ID   RBM19_HUMAN             Reviewed;         960 AA.
AC   Q9Y4C8; Q9BPY6; Q9UFN5;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   05-OCT-2010, entry version 96.
DE   RecName: Full=Probable RNA-binding protein 19;
DE   AltName: Full=RNA-binding motif protein 19;
GN   Name=RBM19; Synonyms=KIAA0682;
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 [LARGE SCALE MRNA], AND VARIANTS GLU-602; ARG-609;
RP   THR-623 AND ALA-665.
RC   TISSUE=Brain;
RX   MEDLINE=98403880; PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA   Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA   Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. X.
RT   The complete sequences of 100 new cDNA clones from brain which can
RT   code for large proteins in vitro.";
RL   DNA Res. 5:169-176(1998).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS.
RA   Ohara O., Suyama M., Nagase T., Ishikawa K.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-602 AND
RP   GLN-921.
RC   TISSUE=Uterus;
RX   MEDLINE=21154917; PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA   Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA   Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA   Wambutt R., Korn B., Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and
RT   analysis of 500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-602; ARG-609;
RP   THR-623 AND ALA-665.
RC   TISSUE=Lymph;
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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   MEDLINE=22317277; PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
RA   Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA   Greco A., Hochstrasser D.F., Diaz J.-J.;
RT   "Functional proteomic analysis of human nucleolus.";
RL   Mol. Biol. Cell 13:4100-4109(2002).
RN   [7]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16027046; DOI=10.1016/j.modgep.2005.05.001;
RA   Lorenzen J.A., Bonacci B.B., Palmer R.E., Wells C., Zhang J.,
RA   Haber D.A., Goldstein A.M., Mayer A.N.;
RT   "Rbm19 is a nucleolar protein expressed in crypt/progenitor cells of
RT   the intestinal epithelium.";
RL   Gene Expr. Patterns 6:45-56(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-949; SER-951 AND
RP   THR-957, AND MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-176 AND
RP   SER-180, AND MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   STRUCTURE BY NMR OF 291-373.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the second RNA recognition motif in RNA-binding
RT   protein 19.";
RL   Submitted (SEP-2006) to the PDB data bank.
CC   -!- FUNCTION: Plays a role in embryo pre-implantation development (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm (By
CC       similarity). Cytoplasm (By similarity). Chromosome (By
CC       similarity). Note=In discrete foci distributed throughout the
CC       cytoplasm and nucleoplasm during the 4 to 8 cell stages and the
CC       morula stage, but not in the periphery of the nucleolar precursor
CC       body (NPB). During blastocyst development, becomes increasingly
CC       localized to the nucleolus and less to the cytoplasm. At the late
CC       blastocyst stage, localized predominantly in the nucleolus.
CC       Localized in the nucleolus during interphase and to the
CC       perichromosomal sheath during mitosis. Does not colocalize in the
CC       cytoplasm with GW182 in P-bodies. May translocate to the nucleolus
CC       upon early embryonic development (By similarity). Colocalizes with
CC       NPM1 during interphase. By late prophase, metaphase, anaphase and
CC       telophase, associates with the chromosome periphery. By telophase
CC       localizes to NPB.
CC   -!- TISSUE SPECIFICITY: Expressed in the crypts of Lieberkuhn of the
CC       intestine and in intestinal neoplasia (at protein level).
CC   -!- SIMILARITY: Belongs to the RRM MRD1 family.
CC   -!- SIMILARITY: Contains 6 RRM (RNA recognition motif) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA31657.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AB014582; BAA31657.2; ALT_INIT; mRNA.
DR   EMBL; AL117547; CAB55987.1; -; mRNA.
DR   EMBL; AC009731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC073863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC004289; AAH04289.1; -; mRNA.
DR   EMBL; BC006137; AAH06137.1; -; mRNA.
DR   IPI; IPI00000686; -.
DR   PIR; T17297; T17297.
DR   RefSeq; NP_001140170.1; -.
DR   RefSeq; NP_057280.2; -.
DR   UniGene; Hs.7482; -.
DR   PDB; 2DGW; NMR; -; A=291-368.
DR   PDBsum; 2DGW; -.
DR   ProteinModelPortal; Q9Y4C8; -.
DR   SMR; Q9Y4C8; 295-479, 403-810, 587-913, 824-918.
DR   MINT; MINT-1196129; -.
DR   STRING; Q9Y4C8; -.
DR   PhosphoSite; Q9Y4C8; -.
DR   SWISS-2DPAGE; Q9Y4C8; -.
DR   PRIDE; Q9Y4C8; -.
DR   Ensembl; ENST00000261741; ENSP00000261741; ENSG00000122965.
DR   Ensembl; ENST00000392561; ENSP00000376344; ENSG00000122965.
DR   GeneID; 9904; -.
DR   KEGG; hsa:9904; -.
DR   CTD; 9904; -.
DR   GeneCards; GC12M114259; -.
DR   HGNC; HGNC:29098; RBM19.
DR   PharmGKB; PA134886784; -.
DR   eggNOG; prNOG12426; -.
DR   HOGENOM; HBG412223; -.
DR   HOVERGEN; HBG055637; -.
DR   InParanoid; Q9Y4C8; -.
DR   PhylomeDB; Q9Y4C8; -.
DR   NextBio; 37345; -.
DR   ArrayExpress; Q9Y4C8; -.
