RB12B_PONAB
ID RB12B_PONAB Reviewed; 761 AA.
AC Q5RFT7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=RNA-binding protein 12B;
DE AltName: Full=RNA-binding motif protein 12B;
GN Name=RBM12B;
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.
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DR EMBL; CR857063; CAH89370.1; -; mRNA.
DR AlphaFoldDB; Q5RFT7; -.
DR STRING; 9601.ENSPPYP00000021025; -.
DR eggNOG; KOG4307; Eukaryota.
DR InParanoid; Q5RFT7; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR CDD; cd12746; RRM2_RBM12B; 1.
DR CDD; cd12513; RRM3_RBM12B; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034588; RBM12B_RRM2.
DR InterPro; IPR034858; RBM12B_RRM3.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF54928; SSF54928; 4.
DR PROSITE; PS50102; RRM; 3.
PE 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..761
FT /note="RNA-binding protein 12B"
FT /id="PRO_0000273367"
FT DOMAIN 155..230
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 284..360
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 400..477
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 120..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT MOD_RES 276
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT MOD_RES 319
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT CROSSLNK 114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT CROSSLNK 335
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT CROSSLNK 514
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
FT CROSSLNK 541
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IXT5"
SQ SEQUENCE 761 AA; 86780 MW; 6333B21574CEB939 CRC64;
MAVVIRLLGL PFIAGPVDIR HFFTGLTIPD GGVHIIGGEI GEAFIIFATD EDARRAISRS
GGFIKDSSVE LFLSSKAEMQ KTIEMKRTDR VGRGRPGSGT SGVGSLSNII ESVKEEASNS
GYGSSINQDA GFHSNGTGHG NLRPRKTRPL KAENPYLFLR GLPYLVNEDD VRVFFSGLCV
DGVIFLKHHD GRNNGDAIVK FASCVDASGG LKCHRSFMGS RFIEVMQGSE QQWIEFGGNA
VKEGDVLRRS EEHSPPRGIN DRHFRKRSHS KSPRRTRSRS PLGFYVHLKN LSLSIDERDL
RNFFRGTDLT DEQIRFLYKD ENRTRYAFVM FKTLKDYNTA LSLHKTVLQY RPVHIDPISR
KQMLKFIARY EKKRSGSPER DRPGHVSQKY SQEGNSGQKL CIYIRNFPFD VTKVEVQKFF
ADFLLAEDDI YLLYDDKGVG LGEALVKFKS EEQAMKAERL NRRRFLGTEV LLRLISEAQM
QEFGVNFSLM SSEKMQARSQ SRERGDHSQL FDSKDPPVYS VGAFENFKHH IEDLRQLDNF
KHPQRDFRQP DRHPPEEFRH SSEDFRFPPE DFRHSPEDFR RPREEDFRRP SEEDFRRPWE
EDFRRPPEDD FRHPREEDWR RPLGGLLQST SGGHPQSISG GHPQSISGAR PRSTSGDRPR
SISGGRLRSI SGAPERKISG THQMKTSGAL PMKTLGTLLM RTSGAPRRKI LDALLMRTSG
SSQRKTLGKL RRRTLDFLTI LDLLVRILGA RLMILEVTAL L
