RBM38_HUMAN
ID RBM38_HUMAN Reviewed; 239 AA.
AC Q9H0Z9; A6NDK1; A6NMU6; Q15350; Q15351; Q9BYK3; Q9BYK4;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=RNA-binding protein 38;
DE AltName: Full=CLL-associated antigen KW-5;
DE AltName: Full=HSRNASEB;
DE AltName: Full=RNA-binding motif protein 38;
DE AltName: Full=RNA-binding region-containing protein 1;
DE AltName: Full=ssDNA-binding protein SEB4;
GN Name=RBM38; Synonyms=RNPC1, SEB4;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leukemia;
RX PubMed=12200376; DOI=10.1182/blood-2002-02-0513;
RA Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M.,
RA Barrett P., Gribben J.G.;
RT "Identification of tumor-associated antigens in chronic lymphocytic
RT leukemia by SEREX.";
RL Blood 100:2123-2131(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-239, AND VARIANTS VAL-178; ASP-200 AND
RP HIS-212.
RC TISSUE=Thymus;
RA Ruehlmann A., Gupta A., Terhorst C.;
RT "A novel murine RRM-type protein and its human homolog.";
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-239.
RC TISSUE=Tonsil;
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 [6]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), RNA-BINDING, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=17050675; DOI=10.1101/gad.1463306;
RA Shu L., Yan W., Chen X.;
RT "RNPC1, an RNA-binding protein and a target of the p53 family, is required
RT for maintaining the stability of the basal and stress-induced p21
RT transcript.";
RL Genes Dev. 20:2961-2972(2006).
RN [7]
RP FUNCTION.
RX PubMed=19285943; DOI=10.1016/j.molcel.2009.01.025;
RA Warzecha C.C., Sato T.K., Nabet B., Hogenesch J.B., Carstens R.P.;
RT "ESRP1 and ESRP2 are epithelial cell-type-specific regulators of FGFR2
RT splicing.";
RL Mol. Cell 33:591-601(2009).
RN [8]
RP STRUCTURE BY NMR OF 24-126.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA recognition motif in RNA-binding region
RT containing protein 1.";
RL Submitted (MAY-2005) to the PDB data bank.
RN [9]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=29437973; DOI=10.1128/jvi.02050-17;
RA Ganaie S.S., Chen A.Y., Huang C., Xu P., Kleiboeker S., Du A., Qiu J.;
RT "RNA binding protein RBM38 regulates expression of the 11-Kilodalton
RT protein of Parvovirus B19, which facilitates viral DNA replication.";
RL J. Virol. 92:0-0(2018).
CC -!- FUNCTION: RNA-binding protein that specifically bind the 3'-UTR of
CC CDKN1A transcripts, leading to maintain the stability of CDKN1A
CC transcripts, thereby acting as a mediator of the p53/TP53 family to
CC regulate CDKN1A. CDKN1A is a cyclin-dependent kinase inhibitor
CC transcriptionally regulated by the p53/TP53 family to induce cell cycle
CC arrest. Isoform 1, but not isoform 2, has the ability to induce cell
CC cycle arrest in G1 and maintain the stability of CDKN1A transcripts
CC induced by p53/TP53. Also acts as a mRNA splicing factor. Specifically
CC regulates the expression of FGFR2-IIIb, an epithelial cell-specific
CC isoform of FGFR2. Plays a role in myogenic differentiation.
CC {ECO:0000269|PubMed:17050675, ECO:0000269|PubMed:19285943}.
CC -!- FUNCTION: (Microbial infection) Essential factor for the splicing of
CC the pre-mRNAs of human parvovirus B19 (B19V) and for the expression of
CC B19V 11-kDa protein, which enhances viral replication.
CC {ECO:0000269|PubMed:29437973}.
CC -!- INTERACTION:
CC Q9H0Z9; P31943: HNRNPH1; NbExp=3; IntAct=EBI-2840723, EBI-351590;
CC Q9H0Z9; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-2840723, EBI-742550;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17050675}.
CC Nucleus {ECO:0000269|PubMed:17050675}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=RNPC1a;
CC IsoId=Q9H0Z9-1; Sequence=Displayed;
CC Name=2; Synonyms=RNPC1b;
CC IsoId=Q9H0Z9-2; Sequence=VSP_035881;
CC -!- INDUCTION: By p53/TP53 family. Directly induced by p53/TP53, TP63/p63
CC and TP73/p73. {ECO:0000269|PubMed:17050675}.
CC -!- SIMILARITY: Belongs to the RBM38 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-24 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18711.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL99924.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA53064.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
CC Sequence=EAW75522.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF432218; AAL99924.1; ALT_INIT; mRNA.
DR EMBL; AL109955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75522.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X75314; CAA53063.1; -; mRNA.
DR EMBL; X75315; CAA53064.1; ALT_SEQ; mRNA.
DR EMBL; BC018711; AAH18711.1; ALT_INIT; mRNA.
DR CCDS; CCDS46617.1; -. [Q9H0Z9-1]
DR CCDS; CCDS46618.1; -. [Q9H0Z9-2]
DR RefSeq; NP_001278709.1; NM_001291780.1.
DR RefSeq; NP_059965.2; NM_017495.5. [Q9H0Z9-1]
DR RefSeq; NP_906270.1; NM_183425.2. [Q9H0Z9-2]
DR PDB; 2CQD; NMR; -; A=24-126.
DR PDB; 6JVX; X-ray; 2.30 A; A=26-121.
DR PDB; 6JVY; X-ray; 2.00 A; A=26-121.
DR PDBsum; 2CQD; -.
