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Protein

Tubulin polyglutamylase TTLL7

Gene

Ttll7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Polyglutamylase which preferentially modifies beta-tubulin (PubMed:16901895, PubMed:17499049, PubMed:19152315). Mediates both ATP-dependent initiation and elongation of polyglutamylation of microtubules (PubMed:16901895, PubMed:19152315). Required for neurite growth; responsible for the strong increase in tubulin polyglutamylation during postnatal neuronal maturation (PubMed:16901895).3 Publications

Kineticsi

  1. KM=20.2 µM for Glu (with 17 µM of tubulin for adult mouse)1 Publication
  2. KM=19.1 µM for ATP (with 17 µM of tubulin for adult mouse)1 Publication
  3. KM=19.6 µM for Glu (with 17 µM of tubulin for newborn mouse)1 Publication
  4. KM=26.5 µM for ATP (with 17 µM of tubulin for newborn mouse)1 Publication
  5. KM=5.4 µM for Glu (with 50 µM of ATP for adult mouse)1 Publication
  6. KM=21.8 µM for tubulin (with 50 µM of ATP for adult mouse)1 Publication
  7. KM=4.4 µM for Glu (with 50 µM of ATP for newborn mouse)1 Publication
  8. KM=15.8 µM for tubulin (with 50 µM of ATP for newborn mouse)1 Publication
  9. KM=7.5 µM for ATP (with 6 µM of Glu for adult mouse)1 Publication
  10. KM=3.1 µM for tubulin (with 6 µM of Glu for adult mouse)1 Publication
  11. KM=16 µM for ATP (with 6 µM of Glu for newborn mouse)1 Publication
  12. KM=6.7 µM for tubulin (with 6 µM of Glu for newborn mouse)1 Publication

    pH dependencei

    Optimum pH is 7.0.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei106Binds negatively charged residues of beta-tubulin C-terminal tailsBy similarity1
    Binding sitei201ATPBy similarity1
    Binding sitei203ATPBy similarity1
    Sitei352Binds negatively charged residues of beta-tubulin C-terminal tailsBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi188 – 191ATP bindingBy similarity4

    GO - Molecular functioni

    GO - Biological processi

    • cell differentiation Source: UniProtKB-KW
    • nervous system development Source: UniProtKB-KW
    • protein polyglutamylation Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Developmental protein, Ligase

    Keywords - Biological processi

    Differentiation, Neurogenesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tubulin polyglutamylase TTLL7Curated (EC:6.-.-.-1 Publication)
    Alternative name(s):
    Tubulin--tyrosine ligase-like protein 7Curated
    Short name:
    mTTLL71 Publication
    Gene namesi
    Name:Ttll7Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Unplaced

    Organism-specific databases

    MGIiMGI:1918142. Ttll7.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cell projection, Cilium, Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi349E → V: Loss of activity. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL2401604.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003261631 – 912Tubulin polyglutamylase TTLL7Add BLAST912

    Proteomic databases

    PaxDbiA4Q9F0.
    PRIDEiA4Q9F0.

    PTM databases

    iPTMnetiA4Q9F0.
    PhosphoSitePlusiA4Q9F0.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels in brain, testis and trachea. In brain, highly expressed in hippocampus, thalamus, olfactory bulb and cerebellum.2 Publications

    Gene expression databases

    BgeeiENSMUSG00000036745.
    CleanExiMM_TTLL7.

    Interactioni

    Subunit structurei

    Interacts with both alpha- and beta-tubulin (via C-terminal tubulin tails).By similarity

    GO - Molecular functioni

    Protein-protein interaction databases

    IntActiA4Q9F0. 10 interactors.
    STRINGi10090.ENSMUSP00000129369.

    Chemistry databases

    BindingDBiA4Q9F0.

