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Q9UJT0

- TBE_HUMAN

UniProt

Q9UJT0 - TBE_HUMAN

Protein

Tubulin epsilon chain

Gene

TUBE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi148 – 1547GTPSequence Analysis

    GO - Molecular functioni

    1. GTPase activity Source: InterPro
    2. GTP binding Source: UniProtKB-KW
    3. structural constituent of cytoskeleton Source: ProtInc

    GO - Biological processi

    1. centrosome cycle Source: ProtInc
    2. protein polymerization Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tubulin epsilon chain
    Alternative name(s):
    Epsilon-tubulin
    Gene namesi
    Name:TUBE1
    Synonyms:TUBE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:20775. TUBE1.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
    Note: Associated with pericentriolar material.

    GO - Cellular componenti

    1. microtubule Source: UniProtKB-KW
    2. pericentriolar material Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134936770.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 475475Tubulin epsilon chainPRO_0000048486Add
    BLAST

    Proteomic databases

    MaxQBiQ9UJT0.
    PaxDbiQ9UJT0.
    PRIDEiQ9UJT0.

    PTM databases

    PhosphoSiteiQ9UJT0.

    Expressioni

    Gene expression databases

    BgeeiQ9UJT0.
    CleanExiHS_TUBE1.
    GenevestigatoriQ9UJT0.

    Organism-specific databases

    HPAiHPA032073.
    HPA032074.

    Interactioni

    Protein-protein interaction databases

    BioGridi119353. 4 interactions.
    STRINGi9606.ENSP00000357651.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UJT0.
    SMRiQ9UJT0. Positions 5-456.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    eggNOGiCOG5023.
    HOGENOMiHOG000165713.
    HOVERGENiHBG098062.
    InParanoidiQ9UJT0.
    KOiK10391.
    OMAiKKKAHLH.
    PhylomeDBiQ9UJT0.
    TreeFamiTF330882.

    Family and domain databases

    Gene3Di1.10.287.600. 1 hit.
    3.30.1330.20. 1 hit.
    3.40.50.1440. 1 hit.
    InterProiIPR004057. Epsilon_tubulin.
    IPR008280. Tub_FtsZ_C.
    IPR000217. Tubulin.
    IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
    IPR023123. Tubulin_C.
    IPR017975. Tubulin_CS.
    IPR003008. Tubulin_FtsZ_GTPase.
    [Graphical view]
    PANTHERiPTHR11588. PTHR11588. 1 hit.
    PTHR11588:SF13. PTHR11588:SF13. 1 hit.
    PfamiPF00091. Tubulin. 1 hit.
    PF03953. Tubulin_C. 1 hit.
    [Graphical view]
    PRINTSiPR01519. EPSLNTUBULIN.
    PR01161. TUBULIN.
    SMARTiSM00864. Tubulin. 1 hit.
    SM00865. Tubulin_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF52490. SSF52490. 2 hits.
    SSF55307. SSF55307. 1 hit.
    PROSITEiPS00227. TUBULIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UJT0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTQSVVVQVG QCGNQIGCCF WDLALREHAA VNQKGIYDEA ISSFFRNVDT    50
    RVVGDGGSIS KGKICSLKAR AVLIDMEEGV VNEILQGPLR DVFDTKQLIT 100
    DISGSGNNWA VGHKVFGSLY QDQILEKFRK SAEHCDCLQC FFIIHSMGGG 150
    TGSGLGTFLL KVLEDEFPEV YRFVTSIYPS GEDDVITSPY NSILAMKELN 200
    EHADCVLPID NQSLFDIISK IDLMVNSGKL GTTVKPKSLV TSSSGALKKQ 250
    HKKPFDAMNN IVANLLLNLT SSARFEGSLN MDLNEISMNL VPFPQLHYLV 300
    SSLTPLYTLT DVNIPPRRLD QMFSDAFSKD HQLLRADPKH SLYLACALMV 350
    RGNVQISDLR RNIERLKPSL QFVSWNQEGW KTSLCSVPPV GHSHSLLALA 400
    NNTCVKPTFM ELKERFMRLY KKKAHLHHYL QVEGMEESCF TEAVSSLSAL 450
    IQEYDQLDAT KNMPVQDLPR LSIAM 475
    Length:475
    Mass (Da):52,932
    Last modified:May 1, 2000 - v1
    Checksum:i3E8E717CBA6AFC80
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti91 – 911D → G in AAH31101. (PubMed:15489334)Curated
    Sequence conflicti469 – 4691P → R in AAH31101. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF201334 mRNA. Translation: AAF09585.1.
    Z99289 Genomic DNA. Translation: CAI42327.1.
    CH471051 Genomic DNA. Translation: EAW48272.1.
    BC025405 mRNA. Translation: AAH25405.1.
    BC031101 mRNA. Translation: AAH31101.1.
    CCDSiCCDS5100.1.
    RefSeqiNP_057346.1. NM_016262.4.
    UniGeneiHs.34851.

