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Protein

Tubulin polyglutamylase TTLL6

Gene

Ttll6

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

Functioni

Polyglutamylase which preferentially modifies alpha-tubulin (PubMed:17499049, PubMed:21074048). Mediates tubulin polyglutamylation in cilia (PubMed:22246503). Involved in the side-chain elongation step of the polyglutamylation reaction rather than in the initiation step (PubMed:17499049, PubMed:21074048). Generates long side-chains (PubMed:20530212). Generates polyglutamylation of CGAS/MB21D1, leading to impair the DNA-binding activity of CGAS/MB21D1 (PubMed:26829768).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei215 – 2151ATPBy similarity
Binding sitei217 – 2171ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi202 – 2054ATP bindingBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ligase activity Source: UniProtKB-KW
  • tubulin binding Source: UniProtKB

GO - Biological processi

  • microtubule bundle formation Source: MGI
  • microtubule severing Source: MGI
  • positive regulation of cilium movement Source: MGI
  • protein polyglutamylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin polyglutamylase TTLL6 (EC:6.-.-.-)
Alternative name(s):
Tubulin--tyrosine ligase-like protein 6
Gene namesi
Name:Ttll6Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2683461. Ttll6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 822822Tubulin polyglutamylase TTLL6PRO_0000326161Add
BLAST

Proteomic databases

PaxDbiA4Q9E8.
PRIDEiA4Q9E8.

PTM databases

iPTMnetiA4Q9E8.
PhosphoSiteiA4Q9E8.

Expressioni

Tissue specificityi

Widely expressed with highest levels in testis.1 Publication

Gene expression databases

BgeeiA4Q9E8.
CleanExiMM_TTLL6.
GenevisibleiA4Q9E8. MM.

Interactioni

Subunit structurei

Found in a complex with CEP41.By similarity

GO - Molecular functioni

  • tubulin binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000127778.

Structurei

3D structure databases

ProteinModelPortaliA4Q9E8.
SMRiA4Q9E8. Positions 60-390.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 400344TTLPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni371 – 45080c-MTBD regionBy similarityAdd
BLAST

Domaini

The flexible c-MTBD (cationic microtubule binding domain) region mediates binding to microtubules. It is positively charged and becomes ordered when bound to microtubules: it interacts with a negatively charged patch on 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.
GeneTreeiENSGT00760000118951.
HOGENOMiHOG000060129.
HOVERGENiHBG108618.
InParanoidiA4Q9E8.
KOiK16582.
OMAiKMFPKDF.
OrthoDBiEOG7RJPQT.
PhylomeDBiA4Q9E8.
TreeFamiTF313087.

Family and domain databases

InterProiIPR004344. TTL/TTLL_fam.
IPR027754. TTLL6.
[Graphical view]
PANTHERiPTHR12241:SF96. PTHR12241:SF96. 1 hit.
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: A4Q9E8-1) [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
MLQCLTSESE EGAEEREESS TEDLEELKEF VTLAFVRENT QKRLQNAQQH
60 70 80 90 100
GKKKRKKKRL VINLSNCRYD SVRRAAQQYG LREAGDNDDW TLYWTDYSVS
110 120 130 140 150
LERVMEMKSY QKINHFPGMS EICRKDLLAR NMSRMLKLFP KDFHFFPRTW
160 170 180 190 200
CLPADWGDLQ TYSRTRKNKT YICKPDSGCQ GRGIFITRSV KEIKPGEDMI
210 220 230 240 250
CQLYISKPFI IDGFKFDLRV YVLVTSCDPL RVFVYNEGLA RFATTSYSHP
260 270 280 290 300
NLDNLDEICM HLTNYSINKH SSNFVQDAFS GSKRKLSTFN SYMKTHGYDV
310 320 330 340 350
EQIWRGIEDV IIKTLISAHP VIKHNYHTCF PSHTLNSACF EILGFDILLD
360 370 380 390 400
RKLKPWLLEV NHSPSFSTDS KLDKEVKDSL LYDALVLINL GNCDKKKVLE
410 420 430 440 450
EERQRGRFLQ QCPNREIRLE EVKGFQAMRL QKTEEYEKKN CGGFRLIYPG
460 470 480 490 500
LNLEKYDKFF QDNSSLFQNT VASRARELYA RQLIQELRQK QEKKVFLKKA
510 520 530 540 550
RKEETQGESA GEQARDKVVR LQRQRQQPKC KTVATCPPKQ SLHPVTLVSC
560 570 580 590 600
TSGLLLNIRG LKKGEISESL EQKDTKEAML IPCKPVSARN YSSVPDLRSA
610 620 630 640 650
NPSCFEPEFH VPNAKVKEVK SAFMVNIEST AQPITSVESS RDATAPISTS
660 670 680 690 700
LESLASMSLS TSPECSSPES VHMVSYNHKQ QKASFHKPMQ EKKSKPLMFS
710 720 730 740 750
KSRHLDLNCT SMKNDINRQY LMSEILQKVQ MKKKRPLFPA PKSQYPTLSK
760 770 780 790 800
ERCPHSRSSS RKKEMNSPSV FVLQASHSRA ESLNDLLVVA TQARLDPRPS
810 820
RSHSGTTTRD SSTQDPKHTA TA
Length:822
Mass (Da):94,507
Last modified:May 15, 2007 - v1
Checksum:iC262476CB0A937A1
GO
Isoform 22 Publications (identifier: A4Q9E8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-104: Missing.

