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Protein

Polyubiquitin 8

Gene

UBQ8

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

  • ubiquitin-dependent protein catabolic process Source: TAIR
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-ATH-110312. Translesion synthesis by REV1.
R-ATH-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-ATH-110320. Translesion Synthesis by POLH.
R-ATH-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-ATH-179409. APC-Cdc20 mediated degradation of Nek2A.
R-ATH-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-ATH-450302. activated TAK1 mediates p38 MAPK activation.
R-ATH-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
R-ATH-5358346. Hedgehog ligand biogenesis.
R-ATH-5632684. Hedgehog 'on' state.
R-ATH-5655862. Translesion synthesis by POLK.
R-ATH-5656121. Translesion synthesis by POLI.
R-ATH-5656169. Termination of translesion DNA synthesis.
R-ATH-5696394. DNA Damage Recognition in GG-NER.
R-ATH-5696395. Formation of Incision Complex in GG-NER.
R-ATH-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-ATH-5696400. Dual Incision in GG-NER.
R-ATH-6781823. Formation of TC-NER Pre-Incision Complex.
R-ATH-6782135. Dual incision in TC-NER.
R-ATH-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-ATH-68949. Orc1 removal from chromatin.
R-ATH-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-ATH-917729. Endosomal Sorting Complex Required For Transport (ESCRT).
R-ATH-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Gene namesi
Name:UBQ8
Ordered Locus Names:At3g09790
ORF Names:F11F8_38, F8A24.16
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G09790.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: TAIR
  • 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 – 7878Ubiquitin-related 1PRO_0000396915Add
BLAST
Chaini79 – 15476Ubiquitin-related 2PRO_0000396916Add
BLAST
Chaini155 – 23783Ubiquitin-related 3PRO_0000396917Add
BLAST
Chaini238 – 31881Ubiquitin-related 4PRO_0000396918Add
BLAST
Chaini319 – 39274Ubiquitin-related 5PRO_0000396919Add
BLAST
Chaini393 – 46876Ubiquitin-related 6PRO_0000396920Add
BLAST
Chaini469 – 55183Ubiquitin-related 7PRO_0000396921Add
BLAST
Chaini552 – 62776Ubiquitin-related 8PRO_0000396922Add
BLAST
Propeptidei628 – 6314CuratedPRO_0000396923

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki78 – 78Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation
Cross-linki154 – 154Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation
Cross-linki551 – 551Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation

Keywords - PTMi

Isopeptide bond

Proteomic databases

PaxDbiQ39256.
PRIDEiQ39256.

Expressioni

Gene expression databases

GenevisibleiQ39256. AT.

Interactioni

Protein-protein interaction databases

BioGridi5471. 2 interactions.
STRINGi3702.AT3G09790.1.

Structurei

3D structure databases

ProteinModelPortaliQ39256.
SMRiQ39256. Positions 4-625.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 7876Ubiquitin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini79 – 15476Ubiquitin-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini155 – 23783Ubiquitin-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini238 – 31881Ubiquitin-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini319 – 39274Ubiquitin-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini393 – 46876Ubiquitin-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini469 – 55183Ubiquitin-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini552 – 62776Ubiquitin-like 8PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin family.Curated
Contains 8 ubiquitin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0001. Eukaryota.
COG5272. LUCA.
HOGENOMiHOG000233942.
InParanoidiQ39256.
KOiK08770.
OMAiNLEVESW.
PhylomeDBiQ39256.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 8 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 8 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 8 hits.
PROSITEiPS50053. UBIQUITIN_2. 8 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q39256-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIQIYAKTL TEKTITLDVE TSDSIHNVKA KIQNKEGIPL DQQRLIFAGK
60 70 80 90 100
QLEDGLTLAD YNIQKESTLH LVLRLRGGMQ IFVQTLTGKT ITLEVKSSDT
110 120 130 140 150
IDNVKAKIQD KEGILPRQQR LIFAGKQLED GRTLADYNIQ KESTLHLVLR
160 170 180 190 200
LCGGMQIFVS TFSGKNFTSD TLTLKVESSD TIENVKAKIQ DREGLRPDHQ
210 220 230 240 250
RLIFHGEELF TEDNRTLADY GIRNRSTLCL ALRLRGDMYI FVKNLPYNSF
260 270 280 290 300
TGENFILEVE SSDTIDNVKA KLQDKERIPM DLHRLIFAGK PLEGGRTLAH
310 320 330 340 350
YNIQKGSTLY LVTRFRCGMQ IFVKTLTRKR INLEVESWDT IENVKAMVQD
360 370 380 390 400
KEGIQPQPNL QRLIFLGKEL KDGCTLADYS IQKESTLHLV LGMQIFVKLF
410 420 430 440 450
GGKIITLEVL SSDTIKSVKA KIQDKVGSPP DQQILLFRGG QLQDGRTLGD
460 470 480 490 500
YNIRNESTLH LFFHIRHGMQ IFVKTFSFSG ETPTCKTITL EVESSDTIDN
510 520 530 540 550
VKVKIQHKVG IPLDRQRLIF GGRVLVGSRT LLDYNIQKGS TIHQLFLQRG
560 570 580 590 600
GMQIFIKTLT GKTIILEVES SDTIANVKEK IQVKEGIKPD QQMLIFFGQQ
610 620 630
LEDGVTLGDY DIHKKSTLYL VLRLRQRRYD F
Length:631
Mass (Da):71,769
Last modified:November 1, 1996 - v1
Checksum:iF9552A7065689D6F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05917 Genomic DNA. Translation: AAA68879.1.
AC015985 Genomic DNA. Translation: AAF23256.1.
AC016661 Genomic DNA. Translation: AAF23307.1.
CP002686 Genomic DNA. Translation: AEE74813.1.
PIRiS55243.
RefSeqiNP_566357.1. NM_111814.1.
UniGeneiAt.65074.

