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O14907

- TX1B3_HUMAN

UniProt

O14907 - TX1B3_HUMAN

Protein

Tax1-binding protein 3

Gene

TAX1BP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    May regulate a number of protein-protein interactions by competing for PDZ domain binding sites. Binds CTNNB1 and may thereby act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play a role in the Rho signaling pathway. May play a role in activation of CDC42 by the viral protein HPV16 E6.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein C-terminus binding Source: UniProtKB

    GO - Biological processi

    1. activation of Cdc42 GTPase activity Source: BHF-UCL
    2. negative regulation of cell proliferation Source: Ensembl
    3. negative regulation of protein localization to cell surface Source: UniProtKB
    4. negative regulation of Wnt signaling pathway Source: UniProtKB
    5. Rho protein signal transduction Source: UniProtKB
    6. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Biological processi

    Wnt signaling pathway

    Enzyme and pathway databases

    BRENDAi3.5.1.2. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tax1-binding protein 3
    Alternative name(s):
    Glutaminase-interacting protein 3
    Tax interaction protein 1
    Short name:
    TIP-1
    Tax-interacting protein 1
    Gene namesi
    Name:TAX1BP3Imported
    Synonyms:TIP1Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:30684. TAX1BP3.

    Subcellular locationi

    Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein; Cytoplasmic side
    Note: Recruited to the cell membrane by interaction with membrane proteins.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: UniProtKB-SubCell
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi20 – 201K → A: Abolishes interaction with KCNJ4. 1 Publication
    Mutagenesisi90 – 901H → A: Abolishes interaction with KCNJ4. 1 Publication

    Organism-specific databases

    PharmGKBiPA134950693.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 124123Tax1-binding protein 3PRO_0000233943Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei61 – 611Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO14907.
    PaxDbiO14907.
    PRIDEiO14907.

    2D gel databases

    UCD-2DPAGEO14907.

    PTM databases

    PhosphoSiteiO14907.

    Expressioni

    Tissue specificityi

    Ubiquitous. Detected in brain, heart, kidney, lung, small intestine and skeletal muscle. Detected in various cell lines including HeLa. Weakly expressed in peripheral blood leukocytes.2 Publications

    Gene expression databases

    BgeeiO14907.
    CleanExiHS_TAX1BP3.
    GenevestigatoriO14907.

    Interactioni

    Subunit structurei

    Interacts (via its PDZ domain) with GLS2. Interacts (via its PDZ domain) with RTKN (via the C-terminal region); this interaction facilitates Rho-mediated activation of the FOS serum response element (SRE). Interacts (via its PDZ domain) with CTNNB1; this interaction inhibits the transcriptional activity of CTNNB1. Interacts with HTLV-1 TAX protein. Interacts (via PDZ domain) with ARHGEF16. Interacts (via PDZ domain) with KCNJ4 (via C-terminus). Competes with LIN7A for KCNJ4 binding.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    E6P031262EBI-723259,EBI-1177242From a different organism.

    Protein-protein interaction databases

    BioGridi119061. 15 interactions.
    IntActiO14907. 10 interactions.
    MINTiMINT-142501.
    STRINGi9606.ENSP00000225525.

    Structurei

    Secondary structure

    1
    124
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 113
    Beta strandi12 – 198
    Beta strandi21 – 233
    Beta strandi26 – 283
    Beta strandi30 – 356
    Beta strandi37 – 393
    Helixi41 – 433
    Turni45 – 473
    Beta strandi48 – 503
    Beta strandi54 – 607
    Beta strandi62 – 643
    Helixi65 – 695
    Beta strandi76 – 805
    Beta strandi83 – 853
    Helixi90 – 978
    Beta strandi98 – 1014
    Beta strandi103 – 1119
    Beta strandi115 – 1184
    Turni121 – 1233

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KG2NMR-A2-124[»]
    2L4SNMR-A1-124[»]
    2L4TNMR-A1-124[»]
    2VZ5X-ray1.74A13-113[»]
    3GJ9X-ray2.80A/B1-124[»]
    3SFJX-ray1.24A/C10-112[»]
    4E3BX-ray1.50A/B11-112[»]
    ProteinModelPortaliO14907.
    SMRiO14907. Positions 9-112.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14907.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini15 – 11298PDZPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG236405.
    HOGENOMiHOG000015753.
    HOVERGENiHBG052814.
    InParanoidiO14907.
    OMAiDPTQNPF.
    OrthoDBiEOG7S4X7S.
    PhylomeDBiO14907.
    TreeFamiTF318964.

