ID   SAFB1_RAT               Reviewed;         931 AA.
AC   O88453;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2003, sequence version 2.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=Scaffold attachment factor B1;
DE            Short=SAF-B;
DE            Short=SAF-B1;
GN   Name=Safb; Synonyms=Safb1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INTERACTION WITH POLR2A;
RP   SFRS1; SFRS9 AND SFR10, AND SUBCELLULAR LOCATION.
RX   PubMed=9671816; DOI=10.1093/nar/26.15.3542;
RA   Nayler O., Straetling W., Bourquin J.-P., Stagljar I., Lindemann L.,
RA   Jasper H., Hartmann A.M., Fackelmeyer F.O., Ullrich A., Stamm S.;
RT   "SAF-B couples transcription and pre-mRNA splicing to SAR/MAR elements.";
RL   Nucleic Acids Res. 26:3542-3549(1998).
RN   [2]
RP   INTERACTION WITH KHDRBS3 AND CLK2, AND PHOSPHORYLATION.
RC   TISSUE=Brain;
RX   PubMed=11118435; DOI=10.1074/jbc.m006851200;
RA   Stoss O., Olbrich M., Hartmann A.M., Koenig H., Memmott J., Andreadis A.,
RA   Stamm S.;
RT   "The STAR/GSG family protein rSLM-2 regulates the selection of alternative
RT   splice sites.";
RL   J. Biol. Chem. 276:8665-8673(2001).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-208, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Binds to scaffold/matrix attachment region (S/MAR) DNA and
CC       forms a molecular assembly point to allow the formation of a
CC       'transcriptosomal' complex (consisting of SR proteins and RNA
CC       polymerase II) coupling transcription and RNA processing (By
CC       similarity). Functions as an estrogen receptor corepressor and can also
CC       bind to the HSP27 promoter and decrease its transcription (By
CC       similarity). Thereby acts as a negative regulator of cell proliferation
CC       (By similarity). When associated with RBMX, binds to and stimulates
CC       transcription from the SREBF1 promoter (By similarity).
CC       {ECO:0000250|UniProtKB:D3YXK2, ECO:0000250|UniProtKB:Q15424}.
CC   -!- SUBUNIT: Monomer and homodimer (By similarity). Interacts with KHDRBS3
CC       (PubMed:11118435). Interacts with CLK2 (PubMed:11118435). Interacts
CC       with POLR2A, ASF/SRSF1, SRp30c/SRFS9 and TRA2B/SFRS10 (PubMed:9671816).
CC       Interacts with SRPK1 and inhibits its activity (By similarity).
CC       Interacts with RBMX (By similarity). Interacts with FUS (By
CC       similarity). Interacts with ZBED4 (By similarity).
CC       {ECO:0000250|UniProtKB:D3YXK2, ECO:0000250|UniProtKB:Q15424,
CC       ECO:0000269|PubMed:11118435, ECO:0000269|PubMed:9671816}.
CC   -!- INTERACTION:
CC       O88453; Q96SB4: SRPK1; Xeno; NbExp=2; IntAct=EBI-539530, EBI-539478;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9671816}.
CC   -!- PTM: Phosphorylated by CDC-like kinase 2 (CLK2).
CC       {ECO:0000269|PubMed:11118435}.
CC   -!- PTM: Sumoylated by PIAS1 with SUMO1 and SUMO2/3, desumoylated by SENP1.
CC       Sumoylation is required for transcriptional repressor activity.
CC       {ECO:0000250|UniProtKB:Q15424}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC29479.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF056324; AAC29479.1; ALT_FRAME; mRNA.
DR   AlphaFoldDB; O88453; -.
DR   SMR; O88453; -.
DR   BioGRID; 249003; 11.
DR   IntAct; O88453; 3.
DR   MINT; O88453; -.
DR   STRING; 10116.ENSRNOP00000071054; -.
DR   iPTMnet; O88453; -.
DR   PhosphoSitePlus; O88453; -.
DR   jPOST; O88453; -.
DR   PaxDb; 10116-ENSRNOP00000066884; -.
DR   AGR; RGD:620613; -.
DR   RGD; 620613; Safb.
DR   eggNOG; KOG4661; Eukaryota.
DR   InParanoid; O88453; -.
