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O23239

- UBC17_ARATH

UniProt

O23239 - UBC17_ARATH

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Protein

Probable ubiquitin-conjugating enzyme E2 17

Gene

UBC17

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.By similarity

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei99 – 991Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. protein ubiquitination Source: UniProtKB-UniPathway
  2. response to gibberellin Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G36410-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ubiquitin-conjugating enzyme E2 17 (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein 17
Gene namesi
Name:UBC17
Ordered Locus Names:At4g36410
ORF Names:AP22.89, C7A10.950
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G36410.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 161161Probable ubiquitin-conjugating enzyme E2 17PRO_0000345183Add
BLAST

Proteomic databases

PRIDEiO23239.

Expressioni

Inductioni

By biotic stresses.1 Publication

Gene expression databases

GenevestigatoriO23239.

Interactioni

Protein-protein interaction databases

BioGridi15075. 12 interactions.
STRINGi3702.AT4G36410.1-P.

Structurei

3D structure databases

ProteinModelPortaliO23239.
SMRiO23239. Positions 19-154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233453.
InParanoidiO23239.
KOiK10688.
OMAiHYLKNCK.
PhylomeDBiO23239.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O23239-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSSSESTRK GLTKIATNRL QKEFMEWQTN PPSGFKHRVS DNLQRWIIEV
60 70 80 90 100
HGVPGTLYAN ETYQLQVEFP EHYPMEAPQV IFQHPAPLHP HIYSNGHICL
110 120 130 140 150
DVLYDSWSPA MRLSSICLSI LSMLSSSSVK QKPKDNDHYL KNCKHGRSPK
160
ETRWRFHDDK V
Length:161
Mass (Da):18,674
Last modified:January 1, 1998 - v1
Checksum:iC2F62F1FD557FD7D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF028340 mRNA. Translation: AAC39326.1.
DQ027031 mRNA. Translation: AAY44857.1.
Z99708 Genomic DNA. Translation: CAB16814.1.
AL161589 Genomic DNA. Translation: CAB80307.1.
CP002687 Genomic DNA. Translation: AEE86653.1.
AY088076 mRNA. Translation: AAM65622.1.
PIRiT52053.
RefSeqiNP_568004.1. NM_119804.2.
UniGeneiAt.24042.

Genome annotation databases

EnsemblPlantsiAT4G36410.1; AT4G36410.1; AT4G36410.
GeneIDi829793.
KEGGiath:AT4G36410.

Cross-referencesi

Web resourcesi

PlantsUBQ

A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF028340 mRNA. Translation: AAC39326.1 .
DQ027031 mRNA. Translation: AAY44857.1 .
Z99708 Genomic DNA. Translation: CAB16814.1 .
AL161589 Genomic DNA. Translation: CAB80307.1 .
CP002687 Genomic DNA. Translation: AEE86653.1 .
AY088076 mRNA. Translation: AAM65622.1 .
PIRi T52053.
RefSeqi NP_568004.1. NM_119804.2.
UniGenei At.24042.

3D structure databases

ProteinModelPortali O23239.
SMRi O23239. Positions 19-154.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 15075. 12 interactions.
STRINGi 3702.AT4G36410.1-P.

Proteomic databases

PRIDEi O23239.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G36410.1 ; AT4G36410.1 ; AT4G36410 .
GeneIDi 829793.
KEGGi ath:AT4G36410.

Organism-specific databases

TAIRi AT4G36410.

Phylogenomic databases

eggNOGi COG5078.
HOGENOMi HOG000233453.
InParanoidi O23239.
KOi K10688.
OMAi HYLKNCK.
PhylomeDBi O23239.

Enzyme and pathway databases

UniPathwayi UPA00143 .
BioCyci ARA:AT4G36410-MONOMER.

Gene expression databases

Genevestigatori O23239.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A new family of ubiquitin-conjugating enzymes (E2S) AtUBC15/16/17/18 in Arabidopsis thaliana."
    Yan N., Doelling J., Vierstra R.D.
    Plant Gene Register PGR97-174
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis."
    Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W., Callis J.
    Plant Physiol. 139:1597-1611(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, GENE FAMILY, NOMENCLATURE.
  3. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
    Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.
    , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
    Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. "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.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    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].

Entry informationi

Entry nameiUBC17_ARATH
AccessioniPrimary (citable) accession number: O23239
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: January 1, 1998
Last modified: October 1, 2014
This is version 109 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, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3