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G7IBM3 (G7IBM3_MEDTR) Unreviewed, UniProtKB/TrEMBL

Last modified March 6, 2013. Version 10. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling By similarity. SAAS SAAS000558

Subunit structure

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA By similarity. RuleBase RU000451

Subcellular location

Nucleus By similarity RuleBase RU000451.

Sequence similarities

Belongs to the histone H2B family. RuleBase RU000451

Ontologies

Keywords
   Cellular componentChromosome
Nucleosome core SAAS SAAS000558 RuleBase RU000451
Nucleus RuleBase RU000451 SAAS SAAS000558
   LigandDNA-binding
   PTMIsopeptide bond SAAS SAAS000558
Gene Ontology (GO)
   Biological_processnucleosome assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleosome

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
G7IBM3 [UniParc].

Last modified January 25, 2012. Version 1.
Checksum: 3BF6C079AF0D69E4

FASTA13615,139
        10         20         30         40         50         60 
MAPKAEKKPA EKKPAEKSPA EKKPKAEKKI SKEGGDKKKK RVKKSVETYK IYIFKVLKQV 

        70         80         90        100        110        120 
HPDIGISSKA MGIMNSFIND IFEKLAQEAS RLARYNKKPT ITSREIQTAV RLVLPGELAK 

       130 
HAVSEGTKAV TKFTSS 

« Hide

References

[1]"The Medicago genome provides insight into the evolution of rhizobial symbioses."
Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K., Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S., Krishnakumar V. expand/collapse author list , Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y., Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.
Nature 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A17 EMBL AES60762.1.
[2]"The Genome Sequence of the Model Legume, Medicago truncatula."
Young N.D., Debelle F., Oldroyd G., Geurts R., Cannon S.B., Mayer K.F.X., Gouzy J., Van de Peer Y., Schoof H., Udvardi M.K., Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S., Proost S., Krishnakumar V., Gundlach H. expand/collapse author list , Zhou S., Mudge J., Bharti A.K., Benedito V.A., Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R., Deshpande S., Doyle J.J., Dudez A.-M., Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S., Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H., Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E., Samain S., Samson N., Saurat O., Scarpelli C., Schiex T., Segurens B., Seigfried M., Severin A., Sherrier D.J., Shi R., Sims S., Sinharoy S., Sterck L., Vasylenko I., Viollet A., Wang K., Wang B.-B., Wang X., Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.
Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A17 EMBL AES84603.1.
[3]Krishnakumar V., Cheung F., Xiao Y., Chan A., Moskal W.A., Town C.D.
Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM001217 Genomic DNA. Translation: AES60762.1.
GL982937 Genomic DNA. Translation: AES84603.1.
BT143547 mRNA. Translation: AFK43341.1.
RefSeqXP_003590511.1. XM_003590463.1.
XP_003637465.1. XM_003637417.1.
UniGeneMtr.4060.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID11431194.
11449209.
KEGGmtr:MTR_087s0002.
mtr:MTR_1g068600.

Phylogenomic databases

KOK11252.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000558. Histone_H2B.
[Graphical view]
PANTHERPTHR23428. PTHR23428. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00621. HISTONEH2B.
SMARTSM00427. H2B. 1 hit.
[Graphical view]
SUPFAMSSF47113. Histone-fold. 1 hit.
PROSITEPS00357. HISTONE_H2B. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG7IBM3_MEDTR
AccessionPrimary (citable) accession number: G7IBM3
Entry history
Integrated into UniProtKB/TrEMBL: January 25, 2012
Last sequence update: January 25, 2012
Last modified: March 6, 2013
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)