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RBM45_HUMAN
ID   RBM45_HUMAN             Reviewed;         476 AA.
AC   Q8IUH3; Q6NYL0; Q8NFC9;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=RNA-binding protein 45;
DE   AltName: Full=Developmentally-regulated RNA-binding protein 1;
DE            Short=RB-1;
DE   AltName: Full=RNA-binding motif protein 45;
GN   Name=RBM45; Synonyms=DRB1 {ECO:0000312|EMBL:AAH66549.1}, DRBP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAC16207.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Brain {ECO:0000312|EMBL:BAC16207.1};
RX   PubMed=12220514; DOI=10.1016/s0006-291x(02)02132-0;
RA   Tamada H., Sakashita E., Shimazaki K., Ueno E., Hamamoto T., Kagawa Y.,
RA   Endo H.;
RT   "cDNA cloning and characterization of Drb1, a new member of RRM-type neural
RT   RNA-binding protein.";
RL   Biochem. Biophys. Res. Commun. 297:96-104(2002).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAM88417.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Heart {ECO:0000312|EMBL:AAM88417.1};
RA   Chen X.G., Li Y.;
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305, ECO:0000312|EMBL:AAH66549.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Pancreas {ECO:0000312|EMBL:AAH66549.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [5]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-34, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: RNA-binding protein with binding specificity for poly(C). May
CC       play an important role in neural development.
CC       {ECO:0000250|UniProtKB:Q8CFD1, ECO:0000269|PubMed:12220514}.
CC   -!- INTERACTION:
CC       Q8IUH3; Q9NW38: FANCL; NbExp=3; IntAct=EBI-2512147, EBI-2339898;
CC       Q8IUH3; Q9Y316: MEMO1; NbExp=3; IntAct=EBI-2512147, EBI-1104564;
CC       Q8IUH3; Q13077: TRAF1; NbExp=3; IntAct=EBI-2512147, EBI-359224;
CC       Q8IUH3; Q99757: TXN2; NbExp=3; IntAct=EBI-2512147, EBI-2932492;
CC       Q8IUH3-3; Q15699: ALX1; NbExp=3; IntAct=EBI-10964453, EBI-750671;
CC       Q8IUH3-3; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-10964453, EBI-1055254;
CC       Q8IUH3-3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-10964453, EBI-741158;
CC       Q8IUH3-3; Q8IUH3-3: RBM45; NbExp=3; IntAct=EBI-10964453, EBI-10964453;
CC       Q8IUH3-3; O14787-2: TNPO2; NbExp=3; IntAct=EBI-10964453, EBI-12076664;
CC       Q8IUH3-3; Q13077: TRAF1; NbExp=3; IntAct=EBI-10964453, EBI-359224;
CC       Q8IUH3-3; Q99757: TXN2; NbExp=3; IntAct=EBI-10964453, EBI-2932492;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12220514}. Nucleus
CC       {ECO:0000269|PubMed:12220514}. Note=Predominantly cytoplasmic. May
CC       shuttle between cytoplasm and nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000269|PubMed:12220514};
CC         IsoId=Q8IUH3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IUH3-2; Sequence=VSP_021005, VSP_051661, VSP_051662;
CC       Name=3;
CC         IsoId=Q8IUH3-3; Sequence=VSP_021005;
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC       {ECO:0000305}.
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DR   EMBL; AB036991; BAC16207.1; -; mRNA.
DR   EMBL; AF526533; AAM88417.1; -; mRNA.
DR   EMBL; BC066549; AAH66549.1; -; mRNA.
DR   CCDS; CCDS33335.1; -. [Q8IUH3-3]
DR   RefSeq; NP_694453.2; NM_152945.3. [Q8IUH3-3]
DR   RefSeq; XP_005246344.1; XM_005246287.4.
DR   RefSeq; XP_016858811.1; XM_017003322.1.
DR   PDB; 7CSX; X-ray; 2.50 A; A=23-202.
DR   PDB; 7CSZ; X-ray; 1.80 A; A=23-202.
DR   PDBsum; 7CSX; -.
DR   PDBsum; 7CSZ; -.
DR   AlphaFoldDB; Q8IUH3; -.
DR   SMR; Q8IUH3; -.
DR   BioGRID; 126210; 212.
DR   IntAct; Q8IUH3; 55.
DR   MINT; Q8IUH3; -.
DR   STRING; 9606.ENSP00000286070; -.
DR   iPTMnet; Q8IUH3; -.
DR   PhosphoSitePlus; Q8IUH3; -.
DR   BioMuta; RBM45; -.
DR   DMDM; 59797947; -.
DR   EPD; Q8IUH3; -.
DR   jPOST; Q8IUH3; -.
DR   MassIVE; Q8IUH3; -.
DR   MaxQB; Q8IUH3; -.
DR   PaxDb; Q8IUH3; -.
DR   PeptideAtlas; Q8IUH3; -.
DR   PRIDE; Q8IUH3; -.
DR   ProteomicsDB; 70566; -. [Q8IUH3-1]
DR   ProteomicsDB; 70567; -. [Q8IUH3-2]
DR   ProteomicsDB; 70568; -. [Q8IUH3-3]
DR   Antibodypedia; 19584; 138 antibodies from 23 providers.
DR   DNASU; 129831; -.
