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Protein

Auxin-binding protein 1

Gene

ERABP1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Auxin receptor that controls cell elongation and cell division (PubMed:9804548, PubMed:11297513). Involved in embryonic morphogenesis (PubMed:11297513). Acts on the cell cycle, endocycle, cell plate formation, and cell expansion and contributes to the control of auxin-related gene expression (PubMed:18952781). Controls root meristem size and mediates auxin responsiveness (PubMed:19777056). Involved in activation of ROP GTPases in response to auxin and regulation of clathrin-mediated endocytosis in roots (PubMed:20887895, PubMed:22683261). Acts as a positive factor in clathrin recruitment to the plasma membrane, thereby promoting endocytosis (PubMed:20887896, PubMed:25922490). Upon auxin binding, restricts the internalization of PIN proteins by inhibiting clathrin-mediated endocytosis (PubMed:20887896, PubMed:25922490). Involved in the regulation of polar auxin transport (PubMed:21223392). Behaves as a negative regulator of the SCF(TIR1/AFB) signaling pathway, protecting AUX/IAA repressors from degradation (PubMed:24051655). Regulates the expression of cell wall remodeling genes via an SCF(TIR1/AFB)-dependent pathway (PubMed:24424095). Involved in the modulation of hemicellulose xyloglucan structure (PubMed:24424095). Required for rapid auxin-mediated re-orientation of microtubules to regulate cell elongation in roots and dark-grown hypocotyls as well as asymmetric growth during gravitropic responses (PubMed:25409144). Involved in the shade avoidance response (PubMed:24052532). Forms with TMK1 a cell surface auxin perception complex that activates ROP signaling pathways (PubMed:24578577). ABP1 sensing of auxin is important for the ABP1-TMK1 complex formation (PubMed:24578577). Interacts functionaly with phytochrome to regulate growth (PubMed:25392478).15 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei81 – 811Auxin bindingBy similarity
Metal bindingi92 – 921Zinc; via tele nitrogenBy similarity
Metal bindingi94 – 941Zinc; via tele nitrogenBy similarity
Metal bindingi98 – 981ZincBy similarity
Metal bindingi141 – 1411Zinc; via tele nitrogenBy similarity

GO - Molecular functioni

GO - Biological processi

  • auxin-activated signaling pathway Source: UniProtKB-KW
  • cytokinesis by cell plate formation Source: TAIR
  • positive regulation of cell division Source: TAIR
  • positive regulation of cell size Source: TAIR
  • positive regulation of DNA endoreduplication Source: TAIR
  • unidimensional cell growth Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Auxin signaling pathway

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Auxin-binding protein 11 Publication
Short name:
ABP11 Publication
Gene namesi
Name:ERABP11 Publication
Ordered Locus Names:At4g02980Imported
ORF Names:T4I9.14Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G02980.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Embryo lethality, when homozygous (PubMed:11297513). No visible phenotype was found for other null mutants (PubMed:25646447).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi57 – 571R → K: Slight reduction of activation by auxin. Slight reduction of activation by auxin; when associated with V-60. 1 Publication
Mutagenesisi60 – 601L → V: Slight reduction of activation by auxin. Slight reduction of activation by auxin; when associated with K-57. 1 Publication
Mutagenesisi60 – 601L → Y in abp1-9; lower auxin sensitivity and altered responses to continous light and shade. 1 Publication
Mutagenesisi81 – 811Q → D: Slight reduction of activation by auxin. 1 Publication
Mutagenesisi89 – 891T → I in abp1-8; lower auxin sensitivity and altered responses to continous light and shade. 1 Publication
Mutagenesisi89 – 891T → V: Slight reduction of activation by auxin. Slight reduction of activation by auxin; when associated with L-90. 1 Publication
Mutagenesisi90 – 901P → L: Slight reduction of activation by auxin. Slight reduction of activation by auxin; when associated with V-89. 1 Publication
Mutagenesisi92 – 921H → A in ABP-M1X; Strong reduction of activation by auxin. In ABP-M2X; strong reduction of activation by auxin; when associated with A-94. 1 Publication
Mutagenesisi92 – 921H → Y in abp1-5; defects in pavement cells interdigitation and decreased interaction with TMK1. 2 Publications
Mutagenesisi94 – 941H → A in ABP-M2X; strong reduction of activation by auxin; when associated with A-92. 1 Publication
Mutagenesisi99 – 991V → A: No effect on activation by auxin. 1 Publication
Mutagenesisi125 – 1251F → L: No effect on activation by auxin. 1 Publication
Mutagenesisi136 – 1361P → L: No effect on activation by auxin. 1 Publication
Mutagenesisi141 – 1411H → N in abp1-10; lower auxin sensitivity and altered responses to continous light and shade. 1 Publication
Mutagenesisi181 – 1811F → L: Slight reduction of activation by auxin. Slight reduction of activation by auxin; when associated with Y-185. 1 Publication
Mutagenesisi185 – 1851W → Y: Slight reduction of activation by auxin. Slight reduction of activation by auxin; when associated with L-181. 1 Publication
Mutagenesisi188 – 1881Q → D: No effect on activation by auxin. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 33331 PublicationAdd
BLAST
Chaini34 – 198165Auxin-binding protein 1PRO_0000020613Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 189By similarity
Glycosylationi130 – 1301N-linked (GlcNAc...)By similarity

