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P40222

- TXLNA_HUMAN

UniProt

P40222 - TXLNA_HUMAN

Protein

Alpha-taxilin

Gene

TXLNA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 3 (09 Nov 2004)
      Previous versions | rss
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    Functioni

    May be involved in intracellular vesicle traffic and potentially in calcium-dependent exocytosis in neuroendocrine cells.

    GO - Molecular functioni

    1. cytokine activity Source: UniProtKB
    2. high molecular weight B cell growth factor receptor binding Source: UniProtKB
    3. protein binding Source: IntAct

    GO - Biological processi

    1. B cell activation Source: Ensembl
    2. cell proliferation Source: UniProtKB
    3. exocytosis Source: UniProtKB-KW

    Keywords - Biological processi

    Exocytosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-taxilin
    Gene namesi
    Name:TXLNA
    Synonyms:TXLN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:30685. TXLNA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: LIFEdb
    2. extracellular region Source: UniProtKB
    3. membrane Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142670668.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 546546Alpha-taxilinPRO_0000189421Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei515 – 5151Phosphoserine4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP40222.
    PaxDbiP40222.
    PeptideAtlasiP40222.
    PRIDEiP40222.

    PTM databases

    PhosphoSiteiP40222.

    Expressioni

    Tissue specificityi

    Ubiquitous, with much higher expression in heart, kidney, liver and pancreas.1 Publication

    Gene expression databases

    BgeeiP40222.
    GenevestigatoriP40222.

    Organism-specific databases

    HPAiHPA045383.

    Interactioni

    Subunit structurei

    Binds to the C-terminal coiled coil region of syntaxin family members STX1A, STX3A and STX4A, but not when these proteins are complexed with SNAP25, VAMP2 or STXBP1, suggesting that it interacts with syntaxins that do not form the SNARE complex.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Azi2Q9QYP62EBI-359793,EBI-6115874From a different organism.
    CYorf15BQ9BZA42EBI-359793,EBI-6115828
    NACAQ137652EBI-359793,EBI-712216
    TBK1Q9UHD24EBI-359793,EBI-356402
    TXLNBQ8N3L32EBI-359793,EBI-6116822

    Protein-protein interaction databases

    BioGridi128297. 24 interactions.
    DIPiDIP-27612N.
    IntActiP40222. 9 interactions.
    MINTiMINT-1150979.

    Structurei

    3D structure databases

    ProteinModelPortaliP40222.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili186 – 491306Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the taxilin family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG252790.
    HOVERGENiHBG104385.
    InParanoidiP40222.
    OMAiRKPEGAQ.
    OrthoDBiEOG70KGP6.
    PhylomeDBiP40222.
    TreeFamiTF318595.

    Family and domain databases

    InterProiIPR026183. Taxilin_fam.
    [Graphical view]
    PANTHERiPTHR16127. PTHR16127. 1 hit.
    PfamiPF09728. Taxilin. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P40222-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKNQDKKNGA AKQSNPKSSP GQPEAGPEGA QERPSQAAPA VEAEGPGSSQ    50
    APRKPEGAQA RTAQSGALRD VSEELSRQLE DILSTYCVDN NQGGPGEDGA 100
    QGEPAEPEDA EKSRTYVARN GEPEPTPVVN GEKEPSKGDP NTEEIRQSDE 150
    VGDRDHRRPQ EKKKAKGLGK EITLLMQTLN TLSTPEEKLA ALCKKYAELL 200
    EEHRNSQKQM KLLQKKQSQL VQEKDHLRGE HSKAVLARSK LESLCRELQR 250
    HNRSLKEEGV QRAREEEEKR KEVTSHFQVT LNDIQLQMEQ HNERNSKLRQ 300
    ENMELAERLK KLIEQYELRE EHIDKVFKHK DLQQQLVDAK LQQAQEMLKE 350
    AEERHQREKD FLLKEAVESQ RMCELMKQQE THLKQQLALY TEKFEEFQNT 400
    LSKSSEVFTT FKQEMEKMTK KIKKLEKETT MYRSRWESSN KALLEMAEEK 450
    TVRDKELEGL QVKIQRLEKL CRALQTERND LNKRVQDLSA GGQGSLTDSG 500
    PERRPEGPGA QAPSSPRVTE APCYPGAPST EASGQTGPQE PTSARA 546
    Length:546
    Mass (Da):61,891
    Last modified:November 9, 2004 - v3
    Checksum:i698CD74F78897DF6
    GO

