SAFB1_PONAB
ID SAFB1_PONAB Reviewed; 914 AA.
AC Q5R452;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Scaffold attachment factor B1;
DE Short=SAF-B1;
GN Name=SAFB; Synonyms=SAFB1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Interacts with CLK2 (By similarity). Interacts with
CC POLR2A, ASF/SRSF1, SRp30c/SRFS9 and TRA2B/SFRS10 (By similarity).
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:O88453,
CC ECO:0000250|UniProtKB:Q15424}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15424}.
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}.
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DR EMBL; CR861407; CAH93464.1; -; mRNA.
DR RefSeq; NP_001127031.1; NM_001133559.1.
DR AlphaFoldDB; Q5R452; -.
DR SMR; Q5R452; -.
DR STRING; 9601.ENSPPYP00000010573; -.
DR PRIDE; Q5R452; -.
DR GeneID; 100174056; -.
DR KEGG; pon:100174056; -.
DR CTD; 6294; -.
DR eggNOG; KOG4661; Eukaryota.
DR InParanoid; Q5R452; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0050684; P:regulation of mRNA processing; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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; IPR034781; SAFB1.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR PANTHER; PTHR15683:SF6; PTHR15683:SF6; 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 2: Evidence at transcript 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..914
FT /note="Scaffold attachment factor B1"
FT /id="PRO_0000307797"
FT DOMAIN 31..65
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 406..484
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..791
FT /note="Interaction with POLR2A; SFRS1; SFRS9 and SFRS10"
FT /evidence="ECO:0000250|UniProtKB:O88453"
FT REGION 599..914
FT /note="Interaction with SAFB2"
FT /evidence="ECO:0000250"
FT REGION 670..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 599..616
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..117
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..852
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:0000250|UniProtKB:O88453"
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 188
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88453"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 601
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 607
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 810
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 867
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 873
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT MOD_RES 883
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 172
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 231
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 392
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 483
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 514
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 543
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 570
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 578
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 578
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
FT CROSSLNK 846
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15424"
SQ SEQUENCE 914 AA; 102493 MW; 83B7099606DD6AF6 CRC64;
MAETLSGLGD SGAAGAAALS SASSETGTRR LSDLRVIDLR AELRKRNVDS SGNKSVLMER
LKKAIEDEGG NPDEIEITSE GNKKTSKRSS KGRKPEEEGV EDNGLEENSG DGQEDVETSL
ENLQDIDIMD ISVLDEAEID NGSVADCVED DDADNLQESL SDSRELVEGE MKELPEQLQE
HAIEDKETIN NLDTSSSDFT ILQEIEEPSL EPENEKILDI LGETCKSEPV KEESSELEQP
FAQDTSSVGP DRKLAEEEDL FDSAHPEEGD LDLASESTAH AQSSKADSLL AVVKREPAEQ
PGDGERTDCE PVGLEPAVEQ SSAASELAEA SSEELAEAPT EAPSPEARDS KEDGRKFDFD
ACNEVPPAPK ESSTSEGADQ KMSSPEDDSD TKRLSKEEKG RSSCGRNFWV SGLSSTTRAT
DLKNLFSKYG KVVGAKVVTN ARSPGARCYG FVTMSTAEEA TKCINHLHKT ELHGKMISVE
KAKNEPVGKK TSDKRDSDGK KEKSSNSDRS ANLKRDDKCD RKDDAKKGDD GSGEKSKDQD
DQKPGPSERS RATKSGSRGT ERTVVMDKSK GVPVISVKTS GSKERASKSL DRKSASREKR
SVVSFDKVKE PRKSRDSESH RVRERSEREQ RMQAQWEREE RERLEIARER LAFQRQRLER
ERMERERLER ERMHVEHERR REQERIHRER EELRRQQELR YEQERRPAVR RPYDLDRRDD
AYWPEAKRAA LDERYHSDFN RQDRFHDFDH RDRGRYPDHS VDRREGSRSM MGEREGQHYP
ERHGGPERHG RDSRDGWGGY GSDKRMSEGR GLPPPPRRDW GDHGRREDDR AWQGTADGGM
MDRDHKRWQG GERSMSGHSG PGHMMNRGGM SGRGSFAPGG ASRGHPIPHG GMQGGFGGQS
RGSRPSDARF TRRY
