Full text data of RBM38
RBM38
(RNPC1, SEB4)
[Confidence: low (only semi-automatic identification from reviews)]
RNA-binding protein 38 (CLL-associated antigen KW-5; HSRNASEB; RNA-binding motif protein 38; RNA-binding region-containing protein 1; ssDNA-binding protein SEB4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
RNA-binding protein 38 (CLL-associated antigen KW-5; HSRNASEB; RNA-binding motif protein 38; RNA-binding region-containing protein 1; ssDNA-binding protein SEB4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H0Z9
ID RBM38_HUMAN Reviewed; 239 AA.
AC Q9H0Z9; A6NDK1; A6NMU6; Q15350; Q15351; Q9BYK3; Q9BYK4;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-NOV-2008, sequence version 2.
DT 22-JAN-2014, entry version 113.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Chessia M., 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RP AND 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), RNA-BINDING,
RP SUBCELLULAR 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
RT required for maintaining the stability of the basal and stress-induced
RT p21 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.
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
CC to regulate CDKN1A. CDKN1A is a cyclin-dependent kinase inhibitor
CC transcriptionally regulated by the p53/TP53 family to induce cell
CC cycle arrest. Isoform 1, but not isoform 2, has the ability to
CC induce cell cycle arrest in G1 and maintain the stability of
CC CDKN1A transcripts induced by p53/TP53. Also acts as a mRNA
CC splicing factor. Specifically regulates the expression of FGFR2-
CC IIIb, an epithelial cell-specific isoform of FGFR2. Plays a role
CC in myogenic differentiation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus.
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,
CC TP63/p63 and TP73/p73.
CC -!- SIMILARITY: Belongs to the RBM38 family.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-24 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18711.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAL99924.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAA53064.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA;
CC Sequence=EAW75522.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_059965.2; NM_017495.5.
DR RefSeq; NP_906270.1; NM_183425.2.
DR UniGene; Hs.236361; -.
DR PDB; 2CQD; NMR; -; A=24-126.
DR PDBsum; 2CQD; -.
DR ProteinModelPortal; Q9H0Z9; -.
DR SMR; Q9H0Z9; 28-126.
DR IntAct; Q9H0Z9; 6.
DR STRING; 9606.ENSP00000348538; -.
DR PhosphoSite; Q9H0Z9; -.
DR DMDM; 215273895; -.
DR PaxDb; Q9H0Z9; -.
DR PRIDE; Q9H0Z9; -.
DR DNASU; 55544; -.
DR Ensembl; ENST00000356208; ENSP00000348538; ENSG00000132819.
DR Ensembl; ENST00000440234; ENSP00000407848; ENSG00000132819.
DR GeneID; 55544; -.
DR KEGG; hsa:55544; -.
DR UCSC; uc010zzj.2; human.
DR CTD; 55544; -.
DR GeneCards; GC20P055966; -.
DR H-InvDB; HIX0015939; -.
DR HGNC; HGNC:15818; RBM38.
DR HPA; CAB017036; -.
DR MIM; 612428; gene.
DR neXtProt; NX_Q9H0Z9; -.
DR PharmGKB; PA34449; -.
DR eggNOG; COG0724; -.
DR HOVERGEN; HBG108399; -.
DR InParanoid; Q9H0Z9; -.
DR OMA; QSITSPY; -.
DR OrthoDB; EOG77M8Q4; -.
DR EvolutionaryTrace; Q9H0Z9; -.
DR GenomeRNAi; 55544; -.
DR NextBio; 59995; -.
DR PRO; PR:Q9H0Z9; -.
DR ArrayExpress; Q9H0Z9; -.
DR Bgee; Q9H0Z9; -.
DR CleanEx; HS_RBM38; -.
DR Genevestigator; Q9H0Z9; -.
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:0000166; F:nucleotide binding; IEA:InterPro.
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:0007050; P:cell cycle arrest; IDA:UniProtKB.
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:0008285; P:negative regulation of cell proliferation; 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.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Complete proteome;
KW Cytoplasm; Differentiation; mRNA processing; mRNA splicing; Nucleus;
KW Polymorphism; Reference proteome; RNA-binding.
FT CHAIN 1 239 RNA-binding protein 38.
FT /FTId=PRO_0000081812.
FT DOMAIN 34 111 RRM.
FT VAR_SEQ 122 239 Missing (in isoform 2).
FT /FTId=VSP_035881.
FT VARIANT 178 178 A -> V (in dbSNP:rs1065288).
FT /FTId=VAR_015225.
FT VARIANT 200 200 A -> D (in dbSNP:rs1065289).
FT /FTId=VAR_015226.
FT VARIANT 212 212 P -> H (in dbSNP:rs1065290).
FT /FTId=VAR_015227.
FT VARIANT 226 226 V -> L (in dbSNP:rs16980970).
FT /FTId=VAR_059823.
FT CONFLICT 15 15 P -> S (in Ref. 4; CAA53063).
FT CONFLICT 23 25 AMH -> VMY (in Ref. 4; CAA53063).
FT CONFLICT 25 25 H -> Y (in Ref. 4; CAA53063).
FT CONFLICT 30 30 D -> G (in Ref. 4; CAA53063).
FT CONFLICT 116 117 RS -> WC (in Ref. 4; CAA53063/CAA53064).
FT STRAND 32 39
FT HELIX 47 55
FT STRAND 60 66
FT STRAND 69 71
FT STRAND 76 84
FT HELIX 85 92
FT STRAND 105 109
FT TURN 110 112
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
//
ID RBM38_HUMAN Reviewed; 239 AA.
AC Q9H0Z9; A6NDK1; A6NMU6; Q15350; Q15351; Q9BYK3; Q9BYK4;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-NOV-2008, sequence version 2.
DT 22-JAN-2014, entry version 113.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Chessia M., 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RP AND 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), RNA-BINDING,
RP SUBCELLULAR 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
RT required for maintaining the stability of the basal and stress-induced
RT p21 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.
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
CC to regulate CDKN1A. CDKN1A is a cyclin-dependent kinase inhibitor
CC transcriptionally regulated by the p53/TP53 family to induce cell
CC cycle arrest. Isoform 1, but not isoform 2, has the ability to
CC induce cell cycle arrest in G1 and maintain the stability of
CC CDKN1A transcripts induced by p53/TP53. Also acts as a mRNA
CC splicing factor. Specifically regulates the expression of FGFR2-
CC IIIb, an epithelial cell-specific isoform of FGFR2. Plays a role
CC in myogenic differentiation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus.
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,
CC TP63/p63 and TP73/p73.
CC -!- SIMILARITY: Belongs to the RBM38 family.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-24 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18711.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAL99924.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAA53064.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA;
CC Sequence=EAW75522.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_059965.2; NM_017495.5.
DR RefSeq; NP_906270.1; NM_183425.2.
DR UniGene; Hs.236361; -.
DR PDB; 2CQD; NMR; -; A=24-126.
DR PDBsum; 2CQD; -.
DR ProteinModelPortal; Q9H0Z9; -.
DR SMR; Q9H0Z9; 28-126.
DR IntAct; Q9H0Z9; 6.
DR STRING; 9606.ENSP00000348538; -.
DR PhosphoSite; Q9H0Z9; -.
DR DMDM; 215273895; -.
DR PaxDb; Q9H0Z9; -.
DR PRIDE; Q9H0Z9; -.
DR DNASU; 55544; -.
DR Ensembl; ENST00000356208; ENSP00000348538; ENSG00000132819.
DR Ensembl; ENST00000440234; ENSP00000407848; ENSG00000132819.
DR GeneID; 55544; -.
DR KEGG; hsa:55544; -.
DR UCSC; uc010zzj.2; human.
DR CTD; 55544; -.
DR GeneCards; GC20P055966; -.
DR H-InvDB; HIX0015939; -.
DR HGNC; HGNC:15818; RBM38.
DR HPA; CAB017036; -.
DR MIM; 612428; gene.
DR neXtProt; NX_Q9H0Z9; -.
DR PharmGKB; PA34449; -.
DR eggNOG; COG0724; -.
DR HOVERGEN; HBG108399; -.
DR InParanoid; Q9H0Z9; -.
DR OMA; QSITSPY; -.
DR OrthoDB; EOG77M8Q4; -.
DR EvolutionaryTrace; Q9H0Z9; -.
DR GenomeRNAi; 55544; -.
DR NextBio; 59995; -.
DR PRO; PR:Q9H0Z9; -.
DR ArrayExpress; Q9H0Z9; -.
DR Bgee; Q9H0Z9; -.
DR CleanEx; HS_RBM38; -.
DR Genevestigator; Q9H0Z9; -.
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:0000166; F:nucleotide binding; IEA:InterPro.
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:0007050; P:cell cycle arrest; IDA:UniProtKB.
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:0008285; P:negative regulation of cell proliferation; 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.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Complete proteome;
KW Cytoplasm; Differentiation; mRNA processing; mRNA splicing; Nucleus;
KW Polymorphism; Reference proteome; RNA-binding.
FT CHAIN 1 239 RNA-binding protein 38.
FT /FTId=PRO_0000081812.
FT DOMAIN 34 111 RRM.
FT VAR_SEQ 122 239 Missing (in isoform 2).
FT /FTId=VSP_035881.
FT VARIANT 178 178 A -> V (in dbSNP:rs1065288).
FT /FTId=VAR_015225.
FT VARIANT 200 200 A -> D (in dbSNP:rs1065289).
FT /FTId=VAR_015226.
FT VARIANT 212 212 P -> H (in dbSNP:rs1065290).
FT /FTId=VAR_015227.
FT VARIANT 226 226 V -> L (in dbSNP:rs16980970).
FT /FTId=VAR_059823.
FT CONFLICT 15 15 P -> S (in Ref. 4; CAA53063).
FT CONFLICT 23 25 AMH -> VMY (in Ref. 4; CAA53063).
FT CONFLICT 25 25 H -> Y (in Ref. 4; CAA53063).
FT CONFLICT 30 30 D -> G (in Ref. 4; CAA53063).
FT CONFLICT 116 117 RS -> WC (in Ref. 4; CAA53063/CAA53064).
FT STRAND 32 39
FT HELIX 47 55
FT STRAND 60 66
FT STRAND 69 71
FT STRAND 76 84
FT HELIX 85 92
FT STRAND 105 109
FT TURN 110 112
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
//
MIM
612428
*RECORD*
*FIELD* NO
612428
*FIELD* TI
*612428 RNA-BINDING MOTIF PROTEIN 38; RBM38
;;RNPC1
*FIELD* TX
CLONING
Using microarray analysis to identify potential p53 (TP53; 191170)
read moretarget genes in human cell lines, Shu et al. (2006) identified and
cloned 2 variants of RBM38, which they called RNPC1a and RNPC1b. The
deduced proteins contain 239 and 121 amino acids, respectively, and both
contain an identical N-terminal canonical RNA recognition motif made up
of 2 conserved submotifs, RNP1 and RNP2. Immunofluorescence analysis
localized both proteins in the perinuclear membrane and cytosol, with a
larger proportion of RNPC1b localized to the cytosol than the nucleus.
GENE FUNCTION
Shu et al. (2006) found that expression of RNPC1 transcripts in several
human cell lines was induced by wildtype p53, but not by an inactive p53
mutant. Both RNPC1a and RNPC1b were also induced by several p63 (TP63;
603273) and p73 (TP73; 601990) isoforms. RNPC1 expression was induced by
DNA-damaging agents in cells expressing wildtype p53, but not in cells
lacking p53 expression. Shu et al. (2006) identified 2 potential
p53-responsive elements in the promoter region of RNPC1. Chromatin
immunoprecipitation analysis and reporter gene assays showed that p53
bound and activated both sites. Overexpression of RNPC1a, but not
RNPC1b, induced cell cycle arrest in G1, and cell cycle arrest was
independent of p53 or expression of the p53 target protein p21 (CDKN1A;
116899). Both RNPC1a and RNPC1b bound the 3-prime region of the p21
transcript, but only RNPC1a increased p21 mRNA and protein levels.
Northern blot analysis revealed that the half-life of p21 mRNA was more
than doubled by RNPC1a expression. Shu et al. (2006) concluded that
RNPC1a mediates p53-induced cell cycle arrest by stabilizing p21 mRNA.
MAPPING
Hartz (2008) mapped the RBM38 gene to chromosome 20q13.31 based on an
alignment of the RBM38 sequence (GenBank GENBANK BC018711) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 11/20/2008.
2. Shu, L.; Yan, W.; Chen, X.: RNPC1, an RNA-binding protein and
a target of the p53 family, is required for maintaining the stability
of the basal and stress-induced p21 transcript. Genes Dev. 20: 2961-2972,
2006.
*FIELD* CD
Patricia A. Hartz: 11/20/2008
*FIELD* ED
mgross: 11/20/2008
*RECORD*
*FIELD* NO
612428
*FIELD* TI
*612428 RNA-BINDING MOTIF PROTEIN 38; RBM38
;;RNPC1
*FIELD* TX
CLONING
Using microarray analysis to identify potential p53 (TP53; 191170)
read moretarget genes in human cell lines, Shu et al. (2006) identified and
cloned 2 variants of RBM38, which they called RNPC1a and RNPC1b. The
deduced proteins contain 239 and 121 amino acids, respectively, and both
contain an identical N-terminal canonical RNA recognition motif made up
of 2 conserved submotifs, RNP1 and RNP2. Immunofluorescence analysis
localized both proteins in the perinuclear membrane and cytosol, with a
larger proportion of RNPC1b localized to the cytosol than the nucleus.
GENE FUNCTION
Shu et al. (2006) found that expression of RNPC1 transcripts in several
human cell lines was induced by wildtype p53, but not by an inactive p53
mutant. Both RNPC1a and RNPC1b were also induced by several p63 (TP63;
603273) and p73 (TP73; 601990) isoforms. RNPC1 expression was induced by
DNA-damaging agents in cells expressing wildtype p53, but not in cells
lacking p53 expression. Shu et al. (2006) identified 2 potential
p53-responsive elements in the promoter region of RNPC1. Chromatin
immunoprecipitation analysis and reporter gene assays showed that p53
bound and activated both sites. Overexpression of RNPC1a, but not
RNPC1b, induced cell cycle arrest in G1, and cell cycle arrest was
independent of p53 or expression of the p53 target protein p21 (CDKN1A;
116899). Both RNPC1a and RNPC1b bound the 3-prime region of the p21
transcript, but only RNPC1a increased p21 mRNA and protein levels.
Northern blot analysis revealed that the half-life of p21 mRNA was more
than doubled by RNPC1a expression. Shu et al. (2006) concluded that
RNPC1a mediates p53-induced cell cycle arrest by stabilizing p21 mRNA.
MAPPING
Hartz (2008) mapped the RBM38 gene to chromosome 20q13.31 based on an
alignment of the RBM38 sequence (GenBank GENBANK BC018711) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 11/20/2008.
2. Shu, L.; Yan, W.; Chen, X.: RNPC1, an RNA-binding protein and
a target of the p53 family, is required for maintaining the stability
of the basal and stress-induced p21 transcript. Genes Dev. 20: 2961-2972,
2006.
*FIELD* CD
Patricia A. Hartz: 11/20/2008
*FIELD* ED
mgross: 11/20/2008