Genome annotation databases

EnsemblPlantsiAT3G09790.1; AT3G09790.1; AT3G09790.
GeneIDi820137.
GrameneiAT3G09790.1; AT3G09790.1; AT3G09790.
KEGGiath:AT3G09790.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05917 Genomic DNA. Translation: AAA68879.1.
AC015985 Genomic DNA. Translation: AAF23256.1.
AC016661 Genomic DNA. Translation: AAF23307.1.
CP002686 Genomic DNA. Translation: AEE74813.1.
PIRiS55243.
RefSeqiNP_566357.1. NM_111814.1.
UniGeneiAt.65074.

3D structure databases

ProteinModelPortaliQ39256.
SMRiQ39256. Positions 4-625.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi5471. 2 interactions.
STRINGi3702.AT3G09790.1.

Proteomic databases

PaxDbiQ39256.
PRIDEiQ39256.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G09790.1; AT3G09790.1; AT3G09790.
GeneIDi820137.
GrameneiAT3G09790.1; AT3G09790.1; AT3G09790.
KEGGiath:AT3G09790.

Organism-specific databases

TAIRiAT3G09790.

Phylogenomic databases

eggNOGiKOG0001. Eukaryota.
COG5272. LUCA.
HOGENOMiHOG000233942.
InParanoidiQ39256.
KOiK08770.
OMAiNLEVESW.
PhylomeDBiQ39256.

Enzyme and pathway databases

ReactomeiR-ATH-110312. Translesion synthesis by REV1.
R-ATH-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-ATH-110320. Translesion Synthesis by POLH.
R-ATH-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-ATH-179409. APC-Cdc20 mediated degradation of Nek2A.
R-ATH-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-ATH-450302. activated TAK1 mediates p38 MAPK activation.
R-ATH-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
R-ATH-5358346. Hedgehog ligand biogenesis.
R-ATH-5632684. Hedgehog 'on' state.
R-ATH-5655862. Translesion synthesis by POLK.
R-ATH-5656121. Translesion synthesis by POLI.
R-ATH-5656169. Termination of translesion DNA synthesis.
R-ATH-5696394. DNA Damage Recognition in GG-NER.
R-ATH-5696395. Formation of Incision Complex in GG-NER.
R-ATH-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-ATH-5696400. Dual Incision in GG-NER.
R-ATH-6781823. Formation of TC-NER Pre-Incision Complex.
R-ATH-6782135. Dual incision in TC-NER.
R-ATH-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-ATH-68949. Orc1 removal from chromatin.
R-ATH-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-ATH-917729. Endosomal Sorting Complex Required For Transport (ESCRT).
R-ATH-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiQ39256.

Gene expression databases

GenevisibleiQ39256. AT.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 8 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 8 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 8 hits.
PROSITEiPS50053. UBIQUITIN_2. 8 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. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.

Entry informationi

Entry nameiUBQ8_ARATH
AccessioniPrimary (citable) accession number: Q39256
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: November 1, 1996
Last modified: February 17, 2016
This is version 91 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.

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

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 one 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.