UBA2A_ARATH
ID UBA2A_ARATH Reviewed; 478 AA.
AC Q9LES2; C0Z2A5; Q94B29;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 157.
DE RecName: Full=UBP1-associated protein 2A;
DE AltName: Full=UBP1-interacting protein 2a;
GN Name=UBA2A; OrderedLocusNames=At3g56860; ORFNames=T8M16.190;
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 [MRNA], FUNCTION, INTERACTION WITH UBA1A; UBA2A; UBP1A;
RP UBP1B AND UBP1C, AND SUBCELLULAR LOCATION.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP INTERACTION WITH SRK2E, AND SUBCELLULAR LOCATION.
RX PubMed=16828085; DOI=10.1016/j.febslet.2006.06.064;
RA Riera M., Redko Y., Leung J.;
RT "Arabidopsis RNA-binding protein UBA2a relocalizes into nuclear speckles in
RT response to abscisic acid.";
RL FEBS Lett. 580:4160-4165(2006).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18278441; DOI=10.1007/s11103-008-9302-z;
RA Bove J., Kim C.Y., Gibson C.A., Assmann S.M.;
RT "Characterization of wound-responsive RNA-binding proteins and their splice
RT variants in Arabidopsis.";
RL Plant Mol. Biol. 67:71-88(2008).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18705666; DOI=10.1111/j.1469-8137.2008.02557.x;
RA Kim C.Y., Bove J., Assmann S.M.;
RT "Overexpression of wound-responsive RNA-binding proteins induces leaf
RT senescence and hypersensitive-like cell death.";
RL New Phytol. 180:57-70(2008).
CC -!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP)-like protein
CC that acts as component of a complex regulating the turnover of mRNAs in
CC the nucleus. Binds with high affinity to RNA molecules that contain U-
CC rich sequences in 3'-UTRs. May function in complex with UBP1 and
CC contribute to the stabilization of mRNAs in the nucleus. However,
CC unlike UBP1, UBA2A does not stimulate pre-mRNA splicing.
CC {ECO:0000269|PubMed:12024044}.
CC -!- SUBUNIT: Interacts with UBA1A, UBA2A, UBP1A, UBP1B, UBP1C and SRK2E.
CC {ECO:0000269|PubMed:12024044, ECO:0000269|PubMed:16828085}.
CC -!- INTERACTION:
CC Q9LES2; Q9SHZ6: UBA1A; NbExp=3; IntAct=EBI-346288, EBI-346271;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12024044,
CC ECO:0000269|PubMed:16828085, ECO:0000269|PubMed:18278441,
CC ECO:0000269|PubMed:18705666}. Note=Relocalizes into nuclear speckles in
CC response to abscisic acid (ABA).
CC -!- TISSUE SPECIFICITY: Expressed in young leaves, flowers and embryos.
CC {ECO:0000269|PubMed:18278441}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:18278441}.
CC -!- MISCELLANEOUS: Plants over-expressing UB2A1 display severe growth
CC defects consisting of premature cell death and chlorosis.
CC {ECO:0000305|PubMed:18705666}.
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DR EMBL; AJ439404; CAD28672.1; -; mRNA.
DR EMBL; AL390921; CAC00749.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79575.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79576.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79577.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79578.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79579.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63908.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63909.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63910.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63911.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63912.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63913.1; -; Genomic_DNA.
DR EMBL; AF367280; AAK56269.1; -; mRNA.
DR EMBL; AY037245; AAK59846.1; -; mRNA.
DR EMBL; AY042885; AAK68825.1; -; mRNA.
DR EMBL; AY081527; AAM10089.1; -; mRNA.
DR EMBL; AY091040; AAM13861.1; -; mRNA.
DR EMBL; AY117351; AAM51426.1; -; mRNA.
DR EMBL; AY133549; AAM91379.1; -; mRNA.
DR EMBL; BT006368; AAP21176.1; -; mRNA.
DR EMBL; AK318719; BAH56834.1; -; mRNA.
DR PIR; T51274; T51274.
DR RefSeq; NP_001190109.1; NM_001203180.2.
DR RefSeq; NP_001190110.1; NM_001203181.1.
DR RefSeq; NP_001319772.1; NM_001339828.1.
DR RefSeq; NP_001325969.1; NM_001339831.1.
DR RefSeq; NP_001325970.1; NM_001339830.1.
DR RefSeq; NP_001325971.1; NM_001339829.1.
DR RefSeq; NP_001325972.1; NM_001339826.1.
DR RefSeq; NP_001325973.1; NM_001339827.1.
DR RefSeq; NP_567042.1; NM_115545.4.
DR RefSeq; NP_850710.1; NM_180379.4.
DR RefSeq; NP_850711.1; NM_180380.3.
