Full text data of HNRNPA3
HNRNPA3
(HNRPA3)
[Confidence: low (only semi-automatic identification from reviews)]
Heterogeneous nuclear ribonucleoprotein A3; hnRNP A3
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Heterogeneous nuclear ribonucleoprotein A3; hnRNP A3
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P51991
ID ROA3_HUMAN Reviewed; 378 AA.
AC P51991; D3DPF4; Q53RW7; Q6URK5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 2.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A3;
DE Short=hnRNP A3;
GN Name=HNRNPA3; Synonyms=HNRPA3;
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] (ISOFORMS 1 AND 2), AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=11886857; DOI=10.1074/jbc.M200050200;
RA Ma A.S.W., Moran-Jones K., Shan J., Munro T.P., Snee M.J., Hoek K.S.,
RA Smith R.;
RT "Heterogeneous nuclear ribonucleoprotein A3, a novel RNA trafficking
RT response element-binding protein.";
RL J. Biol. Chem. 277:18010-18020(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP PROTEIN SEQUENCE OF 36-52; 58-68; 128-143; 152-161 AND 355-376, AND
RP MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 36-73; 114-161; 167-187; 240-257 AND 355-376,
RP METHYLATION AT ARG-52 AND ARG-246, AND MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL C COMPLEX.
RX PubMed=11991638; DOI=10.1017/S1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-360 AND SER-366, AND
RP 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; TYR-360; TYR-364;
RP SER-366 AND SER-370, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-134, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350; SER-358 AND
RP SER-366, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
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.
CC -!- SUBUNIT: Identified in the spliceosome C complex.
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Component of
CC ribonucleosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P51991-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51991-2; Sequence=VSP_011418;
CC -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC -!- CAUTION: An older version of this entry represented the conceptual
CC translation of what was thought to be HNRNPA3 but which was in
CC fact a pseudogene (HNRPA3P1/FBRNP) located on chromosome 10.
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DR EMBL; AY363225; AAQ63629.1; -; mRNA.
DR EMBL; AC079305; AAY14709.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11066.1; -; Genomic_DNA.
DR EMBL; BC112027; AAI12028.1; -; mRNA.
DR EMBL; BC113470; AAI13471.1; -; mRNA.
DR PIR; I52962; I52962.
DR RefSeq; NP_919223.1; NM_194247.2.
DR RefSeq; XP_005246437.1; XM_005246380.1.
DR UniGene; Hs.516539; -.
DR ProteinModelPortal; P51991; -.
DR SMR; P51991; 29-210.
DR IntAct; P51991; 25.
DR MINT; MINT-4999802; -.
DR STRING; 9606.ENSP00000376309; -.
DR PhosphoSite; P51991; -.
DR DMDM; 51338779; -.
DR PaxDb; P51991; -.
DR PRIDE; P51991; -.
DR Ensembl; ENST00000392524; ENSP00000376309; ENSG00000170144.
DR Ensembl; ENST00000411529; ENSP00000408487; ENSG00000170144.
DR Ensembl; ENST00000435711; ENSP00000416340; ENSG00000170144.
DR GeneID; 220988; -.
DR KEGG; hsa:220988; -.
DR UCSC; uc002ulb.1; human.
DR CTD; 220988; -.
DR GeneCards; GC02P178077; -.
DR HGNC; HGNC:24941; HNRNPA3.
DR HPA; HPA001666; -.
DR MIM; 605372; gene.
DR neXtProt; NX_P51991; -.
DR PharmGKB; PA162391169; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000234442; -.
DR HOVERGEN; HBG002295; -.
DR InParanoid; P51991; -.
DR KO; K12741; -.
DR OMA; CSINDIV; -.
DR OrthoDB; EOG715Q6V; -.
DR PhylomeDB; P51991; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; HNRNPA3; human.
DR GeneWiki; HNRPA3; -.
DR GenomeRNAi; 220988; -.
DR NextBio; 91133; -.
DR PMAP-CutDB; P51991; -.
DR PRO; PR:P51991; -.
DR ArrayExpress; P51991; -.
DR Bgee; P51991; -.
DR CleanEx; HS_HNRNPA3; -.
DR Genevestigator; P51991; -.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1 378 Heterogeneous nuclear ribonucleoprotein
FT A3.
FT /FTId=PRO_0000081838.
FT DOMAIN 35 118 RRM 1.
FT DOMAIN 126 205 RRM 2.
FT COMPBIAS 211 378 Gly-rich.
FT MOD_RES 52 52 Dimethylated arginine; alternate.
FT MOD_RES 52 52 Omega-N-methylarginine; alternate.
FT MOD_RES 134 134 N6-acetyllysine.
FT MOD_RES 246 246 Dimethylated arginine.