Show »
Length:718
Mass (Da):82,249
Checksum:i613982821316FB4A
GO

Sequence cautioni

The sequence BAC36577.1 differs from that shown. Reason: Frameshift at position 156. Curated
The sequence CAM18274.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1951P → A in BAC36577 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 104104Missing in isoform 2. 2 PublicationsVSP_052729Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM690749 mRNA. Translation: CAM84326.1.
AK077033 mRNA. Translation: BAC36577.1. Frameshift.
AK145771 mRNA. Translation: BAE26641.1.
AL603682 Genomic DNA. Translation: CAM18273.1.
AL603682 Genomic DNA. Translation: CAM18274.1. Sequence problems.
BC132203 mRNA. Translation: AAI32204.1.
BC138058 mRNA. Translation: AAI38059.1.
BC145131 mRNA. Translation: AAI45132.1.
CCDSiCCDS25290.2. [A4Q9E8-1]
RefSeqiNP_766387.2. NM_172799.4. [A4Q9E8-1]
UniGeneiMm.249912.

Genome annotation databases

EnsembliENSMUST00000107680; ENSMUSP00000103307; ENSMUSG00000038756. [A4Q9E8-2]
ENSMUST00000167258; ENSMUSP00000127778; ENSMUSG00000038756. [A4Q9E8-1]
GeneIDi237930.
KEGGimmu:237930.
UCSCiuc011ydd.1. mouse. [A4Q9E8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM690749 mRNA. Translation: CAM84326.1.
AK077033 mRNA. Translation: BAC36577.1. Frameshift.
AK145771 mRNA. Translation: BAE26641.1.
AL603682 Genomic DNA. Translation: CAM18273.1.
AL603682 Genomic DNA. Translation: CAM18274.1. Sequence problems.
BC132203 mRNA. Translation: AAI32204.1.
BC138058 mRNA. Translation: AAI38059.1.
BC145131 mRNA. Translation: AAI45132.1.
CCDSiCCDS25290.2. [A4Q9E8-1]
RefSeqiNP_766387.2. NM_172799.4. [A4Q9E8-1]
UniGeneiMm.249912.

3D structure databases

ProteinModelPortaliA4Q9E8.
SMRiA4Q9E8. Positions 60-390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000127778.

PTM databases

iPTMnetiA4Q9E8.
PhosphoSiteiA4Q9E8.

Proteomic databases

PaxDbiA4Q9E8.
PRIDEiA4Q9E8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000107680; ENSMUSP00000103307; ENSMUSG00000038756. [A4Q9E8-2]
ENSMUST00000167258; ENSMUSP00000127778; ENSMUSG00000038756. [A4Q9E8-1]
GeneIDi237930.
KEGGimmu:237930.
UCSCiuc011ydd.1. mouse. [A4Q9E8-1]

Organism-specific databases

CTDi284076.
MGIiMGI:2683461. Ttll6.

Phylogenomic databases

eggNOGiKOG2158. Eukaryota.
ENOG410XNWC. LUCA.
GeneTreeiENSGT00760000118951.
HOGENOMiHOG000060129.
HOVERGENiHBG108618.
InParanoidiA4Q9E8.
KOiK16582.
OMAiKMFPKDF.
OrthoDBiEOG7RJPQT.
PhylomeDBiA4Q9E8.
TreeFamiTF313087.

Miscellaneous databases

NextBioi383582.
PROiA4Q9E8.
SOURCEiSearch...

Gene expression databases

BgeeiA4Q9E8.
CleanExiMM_TTLL6.
GenevisibleiA4Q9E8. MM.

Family and domain databases

InterProiIPR004344. TTL/TTLL_fam.
IPR027754. TTLL6.
[Graphical view]
PANTHERiPTHR12241:SF96. PTHR12241:SF96. 1 hit.
PfamiPF03133. TTL. 1 hit.
[Graphical view]
PROSITEiPS51221. TTL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A targeted multienzyme mechanism for selective microtubule polyglutamylation."
    van Dijk J., Rogowski K., Miro J., Lacroix B., Edde B., Janke C.
    Mol. Cell 26:437-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: C57BL/6JImported.
    Tissue: TestisImported.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6JImported.
    Tissue: BlastocystImported and TestisImported.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] (ISOFORM 2).
    Tissue: BrainImported.
  5. Cited for: FUNCTION.
  6. "Tubulin polyglutamylation stimulates spastin-mediated microtubule severing."
    Lacroix B., van Dijk J., Gold N.D., Guizetti J., Aldrian-Herrada G., Rogowski K., Gerlich D.W., Janke C.
    J. Cell Biol. 189:945-954(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: SUBCELLULAR LOCATION, FUNCTION.
  8. "Glutamylation of the DNA sensor cGAS regulates its binding and synthase activity in antiviral immunity."
    Xia P., Ye B., Wang S., Zhu X., Du Y., Xiong Z., Tian Y., Fan Z.
    Nat. Immunol. 17:369-378(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiTTLL6_MOUSE
AccessioniPrimary (citable) accession number: A4Q9E8
Secondary accession number(s): A2A6M6
, B2RQS4, Q3UL10, Q8BVQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 15, 2007
Last modified: May 11, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.