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Protein
Submitted name:

Uncharacterized protein

Gene

TTL

Organism
Gallus gallus (Chicken)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei74 – 741ADPCombined sources
Binding sitei74 – 741ATP analogCombined sources
Binding sitei150 – 1501ADPCombined sources
Binding sitei150 – 1501ATP analogCombined sources
Binding sitei198 – 1981ADPCombined sources
Binding sitei222 – 2221ATP analogCombined sources
Metal bindingi331 – 3311MagnesiumCombined sources
Binding sitei331 – 3311ADPCombined sources
Metal bindingi333 – 3331MagnesiumCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi183 – 1864ADPCombined sources
Nucleotide bindingi183 – 1864ATP analogCombined sources
Nucleotide bindingi198 – 2025ATP analogCombined sources
Nucleotide bindingi239 – 2424ATP analogCombined sources
Nucleotide bindingi241 – 2422ADPCombined sources
Nucleotide bindingi318 – 3203ATP analogCombined sources
Nucleotide bindingi331 – 3333ATP analogCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

MagnesiumCombined sources, Metal-bindingCombined sources, Nucleotide-bindingCombined sources

Names & Taxonomyi

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

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4TUYX-ray2.10F1-378[»]
4TV8X-ray2.10F1-378[»]
4TV9X-ray2.00F1-378[»]
4WBNX-ray2.30F1-378[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains TTL domain.SAAS annotation

Phylogenomic databases

GeneTreeiENSGT00760000118951.
InParanoidiE1BQ43.
OMAiQNYGRYE.
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

        10         20         30         40         50
MYTFVVRDEN SSVYAEVSRL LLATGQWKRL RKDNPRFNLM LGERNRLPFG
60 70 80 90 100
RLGHEPGLVQ LVNYYRGADK LCRKASLVKL IKTSPELSES CTWFPESYVI
110 120 130 140 150
YPTNLKTPVA PAQNGIRHLI NNTRTDEREV FLAAYNRRRE GREGNVWIAK
160 170 180 190 200
SSAGAKGEGI LISSEASELL DFIDEQGQVH VIQKYLEKPL LLEPGHRKFD
210 220 230 240 250
IRSWVLVDHL YNIYLYREGV LRTSSEPYNS ANFQDKTCHL TNHCIQKEYS
260 270 280 290 300
KNYGRYEEGN EMFFEEFNQY LMDALNTTLE NSILLQIKHI IRSCLMCIEP
310 320 330 340 350
AISTKHLHYQ SFQLFGFDFM VDEELKVWLI EVNGAPACAQ KLYAELCQGI
360 370
VDVAISSVFP LADTGQKTSQ PTSIFIKL
Length:378
Mass (Da):43,496
Last modified:November 2, 2010 - v1
Checksum:i4F4734154DF09BBD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AADN03003139 Genomic DNA. No translation available.
RefSeqiNP_001186321.1. NM_001199392.2.
UniGeneiGga.14457.

Genome annotation databases

EnsembliENSGALT00000014035; ENSGALP00000014019; ENSGALG00000008614.
GeneIDi416711.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AADN03003139 Genomic DNA. No translation available.
RefSeqiNP_001186321.1. NM_001199392.2.
UniGeneiGga.14457.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4TUYX-ray2.10F1-378[»]
4TV8X-ray2.10F1-378[»]
4TV9X-ray2.00F1-378[»]
4WBNX-ray2.30F1-378[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000014035; ENSGALP00000014019; ENSGALG00000008614.
GeneIDi416711.

Organism-specific databases

CTDi150465.

Phylogenomic databases

GeneTreeiENSGT00760000118951.
InParanoidiE1BQ43.
OMAiQNYGRYE.
OrthoDBiEOG72ZCDZ.
PhylomeDBiE1BQ43.
TreeFamiTF350555.

Miscellaneous databases

NextBioi20820133.
PROiE1BQ43.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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 ATP ANALOG 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 ATP ANALOG.
  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 ATP ANALOG.
  7. "A new tubulin-binding site and pharmacophore for microtubule-destabilizing anticancer drugs."
    Prota A.E., Bargsten K., Diaz J.F., Marsh M., Cuevas C., Liniger M., Neuhaus C., Andreu J.M., Altmann K.H., Steinmetz M.O.
    Proc. Natl. Acad. Sci. U.S.A. 111:13817-13821(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ATP ANALOG.

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: May 27, 2015
This is version 42 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-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.