Protein detail

TTL13

Tubulin polyglutamylase TTLL13 (EC 6.3.2.-) (Tubulin tyrosine ligase like 13) (Tubulin tyrosine ligase-like family member 13 pseudogene) (Tubulin--tyrosine ligase-like protein 13)

Protein symbol
TTL13
UniProt ID
EVMP score
0.38
Frequency
1
Transmembrane count
Protein classification
Predicted intracellular proteins
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Tubulin polyglutamylase TTLL13 (EC 6.3.2.-) (Tubulin tyrosine ligase like 13) (Tubulin tyrosine ligase-like family member 13 pseudogene) (Tubulin--tyrosine ligase-like protein 13)
Protein Class
Predicted intracellular proteins
Protein Function
Predicted intracellular proteins
Entrez Gene Symbol
Gene Synonym
FLJ46079MGC33417TTLL13P
Gene Description
Tubulin tyrosine ligase like 13
Chromosome
15
Position
90249530-90265482
Frequency
1
EVMP Score
0.38
Fluorescence & Localization
Tissue Specificparathyroid glandCell SpecificCorticotrophs
Function & Pathway
Relations & Evidence

Enzyme-Mediated Modification

0 records.

Ligand-Receptor Signaling

2 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo

Regulatory Interaction Network

0 records.

Protein Complex Composition

0 records.

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyMass spectrometry24068942239408670
Sequence, Structure & Domains

Sequences

Length
815
Mass
93,645
Sequence
MEPSTCRTMESEEDYVEEKESEKCVKEGVTNPSNSSQQALLKADYKALKNGVPSPIMATKIPKKVIAPVDTGDLEAGRRKRRRKRRSLAINLTNCKYESVRRAAQMCGLKEVGEDEEWTLYWTDCAVSLERVMDMKRFQKINHFPGMTEICRKDLLARNLNRMYKLYPSEYNIFPRTWCLPADYGDFQSYGRQRKARTYICKPDSGCQGRGIFITRNPREIKPGEHMICQQYISKPLLIDGFKFDMRVYVLITSCDPLRIFTYEEGLARFATTPYMEPSHNNLDNVCMHLTNYAINKHNENFVRDGAVGSKRKLSTLNIWLQEHSYNPGELWGDIEDIIIKTIISAHSVLRHNYRTCFPQYLNGGTCACFEILGFDILLDHKLKPWLLEVNHSPSFTTDSCLDQEVKDALLCDAMTLVNLRGCDKRKVMEEDKRRVKERLFQCYRQPRESRKEKTESSHVAMLDQERYEDSHLGKYRRIYPGPDTEKYARFFKHNGSLFQETAASKAREECARQQLEEIRLKQEQQETSGTKRQKARDQNQGESAGEKSRPRAGLQSLSTHLAYRNRNWEKELLPGQLDTMRPQEIVEEEELERMKALLQRETLIRSLGIVEQLTRLQHPGPQGQKKLHESRDRLGSQELKSMSLVLLVLLRGAATEQGAPHFLHPVLPHESIPRILGALPSMNAAIPHVPRYHLQPKNFNWTGEPAAINSCSLSMKKAGRCYFSSARIRLTSQGQASRRLEAINRVLAGSVPPTLTPKQGYFLQPERVASDSWTECTLPSMVNSEHRAAKVPLCPASAPMLQRSRALLNINQFR
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=A6NNM8-1; Sequence=Displayed; Name=2; IsoId=A6NNM8-2; Sequence=VSP_052720, VSP_052721
Alternative Sequence
452..459; KEKTESSH -> CARCLACV (in isoform 2); 460..815; Missing (in isoform 2)

3D Structural Models

Domain & Motif Annotations

Compositional Bias
536..550; Basic and acidic residues
Coiled Coil
504..528
Domain (CC)
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.; DOMAIN: Gln-208 is the main determinant for regioselectivity, which segregates between initiases and elongases in all tubulin--tyrosine ligase family. A glutamine residue at this position is found in elongases TTLL6, TTLL9, TTLL11, TTLL13, TTLL10 and favors glutamate-chain elongation, whereas an arginine residue is found in initiases TTLL2, TTLL4, TTLL5, TTLL3, TTLL8 and favors initiation.
Domain (FT)
85..430; TTL
Region
401..482; c-MTBD region; 520..556; Disordered
Protein Families
Tubulin--tyrosine ligase family
Sequence Similarities
Belongs to the tubulin--tyrosine ligase family.
Clinical Relevance