DR PDBsum; 6JVX; -.
DR PDBsum; 6JVY; -.
DR AlphaFoldDB; Q9H0Z9; -.
DR SMR; Q9H0Z9; -.
DR BioGRID; 120710; 27.
DR IntAct; Q9H0Z9; 13.
DR STRING; 9606.ENSP00000348538; -.
DR iPTMnet; Q9H0Z9; -.
DR PhosphoSitePlus; Q9H0Z9; -.
DR BioMuta; RBM38; -.
DR DMDM; 215273895; -.
DR EPD; Q9H0Z9; -.
DR jPOST; Q9H0Z9; -.
DR MassIVE; Q9H0Z9; -.
DR MaxQB; Q9H0Z9; -.
DR PaxDb; Q9H0Z9; -.
DR PeptideAtlas; Q9H0Z9; -.
DR PRIDE; Q9H0Z9; -.
DR ProteomicsDB; 80346; -. [Q9H0Z9-1]
DR ProteomicsDB; 80347; -. [Q9H0Z9-2]
DR Antibodypedia; 28985; 137 antibodies from 21 providers.
DR DNASU; 55544; -.
DR Ensembl; ENST00000356208.10; ENSP00000348538.5; ENSG00000132819.17. [Q9H0Z9-1]
DR Ensembl; ENST00000440234.6; ENSP00000407848.2; ENSG00000132819.17. [Q9H0Z9-2]
DR GeneID; 55544; -.
DR KEGG; hsa:55544; -.
DR MANE-Select; ENST00000356208.10; ENSP00000348538.5; NM_017495.6; NP_059965.2.
DR UCSC; uc010zzj.3; human. [Q9H0Z9-1]
DR CTD; 55544; -.
DR DisGeNET; 55544; -.
DR GeneCards; RBM38; -.
DR HGNC; HGNC:15818; RBM38.
DR HPA; ENSG00000132819; Tissue enhanced (bone marrow, skeletal muscle).
DR MIM; 612428; gene.
DR neXtProt; NX_Q9H0Z9; -.
DR OpenTargets; ENSG00000132819; -.
DR PharmGKB; PA34449; -.
DR VEuPathDB; HostDB:ENSG00000132819; -.
DR eggNOG; KOG0149; Eukaryota.
DR GeneTree; ENSGT00940000158489; -.
DR HOGENOM; CLU_065652_0_1_1; -.
DR InParanoid; Q9H0Z9; -.
DR OMA; HLQPERM; -.
DR OrthoDB; 1579773at2759; -.
DR PhylomeDB; Q9H0Z9; -.
DR TreeFam; TF314235; -.
DR PathwayCommons; Q9H0Z9; -.
DR SignaLink; Q9H0Z9; -.
DR SIGNOR; Q9H0Z9; -.
DR BioGRID-ORCS; 55544; 26 hits in 1081 CRISPR screens.
DR ChiTaRS; RBM38; human.
DR EvolutionaryTrace; Q9H0Z9; -.
DR GenomeRNAi; 55544; -.
DR Pharos; Q9H0Z9; Tbio.
DR PRO; PR:Q9H0Z9; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H0Z9; protein.
DR Bgee; ENSG00000132819; Expressed in hindlimb stylopod muscle and 193 other tissues.
DR ExpressionAtlas; Q9H0Z9; baseline and differential.
DR Genevisible; Q9H0Z9; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IDA:UniProtKB.
DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:0010830; P:regulation of myotube differentiation; IEA:Ensembl.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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 Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cytoplasm; Differentiation;
KW Host-virus interaction; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1..239
FT /note="RNA-binding protein 38"
FT /id="PRO_0000081812"
FT DOMAIN 34..111
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT VAR_SEQ 122..239
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035881"
FT VARIANT 178
FT /note="A -> V (in dbSNP:rs1065288)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_015225"
FT VARIANT 200
FT /note="A -> D (in dbSNP:rs1065289)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_015226"
FT VARIANT 212
FT /note="P -> H (in dbSNP:rs1065290)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_015227"
FT VARIANT 226
FT /note="V -> L (in dbSNP:rs16980970)"
FT /id="VAR_059823"
FT CONFLICT 15
FT /note="P -> S (in Ref. 4; CAA53063)"
FT /evidence="ECO:0000305"
FT CONFLICT 23..25
FT /note="AMH -> VMY (in Ref. 4; CAA53063)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="H -> Y (in Ref. 4; CAA53063)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="D -> G (in Ref. 4; CAA53063)"
FT /evidence="ECO:0000305"
FT CONFLICT 116..117
FT /note="RS -> WC (in Ref. 4; CAA53063/CAA53064)"
FT /evidence="ECO:0000305"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:6JVY"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:6JVY"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:6JVY"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:6JVY"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:6JVY"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:6JVY"
FT STRAND 73..84
FT /evidence="ECO:0007829|PDB:6JVY"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:6JVY"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:6JVY"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:6JVY"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:6JVY"
SQ SEQUENCE 239 AA; 25498 MW; F20038A92C980757 CRC64;
MLLQPAPCAP SAGFPRPLAA PGAMHGSQKD TTFTKIFVGG LPYHTTDASL RKYFEGFGDI
EEAVVITDRQ TGKSRGYGFV TMADRAAAER ACKDPNPIID GRKANVNLAY LGAKPRSLQT
GFAIGVQQLH PTLIQRTYGL TPHYIYPPAI VQPSVVIPAA PVPSLSSPYI EYTPASPAYA
QYPPATYDQY PYAASPATAA SFVGYSYPAA VPQALSAAAP AGTTFVQYQA PQLQPDRMQ
