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MOB1B_ARATH
ID   MOB1B_ARATH             Reviewed;         215 AA.
AC   Q8GYX0; O50052;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=MOB kinase activator-like 1B {ECO:0000303|PubMed:19468312};
DE   AltName: Full=Mob1 homolog 1B {ECO:0000303|PubMed:19468312};
DE   AltName: Full=Mps one binder kinase activator-like 1B {ECO:0000303|PubMed:19468312};
GN   Name=MOB1B {ECO:0000303|PubMed:19468312};
GN   OrderedLocusNames=At4g19045 {ECO:0000312|Araport:AT4G19045};
GN   ORFNames=F13C5.220 {ECO:0000312|EMBL:CAA16762.1},
GN   T18B16.1 {ECO:0000312|EMBL:AL021687};
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
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   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19468312;
RA   Vitulo N., Vezzi A., Galla G., Citterio S., Marino G., Ruperti B.,
RA   Zermiani M., Albertini E., Valle G., Barcaccia G.;
RT   "Characterization and evolution of the cell cycle-associated mob domain-
RT   containing proteins in eukaryotes.";
RL   Evol. Bioinform. Online 3:121-158(2007).
RN   [6]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=24201137; DOI=10.1093/aob/mct235;
RA   Pinosa F., Begheldo M., Pasternak T., Zermiani M., Paponov I.A.,
RA   Dovzhenko A., Barcaccia G., Ruperti B., Palme K.;
RT   "The Arabidopsis thaliana Mob1A gene is required for organ growth and
RT   correct tissue patterning of the root tip.";
RL   Ann. Bot. 112:1803-1814(2013).
RN   [7]
RP   INTERACTION WITH SIK1.
RC   STRAIN=cv. Columbia;
RX   PubMed=26685188; DOI=10.1093/jxb/erv538;
RA   Xiong J., Cui X., Yuan X., Yu X., Sun J., Gong Q.;
RT   "The Hippo/STE20 homolog SIK1 interacts with MOB1 to regulate cell
RT   proliferation and cell expansion in Arabidopsis.";
RL   J. Exp. Bot. 67:1461-1475(2016).
CC   -!- SUBUNIT: Interacts with SIK1. {ECO:0000269|PubMed:26685188}.
CC   -!- TISSUE SPECIFICITY: Expression is detected along the vasculature in
CC       cotyledons, hypocotyls and roots of 3- to 4-day-old seedlings.
CC       {ECO:0000269|PubMed:24201137}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:24201137}.
CC   -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA16762.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g19050 has been split into 2 genes: At4g19045 and At4g19050.; Evidence={ECO:0000305};
CC       Sequence=CAB78907.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g19050 has been split into 2 genes: At4g19045 and At4g19050.; Evidence={ECO:0000305};
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DR   EMBL; AL021687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL021711; CAA16762.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161550; CAB78907.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84133.1; -; Genomic_DNA.
DR   EMBL; AK117341; BAC42011.1; -; mRNA.
DR   EMBL; BT006214; AAP12863.1; -; mRNA.
DR   PIR; T04426; T04426.
DR   RefSeq; NP_001154253.1; NM_001160781.1.
DR   AlphaFoldDB; Q8GYX0; -.
DR   SMR; Q8GYX0; -.
DR   IntAct; Q8GYX0; 1.
DR   STRING; 3702.AT4G19045.1; -.
DR   iPTMnet; Q8GYX0; -.
DR   PaxDb; Q8GYX0; -.
DR   PRIDE; Q8GYX0; -.
DR   EnsemblPlants; AT4G19045.1; AT4G19045.1; AT4G19045.
DR   GeneID; 7922308; -.
DR   Gramene; AT4G19045.1; AT4G19045.1; AT4G19045.
DR   KEGG; ath:AT4G19045; -.
DR   Araport; AT4G19045; -.
DR   TAIR; locus:5019474836; AT4G19045.
DR   eggNOG; KOG0440; Eukaryota.
DR   HOGENOM; CLU_038321_3_1_1; -.
DR   OMA; EWIAVNX; -.
DR   OrthoDB; 1127941at2759; -.
DR   PhylomeDB; Q8GYX0; -.
DR   PRO; PR:Q8GYX0; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8GYX0; baseline and differential.
DR   Genevisible; Q8GYX0; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR   GO; GO:0008283; P:cell population proliferation; IGI:TAIR.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0080141; P:regulation of jasmonic acid biosynthetic process; IGI:TAIR.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   Gene3D; 1.20.140.30; -; 1.
DR   InterPro; IPR005301; MOB_kinase_act_fam.
DR   InterPro; IPR036703; MOB_kinase_act_sf.
DR   PANTHER; PTHR22599; PTHR22599; 1.
DR   Pfam; PF03637; Mob1_phocein; 1.
DR   SMART; SM01388; Mob1_phocein; 1.
DR   SUPFAM; SSF101152; SSF101152; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..215
FT                   /note="MOB kinase activator-like 1B"
FT                   /id="PRO_0000380716"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P40484"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P40484"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P40484"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P40484"
SQ   SEQUENCE   215 AA;  24668 MW;  6D3FE67DA222CBE1 CRC64;
     MSLFGLGRNQ KTFRPKKSAP SGTKGAELRK HIDATLGSGN LREAVKLPPG EDLNEWLAVN
     TVDFFNQVNL LFGTLTEFCT PENCSTMTAG PKYEYRWADG VQIKKPIEVS APKYVEYLMD
     WIETQLDDET IFPQKLGAAF PPNFKEVVKT IFKRLFRVYA HIYHSHFQKI VSLKEEAHLN
     TCFKHFILFT HEFVLIDKKE LAPLQELIES IIAPY
 
 
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