DR AlphaFoldDB; Q9LES2; -.
DR SMR; Q9LES2; -.
DR BioGRID; 10169; 11.
DR IntAct; Q9LES2; 10.
DR STRING; 3702.AT3G56860.3; -.
DR iPTMnet; Q9LES2; -.
DR PaxDb; Q9LES2; -.
DR PRIDE; Q9LES2; -.
DR ProteomicsDB; 228735; -.
DR EnsemblPlants; AT3G56860.1; AT3G56860.1; AT3G56860.
DR EnsemblPlants; AT3G56860.10; AT3G56860.10; AT3G56860.
DR EnsemblPlants; AT3G56860.11; AT3G56860.11; AT3G56860.
DR EnsemblPlants; AT3G56860.2; AT3G56860.2; AT3G56860.
DR EnsemblPlants; AT3G56860.3; AT3G56860.3; AT3G56860.
DR EnsemblPlants; AT3G56860.4; AT3G56860.4; AT3G56860.
DR EnsemblPlants; AT3G56860.5; AT3G56860.5; AT3G56860.
DR EnsemblPlants; AT3G56860.6; AT3G56860.6; AT3G56860.
DR EnsemblPlants; AT3G56860.7; AT3G56860.7; AT3G56860.
DR EnsemblPlants; AT3G56860.8; AT3G56860.8; AT3G56860.
DR EnsemblPlants; AT3G56860.9; AT3G56860.9; AT3G56860.
DR GeneID; 824853; -.
DR Gramene; AT3G56860.1; AT3G56860.1; AT3G56860.
DR Gramene; AT3G56860.10; AT3G56860.10; AT3G56860.
DR Gramene; AT3G56860.11; AT3G56860.11; AT3G56860.
DR Gramene; AT3G56860.2; AT3G56860.2; AT3G56860.
DR Gramene; AT3G56860.3; AT3G56860.3; AT3G56860.
DR Gramene; AT3G56860.4; AT3G56860.4; AT3G56860.
DR Gramene; AT3G56860.5; AT3G56860.5; AT3G56860.
DR Gramene; AT3G56860.6; AT3G56860.6; AT3G56860.
DR Gramene; AT3G56860.7; AT3G56860.7; AT3G56860.
DR Gramene; AT3G56860.8; AT3G56860.8; AT3G56860.
DR Gramene; AT3G56860.9; AT3G56860.9; AT3G56860.
DR KEGG; ath:AT3G56860; -.
DR Araport; AT3G56860; -.
DR TAIR; locus:2103670; AT3G56860.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_012062_1_6_1; -.
DR InParanoid; Q9LES2; -.
DR OMA; PGIGFNQ; -.
DR OrthoDB; 1202220at2759; -.
DR PhylomeDB; Q9LES2; -.
DR PRO; PR:Q9LES2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LES2; baseline and differential.
DR Genevisible; Q9LES2; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; TAS:TAIR.
DR GO; GO:0008219; P:cell death; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0009693; P:ethylene biosynthetic process; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0048255; P:mRNA stabilization; NAS:TAIR.
DR Gene3D; 3.30.70.330; -; 2.
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; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..478
FT /note="UBP1-associated protein 2A"
FT /id="PRO_0000425440"
FT DOMAIN 140..217
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 245..328
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..74
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 90
FT /note="N -> D (in Ref. 4; AAK68825/AAM10089)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="V -> D (in Ref. 5; BAH56834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 51439 MW; 0CD3653669BE2DA4 CRC64;
MTKKRKLEGE ESNEAEEPSQ KLKQTPEEEQ QLVIKNQDNQ GDVEEVEYEE VEEEQEEEVE
DDDDEDDGDE NEDQTDGNRI EAAATSGSGN QEDDDDEPIQ DLLEPFSKEQ VLSLLKEAAE
KHVDVANRIR EVADEDPVHR KIFVHGLGWD TKTETLIEAF KQYGEIEDCK AVFDKISGKS
KGYGFILYKS RSGARNALKQ PQKKIGSRMT ACQLASKGPV FGGAPIAAAA VSAPAQHSNS
EHTQKKIYVS NVGAELDPQK LLMFFSKFGE IEEGPLGLDK YTGRPKGFCL FVYKSSESAK
RALEEPHKTF EGHILHCQKA IDGPKPGKQQ QHHHNPHAYN NPRYQRNDNN GYGPPGGHGH
LMAGNPAGMG GPTAQVINPA IGQALTALLA SQGAGLAFNP AIGQALLGSL GTAAGVNPGN
GVGMPTGYGT QAMAPGTMPG YGTQPGLQGG YQTPQPGQGG TSRGQHGVGP YGTPYMGH
