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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)DescriptionActionsGraphical viewLength
Sitei106Binds negatively charged residues of beta-tubulin C-terminal tails1 Publication1
Binding sitei201ATP1 Publication1
Binding sitei203ATP1 Publication1
Sitei352Binds negatively charged residues of beta-tubulin C-terminal tails1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi188 – 191ATP binding1 Publication4

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)DescriptionActionsGraphical viewLength
Mutagenesisi106R → E: Nearly abolished polyglutamylase activity. 1 Publication1
Mutagenesisi143 – 146NYVK → EYVE: 70% decreased polyglutamylase activity. 1 Publication4
Mutagenesisi178K → E: Decreased polyglutamylase activity. 1 Publication1
Mutagenesisi205R → E: Nearly abolished polyglutamylase activity. 1 Publication1
Mutagenesisi227R → E: Nearly abolished polyglutamylase activity. 1 Publication1
Mutagenesisi271K → E: Nearly abolished polyglutamylase activity. 1 Publication1
Mutagenesisi349E → Q: Loss of polyglutamylase activity. 1 Publication1
Mutagenesisi352R → A or E: Nearly abolished polyglutamylase activity. 1 Publication1
Mutagenesisi385 – 393KRRNLAKQK → EEENLAEQE: 45% decreased binding to microtubules. Decreased polyglutamylase activity. 76% decreased binding to microtubules; when associated with 425-E--E-427. 1 Publication9
Mutagenesisi425 – 427RRK → EEE: 76% decreased binding to microtubules; when associated with 385-E--E-393. 1 Publication3
Mutagenesisi477 – 480FQTF → AQTA: 40% decreased polyglutamylase activity. 1 Publication4
Mutagenesisi490 – 500RELNNPLKRMK → DELNNPLDDMD: 69% decreased polyglutamylase activity. 1 PublicationAdd BLAST11

Organism-specific databases

OpenTargetsiENSG00000137941.
PharmGKBiPA142670678.

Polymorphism and mutation databases

BioMutaiTTLL7.
DMDMi73920151.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002124441 – 887Tubulin polyglutamylase TTLL7Add BLAST887

Proteomic databases

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

PTM databases

iPTMnetiQ6ZT98.
PhosphoSitePlusiQ6ZT98.

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 interactors.
IntActiQ6ZT98. 2 interactors.
STRINGi9606.ENSP00000260505.

Structurei

Secondary structure

1887
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi42 – 47Combined sources6
Helixi51 – 60Combined sources10
Beta strandi73 – 79Combined sources7
Helixi83 – 87Combined sources5
Beta strandi94 – 96Combined sources3
Turni99 – 101Combined sources3
Helixi102 – 105Combined sources4
Helixi107 – 118Combined sources12
Turni122 – 124Combined sources3
Beta strandi131 – 133Combined sources3
Turni134 – 136Combined sources3
Helixi138 – 150Combined sources13
Beta strandi157 – 160Combined sources4
Beta strandi171 – 173Combined sources3
Beta strandi186 – 189Combined sources4
Beta strandi192 – 194Combined sources3
Beta strandi196 – 199Combined sources4
Beta strandi201 – 212Combined sources12
Turni213 – 216Combined sources4
Beta strandi217 – 228Combined sources12
Beta strandi271 – 273Combined sources3
Helixi274 – 283Combined sources10
Helixi288 – 317Combined sources30
Beta strandi331 – 340Combined sources10
Beta strandi345 – 353Combined sources9
Helixi361 – 378Combined sources18
Beta strandi454 – 459Combined sources6
Helixi463 – 483Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4YLRX-ray2.55A36-518[»]
4YLSX-ray2.60A36-518[»]
ProteinModelPortaliQ6ZT98.
SMRiQ6ZT98.
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 region1 PublicationAdd 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.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)DescriptionActionsGraphical viewLength
Sequence conflicti13P → S in AAO37763 (Ref. 1) Curated1
Sequence conflicti48T → A in BAC86695 (PubMed:14702039).Curated1
Sequence conflicti298L → M in AAH60878 (PubMed:15489334).Curated1
Sequence conflicti489Q → R in AAH60878 (PubMed:15489334).Curated1
Sequence conflicti493N → D in AAH60878 (PubMed:15489334).Curated1
Sequence conflicti575R → G in AAH60878 (PubMed:15489334).Curated1
Sequence conflicti609S → F in BAB15526 (PubMed:14702039).Curated1
Sequence conflicti677E → G in AAH60878 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_015199665 – 669SESLR → IILAQ in isoform 2. 1 Publication5
Alternative sequenceiVSP_015200670 – 887Missing in isoform 2. 1 PublicationAdd BLAST218
Alternative sequenceiVSP_015201791 – 792SS → YV in isoform 3. 1 Publication2
Alternative sequenceiVSP_015202793 – 887Missing in isoform 3. 1 PublicationAdd BLAST95

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]
XP_016857836.1. XM_017002347.1. [Q6ZT98-1]
UniGeneiHs.445826.
Hs.594267.

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]
XP_016857836.1. XM_017002347.1. [Q6ZT98-1]
UniGeneiHs.445826.
Hs.594267.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4YLRX-ray2.55A36-518[»]
4YLSX-ray2.60A36-518[»]
ProteinModelPortaliQ6ZT98.
SMRiQ6ZT98.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122852. 7 interactors.
IntActiQ6ZT98. 2 interactors.
STRINGi9606.ENSP00000260505.

PTM databases

iPTMnetiQ6ZT98.
PhosphoSitePlusiQ6ZT98.

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.
OpenTargetsiENSG00000137941.
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: November 2, 2016
This is version 108 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.