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Protein Overview: gi|17943410, gi|...

General Information:
Name(s) found: gi|242556271 [NCBI NR]
gi|242556270 [NCBI NR]
gi|242556269 [NCBI NR]
gi|242556268 [NCBI NR]
gi|242556267 [NCBI NR]
gi|242556266 [NCBI NR]
gi|242556263 [NCBI NR]
gi|242556262 [NCBI NR]
gi|242556261 [NCBI NR]
gi|242556260 [NCBI NR]
gi|242556259 [NCBI NR]
gi|242556258 [NCBI NR]
gi|17943412 [NCBI NR]
gi|17943411 [NCBI NR]
gi|17943410 [NCBI NR]
gi|17943409 [NCBI NR]
gi|17943408 [NCBI NR]
gi|17943407 [NCBI NR]
Description(s) found:
Found 25 descriptions.
SHOW ALL
  • gi|242556271|pdb|2ZQR|F Chain F, Crystal Structure Of Auh Without Rna [NCBI NR]
  • gi|242556270|pdb|2ZQR|E Chain E, Crystal Structure Of Auh Without Rna [NCBI NR]
  • gi|242556269|pdb|2ZQR|D Chain D, Crystal Structure Of Auh Without Rna [NCBI NR]
  • gi|242556268|pdb|2ZQR|C Chain C, Crystal Structure Of Auh Without Rna [NCBI NR]
  • gi|242556267|pdb|2ZQR|B Chain B, Crystal Structure Of Auh Without Rna [NCBI NR]
  • gi|242556266|pdb|2ZQR|A Chain A, Crystal Structure Of Auh Without Rna [NCBI NR]
  • gi|242556263|pdb|2ZQQ|F Chain F, Crystal Structure Of Human Auh (3-Methylglutaconyl-Coa Hydratase) Mixed With (Auuu)24a Rna [NCBI NR]
  • gi|242556262|pdb|2ZQQ|E Chain E, Crystal Structure Of Human Auh (3-Methylglutaconyl-Coa Hydratase) Mixed With (Auuu)24a Rna [NCBI NR]
  • gi|242556261|pdb|2ZQQ|D Chain D, Crystal Structure Of Human Auh (3-Methylglutaconyl-Coa Hydratase) Mixed With (Auuu)24a Rna [NCBI NR]
  • gi|242556260|pdb|2ZQQ|C Chain C, Crystal Structure Of Human Auh (3-Methylglutaconyl-Coa Hydratase) Mixed With (Auuu)24a Rna [NCBI NR]
  • gi|242556259|pdb|2ZQQ|B Chain B, Crystal Structure Of Human Auh (3-Methylglutaconyl-Coa Hydratase) Mixed With (Auuu)24a Rna [NCBI NR]
  • gi|242556258|pdb|2ZQQ|A Chain A, Crystal Structure Of Human Auh (3-Methylglutaconyl-Coa Hydratase) Mixed With (Auuu)24a Rna [NCBI NR]
  • gi|17943412|pdb|1HZD|F Chain F, Crystal Structure Of Human Auh Protein, An Rna-Binding Homologue Of Enoyl-Coa Hydratase [NCBI NR]
  • gi|17943411|pdb|1HZD|E Chain E, Crystal Structure Of Human Auh Protein, An Rna-Binding Homologue Of Enoyl-Coa Hydratase [NCBI NR]
  • gi|17943410|pdb|1HZD|D Chain D, Crystal Structure Of Human Auh Protein, An Rna-Binding Homologue Of Enoyl-Coa Hydratase [NCBI NR]
  • gi|17943409|pdb|1HZD|C Chain C, Crystal Structure Of Human Auh Protein, An Rna-Binding Homologue Of Enoyl-Coa Hydratase [NCBI NR]
  • gi|17943408|pdb|1HZD|B Chain B, Crystal Structure Of Human Auh Protein, An Rna-Binding Homologue Of Enoyl-Coa Hydratase [NCBI NR]
  • gi|17943407|pdb|1HZD|A Chain A, Crystal Structure Of Human Auh Protein, An Rna-Binding Homologue Of Enoyl-Coa Hydratase [NCBI NR]
    • Organism: Homo sapiens
    Length: 272 amino acids