    Structurei

    3D structure databases

    ProteinModelPortaliA4Q9F0.
    SMRiA4Q9F0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini38 – 390TTLPROSITE-ProRule annotationAdd BLAST353

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni388 – 450c-MTBD regionBy similarityAdd BLAST63

    Domaini

    The enzyme uses its core to engage the disordered anionic tails of alpha- and beta-tubulin and the flexible c-MTBD (cationic microtubule binding domain) region to bind the microtubule and position itself for beta-tail modification. The c-MTBD region is positively charged and becomes ordered when bound to microtubules: it interacts with a negatively charged patch on alpha-tubulin. The presence of positive charges in the c-MTBD region is essential for proper binding.By similarity

    Sequence similaritiesi

    Belongs to the tubulin--tyrosine ligase family.Sequence analysis
    Contains 1 TTL domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiKOG2158. Eukaryota.
    ENOG410XNWC. LUCA.
    HOGENOMiHOG000045569.
    HOVERGENiHBG073374.
    InParanoidiA4Q9F0.
    KOiK16583.

    Family and domain databases

    InterProiIPR004344. TTL/TTLL_fam.
    [Graphical view]
    PfamiPF03133. TTL. 1 hit.
    [Graphical view]
    PROSITEiPS51221. TTL. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 11 Publication (identifier: A4Q9F0-1) [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

            10         20         30         40         50
    MPSLPQDGVI QGSSPVDLGT ELPYQCTMKR KVRKKKKKGI ITANVAGTKF
    60 70 80 90 100
    EIVRLVIDEM GFMKTPDEDE TSNLIWCDAA VQQEKITDLQ NYQRINHFPG
    110 120 130 140 150
    MGEICRKDFL ARNMTKMIKS RPMDYTFVPR TWIFPSEYTQ FQNYVKELKK
    160 170 180 190 200
    KRKQKTFIVK PANGAMGHGI SLIRNGDKVP SQDHLIVQEY IEKPFLMEGY
    210 220 230 240 250
    KFDLRIYILV TSCDPLKIFL YHDGLVRMGT EKYIPPNESN LTQLYMHLTN
    260 270 280 290 300
    YSVNKHNERF ERNETEDKGS KRSIKWFTEF LQANQHDVTK FWSDISELVV
    310 320 330 340 350
    KTLIVAEPHV LHAYRMCRPG QPPGSESVCF EVLGFDILLD RKLKPWLLEI
    360 370 380 390 400
    NRAPSFGTDQ KIDYDVKRGV LLNALKLLNI RTSDKRKNLA KQKAEAQRRL
    410 420 430 440 450
    YGQNPVRRLS PGSSDWEQQR HQLERRKEEL KERLLQVRKQ VSQEEHENRH
    460 470 480 490 500
    MGNYRRIYPP EDKALLEKYE GLLAVAFQTF LSGRAASFQR EMNNPLKKMR
    510 520 530 540 550
    EEDLLDLLEQ CEIDDEKLMG KTGRVRGPKP LCCMPECAEV TKKQKYYGSS
    560 570 580 590 600
    DSSYDSSSSS SNSELDENEK ELCQKRLDQV PYSLKHTSHC KIIQQPSGSH
    610 620 630 640 650
    NLIYSESPVY LTTLVFLSEF PDSMRRSVSC PRSISAHLPS RGDVRPFSSQ
    660 670 680 690 700
    QVIPLARPTS ASRSHSLNRA SSYARHLPHG SDTGSTNTLN ESLRQLKTKE
    710 720 730 740 750
    QEDDLTSQTL FVLKDMRIRF PGKSDAESEL LIEDIMDNWK HYKTKVASYW
    760 770 780 790 800
    LIKLDSVKQR KVLDIVKSSI RTVLPRIWRV PDAEELSLYR IFNRVFNRLL
    810 820 830 840 850
    WSHGQGLWSC FCDSGSSWES IFSKSPEVVT PLQLQCCQRL VELCKQCLLV
    860 870 880 890 900
    VYKYTTETRG PISGIGPDWG NSRYLLPGST QFLMRSPLYN MKYNSPGMTR
    910
    SNVLFTSRYG RL
    Length:912
    Mass (Da):105,501
    Last modified:May 15, 2007 - v1
    Checksum:iABCDD119BFF29336
    GO
    Isoform 21 Publication (identifier: A4Q9F0-2) [UniParc]FASTAAdd to basket
    Also known as: TTLL7S1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         596-609: PSGSHNLIYSESPV → SSKSISPTSLEEEL
         610-912: Missing.

