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E1BQ43

- E1BQ43_CHICK

UniProt

E1BQ43 - E1BQ43_CHICK

Protein
Submitted name:

Uncharacterized protein

Gene

TTL

Organism
Gallus gallus (Chicken)
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 35 (01 Oct 2014)
      Sequence version 1 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei74 – 741ADPImported
    Binding sitei74 – 741ATPanalogImported
    Binding sitei150 – 1501ADPImported
    Binding sitei150 – 1501ATPanalogImported
    Binding sitei198 – 1981ADPImported
    Metal bindingi331 – 3311MagnesiumImported
    Binding sitei331 – 3311ADPImported
    Metal bindingi333 – 3331MagnesiumImported

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi183 – 1864ADPImported
    Nucleotide bindingi183 – 1864ATPanalogImported
    Nucleotide bindingi198 – 2025ATPanalogImported
    Nucleotide bindingi239 – 2424ATPanalogImported
    Nucleotide bindingi241 – 2422ADPImported
    Nucleotide bindingi318 – 3203ATPanalogImported
    Nucleotide bindingi331 – 3333ATPanalogImported

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. nucleotide binding Source: UniProtKB-KW
    3. tubulin-tyrosine ligase activity Source: Ensembl

    GO - Biological processi

    1. cellular protein modification process Source: InterPro
    2. microtubule cytoskeleton organization Source: Ensembl
    3. regulation of axon extension Source: Ensembl

    Keywords - Ligandi

    MagnesiumImported, Metal-bindingImported, Nucleotide-bindingImported

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Uncharacterized proteinImported
    Gene namesi
    Name:TTLImported
    OrganismiGallus gallus (Chicken)Imported
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Chromosome 3

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4I4TX-ray1.80F1-378[»]
    4I50X-ray2.30F1-378[»]
    4I55X-ray2.20F1-378[»]
    4IHJX-ray2.00F1-378[»]
    4IIJX-ray2.60F1-378[»]
    4O2AX-ray2.50F1-378[»]
    4O2BX-ray2.30F1-378[»]
    4O4HX-ray2.10F1-378[»]
    4O4IX-ray2.40F1-378[»]
    4O4JX-ray2.20F1-378[»]
    4O4LX-ray2.20F1-378[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Contains TTL domain.SAAS annotation

    Phylogenomic databases

    GeneTreeiENSGT00750000117283.
    KOiK06047.
    OMAiKLYPELC.
    OrthoDBiEOG72ZCDZ.
    PhylomeDBiE1BQ43.
    TreeFamiTF350555.

    Family and domain databases

    InterProiIPR004344. TTL/TTLL_fam.
    [Graphical view]
    PfamiPF03133. TTL. 1 hit.
    [Graphical view]
    PROSITEiPS51221. TTL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    E1BQ43-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYTFVVRDEN SSVYAEVSRL LLATGQWKRL RKDNPRFNLM LGERNRLPFG    50
    RLGHEPGLVQ LVNYYRGADK LCRKASLVKL IKTSPELSES CTWFPESYVI 100
    YPTNLKTPVA PAQNGIRHLI NNTRTDEREV FLAAYNRRRE GREGNVWIAK 150
    SSAGAKGEGI LISSEASELL DFIDEQGQVH VIQKYLEKPL LLEPGHRKFD 200
    IRSWVLVDHL YNIYLYREGV LRTSSEPYNS ANFQDKTCHL TNHCIQKEYS 250
    KNYGRYEEGN EMFFEEFNQY LMDALNTTLE NSILLQIKHI IRSCLMCIEP 300
    AISTKHLHYQ SFQLFGFDFM VDEELKVWLI EVNGAPACAQ KLYAELCQGI 350
    VDVAISSVFP LADTGQKTSQ PTSIFIKL 378
    Length:378
    Mass (Da):43,496
    Last modified:November 2, 2010 - v1
    Checksum:i4F4734154DF09BBD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AADN03003139 Genomic DNA. No translation available.
    RefSeqiNP_001186321.1. NM_001199392.2.
    UniGeneiGga.14457.