    Gene Ontology:
    Cellular Component: NONE FOUND
    Biological Process: NONE FOUND
    Molecular Function: NONE FOUND


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 SSEMKTEDEL RVRHLEEENR GIVVLGINRA YGKNSLSKNL IKMLSKAVDA LKSDKKVRTI  60
   61 IIRSEVPGIF CAGADLKERA KMSSSEVGPF VSKIRAVIND IANLPVPTIA AIDGLALGGG 120
  121 LELALACDIR VAASSAKMGL VETKLAIIPG GGGTQRLPRA IGMSLAKELI FSARVLDGKE 180
  181 AKAVGLISHV LEQNQEGDAA YRKALDLARE FLPQGPVAMR VAKLAINQGM EVDLVTGLAI 240
  241 EEACYAQTIP TKDRLEGLLA FKEKRPPRYK GE

    Protein Complex Data

      PUBLICATION TOPOLOGY COCOMPLEXED PROTEINS
    View Details Noble WS, et al. (2009) Manuscript in preparation. gi|112491310 gi|13786858 gi|150261449 gi|17943410, gi|... gi|197725196 gi|219109210, gi... gi|3659984 gi|56554577 gi|56966260, gi|...

    Mass Spectrometry Data

    No mass spectrometry results found for this protein.

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    NOT SHOWING SINGLE HITS. [ Show Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

    No yeast two-hybrid interactions found for this protein.

    Microscopy / Localization Data

    New Feature: Upload Your Own Microscopy Data

    No microscopy data found in the PDR for this protein.

    Protein Structure Data


    [What does the above image mean?]
    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..272] PSI-BLAST 63.30103 AUH protein

    Functions predicted (by domain):

    # Gene Ontology predictions
    1
    Term Confidence Notes
  • enoyl-CoA hydratase activity
    		•  3.92947460544831 bayes_pls_golite062009
  • CoA carboxylase activity
    		•  3.59076614105466 bayes_pls_golite062009
  • ligase activity, forming carbon-carbon bonds
    		•  3.4980371783229 bayes_pls_golite062009
  • acetyl-CoA carboxylase activity
    		•  3.34692152434862 bayes_pls_golite062009
  • 3-hydroxyacyl-CoA dehydrogenase activity
    		•  2.44182589784656 bayes_pls_golite062009
  • dodecenoyl-CoA delta-isomerase activity
    		•  1.80820904754223 bayes_pls_golite062009
  • catalytic activity
    		•  1.46154163027498 bayes_pls_golite062009
  • propionyl-CoA carboxylase activity
    		•  1.20853698666984 bayes_pls_golite062009
  • long-chain-3-hydroxyacyl-CoA dehydrogenase activity
    		•  1.03484393216342 bayes_pls_golite062009
  • ligase activity
    		•  0.98581896521131 bayes_pls_golite062009
  • RNA binding
    		•  0.599974851773164 bayes_pls_golite062009
  • binding
    		•  0.578223105269736 bayes_pls_golite062009
  • long-chain-enoyl-CoA hydratase activity
    		•  0.571617594666499 bayes_pls_golite062009
  • nucleic acid binding
    		•  0.472835473017362 bayes_pls_golite062009
  • 3-hydroxybutyryl-CoA epimerase activity
    		•  0.241955774397835 bayes_pls_golite062009
  • hydrolase activity
    		•  0.167287221009063 bayes_pls_golite062009
  • racemase and epimerase activity, acting on hydroxy acids and derivatives
    		•  0.099208209617217 bayes_pls_golite062009
  • intramolecular oxidoreductase activity, transposing C=C bonds
    		•  0.0918189681606029 bayes_pls_golite062009


    Reference: Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16


    Philius Transmembrane Prediction:

    Protein predicted to be: GLOBULAR (No transmembrane regions or signal peptide)
    Confidence of classification: 0.98

    Source: Reynolds et al. (2008)

    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle