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A6NHL2

- TBAL3_HUMAN

UniProt

A6NHL2 - TBAL3_HUMAN

Protein

Tubulin alpha chain-like 3

Gene

TUBAL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi149 – 1557GTPSequence Analysis

    GO - Molecular functioni

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

    GO - Biological processi

    1. microtubule-based process Source: InterPro
    2. protein polymerization Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tubulin alpha chain-like 3
    Gene namesi
    Name:TUBAL3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:23534. TUBAL3.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. microtubule Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134953102.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 446446Tubulin alpha chain-like 3PRO_0000313709Add
    BLAST

    Proteomic databases

    MaxQBiA6NHL2.
    PaxDbiA6NHL2.
    PRIDEiA6NHL2.

    Expressioni

    Gene expression databases

    BgeeiA6NHL2.
    CleanExiHS_TUBAL3.
    GenevestigatoriA6NHL2.

    Organism-specific databases

    HPAiHPA045900.

    Interactioni

    Subunit structurei

    Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

    Protein-protein interaction databases

    BioGridi122949. 4 interactions.
    IntActiA6NHL2. 2 interactions.
    MINTiMINT-4994564.
    STRINGi9606.ENSP00000369784.

    Structurei

    3D structure databases

    ProteinModelPortaliA6NHL2.
    SMRiA6NHL2. Positions 1-443.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    eggNOGiCOG5023.
    HOGENOMiHOG000165711.
    HOVERGENiHBG000089.
    InParanoidiA6NHL2.
    KOiK07374.
    OMAiRIHFPMT.
    OrthoDBiEOG7966GH.
    PhylomeDBiA6NHL2.
    TreeFamiTF300314.

    Family and domain databases

    Gene3Di1.10.287.600. 1 hit.
    3.30.1330.20. 1 hit.
    3.40.50.1440. 1 hit.
    InterProiIPR002452. Alpha_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.
    PfamiPF00091. Tubulin. 1 hit.
    PF03953. Tubulin_C. 1 hit.
    [Graphical view]
    PRINTSiPR01162. ALPHATUBULIN.
    PR01161. TUBULIN.
    SMARTiSM00864. Tubulin. 1 hit.
    SM00865. Tubulin_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF52490. SSF52490. 1 hit.
    SSF55307. SSF55307. 1 hit.
    PROSITEiPS00227. TUBULIN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: A6NHL2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MRECLSIHIG QAGIQIGDAC WELYCLEHGI QPNGVVLDTQ QDQLENAKME    50
    HTNASFDTFF CETRAGKHVP RALFVDLEPT VIDGIRTGQH RSLFHPEQLL 100
    SGKEDAANNY ARGRYSVGSE VIDLVLERTR KLAEQCGGLQ GFLIFRSFGG 150
    GTGSGFTSLL MERLTGEYSR KTKLEFSVYP APRISTAVVE PYNSVLTTHS 200
    TTEHTDCTFM VDNEAVYDIC HRKLGVECPS HASINRLVVQ VVSSITASLR 250
    FEGPLNVDLI EFQTNLVPYP RIHFPMTAFA PIVSADKAYH EQFSVSDITT 300
    ACFESSNQLV KCDPRLGKYM ACCLLYRGDV VPKEVNAAIA ATKSRHSVQF 350
    VDWCPTGFKV GINNRPPTVM PGGDLAKVHR SICMLSNTTA IVEAWARLDH 400
    KFDLMYAKRA FLHWYLREGM EEAEFLEARE DLAALERDYE EVAQSF 446
    Length:446
    Mass (Da):49,909
    Last modified:January 15, 2008 - v2
    Checksum:iD826240ACC90B6EC
    GO
    Isoform 2 (identifier: A6NHL2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-41: MRECLSIHIGQAGIQIGDACWELYCLEHGIQPNGVVLDTQQ → M

    Show »
    Length:406
    Mass (Da):45,518
    Checksum:i461A205AAD34DB4C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti128 – 1281R → G in BAG59224. (PubMed:14702039)Curated
    Sequence conflicti134 – 1341E → K in EAW86447. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti135 – 1351Q → H.
    Corresponds to variant rs11818372 [ dbSNP | Ensembl ].
    VAR_037706
    Natural varianti250 – 2501R → W.
    Corresponds to variant rs34080891 [ dbSNP | Ensembl ].
    VAR_037707

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4141MRECL…LDTQQ → M in isoform 2. 2 PublicationsVSP_030108Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK025318 mRNA. Translation: BAB15110.1.
    AK296616 mRNA. Translation: BAG59224.1.
    AL683826 Genomic DNA. Translation: CAI23625.1.
    CH471072 Genomic DNA. Translation: EAW86447.1.
    BC098247 mRNA. Translation: AAH98247.1.
    BC099716 mRNA. Translation: AAH99716.1.
    BC105634 mRNA. Translation: AAI05635.1.
    CCDSiCCDS53491.1. [A6NHL2-2]
    CCDS7066.2. [A6NHL2-1]
    RefSeqiNP_001165335.1. NM_001171864.1. [A6NHL2-2]
    NP_079079.1. NM_024803.2. [A6NHL2-1]
    UniGeneiHs.163079.