DR   Bgee; Q9Y4C8; -.
DR   CleanEx; HS_RBM19; -.
DR   Genevestigator; Q9Y4C8; -.
DR   GermOnline; ENSG00000122965; Homo sapiens.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
DR   InterPro; IPR012677; a_b_plait_nuc-bd.
DR   InterPro; IPR000504; RRM_RNP1.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 6.
DR   Pfam; PF00076; RRM_1; 5.
DR   SMART; SM00360; RRM; 6.
DR   PROSITE; PS50102; RRM; 6.
PE   1: Evidence at protein level;
KW   3D-structure; Chromosome; Complete proteome; Cytoplasm;
KW   Developmental protein; Nucleus; Phosphoprotein; Polymorphism; Repeat;
KW   RNA-binding.
FT   CHAIN         1    960       Probable RNA-binding protein 19.
FT                                /FTId=PRO_0000081781.
FT   DOMAIN        2     79       RRM 1.
FT   DOMAIN      294    369       RRM 2.
FT   DOMAIN      402    480       RRM 3.
FT   DOMAIN      587    659       RRM 4.
FT   DOMAIN      730    811       RRM 5.
FT   DOMAIN      832    912       RRM 6.
FT   COMPBIAS    225    232       Poly-Glu.
FT   COMPBIAS    391    396       Poly-Glu.
FT   COMPBIAS    714    725       Poly-Glu.
FT   MOD_RES     174    174       Phosphoserine.
FT   MOD_RES     176    176       Phosphoserine.
FT   MOD_RES     180    180       Phosphoserine.
FT   MOD_RES     949    949       Phosphoserine.
FT   MOD_RES     951    951       Phosphoserine.
FT   MOD_RES     957    957       Phosphothreonine.
FT   VARIANT     602    602       Q -> E (in dbSNP:rs7299217).
FT                                /FTId=VAR_059822.
FT   VARIANT     609    609       H -> R (in dbSNP:rs2290789).
FT                                /FTId=VAR_023114.
FT   VARIANT     623    623       I -> T (in dbSNP:rs2290788).
FT                                /FTId=VAR_023115.
FT   VARIANT     665    665       T -> A (in dbSNP:rs2290787).
FT                                /FTId=VAR_023116.
FT   VARIANT     821    821       R -> G (in dbSNP:rs16943379).
FT                                /FTId=VAR_057246.
FT   VARIANT     921    921       R -> Q (in dbSNP:rs2075387).
FT                                /FTId=VAR_023117.
FT   CONFLICT    141    141       Q -> R (in Ref. 1; BAA31657).
FT   CONFLICT    259    259       K -> R (in Ref. 1; BAA31657 and 5;
FT                                AAH06137/AAH04289).
FT   STRAND      295    299
FT   HELIX       307    314
FT   STRAND      320    326
FT   STRAND      332    339
FT   HELIX       343    351
FT   STRAND      354    357
SQ   SEQUENCE   960 AA;  107332 MW;  28B6F37B18D7B9B1 CRC64;
     MSRLIVKNLP NGMKEERFRQ LFAAFGTLTD CSLKFTKDGK FRKFGFIGFK SEEEAQKAQK
     HFNKSFIDTS RITVEFCKSF GDPAKPRAWS KHAQKPSQPK QPPKDSTTPE IKKDEKKKKV
     AGQLEKLKED TEFQEFLSVH QRRAQAATWA NDGLDAEPSK GKSKPASDYL NFDSDSGQES
     EEEGAGEDLE EEASLEPKAA VQKELSDMDY LKSKMVKAGS SSSSEEEESE DEAVHCDEGS
     EAEEEDSSAT PVLQERDSKG AGQEQGMPAG KKRPPEARAE TEKPANQKEP TTCHTVKLRG
     APFNVTEKNV MEFLAPLKPV AIRIVRNAHG NKTGYIFVDF SNEEEVKQAL KCNREYMGGR
     YIEVFREKNV PTTKGAPKNT TKSWQGRILG ENEEEEDLAE SGRLFVRNLP YTSTEEDLEK
     LFSKYGPLSE LHYPIDSLTK KPKGFAFITF MFPEHAVKAY SEVDGQVFQG RMLHVLPSTI
     KKEASEDASA LGSSSYKKKK EAQDKANSAS SHNWNTLFMG PNAVADAIAQ KYNATKSQVF
     DHETKGSVAV RVALGETQLV QEVRRFLIDN GVSLDSFSQA AAERSKTVIL VKNLPAGTLA
     AQLQETFGHF GSLGRVLLPE GGITAIVEFL EPLEARKAFR HLAYSKFHHV PLYLEWAPVG
     VFSSTAPQKK KLQDTPSEPM EKDPAEPETV PDGETPEDEN PTEEGADNSS AKMEEEEEEE
     EEEEESLPGC TLFIKNLNFD TTEEKLKEVF SKVGTVKSCS ISKKKNKAGV LLSMGFGFVE
     YRKPEQAQKA LKQLQGHVVD GHKLEVRISE RATKPAVTLA RKKQVPRKQT TSKILVRNIP
     FQAHSREIRE LFSTFGELKT VRLPKKMTGT GTHRGFGFVD FLTKQDAKRA FNALCHSTHL
     YGRRLVLEWA DSEVTLQALR RKTAAHFHEP PKKKRSVVLD EILEQLEGSD SDSEEQTLQL
//