    Genome annotation databases

    EnsembliENSGALT00000014035; ENSGALP00000014019; ENSGALG00000008614.
    GeneIDi416711.
    KEGGigga:416711.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AADN03003139 Genomic DNA. No translation available.
    RefSeqi NP_001186321.1. NM_001199392.2.
    UniGenei Gga.14457.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4I4T X-ray 1.80 F 1-378 [» ]
    4I50 X-ray 2.30 F 1-378 [» ]
    4I55 X-ray 2.20 F 1-378 [» ]
    4IHJ X-ray 2.00 F 1-378 [» ]
    4IIJ X-ray 2.60 F 1-378 [» ]
    4O2A X-ray 2.50 F 1-378 [» ]
    4O2B X-ray 2.30 F 1-378 [» ]
    4O4H X-ray 2.10 F 1-378 [» ]
    4O4I X-ray 2.40 F 1-378 [» ]
    4O4J X-ray 2.20 F 1-378 [» ]
    4O4L X-ray 2.20 F 1-378 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSGALT00000014035 ; ENSGALP00000014019 ; ENSGALG00000008614 .
    GeneIDi 416711.
    KEGGi gga:416711.

    Organism-specific databases

    CTDi 150465.

    Phylogenomic databases

    GeneTreei ENSGT00750000117283.
    KOi K06047.
    OMAi KLYPELC.
    OrthoDBi EOG72ZCDZ.
    PhylomeDBi E1BQ43.
    TreeFami TF350555.

    Miscellaneous databases

    NextBioi 20820133.
    PROi E1BQ43.

    Family and domain databases

    InterProi IPR004344. TTL/TTLL_fam.
    [Graphical view ]
    Pfami PF03133. TTL. 1 hit.
    [Graphical view ]
    PROSITEi PS51221. TTL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution."
      International Chicken Genome Sequencing Consortium
      Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A.
      , Kremitzki C., Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., Wilson R.K.
      Nature 432:695-716(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Red jungle fowlImported.
    2. Ensembl
      Submitted (JUL-2011) to UniProtKB
      Cited for: IDENTIFICATION.
      Strain: Red jungle fowlImported.
    3. "Structural basis of tubulin tyrosination by tubulin tyrosine ligase."
      Prota A.E., Magiera M.M., Kuijpers M., Bargsten K., Frey D., Wieser M., Jaussi R., Hoogenraad C.C., Kammerer R.A., Janke C., Steinmetz M.O.
      J. Cell Biol. 200:259-270(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ADP AND MAGNESIUM.
    4. "Molecular mechanism of action of microtubule-stabilizing anticancer agents."
      Prota A.E., Bargsten K., Zurwerra D., Field J.J., Diaz J.F., Altmann K.H., Steinmetz M.O.
      Science 339:587-590(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ATPANALOG AND MAGNESIUM.
    5. "Structural basis of microtubule stabilization by laulimalide and peloruside A."
      Prota A.E., Bargsten K., Northcote P.T., Marsh M., Altmann K.H., Miller J.H., Diaz J.F., Steinmetz M.O.
      Angew. Chem. Int. Ed. 53:1621-1625(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ATPANALOG.
    6. "The novel microtubule-destabilizing drug BAL27862 binds to the colchicine site of tubulin with distinct effects on microtubule organization."
      Prota A.E., Danel F., Bachmann F., Bargsten K., Buey R.M., Pohlmann J., Reinelt S., Lane H., Steinmetz M.O.
      J. Mol. Biol. 426:1848-1860(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ADP AND ATPANALOG.

    Entry informationi

    Entry nameiE1BQ43_CHICK
    AccessioniPrimary (citable) accession number: E1BQ43
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 2, 2010
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 35 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Caution

    The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

    Keywords - Technical termi

    3D-structureImported, Complete proteome, Reference proteomeImported

    External Data

    Dasty 3