    Family and domain databases

    Gene3Di2.30.42.10. 1 hit.
    InterProiIPR001478. PDZ.
    IPR017268. Tax1-binding_p3.
    [Graphical view]
    PfamiPF00595. PDZ. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037712. Tax1-binding_p3. 1 hit.
    SMARTiSM00228. PDZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 1 hit.
    PROSITEiPS50106. PDZ. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O14907-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSYIPGQPVT AVVQRVEIHK LRQGENLILG FSIGGGIDQD PSQNPFSEDK    50
    TDKGIYVTRV SEGGPAEIAG LQIGDKIMQV NGWDMTMVTH DQARKRLTKR 100
    SEEVVRLLVT RQSLQKAVQQ SMLS 124
    Length:124
    Mass (Da):13,735
    Last modified:March 1, 2001 - v2
    Checksum:iFF0BCDF475F682CD
    GO

    Sequence cautioni

    The sequence AAF43104.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF028823 mRNA. Translation: AAB84248.2.
    AF168787 Genomic DNA. Translation: AAF43104.1. Different initiation.
    AF234997 mRNA. Translation: AAG44368.1.
    AF277318 mRNA. Translation: AAK69111.1.
    AK315408 mRNA. Translation: BAG37800.1.
    CH471108 Genomic DNA. Translation: EAW90491.1.
    CH471108 Genomic DNA. Translation: EAW90492.1.
    BC023980 mRNA. Translation: AAH23980.1.
    CCDSiCCDS11032.1.
    RefSeqiNP_001191627.1. NM_001204698.1.
    NP_055419.1. NM_014604.3.
    UniGeneiHs.12956.
    Hs.731607.

    Genome annotation databases

    EnsembliENST00000225525; ENSP00000225525; ENSG00000213977.
    GeneIDi30851.
    KEGGihsa:30851.
    UCSCiuc002fwc.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF028823 mRNA. Translation: AAB84248.2 .
    AF168787 Genomic DNA. Translation: AAF43104.1 . Different initiation.
    AF234997 mRNA. Translation: AAG44368.1 .
    AF277318 mRNA. Translation: AAK69111.1 .
    AK315408 mRNA. Translation: BAG37800.1 .
    CH471108 Genomic DNA. Translation: EAW90491.1 .
    CH471108 Genomic DNA. Translation: EAW90492.1 .
    BC023980 mRNA. Translation: AAH23980.1 .
    CCDSi CCDS11032.1.
    RefSeqi NP_001191627.1. NM_001204698.1.
    NP_055419.1. NM_014604.3.
    UniGenei Hs.12956.
    Hs.731607.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KG2 NMR - A 2-124 [» ]
    2L4S NMR - A 1-124 [» ]
    2L4T NMR - A 1-124 [» ]
    2VZ5 X-ray 1.74 A 13-113 [» ]
    3GJ9 X-ray 2.80 A/B 1-124 [» ]
    3SFJ X-ray 1.24 A/C 10-112 [» ]
    4E3B X-ray 1.50 A/B 11-112 [» ]
    ProteinModelPortali O14907.
    SMRi O14907. Positions 9-112.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119061. 15 interactions.
    IntActi O14907. 10 interactions.
    MINTi MINT-142501.
    STRINGi 9606.ENSP00000225525.

    PTM databases

    PhosphoSitei O14907.

    2D gel databases

    UCD-2DPAGE O14907.

    Proteomic databases

    MaxQBi O14907.
    PaxDbi O14907.
    PRIDEi O14907.

    Protocols and materials databases

    DNASUi 30851.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000225525 ; ENSP00000225525 ; ENSG00000213977 .
    GeneIDi 30851.
    KEGGi hsa:30851.
    UCSCi uc002fwc.3. human.

