RBM10_RAT
ID RBM10_RAT Reviewed; 852 AA.
AC P70501;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=RNA-binding protein 10;
DE AltName: Full=RNA-binding motif protein 10;
DE AltName: Full=RNA-binding protein S1-1 {ECO:0000303|PubMed:8760884};
GN Name=Rbm10 {ECO:0000312|RGD:631366};
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], AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8760884; DOI=10.1093/nar/24.15.2990;
RA Inoue A., Takahashi K., Kimura M., Watanabe T., Morisawa S.;
RT "Molecular cloning of a RNA binding protein, S1-1.";
RL Nucleic Acids Res. 24:2990-2997(1996).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645; SER-655; SER-658;
RP SER-660 AND SER-719, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Not known. Binds to RNA homopolymers, with a preference for
CC poly(G) and poly(U) and little for poly(A) (PubMed:8760884). May bind
CC to specific miRNA hairpins (By similarity).
CC {ECO:0000250|UniProtKB:P98175, ECO:0000269|PubMed:8760884}.
CC -!- SUBUNIT: Associates with the spliceosome. Component of a large
CC chromatin remodeling complex, at least composed of MYSM1, PCAF, RBM10
CC and KIF11/TRIP5 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; D83948; BAA12144.1; -; mRNA.
DR RefSeq; NP_690600.1; NM_152861.4.
DR AlphaFoldDB; P70501; -.
DR BMRB; P70501; -.
DR STRING; 10116.ENSRNOP00000011317; -.
DR iPTMnet; P70501; -.
DR PhosphoSitePlus; P70501; -.
DR jPOST; P70501; -.
DR PaxDb; P70501; -.
DR PRIDE; P70501; -.
DR Ensembl; ENSRNOT00000011317; ENSRNOP00000011317; ENSRNOG00000008472.
DR GeneID; 64510; -.
DR KEGG; rno:64510; -.
DR UCSC; RGD:631366; rat.
DR CTD; 8241; -.
DR RGD; 631366; Rbm10.
DR eggNOG; KOG0154; Eukaryota.
DR GeneTree; ENSGT00940000160369; -.
DR HOGENOM; CLU_010527_0_0_1; -.
DR InParanoid; P70501; -.
DR OrthoDB; 786674at2759; -.
DR PhylomeDB; P70501; -.
DR PRO; PR:P70501; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000008472; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; P70501; baseline and differential.
DR Genevisible; P70501; RN.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISO:RGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0034393; P:positive regulation of smooth muscle cell apoptotic process; ISO:RGD.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0034391; P:regulation of smooth muscle cell apoptotic process; ISO:RGD.
DR CDD; cd16167; OCRE_RBM10; 1.
DR CDD; cd12754; RRM2_RBM10; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR041591; OCRE.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR033095; RBM10.
DR InterPro; IPR035618; RBM10_OCRE.
DR InterPro; IPR034992; RBM10_RRM2.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR13948:SF4; PTHR13948:SF4; 2.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF17780; OCRE; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..852
FT /note="RNA-binding protein 10"
FT /id="PRO_0000081768"
FT DOMAIN 37..132
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 223..307
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 780..826
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 135..165
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 681..706
FT /note="C2H2-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98175"
FT MOD_RES 306
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P98175"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98175"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98175"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98175"
FT MOD_RES 824
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P98175"
SQ SEQUENCE 852 AA; 94388 MW; D6D2EECFEECBE189 CRC64;
MEYERRGGRG DRTGRYGATD RSQDDGGENR SRDHDYRDMD YRSYPREYGS QEGKHEYDDS
SEEQSAEIRG QLQSHGVQAR EVRLMRNKSS GQSRGFAFVE FSHLQDATRW MEANQHSLNI
LGQKVSMHYS DPKPKINEDW LCNKCGVQNF KRREKCFKCG VPKSEAEQKL PLGTRLDQQA
LPLGGRELSQ GLLPLPQPYQ AQGVLTSQAL SQGSEPSSEN ANDTIILRNL NPHSTMDSIL
GALAPYAVLS SSNVRVIKDK QTQLNRGFAF IQLSTIVEAA QLLQILQALH PPLTIDGKTI
NVEFAKGSKR DMASNEGSRI NAASVASTAI AAAQWAISQA SQGGESTWAA PEEPPVDYSY
YQQDEGYGSS QGTDSLYAHG YLKNTKGPGM TGTKGDTSGA GPETSLEGGT DSVSLQAFSR
AQPGAAPGLY QQSAEGSSGQ GTATNSQSYT IMSPAVLKSE LQSPTHPSSA LPPATSPTAP
ESYSQYPVPD VSTYQYDETS GYYYDPQTGL YYDPNSQYYY NAQSQQYLYW DGERRTYIPA
LEQSADGHKD TGASSKEGKE KKEKHKTKTA QQIAKDMERW ARSLNKQKEN FKNSFQPISA
LRDDERRESA TADAGYAILE KKGALAERQH TSMDLPKLAS DDRPSPPRGL VAAYSGESDS
EEEQERGGPE REEKLTDWQK LACLLCRRQF PSKEALIRHQ QLSGLHKQNL EIHRRAHLSE
NELEALEKND MEQMKYRDRA AERREKYGIP EPPEPKRRKY GGISTASVDF EQPTRDGLGS
DNIGSRMLQA MGWKEGSGLG RKKQGIVTPI EAQTRVRGSG LGARGSSYGV TSTESYKETL
HKTMVTRFNE AQ
