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Protein

Tubulin epsilon chain

Gene

TUBE1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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
Complete GO annotation...

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 Componenti: 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
Complete GO annotation...

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.
ExpressionAtlasiQ9UJT0. baseline and differential.
GenevestigatoriQ9UJT0.

Organism-specific databases

HPAiHPA032073.
HPA032074.

Interactioni

Protein-protein interaction databases

BioGridi119353. 5 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.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165713.
HOVERGENiHBG098062.
InParanoidiQ9UJT0.
KOiK10391.
OMAiQEGWKTG.
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

        10         20         30         40         50
MTQSVVVQVG QCGNQIGCCF WDLALREHAA VNQKGIYDEA ISSFFRNVDT
60 70 80 90 100
RVVGDGGSIS KGKICSLKAR AVLIDMEEGV VNEILQGPLR DVFDTKQLIT
110 120 130 140 150
DISGSGNNWA VGHKVFGSLY QDQILEKFRK SAEHCDCLQC FFIIHSMGGG
160 170 180 190 200
TGSGLGTFLL KVLEDEFPEV YRFVTSIYPS GEDDVITSPY NSILAMKELN
210 220 230 240 250
EHADCVLPID NQSLFDIISK IDLMVNSGKL GTTVKPKSLV TSSSGALKKQ
260 270 280 290 300
HKKPFDAMNN IVANLLLNLT SSARFEGSLN MDLNEISMNL VPFPQLHYLV
310 320 330 340 350
SSLTPLYTLT DVNIPPRRLD QMFSDAFSKD HQLLRADPKH SLYLACALMV
360 370 380 390 400
RGNVQISDLR RNIERLKPSL QFVSWNQEGW KTSLCSVPPV GHSHSLLALA
410 420 430 440 450
NNTCVKPTFM ELKERFMRLY KKKAHLHHYL QVEGMEESCF TEAVSSLSAL
460 470
IQEYDQLDAT KNMPVQDLPR LSIAM
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi119353. 5 interactions.
STRINGi9606.ENSP00000357651.

Chemistry

DrugBankiDB00570. Vinblastine.

PTM databases

PhosphoSiteiQ9UJT0.

Polymorphism databases

DMDMi8928405.

Proteomic databases

MaxQBiQ9UJT0.
PaxDbiQ9UJT0.
PRIDEiQ9UJT0.

Protocols and materials databases

DNASUi51175.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51175.
GeneCardsiGC06M112391.
HGNCiHGNC:20775. TUBE1.
HPAiHPA032073.
HPA032074.
MIMi607345. gene.
neXtProtiNX_Q9UJT0.
PharmGKBiPA134936770.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165713.
HOVERGENiHBG098062.
InParanoidiQ9UJT0.
KOiK10391.
OMAiQEGWKTG.
PhylomeDBiQ9UJT0.
TreeFamiTF330882.

Miscellaneous databases

GeneWikiiTUBE1.
GenomeRNAii51175.
NextBioi54129.
PROiQ9UJT0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UJT0.
CleanExiHS_TUBE1.
ExpressionAtlasiQ9UJT0. baseline and differential.
GenevestigatoriQ9UJT0.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1999) [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(2002) [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(2003) [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: April 1, 2015
This is version 119 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

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.