    Sequence cautioni

    The sequence AAH46565.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121K → Q in CAD89951. (PubMed:17974005)Curated
    Sequence conflicti194 – 1941K → R in CAD89952. (PubMed:17974005)Curated
    Sequence conflicti228 – 2281R → C in AAH80578. (PubMed:15489334)Curated
    Sequence conflicti249 – 2502QR → HG(PubMed:8327514)Curated
    Sequence conflicti278 – 2781Q → L in CAD89952. (PubMed:17974005)Curated
    Sequence conflicti368 – 3681E → A in CAD89952. (PubMed:17974005)Curated
    Sequence conflicti412 – 4121K → E in CAD89951. (PubMed:17974005)Curated
    Sequence conflicti530 – 5301T → A in CAD91138. (PubMed:17974005)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF516206 mRNA. Translation: AAO42465.1.
    AL832636 mRNA. Translation: CAD89951.1.
    AL832637 mRNA. Translation: CAD89952.1.
    AL832338 mRNA. Translation: CAD91138.1.
    AL049795 Genomic DNA. Translation: CAI22055.1.
    CH471059 Genomic DNA. Translation: EAX07565.1.
    CH471059 Genomic DNA. Translation: EAX07566.1.
    BC029686 mRNA. Translation: AAH29686.1.
    BC046565 mRNA. Translation: AAH46565.1. Different initiation.
    BC080578 mRNA. Translation: AAH80578.1.
    BC103823 mRNA. Translation: AAI03824.1.
    BC103824 mRNA. Translation: AAI03825.1.
    L15344 mRNA. No translation available.
    CCDSiCCDS353.1.
    PIRiA48203.
    RefSeqiNP_787048.1. NM_175852.3.
    UniGeneiHs.17987.

    Genome annotation databases

    EnsembliENST00000373609; ENSP00000362711; ENSG00000084652.
    ENST00000373610; ENSP00000362712; ENSG00000084652.
    GeneIDi200081.
    KEGGihsa:200081.
    UCSCiuc001bui.3. human.

    Polymorphism databases

    DMDMi55584162.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF516206 mRNA. Translation: AAO42465.1 .
    AL832636 mRNA. Translation: CAD89951.1 .
    AL832637 mRNA. Translation: CAD89952.1 .
    AL832338 mRNA. Translation: CAD91138.1 .
    AL049795 Genomic DNA. Translation: CAI22055.1 .
    CH471059 Genomic DNA. Translation: EAX07565.1 .
    CH471059 Genomic DNA. Translation: EAX07566.1 .
    BC029686 mRNA. Translation: AAH29686.1 .
    BC046565 mRNA. Translation: AAH46565.1 . Different initiation.
    BC080578 mRNA. Translation: AAH80578.1 .
    BC103823 mRNA. Translation: AAI03824.1 .
    BC103824 mRNA. Translation: AAI03825.1 .
    L15344 mRNA. No translation available.
    CCDSi CCDS353.1.
    PIRi A48203.
    RefSeqi NP_787048.1. NM_175852.3.
    UniGenei Hs.17987.

    3D structure databases

    ProteinModelPortali P40222.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128297. 24 interactions.
    DIPi DIP-27612N.
    IntActi P40222. 9 interactions.
    MINTi MINT-1150979.

    PTM databases

    PhosphoSitei P40222.

    Polymorphism databases

    DMDMi 55584162.

    Proteomic databases

    MaxQBi P40222.
    PaxDbi P40222.
    PeptideAtlasi P40222.
    PRIDEi P40222.

    Protocols and materials databases

    DNASUi 200081.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373609 ; ENSP00000362711 ; ENSG00000084652 .
    ENST00000373610 ; ENSP00000362712 ; ENSG00000084652 .
    GeneIDi 200081.
    KEGGi hsa:200081.
    UCSCi uc001bui.3. human.

    Organism-specific databases

    CTDi 200081.
    GeneCardsi GC01P032645.
    HGNCi HGNC:30685. TXLNA.
    HPAi HPA045383.
    MIMi 608676. gene.
    neXtProti NX_P40222.
    PharmGKBi PA142670668.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG252790.
    HOVERGENi HBG104385.
    InParanoidi P40222.
    OMAi RKPEGAQ.
    OrthoDBi EOG70KGP6.
    PhylomeDBi P40222.
    TreeFami TF318595.

    Miscellaneous databases

    ChiTaRSi TXLNA. human.
    GeneWikii TXLNA.
    GenomeRNAii 200081.
    NextBioi 89822.
    PROi P40222.
    SOURCEi Search...

    Gene expression databases

    Bgeei P40222.
    Genevestigatori P40222.

    Family and domain databases

    InterProi IPR026183. Taxilin_fam.
    [Graphical view ]
    PANTHERi PTHR16127. PTHR16127. 1 hit.
    Pfami PF09728. Taxilin. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Taxilin; a novel syntaxin-binding protein that is involved in Ca2+-dependent exocytosis in neuroendocrine cells."
      Nogami S., Satoh S., Nakano M., Shimizu H., Fukushima H., Maruyama A., Terano A., Shirataki H.
      Genes Cells 8:17-28(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SYNTAXIN, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skeletal muscle and Spinal cord.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Ovary, Placenta and Uterus.
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 234-546.
    7. "Interaction of taxilin with syntaxin which does not form the SNARE complex."
      Nogami S., Satoh S., Nakano M., Terano A., Shirataki H.
      Biochem. Biophys. Res. Commun. 311:797-802(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STX1A; STX3A AND STX4A.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTXLNA_HUMAN
    AccessioniPrimary (citable) accession number: P40222
    Secondary accession number(s): D3DPP6
    , Q5TFJ6, Q66K62, Q86T54, Q86T85, Q86T86, Q86Y86, Q86YW3, Q8N2Y3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: November 9, 2004
    Last modified: October 1, 2014
    This is version 124 of the entry and version 3 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

    Caution

    Was originally thought to be a high molecular weight interleukin (IL-14 or IL14).1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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