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DP00286: Protein quaking-A [Isoform 1]FASTA viewXML view

General information
DisProt:DP00286
Name:Protein quaking-A [Isoform 1]
Synonym(s):QKIA_XENLA
Xqua
First appeared in release:Release 3.0 (02/17/2006)
UniProt:Q32NN2-1
UniGene:Xl.55586
SwissProt: QKIA_XENLA
TrEMBL:  
NCBI (GI): 108860915
Source organism:Xenopus laevis (African clawed frog)
Sequence length:341
Percent disordered:6%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MVGEMETKEK PKPTPDYLMQ LMNDKKLMSS LPNFCGIFTH LERLLDEEIS RVRKDMYNDT - 60
MNSSSNEKRT SELPDGIGPI VQLQEKLYVP VKEYPDFNFV GRILGPRGLT AKQLEAETGC - 120
KIMVRGKGSM RDKKKEEQNR GKPNWEHLNE DLHVLITVED AQNRAELKLK RAVEEVKKLL - 180
VPAAEGEDSL KKMQLMELAI LNGTYRDANL KSPALAFSLA ATGQAPRIIT GPAPVLSPAA - 240
LRTPTPAGHT LMPLIRQIQT AVMPNGTPHP TATLMQQAPE GGLIYTPYEY PYTLAPATSI - 300
LEYPIEASGV LGAVATKVRR HDMRVHPYQR IVTADRAATG N

Region 1: 184-189 Region 2: 203-215

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name:flexible linker
Location:184 - 189
Length:6
Region sequence:

AEGEDS

Modification type: Fragment
PDB: 2BL5:A
Structural/functional type: Function arises from the disordered state
Functional classes: Entropic chain
Functional subclasses: Flexible linkers/spacers
Detection methods:
  1. Nuclear magnetic resonance (NMR) (298 K; pH: 6.5; 2H2O (v/v) 10 %; 3,3,3-trimethylsilylpropionate 20 uM; dithio-1,4-threitol 5 mM; pXqua KH-QUA2 (protein) 1 mM; sodium azide (w/v) 0.05 %; sodium phosphate 50 mM)

References:
  1. Maguire ML, Guler-Gane G, Nietlispach D, Raine AR, Zorn AM, Standart N, Broadhurst RW. "Solution structure and backbone dynamics of the KH-QUA2 region of the Xenopus STAR/GSG quaking protein." J Mol Biol. 2005; 348(2): 265-79. PubMed: 15811367

Comments:
 



Region 2
Type:Disordered
Name: 
Location:203 - 215
Length:13
Region sequence:

GTYRDANLKSPAL

Modification type: Fragment
PDB: 2BL5:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. Nuclear magnetic resonance (NMR) (298 K; pH: 6.5; 2H2O (v/v) 10 %; 3,3,3-trimethysilylpropionate 20 uM; dithio-1,4-threitol 5 mM; pXqua KH-QUA2 (protein) 1 mM; sodium azide (w/v) 0.05 %; sodium phosphate 50 mM)

References:
  1. Maguire ML, Guler-Gane G, Nietlispach D, Raine AR, Zorn AM, Standart N, Broadhurst RW. "Solution structure and backbone dynamics of the KH-QUA2 region of the Xenopus STAR/GSG quaking protein." J Mol Biol. 2005; 348(2): 265-79. PubMed: 15811367

Comments:
The Maguire et. al paper has a leucine instead of an alanine at position 127, as determined by the NCBI ID.




References

  1. Zorn AM, Grow M, Patterson KD, Ebersole TA, Chen Q, Artzt K, Krieg PA. "Remarkable sequence conservation of transcripts encoding amphibian and mammalian homologues of quaking, a KH domain RNA-binding protein." Gene. 1997; 188(2): 199-206. PubMed: 9133592



Comments


The sequence taken from the Maguire et al. article matches 99% (139/140 amino acids) with the NCBI reference. The paper has a leucine instead of an alanine at position 127.



There is a mismatch between the sequence in the paper and that provided by UniProt, with a lysine for residue 194 instead of a glutamine.


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