(data stored in ACNUC10243 zone)

SWISSPROT: ROA3_MOUSE

ID   ROA3_MOUSE              Reviewed;         379 AA.
AC   Q8BG05; Q8BHF8;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   30-AUG-2017, entry version 138.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein A3;
DE            Short=hnRNP A3;
GN   Name=Hnrnpa3; Synonyms=Hnrpa3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Bayarsaihan D.;
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Colon, and Eye;
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   [3]
RP   PROTEIN SEQUENCE OF 114-126, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, Pancreas, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-226; ARG-239; ARG-246 AND
RP   ARG-257, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.O113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Plays a role in cytoplasmic trafficking of RNA. Binds to
CC       the cis-acting response element, A2RE. May be involved in pre-mRNA
CC       splicing (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Identified in the spliceosome C complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Component of
CC       ribonucleosomes. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BG05-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BG05-2; Sequence=VSP_007350;
DR   EMBL; AF463524; AAN76992.1; -; mRNA.
DR   EMBL; BC023828; AAH23828.1; -; mRNA.
DR   EMBL; BC023908; AAH23908.1; -; mRNA.
DR   EMBL; BC038364; AAH38364.1; -; mRNA.
DR   EMBL; BC064824; AAH64824.1; -; mRNA.
DR   CCDS; CCDS16149.1; -. [Q8BG05-1]
DR   CCDS; CCDS50610.1; -. [Q8BG05-2]
DR   RefSeq; NP_444493.1; NM_053263.1. [Q8BG05-2]
DR   RefSeq; NP_666242.2; NM_146130.3. [Q8BG05-1]
DR   RefSeq; NP_932758.1; NM_198090.2. [Q8BG05-1]
DR   RefSeq; XP_011237818.1; XM_011239516.2. [Q8BG05-2]
DR   UniGene; Mm.316306; -.
DR   UniGene; Mm.331491; -.
DR   UniGene; Mm.379375; -.
DR   ProteinModelPortal; Q8BG05; -.
DR   SMR; Q8BG05; -.
DR   BioGrid; 230827; 33.
DR   IntAct; Q8BG05; 34.
DR   MINT; MINT-1868174; -.
DR   STRING; 10090.ENSMUSP00000088298; -.
DR   iPTMnet; Q8BG05; -.
DR   PhosphoSitePlus; Q8BG05; -.
DR   SwissPalm; Q8BG05; -.
DR   REPRODUCTION-2DPAGE; Q8BG05; -.
DR   EPD; Q8BG05; -.
DR   PaxDb; Q8BG05; -.
DR   PRIDE; Q8BG05; -.
DR   TopDownProteomics; Q8BG05-1; -. [Q8BG05-1]
DR   Ensembl; ENSMUST00000090792; ENSMUSP00000088298; ENSMUSG00000059005. [Q8BG05-1]
DR   Ensembl; ENSMUST00000111962; ENSMUSP00000107593; ENSMUSG00000059005. [Q8BG05-2]
DR   Ensembl; ENSMUST00000111964; ENSMUSP00000107595; ENSMUSG00000059005. [Q8BG05-1]
DR   Ensembl; ENSMUST00000164947; ENSMUSP00000126069; ENSMUSG00000059005. [Q8BG05-2]
DR   GeneID; 229279; -.
DR   KEGG; mmu:229279; -.
DR   UCSC; uc008ken.2; mouse. [Q8BG05-1]
DR   CTD; 220988; -.
DR   MGI; MGI:1917171; Hnrnpa3.
DR   eggNOG; KOG0118; Eukaryota.
DR   eggNOG; COG0724; LUCA.
DR   GeneTree; ENSGT00760000118873; -.
DR   HOGENOM; HOG000234442; -.
DR   HOVERGEN; HBG002295; -.
DR   InParanoid; Q8BG05; -.
DR   KO; K12741; -.
DR   OMA; YYDSTGY; -.
DR   OrthoDB; EOG091G1CPI; -.
DR   TreeFam; TF314808; -.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   PRO; PR:Q8BG05; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000059005; -.
DR   ExpressionAtlas; Q8BG05; baseline and differential.
DR   Genevisible; Q8BG05; MM.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd12763; RRM1_hnRNPA3; 1.
DR   CDD; cd12582; RRM2_hnRNPA3; 1.
DR   InterPro; IPR034513; hnRNPA3_RRM1.
DR   InterPro; IPR034516; hnRNPA3_RRM2.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; SSF54928; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
DR   PRODOM; Q8BG05.
DR   SWISS-2DPAGE; Q8BG05.
KW   Acetylation; Alternative splicing; Complete proteome;
KW   Direct protein sequencing; Isopeptide bond; Methylation;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW   Spliceosome; Ubl conjugation.
FT   CHAIN         1    379       Heterogeneous nuclear ribonucleoprotein
FT                                A3.
FT                                /FTId=PRO_0000081839.
FT   DOMAIN       35    118       RRM 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00176}.
FT   DOMAIN      126    205       RRM 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00176}.