FT MOD_RES 350 350 Phosphoserine.
FT MOD_RES 358 358 Phosphoserine.
FT MOD_RES 360 360 Phosphotyrosine.
FT MOD_RES 364 364 Phosphotyrosine.
FT MOD_RES 366 366 Phosphoserine.
FT MOD_RES 370 370 Phosphoserine.
FT VAR_SEQ 1 23 MEVKPPPGRPQPDSGRRRRRRGE -> M (in isoform
FT 2).
FT /FTId=VSP_011418.
SQ SEQUENCE 378 AA; 39595 MW; 832372C4C29547B1 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
GGYGGGGGYD GYNEGGNFGG GNYGGGGNYN DFGNYSGQQQ SNYGPMKGGS FGGRSSGSPY
GGGYGSGGGS GGYGSRRF
//
ID ROA3_HUMAN Reviewed; 378 AA.
AC P51991; D3DPF4; Q53RW7; Q6URK5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 2.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A3;
DE Short=hnRNP A3;
GN Name=HNRNPA3; Synonyms=HNRPA3;
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] (ISOFORMS 1 AND 2), AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=11886857; DOI=10.1074/jbc.M200050200;
RA Ma A.S.W., Moran-Jones K., Shan J., Munro T.P., Snee M.J., Hoek K.S.,
RA Smith R.;
RT "Heterogeneous nuclear ribonucleoprotein A3, a novel RNA trafficking
RT response element-binding protein.";
RL J. Biol. Chem. 277:18010-18020(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP PROTEIN SEQUENCE OF 36-52; 58-68; 128-143; 152-161 AND 355-376, AND
RP MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 36-73; 114-161; 167-187; 240-257 AND 355-376,
RP METHYLATION AT ARG-52 AND ARG-246, AND MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL C COMPLEX.
RX PubMed=11991638; DOI=10.1017/S1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-360 AND SER-366, AND
RP 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; TYR-360; TYR-364;
RP SER-366 AND SER-370, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-134, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350; SER-358 AND
RP SER-366, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
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.
CC -!- SUBUNIT: Identified in the spliceosome C complex.
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Component of
CC ribonucleosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P51991-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51991-2; Sequence=VSP_011418;
CC -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC -!- CAUTION: An older version of this entry represented the conceptual
CC translation of what was thought to be HNRNPA3 but which was in
CC fact a pseudogene (HNRPA3P1/FBRNP) located on chromosome 10.
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DR EMBL; AY363225; AAQ63629.1; -; mRNA.
DR EMBL; AC079305; AAY14709.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11066.1; -; Genomic_DNA.
DR EMBL; BC112027; AAI12028.1; -; mRNA.
DR EMBL; BC113470; AAI13471.1; -; mRNA.
DR PIR; I52962; I52962.
DR RefSeq; NP_919223.1; NM_194247.2.
DR RefSeq; XP_005246437.1; XM_005246380.1.
DR UniGene; Hs.516539; -.
DR ProteinModelPortal; P51991; -.
DR SMR; P51991; 29-210.
DR IntAct; P51991; 25.
DR MINT; MINT-4999802; -.
DR STRING; 9606.ENSP00000376309; -.
DR PhosphoSite; P51991; -.
DR DMDM; 51338779; -.
DR PaxDb; P51991; -.
DR PRIDE; P51991; -.
DR Ensembl; ENST00000392524; ENSP00000376309; ENSG00000170144.
DR Ensembl; ENST00000411529; ENSP00000408487; ENSG00000170144.
DR Ensembl; ENST00000435711; ENSP00000416340; ENSG00000170144.
DR GeneID; 220988; -.
DR KEGG; hsa:220988; -.
DR UCSC; uc002ulb.1; human.
DR CTD; 220988; -.
DR GeneCards; GC02P178077; -.
DR HGNC; HGNC:24941; HNRNPA3.
DR HPA; HPA001666; -.
DR MIM; 605372; gene.
DR neXtProt; NX_P51991; -.
DR PharmGKB; PA162391169; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000234442; -.
DR HOVERGEN; HBG002295; -.
DR InParanoid; P51991; -.
DR KO; K12741; -.
DR OMA; CSINDIV; -.
DR OrthoDB; EOG715Q6V; -.
DR PhylomeDB; P51991; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; HNRNPA3; human.
DR GeneWiki; HNRPA3; -.
DR GenomeRNAi; 220988; -.
DR NextBio; 91133; -.
DR PMAP-CutDB; P51991; -.
DR PRO; PR:P51991; -.
DR ArrayExpress; P51991; -.
DR Bgee; P51991; -.
DR CleanEx; HS_HNRNPA3; -.
DR Genevestigator; P51991; -.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1 378 Heterogeneous nuclear ribonucleoprotein
FT A3.
