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Protein

Tubulin polyglutamylase TTLL7

Gene

TTLL7

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

Functioni

Polyglutamylase which preferentially modifies beta-tubulin (PubMed:25959773). Mediates both ATP-dependent initiation and elongation of polyglutamylation of microtubules (PubMed:25959773). Required for neurite growth; responsible for the strong increase in tubulin polyglutamylation during postnatal neuronal maturation (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei106 – 1061Binds negatively charged residues of beta-tubulin C-terminal tails1 Publication
Binding sitei201 – 2011ATP1 Publication
Binding sitei203 – 2031ATP1 Publication
Sitei352 – 3521Binds negatively charged residues of beta-tubulin C-terminal tails1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi188 – 1914ATP binding1 Publication

GO - Molecular functioni

  • alpha-tubulin binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • beta-tubulin binding Source: UniProtKB
  • tubulin-glutamic acid ligase activity Source: UniProtKB

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):
Testis development protein NYD-SP301 Publication
Tubulin--tyrosine ligase-like protein 7Curated
Gene namesi
Name:TTLL7Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:26242. TTLL7.

Subcellular locationi

  • Cell projectioncilium By similarity
  • Cytoplasmcytoskeletoncilium basal body By similarity
  • Cell projectiondendrite By similarity
  • Perikaryon By similarity

  • Note: In cells with primary cilia, found in both cilia and basal bodies. In neuronal cells, found in dendrites and perikaryon.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi106 – 1061R → E: Nearly abolished polyglutamylase activity. 1 Publication
Mutagenesisi143 – 1464NYVK → EYVE: 70% decreased polyglutamylase activity. 1 Publication
Mutagenesisi178 – 1781K → E: Decreased polyglutamylase activity. 1 Publication
Mutagenesisi205 – 2051R → E: Nearly abolished polyglutamylase activity. 1 Publication
Mutagenesisi227 – 2271R → E: Nearly abolished polyglutamylase activity. 1 Publication
Mutagenesisi271 – 2711K → E: Nearly abolished polyglutamylase activity. 1 Publication
Mutagenesisi349 – 3491E → Q: Loss of polyglutamylase activity. 1 Publication
Mutagenesisi352 – 3521R → A or E: Nearly abolished polyglutamylase activity. 1 Publication
Mutagenesisi385 – 3939KRRNLAKQK → EEENLAEQE: 45% decreased binding to microtubules. Decreased polyglutamylase activity. 76% decreased binding to microtubules; when associated with 425-E--E-427. 1 Publication
Mutagenesisi425 – 4273RRK → EEE: 76% decreased binding to microtubules; when associated with 385-E--E-393. 1 Publication
Mutagenesisi477 – 4804FQTF → AQTA: 40% decreased polyglutamylase activity. 1 Publication
Mutagenesisi490 – 50011RELNNPLKRMK → DELNNPLDDMD: 69% decreased polyglutamylase activity. 1 PublicationAdd
BLAST

Organism-specific databases

PharmGKBiPA142670678.

Polymorphism and mutation databases

BioMutaiTTLL7.
DMDMi73920151.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 887887Tubulin polyglutamylase TTLL7PRO_0000212444Add
BLAST

Proteomic databases

EPDiQ6ZT98.
PaxDbiQ6ZT98.
PeptideAtlasiQ6ZT98.
PRIDEiQ6ZT98.
TopDownProteomicsiQ6ZT98-2. [Q6ZT98-2]

PTM databases

iPTMnetiQ6ZT98.
PhosphoSiteiQ6ZT98.

Expressioni

Tissue specificityi

Highly expressed in the nervous system including spinal cord, thalamus, hippocampus, hypothalamus and cerebellum.1 Publication

Gene expression databases

BgeeiENSG00000137941.
CleanExiHS_TTLL7.
ExpressionAtlasiQ6ZT98. baseline and differential.
GenevisibleiQ6ZT98. HS.

Organism-specific databases

HPAiHPA052249.
HPA059321.

Interactioni

Subunit structurei

Interacts with both alpha- and beta-tubulin (via C-terminal tubulin tails).1 Publication

GO - Molecular functioni

  • alpha-tubulin binding Source: UniProtKB
  • beta-tubulin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122852. 7 interactions.
IntActiQ6ZT98. 2 interactions.
STRINGi9606.ENSP00000260505.