    Organism-specific databases

    CTDi 30851.
    GeneCardsi GC17M003566.
    HGNCi HGNC:30684. TAX1BP3.
    neXtProti NX_O14907.
    PharmGKBi PA134950693.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG236405.
    HOGENOMi HOG000015753.
    HOVERGENi HBG052814.
    InParanoidi O14907.
    OMAi DPTQNPF.
    OrthoDBi EOG7S4X7S.
    PhylomeDBi O14907.
    TreeFami TF318964.

    Enzyme and pathway databases

    BRENDAi 3.5.1.2. 2681.

    Miscellaneous databases

    ChiTaRSi TAX1BP3. human.
    EvolutionaryTracei O14907.
    GeneWikii TAX1BP3.
    GenomeRNAii 30851.
    NextBioi 52992.
    PROi O14907.

    Gene expression databases

    Bgeei O14907.
    CleanExi HS_TAX1BP3.
    Genevestigatori O14907.

    Family and domain databases

    Gene3Di 2.30.42.10. 1 hit.
    InterProi IPR001478. PDZ.
    IPR017268. Tax1-binding_p3.
    [Graphical view ]
    Pfami PF00595. PDZ. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037712. Tax1-binding_p3. 1 hit.
    SMARTi SM00228. PDZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    PROSITEi PS50106. PDZ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins."
      Rousset R., Fabre S., Desbois C., Bantignies F., Jalinot P.
      Oncogene 16:643-654(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH HTLV-1 TAX.
      Tissue: Peripheral blood lymphocyteImported.
    2. "The genomic region encompassing the nephropathic cystinosis gene (CTNS): complete sequencing of a 200-kb segment and discovery of a novel gene within the common cystinosis-causing deletion."
      Touchman J.W., Anikster Y., Dietrich N.L., Maduro V.V.B., McDowell G., Shotelersuk V., Bouffard G.G., Beckstrom-Sternberg S.M., Gahl W.A., Green E.D.
      Genome Res. 10:165-173(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The C-terminus of human glutaminase L mediates association with PDZ domain-containing proteins."
      Olalla L., Aledo J.C., Bannenberg G., Marquez J.
      FEBS Lett. 488:116-122(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GLS2.
      Tissue: BrainImported.
    4. "hPWP1-interacting proteins 2 and 11 (Tax-interacting protein 1)."
      Honore B.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: OvaryImported.
    5. "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].
      Tissue: Tongue.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: KidneyImported.
    8. "The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is involved in Rho signaling to the serum response element."
      Reynaud C., Fabre S., Jalinot P.
      J. Biol. Chem. 275:33962-33968(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RTKN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    9. Cited for: FUNCTION, INTERACTION WITH KCNJ4, MUTAGENESIS OF LYS-20 AND HIS-90, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "The HPV16 E6 binding protein Tip-1 interacts with ARHGEF16, which activates Cdc42."
      Oliver A.W., He X., Borthwick K., Donne A.J., Hampson L., Hampson I.N.
      Br. J. Cancer 104:324-331(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ARHGEF16.
    14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Solution structure of the human Tax-interacting protein-1."
      Durney M.A., Birrane G., Anklin C., Soni A., Ladias J.A.
      J. Biomol. NMR 45:329-334(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR, INTERACTION WITH KCNJ4.
    17. "Molecular mechanism of inward rectifier potassium channel 2.3 regulation by tax-interacting protein-1."
      Yan X., Zhou H., Zhang J., Shi C., Xie X., Wu Y., Tian C., Shen Y., Long J.
      J. Mol. Biol. 392:967-976(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), INTERACTION WITH KCNJ4.
    18. "The structure of the PDZ domain of TAX1BP."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 13-124.
    19. "Promiscuous binding at the crossroads of numerous cancer pathways: insight from the binding of glutaminase interacting protein with glutaminase L."
      Zoetewey D.L., Ovee M., Banerjee M., Bhaskaran R., Mohanty S.
      Biochemistry 50:3528-3539(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR IN COMPLEX WITH GLS2, INTERACTION WITH GLS2.

    Entry informationi

    Entry nameiTX1B3_HUMAN
    AccessioniPrimary (citable) accession number: O14907
    Secondary accession number(s): B2RD53, D3DTJ6, Q7LCQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2006
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 114 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3