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Q8RXD6

- BRE1A_ARATH

UniProt

Q8RXD6 - BRE1A_ARATH

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Protein

E3 ubiquitin-protein ligase BRE1-like 1

Gene

HUB1

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

Functioni

E3 ubiquitin-protein ligase that monoubiquitinates H2B to form H2BK143ub1. H2BK143ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and maybe H3K79me. It thereby plays a central role in histone code and gene regulation. Forms a ubiquitin ligase complex in cooperation with the E2 enzyme UBC2/RAD6. Required for the regulation of flowering time and defense against necrotrophic fungal pathogens.3 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri826 – 86540RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. protein homodimerization activity Source: TAIR
  3. ubiquitin-protein transferase activity Source: TAIR
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell division Source: TAIR
  2. cell growth Source: TAIR
  3. defense response to fungus, incompatible interaction Source: TAIR
  4. histone H2B ubiquitination Source: TAIR
  5. histone monoubiquitination Source: TAIR
  6. leaf morphogenesis Source: TAIR
  7. protein monoubiquitination Source: TAIR
  8. regulation of G2/M transition of mitotic cell cycle Source: TAIR
  9. seed dormancy process Source: TAIR
  10. vegetative to reproductive phase transition of meristem Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:GQT-2085-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase BRE1-like 1 (EC:6.3.2.-)
Short name:
AtBRE1
Alternative name(s):
Protein HISTONE MONOUBIQUITINATION 1
Short name:
AtHUB1
Gene namesi
Name:HUB1
Synonyms:BRE1A
Ordered Locus Names:At2g44950/At2g44960
ORF Names:T13E15.24/T13E15.23, T14P1.25/T14P1.24
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 2

Organism-specific databases

TAIRiAT2G44950.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. mitochondrion Source: TAIR
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Plants have reduced seed dormancy and several pleiotropic phenotypes, including alterations in leaf color, plant architecture and flower morphology.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi712 – 878167Missing in hub1-1/ang4-1; loss of function. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 878878E3 ubiquitin-protein ligase BRE1-like 1PRO_0000293108Add
BLAST

Proteomic databases

PaxDbiQ8RXD6.
PRIDEiQ8RXD6.

Expressioni

Tissue specificityi

Ubiquitously expressed.2 Publications

Developmental stagei

Constant throughout the cell cycle.1 Publication

Inductioni

By infection with fungal pathogens.1 Publication

Gene expression databases

ExpressionAtlasiQ8RXD6. baseline and differential.
GenevestigatoriQ8RXD6.

Interactioni

Subunit structurei

May act as a tetramer consisting of two copies of HUB1 and two copies of HUB2 (By similarity). Interacts with MED21.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MED11Q6ID772EBI-2012188,EBI-1386244

Protein-protein interaction databases

BioGridi4440. 37 interactions.
IntActiQ8RXD6. 37 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8RXD6.
SMRiQ8RXD6. Positions 817-877.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili48 – 7629Sequence AnalysisAdd
BLAST
Coiled coili200 – 26162Sequence AnalysisAdd
BLAST
Coiled coili293 – 38290Sequence AnalysisAdd
BLAST
Coiled coili537 – 62488Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi22 – 254Poly-Ala
Compositional biasi142 – 1454Poly-Ser

Domaini

The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.By similarity

Sequence similaritiesi

Belongs to the BRE1 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri826 – 86540RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG263074.
HOGENOMiHOG000006004.
InParanoidiQ8RXD6.
KOiK10696.
OMAiFCNPCVQ.
PhylomeDBiQ8RXD6.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8RXD6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASTGEPDRK RRHFSSISPS EAAAAVKKQP FFWPSSEDKL DTAVLQFQNL
60 70 80 90 100
KLSQKLEAQQ VECSILEDKL SQIKEKQLPY NSSLKTVHKS WEKLTASVES
110 120 130 140 150
CSVRVSDSSS GAHRFVNKED GSSPAVKNDF INRLLETGAT ESSSSNICSN
160 170 180 190 200
QMEENGVNTS SQMTQTLYNL VAATEDLRCL KDELYPTVLR TNLGKDLCGQ
210 220 230 240 250
LALSELESEI KSFRGDLDDV LVKFKSLSRE LQSHRDADAK VRVDLKRIRG
260 270 280 290 300
ELEDEVVELQ QCNGDLSALR AERDATAGAF FPVLSLGNKL ATSDRERDKQ
310 320 330 340 350
RDLQDMETVL KELTVLASGR LQQLKNLHEE RTKMLGKMSN LQNKSKSVRC
360 370 380 390 400
ISSSQACLSL KDQLEKSKEA VFQYMALLEK LQVEKDSIVW KEREINIKNE
410 420 430 440 450
LGDVSRKTSA VTDSRMASLD SEIQKQLDEK MRIKTRLGNI SRERGRKEIF
460 470 480 490 500
ADMKALISSF PEEMSSMRSQ LNNYKETAGG IHSLRADVQS LSGVLCRKTK
510 520 530 540 550
EYEALQLRSA DYASQLGDLN ATVCDLKNSH EELKLFLDMY KRESTDARDI
560 570 580 590 600
AEAKEQEYRA WAHVQSLKSS LDEQNLELRV KAANEAEAVS QQMLAAAEAE
610 620 630 640 650
IADLRQKMDD CKRDVAKHSD ILKSKHEEHG TYLSEIQTIG SAYEDIVPQN
660 670 680 690 700
QQLLLQVTER DDYNIKLFLE GITSRQMQDT LLIDKYIMDK DIQQGSAYAS
710 720 730 740 750
FLSKKSSRIE DQLRFCTDQF QKLAEDKYQK SVSLENLQKK RADIGNGLEQ
760 770 780 790 800
ARSRLEESHS KVEQSRLDYG ALELELEIER FNRRRIEEEM EIAKKKVSRL
810 820 830 840 850
RSLIEGSSAI QKLRQELSEF KEILKCKACN DRPKEVVITK CYHLFCNPCV
860 870
QKLTGTRQKK CPTCSASFGP NDIKPIYI
Length:878
Mass (Da):99,719
Last modified:June 1, 2002 - v1
Checksum:i483445F94F87C291
GO