Structurei

Secondary structure

1
887
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 476Combined sources
Helixi51 – 6010Combined sources
Beta strandi73 – 797Combined sources
Helixi83 – 875Combined sources
Beta strandi94 – 963Combined sources
Turni99 – 1013Combined sources
Helixi102 – 1054Combined sources
Helixi107 – 11812Combined sources
Turni122 – 1243Combined sources
Beta strandi131 – 1333Combined sources
Turni134 – 1363Combined sources
Helixi138 – 15013Combined sources
Beta strandi157 – 1604Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi186 – 1894Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi196 – 1994Combined sources
Beta strandi201 – 21212Combined sources
Turni213 – 2164Combined sources
Beta strandi217 – 22812Combined sources
Beta strandi271 – 2733Combined sources
Helixi274 – 28310Combined sources
Helixi288 – 31730Combined sources
Beta strandi331 – 34010Combined sources
Beta strandi345 – 3539Combined sources
Helixi361 – 37818Combined sources
Beta strandi454 – 4596Combined sources
Helixi463 – 48321Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YLRX-ray2.55A36-518[»]
4YLSX-ray2.60A36-518[»]
ProteinModelPortaliQ6ZT98.
SMRiQ6ZT98. Positions 40-389, 449-484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 390353TTLPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni388 – 45063c-MTBD region1 PublicationAdd
BLAST

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.1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2158. Eukaryota.
ENOG410XNWC. LUCA.
GeneTreeiENSGT00760000118951.
HOGENOMiHOG000045569.
HOVERGENiHBG073374.
InParanoidiQ6ZT98.
KOiK16583.
OMAiEDIMDNW.
OrthoDBiEOG091G01RO.
PhylomeDBiQ6ZT98.
TreeFamiTF313087.

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6ZT98-1) [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
MPSLPQEGVI QGPSPLDLNT ELPYQSTMKR KVRKKKKKGT ITANVAGTKF
60 70 80 90 100
EIVRLVIDEM GFMKTPDEDE TSNLIWCDSA VQQEKISELQ NYQRINHFPG
110 120 130 140 150
MGEICRKDFL ARNMTKMIKS RPLDYTFVPR TWIFPAEYTQ FQNYVKELKK
160 170 180 190 200
KRKQKTFIVK PANGAMGHGI SLIRNGDKLP SQDHLIVQEY IEKPFLMEGY
210 220 230 240 250
KFDLRIYILV TSCDPLKIFL YHDGLVRMGT EKYIPPNESN LTQLYMHLTN
260 270 280 290 300
YSVNKHNEHF ERDETENKGS KRSIKWFTEF LQANQHDVAK FWSDISELVV
310 320 330 340 350
KTLIVAEPHV LHAYRMCRPG QPPGSESVCF EVLGFDILLD RKLKPWLLEI
360 370 380 390 400
NRAPSFGTDQ KIDYDVKRGV LLNALKLLNI RTSDKRRNLA KQKAEAQRRL
410 420 430 440 450
YGQNSIKRLL PGSSDWEQQR HQLERRKEEL KERLAQVRKQ ISREEHENRH
460 470 480 490 500
MGNYRRIYPP EDKALLEKYE NLLAVAFQTF LSGRAASFQR ELNNPLKRMK
510 520 530 540 550
EEDILDLLEQ CEIDDEKLMG KTTKTRGPKP LCSMPESTEI MKRPKYCSSD
560 570 580 590 600
SSYDSSSSSS ESDENEKEEY QNKKREKQVT YNLKPSNHYK LIQQPSSIRR
610 620 630 640 650
SVSCPRSISA QSPSSGDTRP FSAQQMISVS RPTSASRSHS LNRASSYMRH
660 670 680 690 700
LPHSNDACST NSQVSESLRQ LKTKEQEDDL TSQTLFVLKD MKIRFPGKSD
710 720 730 740 750
AESELLIEDI IDNWKYHKTK VASYWLIKLD SVKQRKVLDI VKTSIRTVLP
760 770 780 790 800
RIWKVPDVEE VNLYRIFNRV FNRLLWSRGQ GLWNCFCDSG SSWESIFNKS
810 820 830 840 850
PEVVTPLQLQ CCQRLVELCK QCLLVVYKYA TDKRGSLSGI GPDWGNSRYL
860 870 880
LPGSTQFFLR TPTYNLKYNS PGMTRSNVLF TSRYGHL
Length:887
Mass (Da):102,999
Last modified:August 30, 2005 - v2
Checksum:i881C46437FB385EA
GO
Isoform 2 (identifier: Q6ZT98-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     665-669: SESLR → IILAQ
     670-887: Missing.

Show »
Length:669
Mass (Da):77,555
Checksum:iD7A4167627FA53EB
GO
Isoform 3 (identifier: Q6ZT98-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     791-792: SS → YV
     793-887: Missing.