Post-translational modificationi

Glycosylated.By similarity
Ubiquitinated by RMA2, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Ubl conjugation

Proteomic databases

PaxDbiP33487.
PRIDEiP33487.

Expressioni

Inductioni

Up-regulated by auxin.1 Publication

Interactioni

Subunit structurei

Homodimer (By similarity). May interact with the GPI-anchored plasma membrane protein SKU5 and its family members (PubMed:16649105). Interacts with TMK1 (via extracellular domain) (PubMed:24578577).1 PublicationBy similarity1 Publication

Protein-protein interaction databases

BioGridi13409. 1 interaction.
DIPiDIP-61369N.
STRINGi3702.AT4G02980.1.

Structurei

3D structure databases

ProteinModelPortaliP33487.
SMRiP33487. Positions 43-194.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 604Auxin bindingBy similarity
Regioni89 – 902Auxin bindingBy similarity
Regioni183 – 1853Auxin bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi195 – 1984Prevents secretion from ER

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG123185.
HOGENOMiHOG000030816.
InParanoidiP33487.
OMAiPYYWDEQ.
PhylomeDBiP33487.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR000526. Auxin-bd.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF02041. Auxin_BP. 1 hit.
[Graphical view]
PRINTSiPR00655. AUXINBINDNGP.
SUPFAMiSSF51182. SSF51182. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33487-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVLSVGSAS SSPIVVVFSV ALLLFYFSET SLGAPCPING LPIVRNISDL
60 70 80 90 100
PQDNYGRPGL SHMTVAGSVL HGMKEVEIWL QTFAPGSETP IHRHSCEEVF
110 120 130 140 150
VVLKGSGTLY LAETHGNFPG KPIEFPIFAN STIHIPINDA HQVKNTGHED
160 170 180 190
LQVLVIISRP PIKIFIYEDW FMPHTAARLK FPYYWDEQCI QESQKDEL
Length:198
Mass (Da):22,044
Last modified:February 1, 1994 - v1
Checksum:i43440CFDCE9EFD67
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021V → L in AAM64865 (Ref. 6) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55111 Genomic DNA. Translation: CAA38909.1.
X69901 Genomic DNA. Translation: CAA49526.1.
S40550 mRNA. Translation: AAB22612.1.
AF069442 Genomic DNA. Translation: AAC79108.1.
AL161495 Genomic DNA. Translation: CAB77783.1.
CP002687 Genomic DNA. Translation: AEE82256.1.
AF389278 mRNA. Translation: AAK63851.1.
AY093754 mRNA. Translation: AAM10378.1.
AY087315 mRNA. Translation: AAM64865.1.
PIRiS31584.
RefSeqiNP_192207.1. NM_116532.2.
UniGeneiAt.148.

