RBP1B_ARATH
ID RBP1B_ARATH Reviewed; 217 AA.
AC Q8RWG8; O04150; O64739; Q2HIH4;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Ran-binding protein 1 homolog b;
GN Name=RANBP1B; OrderedLocusNames=At2g30060; ORFNames=F23F1.1, T27E13.20;
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], CHARACTERIZATION, AND INTERACTION WITH RAN1;
RP RAN2 AND RAN3.
RX PubMed=9025305; DOI=10.1046/j.1365-313x.1997.11010093.x;
RA Haizel T., Merkle T., Pay A., Fejes E., Nagy F.;
RT "Characterization of proteins that interact with the GTP-bound form of the
RT regulatory GTPase Ran in Arabidopsis.";
RL Plant J. 11:93-103(1997).
RN [2]
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 [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;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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).
CC -!- SUBUNIT: Interacts with the GTP-bound form of RAN1, RAN2 and RAN3.
CC {ECO:0000269|PubMed:9025305}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X97378; CAA66046.1; -; mRNA.
DR EMBL; AC004165; AAC16966.1; -; Genomic_DNA.
DR EMBL; AC004680; AAM14982.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08340.1; -; Genomic_DNA.
DR EMBL; AY093099; AAM13098.1; -; mRNA.
DR EMBL; BT020304; AAV84525.1; -; mRNA.
DR EMBL; BT020473; AAW38974.1; -; mRNA.
DR EMBL; BT024607; ABD43005.1; -; mRNA.
DR PIR; T00592; T00592.
DR RefSeq; NP_180567.1; NM_128561.5.
DR AlphaFoldDB; Q8RWG8; -.
DR SMR; Q8RWG8; -.
DR BioGRID; 2906; 8.
DR IntAct; Q8RWG8; 3.
DR STRING; 3702.AT2G30060.1; -.
DR iPTMnet; Q8RWG8; -.
DR MetOSite; Q8RWG8; -.
DR PaxDb; Q8RWG8; -.
DR PRIDE; Q8RWG8; -.
DR ProteomicsDB; 225976; -.
DR EnsemblPlants; AT2G30060.1; AT2G30060.1; AT2G30060.
DR GeneID; 817557; -.
DR Gramene; AT2G30060.1; AT2G30060.1; AT2G30060.
DR KEGG; ath:AT2G30060; -.
DR Araport; AT2G30060; -.
DR TAIR; locus:2060837; AT2G30060.
DR eggNOG; KOG0864; Eukaryota.
DR HOGENOM; CLU_067861_1_0_1; -.
DR InParanoid; Q8RWG8; -.
DR OMA; KIRANHI; -.
DR OrthoDB; 1573143at2759; -.
DR PhylomeDB; Q8RWG8; -.
DR PRO; PR:Q8RWG8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RWG8; baseline and differential.
DR Genevisible; Q8RWG8; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR CDD; cd13179; RanBD_RanBP1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR InterPro; IPR045256; RanBP1_RanBD.
DR PANTHER; PTHR23138; PTHR23138; 1.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR PROSITE; PS50196; RANBD1; 1.
PE 1: Evidence at protein level;
KW Acetylation; mRNA transport; Nuclear pore complex; Nucleus;
KW Protein transport; Reference proteome; Translocation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..217
FT /note="Ran-binding protein 1 homolog b"
FT /id="PRO_0000097188"
FT DOMAIN 29..164
FT /note="RanBD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 9
FT /note="E -> K (in Ref. 4; AAM13098)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="L -> V (in Ref. 1; CAA66046)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="A -> G (in Ref. 1; CAA66046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 24389 MW; 5F2E141A330CDAFE CRC64;
MASISNEPER ENRDEEETGA NEDEDTGAQV APIVRLEEVA VTTGEEDEDT ILDLKSKLYR
FDKDGSQWKE RGAGTVKFLK HRVSGKIRLV MRQSKTLKIC ANHLVGSGMS VQEHAGNDKS
CVWHARDFSD GELKDELFCI RFASVENCKA FMQKFKEVAE SEEEKEESKD ASDTAGLLEK
LTVEEKESEK KPVEKAEENK KSEAVEEKKT EESVPSA
