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Protein

Polyubiquitin 3

Gene

UBQ3

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

Functioni

Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).By similarity

GO - Biological processi

  • response to UV-B Source: TAIR
  • ubiquitin-dependent protein catabolic process Source: TAIR
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Polyubiquitin 3
Cleaved into the following chain:
Gene namesi
Name:UBQ3
Ordered Locus Names:At5g03240
ORF Names:F15A17_270, MOK16.15
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G03240.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB-SubCell
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676UbiquitinPRO_0000396877Add
BLAST
Chaini77 – 15276UbiquitinPRO_0000396878Add
BLAST
Chaini153 – 22876UbiquitinPRO_0000396879Add
BLAST
Chaini229 – 30476UbiquitinPRO_0000396880Add
BLAST
Propeptidei305 – 3062CuratedPRO_0000396881

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki29 – 29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki33 – 33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki48 – 48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki63 – 63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki76 – 76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PRIDEiQ1EC66.

Interactioni

Protein-protein interaction databases

BioGridi17175. 1309 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ1EC66.
SMRiQ1EC66. Positions 1-304.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Ubiquitin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini77 – 15276Ubiquitin-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini153 – 22876Ubiquitin-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini229 – 30476Ubiquitin-like 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin family.Curated
Contains 4 ubiquitin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

InParanoidiQ1EC66.
KOiK08770.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamiPF00240. ubiquitin. 4 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 4 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 4 hits.
PROSITEiPS00299. UBIQUITIN_1. 4 hits.
PS50053. UBIQUITIN_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q1EC66-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLADYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVESSDTID
110 120 130 140 150
NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLADYNIQKE STLHLVLRLR
160 170 180 190 200
GGMQIFVKTL TGKTITLEVE SSDTIDNVKA KIQDKEGIPP DQQRLIFAGK
210 220 230 240 250
QLEDGRTLAD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT ITLEVESSDT
260 270 280 290 300
IDNVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLADYNIQ KESTLHLVLR

LRGGSF
Length:306
Mass (Da):34,279
Last modified:July 11, 2006 - v1
Checksum:iB8BC6C32F1D4F3BE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05363 Genomic DNA. No translation available.
AB005240 Genomic DNA. Translation: BAB08384.1.
AL163002 Genomic DNA. Translation: CAB86091.1.
CP002688 Genomic DNA. Translation: AED90574.1.
CP002688 Genomic DNA. Translation: AED90575.1.
CP002688 Genomic DNA. Translation: AED90576.1.
BT002420 mRNA. Translation: AAO00780.1.
BT025868 mRNA. Translation: ABF85770.1.
AK317101 mRNA. Translation: BAH19791.1.
RefSeqiNP_001031824.1. NM_001036747.1.
NP_568112.2. NM_120402.2.
NP_851029.1. NM_180698.2.
UniGeneiAt.46169.
At.49314.
At.68083.
At.75559.
At.75636.

Genome annotation databases

EnsemblPlantsiAT5G03240.1; AT5G03240.1; AT5G03240.
AT5G03240.2; AT5G03240.2; AT5G03240.
AT5G03240.3; AT5G03240.3; AT5G03240.
GeneIDi831899.
KEGGiath:AT5G03240.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05363 Genomic DNA. No translation available.
AB005240 Genomic DNA. Translation: BAB08384.1.
AL163002 Genomic DNA. Translation: CAB86091.1.
CP002688 Genomic DNA. Translation: AED90574.1.
CP002688 Genomic DNA. Translation: AED90575.1.
CP002688 Genomic DNA. Translation: AED90576.1.
BT002420 mRNA. Translation: AAO00780.1.
BT025868 mRNA. Translation: ABF85770.1.
AK317101 mRNA. Translation: BAH19791.1.
RefSeqiNP_001031824.1. NM_001036747.1.
NP_568112.2. NM_120402.2.
NP_851029.1. NM_180698.2.
UniGeneiAt.46169.
At.49314.
At.68083.
At.75559.
At.75636.

3D structure databases

ProteinModelPortaliQ1EC66.
SMRiQ1EC66. Positions 1-304.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi17175. 1309 interactions.

Proteomic databases

PRIDEiQ1EC66.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G03240.1; AT5G03240.1; AT5G03240.
AT5G03240.2; AT5G03240.2; AT5G03240.
AT5G03240.3; AT5G03240.3; AT5G03240.
GeneIDi831899.
KEGGiath:AT5G03240.

Organism-specific databases

TAIRiAT5G03240.

Phylogenomic databases

InParanoidiQ1EC66.
KOiK08770.

Miscellaneous databases

PROiQ1EC66.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamiPF00240. ubiquitin. 4 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 4 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 4 hits.
PROSITEiPS00299. UBIQUITIN_1. 4 hits.
PS50053. UBIQUITIN_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and evolution of genes encoding polyubiquitin and ubiquitin-like proteins in Arabidopsis thaliana ecotype Columbia."
    Callis J., Carpenter T., Sun C.W., Vierstra R.D.
    Genetics 139:921-939(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones."
    Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S.
    DNA Res. 4:215-230(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [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. "Arabidopsis ORF clones."
    Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
    Tissue: Rosette leaf.
  8. "Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants."
    Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.
    Mol. Cell. Proteomics 6:601-610(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-29; LYS-33; LYS-48 AND LYS-63.
    Strain: cv. Landsberg erecta.

Entry informationi

Entry nameiUBQ3_ARATH
AccessioniPrimary (citable) accession number: Q1EC66
Secondary accession number(s): O80715
, P59263, Q38875, Q9LDJ2, Q9LYW1, Q9M0W3, Q9M1P9, Q9S7X3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: July 11, 2006
Last modified: June 24, 2015
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Ubiquitin is encoded by 16 different genes. Ubiquitin is generally synthesized as a polyubiquitin precursor with tandem head to tail repeats. Often, there is one to three additional amino acids after the last repeat, removed in the mature protein. Alternatively, ubiquitin extension protein is synthesized as a single copy of ubiquitin fused to a ribosomal protein (either L40 or S27A) or to a ubiquitin-related protein (either RUB1 or RUB2). Following translation, extension protein is cleaved from ubiquitin.
For the sake of clarity sequence features are annotated only for the first chain, and are not repeated for each of the following chains.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.