Genome annotation databases

EnsemblPlantsiAT4G02980.1; AT4G02980.1; AT4G02980.
GeneIDi828120.
KEGGiath:AT4G02980.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55111 Genomic DNA. Translation: CAA38909.1.
X69901 Genomic DNA. Translation: CAA49526.1.
S40550 mRNA. Translation: AAB22612.1.
AF069442 Genomic DNA. Translation: AAC79108.1.
AL161495 Genomic DNA. Translation: CAB77783.1.
CP002687 Genomic DNA. Translation: AEE82256.1.
AF389278 mRNA. Translation: AAK63851.1.
AY093754 mRNA. Translation: AAM10378.1.
AY087315 mRNA. Translation: AAM64865.1.
PIRiS31584.
RefSeqiNP_192207.1. NM_116532.2.
UniGeneiAt.148.

3D structure databases

ProteinModelPortaliP33487.
SMRiP33487. Positions 43-194.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi13409. 1 interaction.
DIPiDIP-61369N.
STRINGi3702.AT4G02980.1.

Proteomic databases

PaxDbiP33487.
PRIDEiP33487.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G02980.1; AT4G02980.1; AT4G02980.
GeneIDi828120.
KEGGiath:AT4G02980.

Organism-specific databases

TAIRiAT4G02980.

Phylogenomic databases

eggNOGiNOG123185.
HOGENOMiHOG000030816.
InParanoidiP33487.
OMAiPYYWDEQ.
PhylomeDBiP33487.

