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P33487

- ABP1_ARATH

UniProt

P33487 - ABP1_ARATH

Protein

Auxin-binding protein 1

Gene

ERABP1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    Functioni

    This is probably a receptor for the plant hormone auxin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi92 – 921ZincBy similarity
    Binding sitei92 – 921AuxinBy similarity
    Metal bindingi94 – 941ZincBy similarity
    Metal bindingi98 – 981ZincBy similarity
    Binding sitei98 – 981AuxinBy similarity
    Metal bindingi141 – 1411ZincBy similarity

    GO - Molecular functioni

    1. auxin binding Source: UniProtKB
    2. receptor activity Source: InterPro
    3. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. auxin-activated signaling pathway Source: UniProtKB-KW
    2. positive regulation of cell division Source: TAIR
    3. positive regulation of cell size Source: TAIR
    4. positive regulation of DNA endoreduplication Source: TAIR
    5. unidimensional cell growth Source: TAIR

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Auxin signaling pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Auxin-binding protein 1
    Short name:
    ABP
    Gene namesi
    Name:ERABP1
    Ordered Locus Names:At4g02980
    ORF Names:T4I9.14
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G02980.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    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
    Glycosylationi46 – 461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Ubiquitinated by RMA2, leading to proteasomal degradation.1 Publication

    Keywords - PTMi

    Glycoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP33487.
    PRIDEiP33487.

    Expressioni

    Gene expression databases

    ArrayExpressiP33487.
    GenevestigatoriP33487.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi13409. 1 interaction.
    STRINGi3702.AT4G02980.1-P.

    Structurei

    3D structure databases

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

    Family & Domainsi

    Motif

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG123185.
    HOGENOMiHOG000030816.
    InParanoidiP33487.
    OMAiKFPYYWD.
    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

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    MIVLSVGSAS SSPIVVVFSV ALLLFYFSET SLGAPCPING LPIVRNISDL    50
    PQDNYGRPGL SHMTVAGSVL HGMKEVEIWL QTFAPGSETP IHRHSCEEVF 100
    VVLKGSGTLY LAETHGNFPG KPIEFPIFAN STIHIPINDA HQVKNTGHED 150
    LQVLVIISRP PIKIFIYEDW FMPHTAARLK FPYYWDEQCI QESQKDEL 198
    Length:198
    Mass (Da):22,044
    Last modified:February 1, 1994 - v1
    Checksum:i43440CFDCE9EFD67
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi S31584.
    RefSeqi NP_192207.1. NM_116532.2.
    UniGenei At.148.

    3D structure databases

    ProteinModelPortali P33487.
    SMRi P33487. Positions 43-194.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 13409. 1 interaction.
    STRINGi 3702.AT4G02980.1-P.

    Proteomic databases

    PaxDbi P33487.
    PRIDEi P33487.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G02980.1 ; AT4G02980.1 ; AT4G02980 .
    GeneIDi 828120.
    KEGGi ath:AT4G02980.

    Organism-specific databases

    TAIRi AT4G02980.

    Phylogenomic databases

    eggNOGi NOG123185.
    HOGENOMi HOG000030816.
    InParanoidi P33487.
    OMAi KFPYYWD.
    PhylomeDBi P33487.

    Gene expression databases

    ArrayExpressi P33487.
    Genevestigatori P33487.

    Family and domain databases

    Gene3Di 2.60.120.10. 1 hit.
    InterProi IPR000526. Auxin-bd.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view ]
    Pfami PF02041. Auxin_BP. 1 hit.
    [Graphical view ]
    PRINTSi PR00655. AUXINBINDNGP.
    SUPFAMi SSF51182. SSF51182. 1 hit.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.

    Entry informationi

    Entry nameiABP1_ARATH
    AccessioniPrimary (citable) accession number: P33487
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names

    External Data

    Dasty 3