Protein detail

TULP3

Tubby-related protein 3 (Tubby-like protein 3)

Entry name TULP3	UniProt ID O75386	EVMP confidence score 0.38
Supporting publications (n) 1	Transmembrane count	Protein classification Disease related genesPredicted 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

Tubby-related protein 3 (Tubby-like protein 3)

Protein Class (2)

Disease related genesPredicted intracellular proteins

Protein Function (2)

Disease related genes
Predicted intracellular proteins

Ensembl

ENSG00000078246

Entrez Gene Symbol

TULP3

Gene Synonym

TUBL3

Gene Description

TUB like protein 3

Chromosome

Position

2877223-2941138

Supporting publications (n)

EVMP confidence score

0.38

Fluorescence & Localization4

Tissue SpecificbrainCell SpecificEarly spermatidsBlood Cell Specificneutrophil

Function & Pathway6

Protein Function (2)

Disease related genes
Predicted intracellular proteins

Cellular Component (9)

Molecular Function (7)

Biological Process (3)

Reactome (2)

Mediation Categories

Receptor-signaling mediation

Relations & Evidence16

Ligand-Receptor Signaling (14)

14 records.

Category	Parent	Database	Transmitter	Receiver	Secreted	Plasma Membrane (Transmembrane)	Plasma Membrane (Peripheral)
ecm	ecm	MatrixDB	Yes	No	Yes	No	No
ecm	ecm	OmniPath	Yes	No	Yes	No	No
extracellular	extracellular	OmniPath	No	No	Yes	No	No
intracellular	intracellular	LOCATE	No	No	Yes	No	No
intracellular	intracellular	ComPPI	No	No	Yes	No	No
intracellular	intracellular	GO_Intercell	No	No	Yes	No	No
intracellular	intracellular	UniProt_location	No	No	Yes	No	No
intracellular	intracellular	OmniPath	No	No	Yes	No	No
plasma_membrane	plasma_membrane	UniProt_location	No	No	Yes	No	No
plasma_membrane	plasma_membrane	OmniPath	No	No	Yes	No	No

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Regulatory Interaction Network (1)

1 record.

Source Protein Symbol	Source UniProt ID	Target Protein Symbol	Target UniProt ID	Is Directed	Is Stimulation	Is Inhibition	Database	References
TULP3	O75386	GP161	Q8N6U8	Yes	Yes	No	SIGNOR	SIGNOR:23332756

Isolation & Detection Technology (1)

1 record.

EV Isolation Method	Detection Method	Number of References	References
Differential Ultracentrifugation	R Sequencing	1	31805958

Sequence, Structure & Domains10

Sequences

Length

442

Mass

49,642

Sequence

MEASRCRLSPSGDSVFHEEMMKMRQAKLDYQRLLLEKRQRKKRLEPFMVQPNPEARLRRAKPRASDEQTPLVNCHTPHSNVILHGIDGPAAVLKPDEVHAPSVSSSVVEEDAENTVDTASKPGLQERLQKHDISESVNFDEETDGISQSACLERPNSASSQNSTDTGTSGSATAAQPADNLLGDIDDLEDFVYSPAPQGVTVRCRIIRDKRGMDRGLFPTYYMYLEKEENQKIFLLAARKRKKSKTANYLISIDPVDLSREGESYVGKLRSNLMGTKFTVYDRGICPMKGRGLVGAAHTRQELAAISYETNVLGFKGPRKMSVIIPGMTLNHKQIPYQPQNNHDSLLSRWQNRTMENLVELHNKAPVWNSDTQSYVLNFRGRVTQASVKNFQIVHKNDPDYIVMQFGRVADDVFTLDYNYPLCAVQAFGIGLSSFDSKLACE

Alternative Products

Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=O75386-1; Sequence=Displayed; Name=2; IsoId=O75386-2; Sequence=VSP_054752; Name=3; IsoId=O75386-3; Sequence=VSP_055761, VSP_055762, VSP_055763

Alternative Sequence

1..19; Missing (in isoform 3); 165..189; DTGTSGSATAAQPADNLLGDIDDLE -> FSSFCQKTEDTGYRHFRFCYCRPTS (in isoform 3); 190..442; Missing (in isoform 3); 437..442; SKLACE -> KCIQTLRMQELCELHRQHHSAASLVHRTVCQRWVGHPWRLLPQTSLLWTDLSPPPVVPAPHQISM (in isoform 2)

3D Structural Models

3D Structure

Electron microscopy (1)

Domain & Motif Annotations

Compositional Bias

145..162; Polar residues; 163..175; Low complexity

Region

23..68; Required for association with the IFT complex A (IFT-A); 101..177; Disordered

Protein Families

TUB family

Sequence Similarities

Belongs to the TUB family.

Clinical Relevance5

Disease Involvement (2)

CiliopathyDisease variant

Antibody (2)

HPA015285 HPA018496

Interaction Protein (9)

ENSG00000100124ENSG00000112182ENSG00000118965ENSG00000119650ENSG00000123607ENSG00000141568ENSG00000157796ENSG00000163913ENSG00000187535

Interaction Count

Interaction Dataset (3)

intact_biogrid_opencellintact_biogridintact_biogrid_bioplex

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.