    Genome annotation databases

    EnsembliENST00000368662; ENSP00000357651; ENSG00000074935.
    GeneIDi51175.
    KEGGihsa:51175.
    UCSCiuc003pvq.3. human.

    Polymorphism databases

    DMDMi8928405.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF201334 mRNA. Translation: AAF09585.1 .
    Z99289 Genomic DNA. Translation: CAI42327.1 .
    CH471051 Genomic DNA. Translation: EAW48272.1 .
    BC025405 mRNA. Translation: AAH25405.1 .
    BC031101 mRNA. Translation: AAH31101.1 .
    CCDSi CCDS5100.1.
    RefSeqi NP_057346.1. NM_016262.4.
    UniGenei Hs.34851.

    3D structure databases

    ProteinModelPortali Q9UJT0.
    SMRi Q9UJT0. Positions 5-456.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119353. 4 interactions.
    STRINGi 9606.ENSP00000357651.

    PTM databases

    PhosphoSitei Q9UJT0.

    Polymorphism databases

    DMDMi 8928405.

    Proteomic databases

    MaxQBi Q9UJT0.
    PaxDbi Q9UJT0.
    PRIDEi Q9UJT0.

    Protocols and materials databases

    DNASUi 51175.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368662 ; ENSP00000357651 ; ENSG00000074935 .
    GeneIDi 51175.
    KEGGi hsa:51175.
    UCSCi uc003pvq.3. human.

    Organism-specific databases

    CTDi 51175.
    GeneCardsi GC06M112437.
    HGNCi HGNC:20775. TUBE1.
    HPAi HPA032073.
    HPA032074.
    MIMi 607345. gene.
    neXtProti NX_Q9UJT0.
    PharmGKBi PA134936770.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5023.
    HOGENOMi HOG000165713.
    HOVERGENi HBG098062.
    InParanoidi Q9UJT0.
    KOi K10391.
    OMAi KKKAHLH.
    PhylomeDBi Q9UJT0.
    TreeFami TF330882.

    Miscellaneous databases

    GeneWikii TUBE1.
    GenomeRNAii 51175.
    NextBioi 54129.
    PROi Q9UJT0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UJT0.
    CleanExi HS_TUBE1.
    Genevestigatori Q9UJT0.

    Family and domain databases

    Gene3Di 1.10.287.600. 1 hit.
    3.30.1330.20. 1 hit.
    3.40.50.1440. 1 hit.
    InterProi IPR004057. Epsilon_tubulin.
    IPR008280. Tub_FtsZ_C.
    IPR000217. Tubulin.
    IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
    IPR023123. Tubulin_C.
    IPR017975. Tubulin_CS.
    IPR003008. Tubulin_FtsZ_GTPase.
    [Graphical view ]
    PANTHERi PTHR11588. PTHR11588. 1 hit.
    PTHR11588:SF13. PTHR11588:SF13. 1 hit.
    Pfami PF00091. Tubulin. 1 hit.
    PF03953. Tubulin_C. 1 hit.
    [Graphical view ]
    PRINTSi PR01519. EPSLNTUBULIN.
    PR01161. TUBULIN.
    SMARTi SM00864. Tubulin. 1 hit.
    SM00865. Tubulin_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52490. SSF52490. 2 hits.
    SSF55307. SSF55307. 1 hit.
    PROSITEi PS00227. TUBULIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Delta-tubulin and epsilon-tubulin: two new human centrosomal tubulins reveal new aspects of centrosome structure and function."
      Chang P., Stearns T.
      Nat. Cell Biol. 2:30-35(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.

    Entry informationi

    Entry nameiTBE_HUMAN
    AccessioniPrimary (citable) accession number: Q9UJT0
    Secondary accession number(s): Q5H8W8, Q8NEG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3