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)

Entry name TTL13	UniProt ID A6NNM8	EVMP confidence score 0.38
Supporting publications (n) 1	Transmembrane count	Protein classification Predicted intracellular proteins

EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40

Basic Information11

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

Ensembl

ENSG00000213471

Entrez Gene Symbol

TTLL13

Gene Synonym (3)

FLJ46079MGC33417TTLL13P

Gene Description

Tubulin tyrosine ligase like 13

Chromosome

Position

90249530-90265482

Supporting publications (n)

EVMP confidence score

0.38

Fluorescence & Localization2

Tissue Specificparathyroid glandCell SpecificCorticotrophs

Function & Pathway6

Protein Function

Predicted intracellular proteins

Cellular Component (3)

Molecular Function (4)

Biological Process (3)

Reactome (2)

Mediation Categories

Metabolism mediation

Relations & Evidence3

Ligand-Receptor Signaling (2)

2 records.

Category	Parent	Database	Transmitter	Receiver	Secreted	Plasma Membrane (Transmembrane)	Plasma Membrane (Peripheral)
intracellular	intracellular	GO_Intercell	No	No	No	No	No
intracellular	intracellular	OmniPath	No	No	No	No	No

Isolation & Detection Technology (1)

1 record.

EV Isolation Method	Detection Method	Number of References	References
Differential UltracentrifugationSize Exclusion Chromatography	Mass spectrometry	2	40689422 39408670

Sequence, Structure & Domains12

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)

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 Relevance1

Antibody (2)

HPA040133 HPA041305

Supporting Publications1

PMID	Title	Abstract
34265469	Proteomic Landscape of Exosomes Reveals the Functional Contributions of CD151 in Triple-Negative Breast Cancer.	Furthermore, utilizing quantitative proteomics approach to reveal the proteomes of CD151-deleted exosomes and cells, we found that exosomal CD151 facilitated secretion of ribosomal proteins via exosomes while inhibiting exosome secretion of complement proteins. Moreover, we proved that CD151-deleted exosomes significantly decreased the migration and invasion of TNBC cells. Most importantly, we found that the tetraspanin CD151 expression levels in TNBC-derived serum exosomes were significantly higher than those exosomes from healthy subjects, and we validated our findings with samples from 16 additional donors. This is the first comparative study of the proteomes of TNBC patient-derived and CD151-deleted exosomes.