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Structural genomics, signaling protein PDB id
1m94
Jmol
Contents
Protein chain
73 a.a. *
* Residue conservation analysis
PDB id:
1m94
Name: Structural genomics, signaling protein
Title: Solution structure of the yeast ubiquitin-like modifier protein hub1
Structure: Protein ynr032c-a. Chain: a. Synonym: hub1. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: ynr032c-a/hub1. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: T.A.Ramelot,J.R.Cort,A.A.Yee,A.Semesi,A.M.Edwards, C.H.Arrowsmith,M.A.Kennedy,Northeast Structural Genomics Consortium (Nesg)
Key ref: T.A.Ramelot et al. (2003). Solution structure of the yeast ubiquitin-like modifier protein Hub1. J Struct Funct Genomics, 4, 25-30. PubMed id: 12943364 DOI: 10.1023/A:1024674220425
Date:
26-Jul-02     Release date:   11-Dec-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q6Q546  (HUB1_YEAST) -  Ubiquitin-like modifier HUB1
Seq:
Struc:
73 a.a.
73 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     mating projection   1 term 
  Biological process     cellular morphogenesis during conjugation with cellular fusion   3 terms 
  Biochemical function     protein tag     2 terms  

 

 
DOI no: 10.1023/A:1024674220425 J Struct Funct Genomics 4:25-30 (2003)
PubMed id: 12943364  
 
 
Solution structure of the yeast ubiquitin-like modifier protein Hub1.
T.A.Ramelot, J.R.Cort, A.A.Yee, A.Semesi, A.M.Edwards, C.H.Arrowsmith, M.A.Kennedy.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21196936 B.Fierz, C.Chatterjee, R.K.McGinty, M.Bar-Dagan, D.P.Raleigh, and T.W.Muir (2011).
Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction.
  Nat Chem Biol, 7, 113-119.  
20208522 C.Chatterjee, R.K.McGinty, B.Fierz, and T.W.Muir (2010).
Disulfide-directed histone ubiquitylation reveals plasticity in hDot1L activation.
  Nat Chem Biol, 6, 267-269.  
18588675 L.Sanchez-Pulido, D.Devos, Z.R.Sung, and M.Calonje (2008).
RAWUL: a new ubiquitin-like domain in PRC1 ring finger proteins that unveils putative plant and worm PRC1 orthologs.
  BMC Genomics, 9, 308.  
16396680 D.J.Pugh, E.Ab, A.Faro, P.T.Lutya, E.Hoffmann, and D.J.Rees (2006).
DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways.
  BMC Struct Biol, 6, 1.
PDB code: 2c7h
15917233 J.Narasimhan, M.Wang, Z.Fu, J.M.Klein, A.L.Haas, and J.J.Kim (2005).
Crystal structure of the interferon-induced ubiquitin-like protein ISG15.
  J Biol Chem, 280, 27356-27365.
PDB code: 1z2m
16064136 R.L.Welchman, C.Gordon, and R.J.Mayer (2005).
Ubiquitin and ubiquitin-like proteins as multifunctional signals.
  Nat Rev Mol Cell Biol, 6, 599-609.  
15987890 Y.G.Gao, A.X.Song, Y.H.Shi, Y.G.Chang, S.X.Liu, Y.Z.Yu, X.T.Cao, D.H.Lin, and H.Y.Hu (2005).
Solution structure of the ubiquitin-like domain of human DC-UbP from dendritic cells.
  Protein Sci, 14, 2044-2050.
PDB code: 1ttn
15620657 C.R.Wilkinson, G.A.Dittmar, M.D.Ohi, P.Uetz, N.Jones, and D.Finley (2004).
Ubiquitin-like protein Hub1 is required for pre-mRNA splicing and localization of an essential splicing factor in fission yeast.
  Curr Biol, 14, 2283-2288.  
  15209379 C.R.Wilkinson (2004).
Ubiquitin-like proteins: meet the family.
  Semin Cell Dev Biol, 15, 199-200.  
15569151 H.Yashiroda, and K.Tanaka (2004).
Hub1 is an essential ubiquitin-like protein without functioning as a typical modifier in fission yeast.
  Genes Cells, 9, 1189-1197.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.