    Genome annotation databases

    EnsembliENST00000380419; ENSP00000369784; ENSG00000178462. [A6NHL2-1]
    ENST00000479328; ENSP00000418799; ENSG00000178462. [A6NHL2-2]
    GeneIDi79861.
    KEGGihsa:79861.
    UCSCiuc001ihy.3. human. [A6NHL2-1]
    uc001ihz.3. human. [A6NHL2-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK025318 mRNA. Translation: BAB15110.1 .
    AK296616 mRNA. Translation: BAG59224.1 .
    AL683826 Genomic DNA. Translation: CAI23625.1 .
    CH471072 Genomic DNA. Translation: EAW86447.1 .
    BC098247 mRNA. Translation: AAH98247.1 .
    BC099716 mRNA. Translation: AAH99716.1 .
    BC105634 mRNA. Translation: AAI05635.1 .
    CCDSi CCDS53491.1. [A6NHL2-2 ]
    CCDS7066.2. [A6NHL2-1 ]
    RefSeqi NP_001165335.1. NM_001171864.1. [A6NHL2-2 ]
    NP_079079.1. NM_024803.2. [A6NHL2-1 ]
    UniGenei Hs.163079.

    3D structure databases

    ProteinModelPortali A6NHL2.
    SMRi A6NHL2. Positions 1-443.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122949. 4 interactions.
    IntActi A6NHL2. 2 interactions.
    MINTi MINT-4994564.
    STRINGi 9606.ENSP00000369784.

    Proteomic databases

    MaxQBi A6NHL2.
    PaxDbi A6NHL2.
    PRIDEi A6NHL2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380419 ; ENSP00000369784 ; ENSG00000178462 . [A6NHL2-1 ]
    ENST00000479328 ; ENSP00000418799 ; ENSG00000178462 . [A6NHL2-2 ]
    GeneIDi 79861.
    KEGGi hsa:79861.
    UCSCi uc001ihy.3. human. [A6NHL2-1 ]
    uc001ihz.3. human. [A6NHL2-2 ]

    Organism-specific databases

    CTDi 79861.
    GeneCardsi GC10M005425.
    HGNCi HGNC:23534. TUBAL3.
    HPAi HPA045900.
    neXtProti NX_A6NHL2.
    PharmGKBi PA134953102.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5023.
    HOGENOMi HOG000165711.
    HOVERGENi HBG000089.
    InParanoidi A6NHL2.
    KOi K07374.
    OMAi RIHFPMT.
    OrthoDBi EOG7966GH.
    PhylomeDBi A6NHL2.
    TreeFami TF300314.

    Miscellaneous databases

    GenomeRNAii 79861.
    NextBioi 69592.
    PROi A6NHL2.

    Gene expression databases

    Bgeei A6NHL2.
    CleanExi HS_TUBAL3.
    Genevestigatori A6NHL2.

    Family and domain databases

    Gene3Di 1.10.287.600. 1 hit.
    3.30.1330.20. 1 hit.
    3.40.50.1440. 1 hit.
    InterProi IPR002452. Alpha_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.
    Pfami PF00091. Tubulin. 1 hit.
    PF03953. Tubulin_C. 1 hit.
    [Graphical view ]
    PRINTSi PR01162. ALPHATUBULIN.
    PR01161. TUBULIN.
    SMARTi SM00864. Tubulin. 1 hit.
    SM00865. Tubulin_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52490. SSF52490. 1 hit.
    SSF55307. SSF55307. 1 hit.
    PROSITEi PS00227. TUBULIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Colon.
    2. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [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] (ISOFORMS 1 AND 2).
    5. Lubec G., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 104-112; 147-163; 319-327 AND 402-408, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain.

    Entry informationi

    Entry nameiTBAL3_HUMAN
    AccessioniPrimary (citable) accession number: A6NHL2
    Secondary accession number(s): B4DKL2, Q4QQJ5, Q9H6Z0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 75 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3