FT /FTId=PRO_0000081838.
FT DOMAIN 35 118 RRM 1.
FT DOMAIN 126 205 RRM 2.
FT COMPBIAS 211 378 Gly-rich.
FT MOD_RES 52 52 Dimethylated arginine; alternate.
FT MOD_RES 52 52 Omega-N-methylarginine; alternate.
FT MOD_RES 134 134 N6-acetyllysine.
FT MOD_RES 246 246 Dimethylated arginine.
FT MOD_RES 350 350 Phosphoserine.
FT MOD_RES 358 358 Phosphoserine.
FT MOD_RES 360 360 Phosphotyrosine.
FT MOD_RES 364 364 Phosphotyrosine.
FT MOD_RES 366 366 Phosphoserine.
FT MOD_RES 370 370 Phosphoserine.
FT VAR_SEQ 1 23 MEVKPPPGRPQPDSGRRRRRRGE -> M (in isoform
FT 2).
FT /FTId=VSP_011418.
SQ SEQUENCE 378 AA; 39595 MW; 832372C4C29547B1 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
GGYGGGGGYD GYNEGGNFGG GNYGGGGNYN DFGNYSGQQQ SNYGPMKGGS FGGRSSGSPY
GGGYGSGGGS GGYGSRRF
//
MIM
605372
*RECORD*
*FIELD* NO
605372
*FIELD* TI
*605372 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A3; HNRNPA3
;;HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN-LIKE;;
read moreHNRPA3;;
FBRNP;;
D10S102
*FIELD* TX
CLONING
By screening a human fetal brain cDNA library with sequences obtained
from an approximately 1-Mb contig at the D10S102 locus, which is tightly
linked to the locus for multiple endocrine neoplasia type II (MEN2;
171400), Takiguchi et al. (1993) isolated a cDNA encoding HNRNPA3, which
they designated FBRNP. SDS-PAGE analysis showed that the deduced
270-amino acid protein, which shows significant homology to the murine
heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1; 164017), is
expressed as a 32-kD protein.
MAPPING
Gross (2011) mapped the HNRNPA3 gene to chromosome 2q31.2 based on an
alignment of the HNRNPA3 sequence (GenBank GENBANK AY363225) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Gross, M. B.: Personal Communication. Baltimore, Md. 2/28/2011.
2. Takiguchi, S.; Tokino, T.; Imai, T.; Tanigami, A.; Koyama, K.;
Nakamura, Y.: Identification and characterization of a cDNA, which
is highly homologous to the ribonucleoprotein gene, from a locus (D10S102)
closely linked to MEN2 (multiple endocrine neoplasia type 2). Cytogenet.
Cell Genet. 64: 128-130, 1993.
*FIELD* CN
Matthew B. Gross - updated: 02/28/2011
*FIELD* CD
Paul J. Converse: 10/30/2000
*FIELD* ED
mgross: 02/28/2011
wwang: 8/27/2008
carol: 7/23/2001
carol: 10/31/2000
carol: 10/30/2000
*RECORD*
*FIELD* NO
605372
*FIELD* TI
*605372 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A3; HNRNPA3
;;HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN-LIKE;;
read moreHNRPA3;;
FBRNP;;
D10S102
*FIELD* TX
CLONING
By screening a human fetal brain cDNA library with sequences obtained
from an approximately 1-Mb contig at the D10S102 locus, which is tightly
linked to the locus for multiple endocrine neoplasia type II (MEN2;
171400), Takiguchi et al. (1993) isolated a cDNA encoding HNRNPA3, which
they designated FBRNP. SDS-PAGE analysis showed that the deduced
270-amino acid protein, which shows significant homology to the murine
heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1; 164017), is
expressed as a 32-kD protein.
MAPPING
Gross (2011) mapped the HNRNPA3 gene to chromosome 2q31.2 based on an
alignment of the HNRNPA3 sequence (GenBank GENBANK AY363225) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Gross, M. B.: Personal Communication. Baltimore, Md. 2/28/2011.
2. Takiguchi, S.; Tokino, T.; Imai, T.; Tanigami, A.; Koyama, K.;
Nakamura, Y.: Identification and characterization of a cDNA, which
is highly homologous to the ribonucleoprotein gene, from a locus (D10S102)
closely linked to MEN2 (multiple endocrine neoplasia type 2). Cytogenet.
Cell Genet. 64: 128-130, 1993.
*FIELD* CN
Matthew B. Gross - updated: 02/28/2011
*FIELD* CD
Paul J. Converse: 10/30/2000
*FIELD* ED
mgross: 02/28/2011
wwang: 8/27/2008
carol: 7/23/2001
carol: 10/31/2000
carol: 10/30/2000