Show »
Length:792
Mass (Da):92,222
Checksum:i62CB99ABC6EB205F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131P → S in AAO37763 (Ref. 1) Curated
Sequence conflicti48 – 481T → A in BAC86695 (PubMed:14702039).Curated
Sequence conflicti298 – 2981L → M in AAH60878 (PubMed:15489334).Curated
Sequence conflicti489 – 4891Q → R in AAH60878 (PubMed:15489334).Curated
Sequence conflicti493 – 4931N → D in AAH60878 (PubMed:15489334).Curated
Sequence conflicti575 – 5751R → G in AAH60878 (PubMed:15489334).Curated
Sequence conflicti609 – 6091S → F in BAB15526 (PubMed:14702039).Curated
Sequence conflicti677 – 6771E → G in AAH60878 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei665 – 6695SESLR → IILAQ in isoform 2. 1 PublicationVSP_015199
Alternative sequencei670 – 887218Missing in isoform 2. 1 PublicationVSP_015200Add
BLAST
Alternative sequencei791 – 7922SS → YV in isoform 3. 1 PublicationVSP_015201
Alternative sequencei793 – 88795Missing in isoform 3. 1 PublicationVSP_015202Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY170843 mRNA. Translation: AAO37763.1.
AK026686 mRNA. Translation: BAB15526.1.
AK126792 mRNA. Translation: BAC86695.1.
AL138844, AC104454 Genomic DNA. Translation: CAI22725.1.
BC060878 mRNA. Translation: AAH60878.1.
CCDSiCCDS690.2. [Q6ZT98-1]
RefSeqiNP_078962.4. NM_024686.4. [Q6ZT98-1]
UniGeneiHs.445826.

Genome annotation databases

EnsembliENST00000260505; ENSP00000260505; ENSG00000137941. [Q6ZT98-1]
ENST00000480174; ENSP00000435334; ENSG00000137941. [Q6ZT98-2]
GeneIDi79739.
KEGGihsa:79739.
UCSCiuc001djc.4. human. [Q6ZT98-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY170843 mRNA. Translation: AAO37763.1.
AK026686 mRNA. Translation: BAB15526.1.
AK126792 mRNA. Translation: BAC86695.1.
AL138844, AC104454 Genomic DNA. Translation: CAI22725.1.
BC060878 mRNA. Translation: AAH60878.1.
CCDSiCCDS690.2. [Q6ZT98-1]
RefSeqiNP_078962.4. NM_024686.4. [Q6ZT98-1]
UniGeneiHs.445826.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YLRX-ray2.55A36-518[»]
4YLSX-ray2.60A36-518[»]
ProteinModelPortaliQ6ZT98.
SMRiQ6ZT98. Positions 40-389, 449-484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122852. 7 interactions.
IntActiQ6ZT98. 2 interactions.
STRINGi9606.ENSP00000260505.

PTM databases

iPTMnetiQ6ZT98.
PhosphoSiteiQ6ZT98.

Polymorphism and mutation databases

BioMutaiTTLL7.
DMDMi73920151.

Proteomic databases

EPDiQ6ZT98.
PaxDbiQ6ZT98.
PeptideAtlasiQ6ZT98.
PRIDEiQ6ZT98.
TopDownProteomicsiQ6ZT98-2. [Q6ZT98-2]

Protocols and materials databases

DNASUi79739.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260505; ENSP00000260505; ENSG00000137941. [Q6ZT98-1]
ENST00000480174; ENSP00000435334; ENSG00000137941. [Q6ZT98-2]
GeneIDi79739.
KEGGihsa:79739.
UCSCiuc001djc.4. human. [Q6ZT98-1]

Organism-specific databases

CTDi79739.
GeneCardsiTTLL7.
H-InvDBHIX0000729.
HGNCiHGNC:26242. TTLL7.
HPAiHPA052249.
HPA059321.
neXtProtiNX_Q6ZT98.
PharmGKBiPA142670678.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2158. Eukaryota.
ENOG410XNWC. LUCA.
GeneTreeiENSGT00760000118951.
HOGENOMiHOG000045569.
HOVERGENiHBG073374.
InParanoidiQ6ZT98.
KOiK16583.
OMAiEDIMDNW.
OrthoDBiEOG091G01RO.
PhylomeDBiQ6ZT98.
TreeFamiTF313087.

Miscellaneous databases

GenomeRNAii79739.
PROiQ6ZT98.

Gene expression databases

BgeeiENSG00000137941.
CleanExiHS_TTLL7.
ExpressionAtlasiQ6ZT98. baseline and differential.
GenevisibleiQ6ZT98. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q6ZT98
Secondary accession number(s): Q5TAX8
, Q5TAX9, Q6P990, Q86YS1, Q9H5U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: September 7, 2016
This is version 106 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 1
    Human chromosome 1: 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

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.