Sequence cautioni

The sequence AAM14833.1 differs from that shown. Reason: Erroneous gene model prediction. Was originally thought to correspond to two different genes At2g44950 and At2g44960.
The sequence AAM14834.1 differs from that shown. Reason: Erroneous gene model prediction. Was originally thought to correspond to two different genes At2g44950 and At2g44960.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC002388 Genomic DNA. Translation: AAM14833.1. Sequence problems.
AC002388 Genomic DNA. Translation: AAM14834.1. Sequence problems.
CP002685 Genomic DNA. Translation: AEC10489.1.
BT010360 mRNA. Translation: AAQ56803.1.
AY081322 mRNA. Translation: AAL91211.1.
PIRiT00397.
T00398.
RefSeqiNP_182022.2. NM_130060.3.
UniGeneiAt.43266.

Genome annotation databases

EnsemblPlantsiAT2G44950.1; AT2G44950.1; AT2G44950.
GeneIDi819104.
KEGGiath:AT2G44950.

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
AC002388 Genomic DNA. Translation: AAM14833.1 . Sequence problems.
AC002388 Genomic DNA. Translation: AAM14834.1 . Sequence problems.
CP002685 Genomic DNA. Translation: AEC10489.1 .
BT010360 mRNA. Translation: AAQ56803.1 .
AY081322 mRNA. Translation: AAL91211.1 .
PIRi T00397.
T00398.
RefSeqi NP_182022.2. NM_130060.3.
UniGenei At.43266.

3D structure databases

ProteinModelPortali Q8RXD6.
SMRi Q8RXD6. Positions 817-877.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 4440. 37 interactions.
IntActi Q8RXD6. 37 interactions.

Proteomic databases

PaxDbi Q8RXD6.
PRIDEi Q8RXD6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT2G44950.1 ; AT2G44950.1 ; AT2G44950 .
GeneIDi 819104.
KEGGi ath:AT2G44950.

Organism-specific databases

TAIRi AT2G44950.

Phylogenomic databases

eggNOGi NOG263074.
HOGENOMi HOG000006004.
InParanoidi Q8RXD6.
KOi K10696.
OMAi FCNPCVQ.
PhylomeDBi Q8RXD6.

Enzyme and pathway databases

UniPathwayi UPA00143 .
BioCyci ARA:GQT-2085-MONOMER.

Miscellaneous databases

PROi Q8RXD6.

Gene expression databases

ExpressionAtlasi Q8RXD6. baseline and differential.
Genevestigatori Q8RXD6.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "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.
  4. "A conserved RING finger protein required for histone H2B monoubiquitination and cell size control."
    Hwang W.W., Venkatasubrahmanyam S., Ianculescu A.G., Tong A., Boone C., Madhani H.D.
    Mol. Cell 11:261-266(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  5. "The Arabidopsis thaliana homolog of yeast BRE1 has a function in cell cycle regulation during early leaf and root growth."
    Fleury D., Himanen K., Cnops G., Nelissen H., Boccardi T.M., Maere S., Beemster G.T.S., Neyt P., Anami S., Robles P., Micol J.L., Inze D., Van Lijsebettens M.
    Plant Cell 19:417-432(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 712-GLN--ILE-878, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  6. "The absence of histone H2B monoubiquitination in the Arabidopsis hub1 (rdo4) mutant reveals a role for chromatin remodeling in seed dormancy."
    Liu Y., Koornneef M., Soppe W.J.J.
    Plant Cell 19:433-444(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  7. "HISTONE MONOUBIQUITINATION1 interacts with a subunit of the mediator complex and regulates defense against necrotrophic fungal pathogens in Arabidopsis."
    Dhawan R., Luo H., Foerster A.M., Abuqamar S., Du H.N., Briggs S.D., Mittelsten Scheid O., Mengiste T.
    Plant Cell 21:1000-1019(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MED21, SUBCELLULAR LOCATION, INDUCTION.

Entry informationi

Entry nameiBRE1A_ARATH
AccessioniPrimary (citable) accession number: Q8RXD6
Secondary accession number(s): O22156, O22157
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: June 1, 2002
Last modified: October 29, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

HUB1 and HUB2 are involved in the same processes, but are weakly or not redundant.

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