
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 560
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 567
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 568
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 584
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 585
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 620
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 628
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 650
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CROSSLNK 658
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14151"
FT CONFLICT 861
FT /note="D -> E (in Ref. 1; AAH28827)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 991 AA; 111838 MW; 7CA49153C897EB2E CRC64;
MAEPGTGSGD PAFGPGASES GTRRLSDLRV IDLRAELKKR NLDTGGNKSV LMERLRKAFK
EEGQEPEEVG ISWGAVSKRA VKRNTKGSKM EEEGSEDNGL EEDSRYGQDG VVILQSSQDR
DTMDTGVPDG MEAEDLSVPC LGKADTVNQI LHAFDDSKEY VAAQLGQLPA QLLKHAVDEE
VFKNTLEASV SDLKVTLADE EAPMEPENEK ILDILGETCK SEPVKEEGSE LEQPFAQATS
SVGPDRKLAE EEDLFESCGH PEEEEEEEEE DQEEEQEEEG DLALASSSKS ESPSTRCQWS
EADAPLAVVK RELADAPGGG GGTRHRRKRK RRRKHQAQAE ALGTGGGAGM NCEPVGLEEP
VEQSSTAAQL PEATSQELVR APTAALSPEP QDSKEDVKKF AFDACNDVPA PPKESSASEG
ADQKMSSVKE EQDIKPVIKD EKGRASCSSG RNLWVSGLSS STRAADLKSL FSKHGKVIGA
KVVTNARSPG ARCYGFVTMS TSDEATKCIS HLHRTELHGR MISVEKAKNE PSEKKSSDRR
ACDQKEKVPG PDRPHPVKIK TEKTVIKKEE KLERKEEKGP EDIKKEKDQD ELTPGAAGHS
RVTKSGSRGM ERTVVMDKSK GEPVISVKAT SRSKDRSSKS QDRKSEGREK RDILSFDKIK
EQRERERQRQ REREIRETER RREREQRERE QRLDAFQERR EKARLQRERM QLQCQRQRLE
RERLERERLE RERMRVERER RKEQQRIMRE REELRRQQEQ LRAEQERRAL RRPYDLDARR
DDGYWPEGKR AALEDRYRDF PRPDHRFHDF DHRDRGHYQE HVIDRRDGSR TRVEERDGQY
YPDDQHSHGR LLEHHAWDSG DGWHGYSSDK KLNEGQGLPP PPRVSREWAE HSSQLEEQQV
PVWHSAVDTN MTGHEHIRWR GAERGLAGGP GHGHVAAGRG GMAGQGSFAH GGHSQGYIVP
SGRLEGGGMA SQDQGGRVPN PHPHPHFTRR Y
