UBP1A_ARATH
ID UBP1A_ARATH Reviewed; 426 AA.
AC Q9SYG4;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Oligouridylate-binding protein 1A;
DE Short=AtUBP1a;
DE AltName: Full=Polyuridylate-binding protein UBP1A;
DE Short=Poly(U)-binding protein UBP1A;
GN Name=UBP1A; OrderedLocusNames=At1g54080; ORFNames=F15I1.16;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP INTERACTION WITH UBA1A AND UBA2A.
RX PubMed=12024044; DOI=10.1128/mcb.22.12.4346-4357.2002;
RA Lambermon M.H., Fu Y., Wieczorek Kirk D.A., Dupasquier M., Filipowicz W.,
RA Lorkovic Z.J.;
RT "UBA1 and UBA2, two proteins that interact with UBP1, a multifunctional
RT effector of pre-mRNA maturation in plants.";
RL Mol. Cell. Biol. 22:4346-4357(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP)-like protein
CC that acts as a component of the pre-mRNA processing machinery.
CC Functions to facilitate the nuclear maturation of plant pre-mRNAs (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with UBA1A and UBA2A. {ECO:0000269|PubMed:12024044}.
CC -!- INTERACTION:
CC Q9SYG4; Q9SHZ6: UBA1A; NbExp=4; IntAct=EBI-346310, EBI-346271;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SYG4-1; Sequence=Displayed;
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DR EMBL; AC006577; AAD25780.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33045.1; -; Genomic_DNA.
DR EMBL; AF348587; AAK15558.1; -; mRNA.
DR EMBL; AF361639; AAK32807.1; -; mRNA.
DR EMBL; AY133610; AAM91440.1; -; mRNA.
DR PIR; E96581; E96581.
DR RefSeq; NP_175810.1; NM_104285.5. [Q9SYG4-1]
DR AlphaFoldDB; Q9SYG4; -.
DR SMR; Q9SYG4; -.
DR BioGRID; 27071; 1.
DR IntAct; Q9SYG4; 2.
DR STRING; 3702.AT1G54080.2; -.
DR iPTMnet; Q9SYG4; -.
DR PaxDb; Q9SYG4; -.
DR PRIDE; Q9SYG4; -.
DR ProteomicsDB; 228482; -. [Q9SYG4-1]
DR EnsemblPlants; AT1G54080.1; AT1G54080.1; AT1G54080. [Q9SYG4-1]
DR GeneID; 841846; -.
DR Gramene; AT1G54080.1; AT1G54080.1; AT1G54080. [Q9SYG4-1]
DR KEGG; ath:AT1G54080; -.
DR Araport; AT1G54080; -.
DR eggNOG; KOG0118; Eukaryota.
DR PhylomeDB; Q9SYG4; -.
DR PRO; PR:Q9SYG4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYG4; baseline and differential.
DR Genevisible; Q9SYG4; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 3.
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; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..426
FT /note="Oligouridylate-binding protein 1A"
FT /id="PRO_0000425434"
FT DOMAIN 63..137
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 148..226
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 269..344
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LQI9"
SQ SEQUENCE 426 AA; 47234 MW; 2BD1660FBB6EC358 CRC64;
MQNQRLIKQQ QQQQQQQHQQ AMIQQAMMQQ HPSLYHPGVM APPQMEPLPS GNLPPGFDPT
TCRSVYAGNI HTQVTEILLQ EIFASTGPIE SCKLIRKDKS SYGFVHYFDR RCASMAIMTL
NGRHIFGQPM KVNWAYATGQ REDTSSHFNI FVGDLSPEVT DAALFDSFSA FNSCSDARVM
WDQKTGRSRG FGFVSFRNQQ DAQTAINEMN GKWVSSRQIR CNWATKGATF GEDKHSSDGK
SVVELTNGSS EDGRELSNED APENNPQFTT VYVGNLSPEV TQLDLHRLFY TLGAGVIEEV
RVQRDKGFGF VRYNTHDEAA LAIQMGNAQP FLFSRQIRCS WGNKPTPSGT ASNPLPPPAP
ASVPSLSAMD LLAYERQLAL AKMHPQAQHS LRQAGLGVNV AGGTAAMYDG GYQNVAAAHQ
QLMYYQ
