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THO4B_ARATH
ID   THO4B_ARATH             Reviewed;         292 AA.
AC   Q8L719; Q9LZ49;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 145.
DE   RecName: Full=THO complex subunit 4B;
DE   AltName: Full=ALYREF homolog 2;
DE            Short=AtALY2;
GN   Name=ALY2; Synonyms=THO4B; OrderedLocusNames=At5g02530;
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] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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] (ISOFORM 1).
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   SUBCELLULAR LOCATION.
RX   PubMed=15299117; DOI=10.1104/pp.104.046086;
RA   Uhrig J.F., Canto T., Marshall D., MacFarlane S.A.;
RT   "Relocalization of nuclear ALY proteins to the cytoplasm by the tomato
RT   bushy stunt virus P19 pathogenicity protein.";
RL   Plant Physiol. 135:2411-2423(2004).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [6]
RP   INTERACTION WITH RH15 AND RH56.
RX   PubMed=23555998; DOI=10.1371/journal.pone.0060644;
RA   Kammel C., Thomaier M., Sorensen B.B., Schubert T., Langst G., Grasser M.,
RA   Grasser K.D.;
RT   "Arabidopsis DEAD-box RNA helicase UAP56 interacts with both RNA and DNA as
RT   well as with mRNA export factors.";
RL   PLoS ONE 8:E60644-E60644(2013).
CC   -!- FUNCTION: Export adapter involved in nuclear export of spliced and
CC       unspliced mRNA. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RH15 and RH56. {ECO:0000269|PubMed:23555998}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000269|PubMed:15299117}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8L719-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8L719-2; Sequence=VSP_053742;
CC   -!- SIMILARITY: Belongs to the ALYREF family. {ECO:0000305}.
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DR   EMBL; AL162971; CAB85990.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90485.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90486.1; -; Genomic_DNA.
DR   EMBL; AY140010; AAM98152.1; -; mRNA.
DR   EMBL; BT006323; AAP13431.1; -; mRNA.
DR   PIR; T48274; T48274.
DR   RefSeq; NP_001190207.1; NM_001203278.1. [Q8L719-2]
DR   RefSeq; NP_195873.2; NM_120331.5. [Q8L719-1]
DR   AlphaFoldDB; Q8L719; -.
DR   SMR; Q8L719; -.
DR   BioGRID; 17199; 12.
DR   IntAct; Q8L719; 5.
DR   STRING; 3702.AT5G02530.1; -.
DR   iPTMnet; Q8L719; -.
DR   PaxDb; Q8L719; -.
DR   PRIDE; Q8L719; -.
DR   ProteomicsDB; 246422; -. [Q8L719-1]
DR   EnsemblPlants; AT5G02530.1; AT5G02530.1; AT5G02530. [Q8L719-1]
DR   EnsemblPlants; AT5G02530.2; AT5G02530.2; AT5G02530. [Q8L719-2]
DR   GeneID; 831923; -.
DR   Gramene; AT5G02530.1; AT5G02530.1; AT5G02530. [Q8L719-1]
DR   Gramene; AT5G02530.2; AT5G02530.2; AT5G02530. [Q8L719-2]
DR   KEGG; ath:AT5G02530; -.
DR   Araport; AT5G02530; -.
DR   TAIR; locus:2181763; AT5G02530.
DR   eggNOG; KOG0533; Eukaryota.
DR   HOGENOM; CLU_052367_0_0_1; -.
DR   InParanoid; Q8L719; -.
DR   OMA; EDYTANN; -.
DR   OrthoDB; 1369069at2759; -.
DR   PhylomeDB; Q8L719; -.
DR   PRO; PR:Q8L719; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8L719; baseline and differential.
DR   Genevisible; Q8L719; AT.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR025715; FoP_C.
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; 1.
DR   SMART; SM01218; FoP_duplication; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; mRNA transport; Nucleus;
KW   Reference proteome; RNA-binding; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..292
FT                   /note="THO complex subunit 4B"
FT                   /id="PRO_0000425586"
FT   DOMAIN          108..185
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..292
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   VAR_SEQ         228..229
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_053742"
SQ   SEQUENCE   292 AA;  30780 MW;  3F70C679E7F02E1D CRC64;
     MSGGLDMSLD DIIKSNRKPT GSRGRGGIGG GNNTGGRGGS GSNSGPSRRF ANRVGARTAP
     YSRPIQQQQA HDAMWQNDVF ATDASVAAAF GHHQTAVVGG GSSIETGTKL YISNLDYGVS
     NEDIKELFSE VGDLKRYGIH YDRSGRSKGT AEVVFSRRGD ALAAVKRYNN VQLDGKLMKI
     EIVGTNLSAP ALPILATAQI PFPTNGILGN FNENFNGNFN GNFNGNFRGR GRGGFMGRPR
     GGGFGGGNFR GGRGARGRGG RGSGGRGRDE NVSAEDLDAE LDKYHKEAME TS
 
 
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