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P33487 (ABP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Auxin-binding protein 1

Short name=ABP
Gene names
Name:ERABP1
Ordered Locus Names:At4g02980
ORF Names:T4I9.14
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is probably a receptor for the plant hormone auxin.

Subunit structure

Homodimer By similarity.

Subcellular location

Endoplasmic reticulum lumen.

Post-translational modification

Ubiquitinated by RMA2, leading to proteasomal degradation. Ref.6

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Ref.2
Chain34 – 198165Auxin-binding protein 1
PRO_0000020613

Regions

Motif195 – 1984Prevents secretion from ER

Sites

Metal binding921Zinc By similarity
Metal binding941Zinc By similarity
Metal binding981Zinc By similarity
Metal binding1411Zinc By similarity
Binding site921Auxin By similarity
Binding site981Auxin By similarity

Amino acid modifications

Glycosylation461N-linked (GlcNAc...) Potential
Glycosylation1301N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P33487 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 43440CFDCE9EFD67

FASTA19822,044
        10         20         30         40         50         60 
MIVLSVGSAS SSPIVVVFSV ALLLFYFSET SLGAPCPING LPIVRNISDL PQDNYGRPGL 

        70         80         90        100        110        120 
SHMTVAGSVL HGMKEVEIWL QTFAPGSETP IHRHSCEEVF VVLKGSGTLY LAETHGNFPG 

       130        140        150        160        170        180 
KPIEFPIFAN STIHIPINDA HQVKNTGHED LQVLVIISRP PIKIFIYEDW FMPHTAARLK 

       190 
FPYYWDEQCI QESQKDEL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS31584.
RefSeqNP_192207.1. NM_116532.2.
UniGeneAt.148.

3D structure databases

ProteinModelPortalP33487.
SMRP33487. Positions 43-194.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid13409. 1 interaction.
STRING3702.AT4G02980.1-P.

Proteomic databases

PaxDbP33487.
PRIDEP33487.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G02980.1; AT4G02980.1; AT4G02980.
GeneID828120.
KEGGath:AT4G02980.

Organism-specific databases

TAIRAT4G02980.

Phylogenomic databases

eggNOGNOG123185.
HOGENOMHOG000030816.
InParanoidP33487.
OMAKFPYYWD.
PhylomeDBP33487.

Gene expression databases

ArrayExpressP33487.
GenevestigatorP33487.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR000526. Auxin-bd.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamPF02041. Auxin_BP. 1 hit.
[Graphical view]
PRINTSPR00655. AUXINBINDNGP.
SUPFAMSSF51182. SSF51182. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameABP1_ARATH
AccessionPrimary (citable) accession number: P33487
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 14, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names