Miscellaneous databases

PROiP33487.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR000526. Auxin-bd.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF02041. Auxin_BP. 1 hit.
[Graphical view]
PRINTSiPR00655. AUXINBINDNGP.
SUPFAMiSSF51182. SSF51182. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the gene for an auxin-binding protein and a gene for 7SL RNA from Arabidopsis thaliana."
    Shimomura S., Liu W., Inohara N., Watanabe S., Futai M.
    Plant Cell Physiol. 34:633-637(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Molecular analysis of an auxin binding protein gene located on chromosome 4 of Arabidopsis."
    Palme K., Hesse T., Campos N., Garbers C., Yanofsky M.F., Schell J.
    Plant Cell 4:193-201(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-68.
  3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Auxin-dependent cell expansion mediated by overexpressed auxin-binding protein 1."
    Jones A.M., Im K.H., Savka M.A., Wu M.J., DeWitt N.G., Shillito R., Binns A.N.
    Science 282:1114-1117(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "ABP1 is required for organized cell elongation and division in Arabidopsis embryogenesis."
    Chen J.G., Ullah H., Young J.C., Sussman M.R., Jones A.M.
    Genes Dev. 15:902-911(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  9. "Identification of a glycosylphosphatidylinositol-anchored plasma membrane protein interacting with the C-terminus of auxin-binding protein 1: a photoaffinity crosslinking study."
    Shimomura S.
    Plant Mol. Biol. 60:663-677(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SKU5.
  10. "Conditional repression of AUXIN BINDING PROTEIN1 reveals that it coordinates cell division and cell expansion during postembryonic shoot development in Arabidopsis and tobacco."
    Braun N., Wyrzykowska J., Muller P., David K., Couch D., Perrot-Rechenmann C., Fleming A.J.
    Plant Cell 20:2746-2762(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "The AUXIN BINDING PROTEIN 1 is required for differential auxin responses mediating root growth."
    Tromas A., Braun N., Muller P., Khodus T., Paponov I.A., Palme K., Ljung K., Lee J.Y., Benfey P., Murray J.A., Scheres B., Perrot-Rechenmann C.
    PLoS ONE 4:E6648-E6648(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "In vitro and in vivo interaction of AtRma2 E3 ubiquitin ligase and auxin-binding protein 1."
    Son O., Cho S.K., Kim S.J., Kim W.T.
    Biochem. Biophys. Res. Commun. 393:492-497(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY RMA2.
  13. "Cell surface- and rho GTPase-based auxin signaling controls cellular interdigitation in Arabidopsis."
    Xu T., Wen M., Nagawa S., Fu Y., Chen J.G., Wu M.J., Perrot-Rechenmann C., Friml J., Jones A.M., Yang Z.
    Cell 143:99-110(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF HIS-92.
  14. Cited for: FUNCTION.
  15. "The heterozygous abp1/ABP1 insertional mutant has defects in functions requiring polar auxin transport and in regulation of early auxin-regulated genes."
    Effendi Y., Rietz S., Fischer U., Scherer G.F.
    Plant J. 65:282-294(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY AUXIN.
  16. "Auxin binding-protein1 (ABP1), a receptor to regulate auxin transport and early auxin genes in an interlocking system with PIN proteins and the receptor TIR1."
    Effendi Y., Scherer G.F.
    Plant Signal. Behav. 6:1101-1103(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  17. "ABP1 and ROP6 GTPase signaling regulate clathrin-mediated endocytosis in Arabidopsis roots."
    Chen X., Naramoto S., Robert S., Tejos R., Loefke C., Lin D., Yang Z., Friml J.
    Curr. Biol. 22:1326-1332(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "AUXIN-BINDING-PROTEIN1 (ABP1) in phytochrome-B-controlled responses."
    Effendi Y., Jones A.M., Scherer G.F.
    J. Exp. Bot. 64:5065-5074(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Auxin-binding protein 1 is a negative regulator of the SCF(TIR1/AFB) pathway."
    Tromas A., Paque S., Stierle V., Quettier A.L., Muller P., Lechner E., Genschik P., Perrot-Rechenmann C.
    Nat. Commun. 4:2496-2496(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Inhibition of cell expansion by rapid ABP1-mediated auxin effect on microtubules."
    Chen X., Grandont L., Li H., Hauschild R., Paque S., Abuzeineh A., Rakusova H., Benkova E., Perrot-Rechenmann C., Friml J.
    Nature 516:90-93(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "AUXIN BINDING PROTEIN1 links cell wall remodeling, auxin signaling, and cell expansion in arabidopsis."
    Paque S., Mouille G., Grandont L., Alabadi D., Gaertner C., Goyallon A., Muller P., Primard-Brisset C., Sormani R., Blazquez M.A., Perrot-Rechenmann C.
    Plant Cell 26:280-295(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TMK1, MUTAGENESIS OF HIS-92.
  23. "Complementation of the embryo-lethal T-DNA insertion mutant of AUXIN-BINDING-PROTEIN 1 (ABP1) with abp1 point mutated versions reveals crosstalk of ABP1 and phytochromes."
    Effendi Y., Ferro N., Labusch C., Geisler M., Scherer G.F.
    J. Exp. Bot. 66:403-418(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LEU-60; THR-89 AND HIS-141.
    Strain: cv. Wassilewskija.
  24. "Auxin binding protein 1 (ABP1) is not required for either auxin signaling or Arabidopsis development."
    Gao Y., Zhang Y., Zhang D., Dai X., Estelle M., Zhao Y.
    Proc. Natl. Acad. Sci. U.S.A. 112:2275-2280(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  25. "Auxin transporters and binding proteins at a glance."
    Grones P., Friml J.
    J. Cell Sci. 128:1-7(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  26. "Auxin-binding pocket of ABP1 is crucial for its gain-of-function cellular and developmental roles."
    Grones P., Chen X., Simon S., Kaufmann W.A., De Rycke R., Nodzynski T., Zazimalova E., Friml J.
    J. Exp. Bot. 0:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-57; LEU-60; GLN-81; THR-89; PRO-90; HIS-92; HIS-94; VAL-99; PHE-125; PRO-136; PHE-181; TRP-185 AND GLN-188.
    Strain: cv. Columbia.

Entry informationi

Entry nameiABP1_ARATH
AccessioniPrimary (citable) accession number: P33487
Secondary accession number(s): Q8LBB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 24, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

Analysis of new null mutants leads to the conclusion that plants do not need ABP1 for auxin signaling and for their growth and development under normal growth conditions.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.