FT   COMPBIAS    211    379       Gly-rich.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES      14     14       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES      43     43       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES      52     52       Dimethylated arginine; alternate.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES      52     52       Omega-N-methylarginine; alternate.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES      76     76       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES     112    112       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES     116    116       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES     124    124       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES     134    134       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES     214    214       Asymmetric dimethylarginine; alternate.
FT                                {ECO:0000250|UniProtKB:Q6URK4}.
FT   MOD_RES     214    214       Omega-N-methylarginine; alternate.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES     216    216       Asymmetric dimethylarginine; alternate.
FT                                {ECO:0000250|UniProtKB:Q6URK4}.
FT   MOD_RES     216    216       Omega-N-methylarginine; alternate.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES     226    226       Asymmetric dimethylarginine; alternate.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     226    226       Omega-N-methylarginine; alternate.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     239    239       Asymmetric dimethylarginine; alternate.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     239    239       Omega-N-methylarginine; alternate.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     246    246       Asymmetric dimethylarginine; alternate.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     246    246       Omega-N-methylarginine; alternate.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     257    257       Omega-N-methylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     286    286       Asymmetric dimethylarginine.
FT                                {ECO:0000250|UniProtKB:Q6URK4}.
FT   MOD_RES     351    351       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES     355    355       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES     359    359       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES     361    361       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES     365    365       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES     367    367       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES     371    371       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES     374    374       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   MOD_RES     376    376       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   CROSSLNK      4      4       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   CROSSLNK     36     36       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   CROSSLNK    118    118       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   CROSSLNK    134    134       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   CROSSLNK    151    151       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   CROSSLNK    182    182       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P51991}.
FT   VAR_SEQ       1     23       MEVKPPPGRPQPDSGRRRRRRGE -> M (in isoform
FT                                2). {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.1}.
FT                                /FTId=VSP_007350.
SQ   SEQUENCE   379 AA;  39652 MW;  D83C400A2B096E9B CRC64;
     MEVKPPPGRP QPDSGRRRRR RGEEGHDPKE PEQLRKLFIG GLSFETTDDS LREHFEKWGT
     LTDCVVMRDP QTKRSRGFGF VTYSCVEEVD AAMCARPHKV DGRVVEPKRA VSREDSVKPG
     AHLTVKKIFV GGIKEDTEEY NLRDYFEKYG KIETIEVMED RQSGKKRGFA FVTFDDHDTV
     DKIVVQKYHT INGHNCEVKK ALSKQEMQSA GSQRGRGGGS GNFMGRGGNF GGGGGNFGRG
     GNFGGRGGYG GGGGGSRGSY GGGDGGYNGF GGDGGNYGGG PGYSSRGGYG GGGPGYGNQG
     GGYGGGGGGY DGYNEGGNFG GGNYGGGGNY NDFGNYSGQQ QSNYGPMKGG SFGGRSSGSP
     YGGGYGSGGG SGGYGSRRF
//

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