UBA2B_ARATH
ID UBA2B_ARATH Reviewed; 451 AA.
AC O80678;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=UBP1-associated protein 2B;
GN Name=UBA2B; OrderedLocusNames=At2g41060; ORFNames=T3K9.17;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {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 shoot meristem and flowers.
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; AC004261; AAD12005.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09920.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09921.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62930.1; -; Genomic_DNA.
DR EMBL; AF439844; AAL27512.1; -; mRNA.
DR EMBL; AY133583; AAM91413.1; -; mRNA.
DR EMBL; AK227158; BAE99200.1; -; mRNA.
DR PIR; T02113; T02113.
DR RefSeq; NP_001078035.1; NM_001084566.2.
DR RefSeq; NP_001318398.1; NM_001336889.1.
DR RefSeq; NP_181639.1; NM_129671.4.
DR AlphaFoldDB; O80678; -.
DR SMR; O80678; -.
DR BioGRID; 4042; 4.
DR IntAct; O80678; 3.
DR STRING; 3702.AT2G41060.1; -.
DR PaxDb; O80678; -.
DR PRIDE; O80678; -.
DR ProteomicsDB; 242620; -.
DR EnsemblPlants; AT2G41060.1; AT2G41060.1; AT2G41060.
DR EnsemblPlants; AT2G41060.2; AT2G41060.2; AT2G41060.
DR EnsemblPlants; AT2G41060.3; AT2G41060.3; AT2G41060.
DR GeneID; 818705; -.
DR Gramene; AT2G41060.1; AT2G41060.1; AT2G41060.
DR Gramene; AT2G41060.2; AT2G41060.2; AT2G41060.
DR Gramene; AT2G41060.3; AT2G41060.3; AT2G41060.
DR KEGG; ath:AT2G41060; -.
DR Araport; AT2G41060; -.
DR TAIR; locus:2063177; AT2G41060.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_012062_1_6_1; -.
DR InParanoid; O80678; -.
DR OMA; IIITEIH; -.
DR OrthoDB; 1202220at2759; -.
DR PhylomeDB; O80678; -.
DR PRO; PR:O80678; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80678; baseline and differential.
DR Genevisible; O80678; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA: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 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 2: Evidence at transcript level;
KW Nucleus; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..451
FT /note="UBP1-associated protein 2B"
FT /id="PRO_0000425441"
FT DOMAIN 128..236
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 227..314
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 49026 MW; 4C6BE8A2A952D17D CRC64;
MTKKRKLESE SNETSEPTEK QQQQCEKEDP EIRNVDNQRD DDEQVVEQDT LKEMHEEEAK
GEDNIEAETS SGSGNQGNED DDEEEPIEDL LEPFSKDQLL ILLKEAAERH RDVANRIRIV
ADEDLVHRKI FVHGLGWDTK ADSLIDAFKQ YGEIEDCKCV VDKVSGQSKG YGFILFKSRS
GARNALKQPQ KKIGTRMTAC QLASIGPVQG NPVVAPAQHF NPENVQRKIY VSNVSADIDP
QKLLEFFSRF GEIEEGPLGL DKATGRPKGF ALFVYRSLES AKKALEEPHK TFEGHVLHCH
KANDGPKQVK QHQHNHNSHN QNSRYQRNDN NGYGAPGGHG HFIAGNNQAV QAFNPAIGQA
LTALLASQGA GLGLNQAFGQ ALLGTLGTAS PGAVGGMPSG YGTQANISPG VYPGYGAQAG
YQGGYQTQQP GQGGAGRGQH GAGYGGPYMG R
