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Q8RXD6 (BRE1A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase BRE1-like 1

Short name=AtBRE1
EC=6.3.2.-
Alternative name(s):
Protein HISTONE MONOUBIQUITINATION 1
Short name=AtHUB1
Gene names
Name:HUB1
Synonyms:BRE1A
Ordered Locus Names:At2g44950/At2g44960
ORF Names:T13E15.24/T13E15.23, T14P1.25/T14P1.24
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length878 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.7

Pathway

Protein modification; protein ubiquitination.

Subunit structure

May act as a tetramer consisting of two copies of HUB1 and two copies of HUB2 By similarity. Interacts with MED21. Ref.7

Subcellular location

Nucleus Ref.6 Ref.7.

Tissue specificity

Ubiquitously expressed. Ref.5 Ref.6

Developmental stage

Constant throughout the cell cycle. Ref.5

Induction

By infection with fungal pathogens. Ref.7

Domain

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

Disruption phenotype

Plants have reduced seed dormancy and several pleiotropic phenotypes, including alterations in leaf color, plant architecture and flower morphology. Ref.6

Miscellaneous

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

Sequence similarities

Belongs to the BRE1 family.

Contains 1 RING-type zinc finger.

Sequence caution

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.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentNucleus
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell division

Inferred from mutant phenotype Ref.5. Source: TAIR

cell growth

Inferred from mutant phenotype Ref.5. Source: TAIR

defense response to fungus, incompatible interaction

Inferred from mutant phenotype Ref.7. Source: TAIR

histone H2B ubiquitination

Inferred from mutant phenotype PubMed 18849490. Source: TAIR

histone monoubiquitination

Inferred from mutant phenotype Ref.6. Source: TAIR

leaf morphogenesis

Inferred from mutant phenotype Ref.5. Source: TAIR

protein monoubiquitination

Inferred from direct assay Ref.5. Source: TAIR

regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype Ref.5. Source: TAIR

seed dormancy process

Inferred from mutant phenotype PubMed 12121467Ref.6. Source: TAIR

vegetative to reproductive phase transition of meristem

Inferred from mutant phenotype PubMed 18849490. Source: TAIR

   Cellular_componentmitochondrion

Inferred from direct assay PubMed 14671022. Source: TAIR

nucleus

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionprotein homodimerization activity

Inferred from physical interaction PubMed 18849490. Source: TAIR

ubiquitin-protein ligase activity

Inferred from direct assay Ref.5. Source: TAIR

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MED11Q6ID772EBI-2012188,EBI-1386244

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 878878E3 ubiquitin-protein ligase BRE1-like 1
PRO_0000293108

Regions

Zinc finger826 – 86540RING-type
Coiled coil48 – 7629 Potential
Coiled coil200 – 26162 Potential
Coiled coil293 – 38290 Potential
Coiled coil537 – 62488 Potential
Compositional bias22 – 254Poly-Ala
Compositional bias142 – 1454Poly-Ser

Experimental info

Mutagenesis712 – 878167Missing in hub1-1/ang4-1; loss of function. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q8RXD6 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 483445F94F87C291

FASTA87899,719
        10         20         30         40         50         60 
MASTGEPDRK RRHFSSISPS EAAAAVKKQP FFWPSSEDKL DTAVLQFQNL KLSQKLEAQQ 

        70         80         90        100        110        120 
VECSILEDKL SQIKEKQLPY NSSLKTVHKS WEKLTASVES CSVRVSDSSS GAHRFVNKED 

       130        140        150        160        170        180 
GSSPAVKNDF INRLLETGAT ESSSSNICSN QMEENGVNTS SQMTQTLYNL VAATEDLRCL 

       190        200        210        220        230        240 
KDELYPTVLR TNLGKDLCGQ LALSELESEI KSFRGDLDDV LVKFKSLSRE LQSHRDADAK 

       250        260        270        280        290        300 
VRVDLKRIRG ELEDEVVELQ QCNGDLSALR AERDATAGAF FPVLSLGNKL ATSDRERDKQ 

       310        320        330        340        350        360 
RDLQDMETVL KELTVLASGR LQQLKNLHEE RTKMLGKMSN LQNKSKSVRC ISSSQACLSL 

       370        380        390        400        410        420 
KDQLEKSKEA VFQYMALLEK LQVEKDSIVW KEREINIKNE LGDVSRKTSA VTDSRMASLD 

       430        440        450        460        470        480 
SEIQKQLDEK MRIKTRLGNI SRERGRKEIF ADMKALISSF PEEMSSMRSQ LNNYKETAGG 

       490        500        510        520        530        540 
IHSLRADVQS LSGVLCRKTK EYEALQLRSA DYASQLGDLN ATVCDLKNSH EELKLFLDMY 

       550        560        570        580        590        600 
KRESTDARDI AEAKEQEYRA WAHVQSLKSS LDEQNLELRV KAANEAEAVS QQMLAAAEAE 

       610        620        630        640        650        660 
IADLRQKMDD CKRDVAKHSD ILKSKHEEHG TYLSEIQTIG SAYEDIVPQN QQLLLQVTER 

       670        680        690        700        710        720 
DDYNIKLFLE GITSRQMQDT LLIDKYIMDK DIQQGSAYAS FLSKKSSRIE DQLRFCTDQF 

       730        740        750        760        770        780 
QKLAEDKYQK SVSLENLQKK RADIGNGLEQ ARSRLEESHS KVEQSRLDYG ALELELEIER 

       790        800        810        820        830        840 
FNRRRIEEEM EIAKKKVSRL RSLIEGSSAI QKLRQELSEF KEILKCKACN DRPKEVVITK 

       850        860        870 
CYHLFCNPCV QKLTGTRQKK CPTCSASFGP NDIKPIYI 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
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. 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.
[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.
+Additional computationally mapped references.

Web resources

PlantsUBQ

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT00397.
T00398.
RefSeqNP_182022.2. NM_130060.3.
UniGeneAt.43266.

3D structure databases

ProteinModelPortalQ8RXD6.
SMRQ8RXD6. Positions 808-878.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid4440. 37 interactions.
IntActQ8RXD6. 37 interactions.

Proteomic databases

PaxDbQ8RXD6.
PRIDEQ8RXD6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G44950.1; AT2G44950.1; AT2G44950.
GeneID819104.
KEGGath:AT2G44950.

Organism-specific databases

TAIRAT2G44950.

Phylogenomic databases

eggNOGNOG263074.
HOGENOMHOG000006004.
InParanoidQ8RXD6.
KOK10696.
OMAMYKREST.
PhylomeDBQ8RXD6.
ProtClustDBCLSN2680249.

Enzyme and pathway databases

BioCycARA:GQT-2085-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorQ8RXD6.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ8RXD6.

Entry information

Entry nameBRE1A_ARATH
AccessionPrimary (citable) accession number: Q8RXD6
Secondary accession number(s): O22156, O22157
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: June 1, 2002
Last modified: April 16, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names