RBM39_PONAB
ID RBM39_PONAB Reviewed; 524 AA.
AC Q5RC80;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=RNA-binding protein 39;
DE AltName: Full=RNA-binding motif protein 39;
GN Name=RBM39;
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: RNA-binding protein that acts as a pre-mRNA splicing factor.
CC Acts by promoting exon inclusion via regulation of exon cassette
CC splicing (By similarity). Also acts as a transcriptional coactivator
CC for steroid nuclear receptors ESR1/ER-alpha and ESR2/ER-beta, and
CC JUN/AP-1, independently of the pre-mRNA splicing factor activity (By
CC similarity). {ECO:0000250|UniProtKB:Q14498,
CC ECO:0000250|UniProtKB:Q8VH51}.
CC -!- SUBUNIT: Interacts with NCOA6 and JUN. Interacts with ESR1 and ESR2, in
CC the presence of estradiol (E2). Interacts with RSRC1 (via Arg/Ser-rich
CC domain). Interacts with SF3B1. Interacts with ZNF106 (via N-terminus).
CC {ECO:0000250|UniProtKB:Q14498, ECO:0000250|UniProtKB:Q8VH51}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle. Note=Concentrated in nuclear
CC speckles. Colocalizes with the core spliceosomal snRNP proteins (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; CR858400; CAH90627.1; -; mRNA.
DR RefSeq; NP_001125339.1; NM_001131867.1.
DR AlphaFoldDB; Q5RC80; -.
DR BMRB; Q5RC80; -.
DR SMR; Q5RC80; -.
DR STRING; 9601.ENSPPYP00000012240; -.
DR Ensembl; ENSPPYT00000012721; ENSPPYP00000012240; ENSPPYG00000010963.
DR GeneID; 100172241; -.
DR KEGG; pon:100172241; -.
DR CTD; 9584; -.
DR eggNOG; KOG0147; Eukaryota.
DR GeneTree; ENSGT00940000154468; -.
DR HOGENOM; CLU_020551_5_1_1; -.
DR InParanoid; Q5RC80; -.
DR Proteomes; UP000001595; Chromosome 20.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0050733; F:RS domain binding; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR029123; RBM39_linker.
DR InterPro; IPR006509; RBM39_SF.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF15519; RBM39linker; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 3.
DR SMART; SM00361; RRM_1; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR TIGRFAMs; TIGR01622; SF-CC1; 1.
DR PROSITE; PS50102; RRM; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT CHAIN 2..524
FT /note="RNA-binding protein 39"
FT /id="PRO_0000268161"
FT DOMAIN 153..230
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 250..328
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 439..502
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..400
FT /note="Interaction with JUN"
FT /evidence="ECO:0000250|UniProtKB:Q8VH51"
FT REGION 291..355
FT /note="Activating domain"
FT /evidence="ECO:0000250|UniProtKB:Q8VH51"
FT REGION 355..400
FT /note="Interaction with ESR1 and ESR2"
FT /evidence="ECO:0000250|UniProtKB:Q8VH51"
FT REGION 400..524
FT /note="Interaction with NCOA6"
FT /evidence="ECO:0000250|UniProtKB:Q8VH51"
FT COMPBIAS 9..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..92
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..146
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:Q14498"
FT MOD_RES 95
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT CROSSLNK 111
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
FT CROSSLNK 244
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14498"
SQ SEQUENCE 524 AA; 58657 MW; 1843A619B1950802 CRC64;
MADDIDIEAM LEAPYKKDEN KLSSANGHEE RSKKRKKSKS RSRSHERKRS KSKERKRSRD
RERKKSKSRE RKRSRSKERR RSRSRSRDRR FRGRYRSPYS GPKFNSAIRG KIGLPHSIKL
SRRRSRSKSP FRKDKSPVRE PIDNLTPEER DARTVFCMQL AARIRPRDLE EFFSTVGKVR
DVRMISDRNS RRSKGIAYVE FVDVSSVPLA IGLTGQRVLG VPIIVQASQA EKNRAAAMAN
NLQKGSAGPM RLYVGSLHFN ITEDMLRGIF EPFGRIESIQ LMMDSETGRS KGYGFITFSD
SECAKKALEQ LNGFELAGRP MKVGHVTERT DASSASSFLD SDELERTGID LGTTGRLQLM
ARLAEGTGLQ IPPAAQQALQ MSGSLAFGAV ADLQTRLSQQ TEASALAAAA SVQPLATQCF
QLSNMFNPQT EEEVGWDTEI KDDVIEECNK HGGVIHIYVD KNSAQGNVYV KCPSIAAAIA
AVNALHGRWF AGKMITAAYV PLPTYHNLFP DSMTATQLLV PSRR