DR   Ensembl; ENST00000286070.10; ENSP00000286070.5; ENSG00000155636.15. [Q8IUH3-3]
DR   Ensembl; ENST00000616198.4; ENSP00000482083.1; ENSG00000155636.15. [Q8IUH3-1]
DR   GeneID; 129831; -.
DR   KEGG; hsa:129831; -.
DR   MANE-Select; ENST00000286070.10; ENSP00000286070.5; NM_152945.4; NP_694453.2. [Q8IUH3-3]
DR   UCSC; uc002ulv.4; human. [Q8IUH3-1]
DR   CTD; 129831; -.
DR   DisGeNET; 129831; -.
DR   GeneCards; RBM45; -.
DR   HGNC; HGNC:24468; RBM45.
DR   HPA; ENSG00000155636; Low tissue specificity.
DR   MIM; 608888; gene.
DR   neXtProt; NX_Q8IUH3; -.
DR   OpenTargets; ENSG00000155636; -.
DR   PharmGKB; PA162400809; -.
DR   VEuPathDB; HostDB:ENSG00000155636; -.
DR   eggNOG; ENOG502QTJ8; Eukaryota.
DR   GeneTree; ENSGT00680000100059; -.
DR   HOGENOM; CLU_035274_1_0_1; -.
DR   InParanoid; Q8IUH3; -.
DR   OMA; ILFHPHP; -.
DR   OrthoDB; 673895at2759; -.
DR   PhylomeDB; Q8IUH3; -.
DR   TreeFam; TF324216; -.
DR   PathwayCommons; Q8IUH3; -.
DR   SignaLink; Q8IUH3; -.
DR   BioGRID-ORCS; 129831; 13 hits in 1032 CRISPR screens.
DR   ChiTaRS; RBM45; human.
DR   GenomeRNAi; 129831; -.
DR   Pharos; Q8IUH3; Tbio.
DR   PRO; PR:Q8IUH3; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q8IUH3; protein.
DR   Bgee; ENSG00000155636; Expressed in mucosa of transverse colon and 162 other tissues.
DR   ExpressionAtlas; Q8IUH3; baseline and differential.
DR   Genevisible; Q8IUH3; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR   CDD; cd12366; RRM1_RBM45; 1.
DR   CDD; cd12367; RRM2_RBM45; 1.
DR   CDD; cd12368; RRM3_RBM45; 1.
DR   CDD; cd12369; RRM4_RBM45; 1.
DR   Gene3D; 3.30.70.330; -; 3.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR033101; RBM45.
DR   InterPro; IPR034203; RBM45_RRM1.
DR   InterPro; IPR034206; RBM45_RRM2.
DR   InterPro; IPR034207; RBM45_RRM3.
DR   InterPro; IPR034208; RBM45_RRM4.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR10352:SF18; PTHR10352:SF18; 1.
DR   Pfam; PF00076; RRM_1; 4.
DR   SMART; SM00360; RRM; 4.
DR   SUPFAM; SSF54928; SSF54928; 2.
DR   PROSITE; PS50102; RRM; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW   Differentiation; Isopeptide bond; Neurogenesis; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT   CHAIN           1..476
FT                   /note="RNA-binding protein 45"
FT                   /id="PRO_0000081572"
FT   DOMAIN          26..106
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          121..195
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          392..464
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BHN5"
FT   MOD_RES         464
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        34
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         225..226
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT                   /id="VSP_021005"
FT   VAR_SEQ         330
FT                   /note="D -> E (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_051661"
FT   VAR_SEQ         331..476
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_051662"
FT   STRAND          27..31
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   HELIX           38..45
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   STRAND          51..58
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   STRAND          65..75
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   HELIX           76..86
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   HELIX           93..95
FT                   /evidence="ECO:0007829|PDB:7CSX"
FT   STRAND          100..103
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   STRAND          121..126
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   HELIX           133..140
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   HELIX           141..143
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   STRAND          146..153
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   TURN            155..157
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   STRAND          160..170
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   HELIX           171..180
FT                   /evidence="ECO:0007829|PDB:7CSZ"
FT   HELIX           183..185
FT                   /evidence="ECO:0007829|PDB:7CSZ"
SQ   SEQUENCE   476 AA;  53502 MW;  06C7806D9079D391 CRC64;
     MDEAGSSASG GGFRPGVDSL DEPPNSRIFL VISKYTPESV LRERFSPFGD IQDIWVVRDK
     HTKESKGIAF VKFARSSQAC RAMEEMHGQC LGPNDTKPIK VFIAQSRSSG SHRDVEDEEL
     TRIFVMIPKS YTEEDLREKF KVYGDIEYCS IIKNKVTGES KGLGYVRYLK PSQAAQAIEN
     CDRSFRAILA EPKNKASESS EQDYYSNMRQ EALGHEPRVN MFPFVGEQQS EFSSFDKNDS
     RGQEAISKRL SVVSRVPFTE EQLFSIFDIV PGLEYCEVQR DPYSNYGHGV VQYFNVASAI
     YAKYKLHGFQ YPPGNRIGVS FIDDGSNATD LLRKMATQMV AAQLASMVWN NPSQQQFMQF
     GGSSGSQLPQ IQTDVVLPSC KKKAPAETPV KERLFIVFNP HPLPLDVLED IFCRFGNLIE
     VYLVSGKNVG YAKYADRISA NDAIATLHGK ILNGVRLKVM LADSPREESN KRQRTY
 
 
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