    Note: May be due to an intron retention.
    Show »
    Length:609
    Mass (Da):70,782
    Checksum:iA63B6BB06FCBFD56
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti98F → Y in BAB29613 (PubMed:16141072).Curated1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_052730596 – 609PSGSH…SESPV → SSKSISPTSLEEEL in isoform 2. 2 PublicationsAdd BLAST14
    Alternative sequenceiVSP_052731610 – 912Missing in isoform 2. 2 PublicationsAdd BLAST303

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AM690750 mRNA. Translation: CAM84327.1.
    AM690751 mRNA. Translation: CAM84328.1.
    AK014905 mRNA. Translation: BAB29613.1.
    AK083236 mRNA. Translation: BAC38821.1.
    CCDSiCCDS51094.2. [A4Q9F0-1]
    RefSeqiNP_001289886.1. NM_001302957.1.
    NP_001289887.1. NM_001302958.1. [A4Q9F0-2]
    UniGeneiMm.187793.
    Mm.401404.

    Genome annotation databases

    GeneIDi70892.
    KEGGimmu:70892.
    UCSCiuc008rrw.2. mouse. [A4Q9F0-2]
    uc008rrx.2. mouse. [A4Q9F0-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AM690750 mRNA. Translation: CAM84327.1.
    AM690751 mRNA. Translation: CAM84328.1.
    AK014905 mRNA. Translation: BAB29613.1.
    AK083236 mRNA. Translation: BAC38821.1.
    CCDSiCCDS51094.2. [A4Q9F0-1]
    RefSeqiNP_001289886.1. NM_001302957.1.
    NP_001289887.1. NM_001302958.1. [A4Q9F0-2]
    UniGeneiMm.187793.
    Mm.401404.

    3D structure databases

    ProteinModelPortaliA4Q9F0.
    SMRiA4Q9F0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiA4Q9F0. 10 interactors.
    STRINGi10090.ENSMUSP00000129369.

    Chemistry databases

    BindingDBiA4Q9F0.
    ChEMBLiCHEMBL2401604.

    PTM databases

    iPTMnetiA4Q9F0.
    PhosphoSitePlusiA4Q9F0.

    Proteomic databases

    PaxDbiA4Q9F0.
    PRIDEiA4Q9F0.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi70892.
    KEGGimmu:70892.
    UCSCiuc008rrw.2. mouse. [A4Q9F0-2]
    uc008rrx.2. mouse. [A4Q9F0-1]

    Organism-specific databases

    CTDi79739.
    MGIiMGI:1918142. Ttll7.

    Phylogenomic databases

    eggNOGiKOG2158. Eukaryota.
    ENOG410XNWC. LUCA.
    HOGENOMiHOG000045569.
    HOVERGENiHBG073374.
    InParanoidiA4Q9F0.
    KOiK16583.

    Miscellaneous databases

    PROiA4Q9F0.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSMUSG00000036745.
    CleanExiMM_TTLL7.

    Family and domain databases

    InterProiIPR004344. TTL/TTLL_fam.
    [Graphical view]
    PfamiPF03133. TTL. 1 hit.
    [Graphical view]
    PROSITEiPS51221. TTL. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiTTLL7_MOUSE
    AccessioniPrimary (citable) accession number: A4Q9F0
    Secondary accession number(s): A4Q9E9, Q8C417, Q9D5V3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: May 15, 2007
    Last modified: November 2, 2016
    This is version 74 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    Was initially though to be involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step (PubMed:17499049). However, it was later shown to be involved in both steps (PubMed:19152315).2 Publications

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    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 one 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.