DR   PhylomeDB; O88453; -.
DR   Reactome; R-RNO-3899300; SUMOylation of transcription cofactors.
DR   PRO; PR:O88453; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:0042445; P:hormone metabolic process; ISO:RGD.
DR   GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0040008; P:regulation of growth; ISO:RGD.
DR   GO; GO:0050684; P:regulation of mRNA processing; IDA:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:RGD.
DR   CDD; cd12679; RRM_SAFB1_SAFB2; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR034781; SAFB1_2_RBD.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   PANTHER; PTHR15683; SCAFFOLD ATTACHMENT FACTOR B-RELATED; 1.
DR   PANTHER; PTHR15683:SF6; SCAFFOLD ATTACHMENT FACTOR B1; 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; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50800; SAP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; 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:Q15424"
FT   CHAIN           2..931
FT                   /note="Scaffold attachment factor B1"
FT                   /id="PRO_0000081906"
FT   DOMAIN          31..65
FT                   /note="SAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT   DOMAIN          428..506
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..816
FT                   /note="Interaction with POLR2A; SFRS1; SFRS9 and SFRS10"
FT                   /evidence="ECO:0000269|PubMed:9671816"
FT   REGION          691..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          759..843
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..931
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           621..638
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        77..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..121
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..287
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..425
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..570
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..663
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..823
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:Q15424"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         405
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         406
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         437
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         602
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         604
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         623
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         626
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         629
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         834
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         892
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         898
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         908
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   MOD_RES         914
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YXK2"
FT   CROSSLNK        171
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   CROSSLNK        185
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   CROSSLNK        230
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        316
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        403
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   CROSSLNK        414
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   CROSSLNK        505
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   CROSSLNK        536
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   CROSSLNK        565
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   CROSSLNK        592
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   CROSSLNK        600
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
FT   CROSSLNK        600
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q15424"
SQ   SEQUENCE   931 AA;  104567 MW;  A5E3FD7AB33341F6 CRC64;
     MAETLSGLGD SGAASAAAVS SAASETGTRR LSDLRVIDLR AELRKRNLTS SGNKSVLMER
     LKKAIEEEGG NPDEIEVISE GNKKMPKRPS KGKKPEDEGV EDNGLEENSG DGQEDVETSL
     ENLQDMDMMD ISVLDEADID NGSVADCVEE EEEATLPEGL GLLRIGRLQS KGLPEQLQEL
     AIDDKEAINN VDTSSSDFTI LQEMEEASLE PENEKILDIL GETCKSEPVK EEGSELEQPF
     AQATSSVGPD RKLAEEEDLF ESCGHPEEEE EEEEEEEQEE EQEEEGDLAL ASSSKSESSS
     TRCQWSEADA LLAVVKREPA EAPGGGTGMD REPVGLEEPV EQSSTAAQLP ETTSQELVRA
     PTAAPSPEPR DSKDDVKKFA FDACNDVPAA PKESSASEGA DQKMSSVEDD SDTKRLSREE
     KGRSSCGRNF WVSGLSSTTR ATDLKNLFSR YGKVVGAKVV TNARSPGARC YGFVTMSTAE
     EATKCINHLH KTELHGKMIS VEKAKSEPAG KRVPDRRDGD SKKEKTSTSD RSANLKREEK
     GDRKDDAKKT DDGSTEKSKD ADDQKPGPSE RSRTTKSGSR GTERTVVMDK SKGVPVISVK
     TSGSKERASK SQDRKSVSRE KRSVVSFDKV KESRKSRDSE SRRERERERS EREQRLQAQW
     EREERERLEI ARERLAFHRH RLERERMERE RLERERMHVE QERRREQERI HREREELRRQ
     QELRYEQERR PAVRRPYEVD GRRDDAYWPE AKRAALDDRY HSDFSRQDRF HDFDHRDRGR
     YPNHSVDRRE GSRSMMGDRE GQHYPERHGG PERHGRDSRD GWGYGSNKRL SEGRGLPLLP
     RRDWGEHARR LEDDRAWQGT ADGGMMERDQ QRWQGGERSM SGHSGPGHMM NRGGMSGRGS
     FAPGGASRRH VIPRGGMQAG FGGTEPGQQT Q
//