TMOD3 tropomodulin 3 [Homo sapiens (human)] - Gene

Summary

Official Symbol: TMOD3provided by HGNC
Official Full Name: tropomodulin 3provided by HGNC
Primary source: HGNC:HGNC:11873
See related: Ensembl:ENSG00000138594 MIM:605112; AllianceGenome:HGNC:11873
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: UTMOD
Summary: Enables cadherin binding activity involved in cell-cell adhesion. Predicted to be involved in actin filament organization; muscle contraction; and myofibril assembly. Predicted to act upstream of or within actin cytoskeleton organization; erythrocyte development; and positive regulation of mitotic cell cycle phase transition. Located in adherens junction. [provided by Alliance of Genome Resources, Apr 2022]
Expression: Ubiquitous expression in esophagus (RPKM 45.0), lung (RPKM 23.8) and 24 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 15q21.2

Exon count:: 10

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	GRCh38.p14 (GCF_000001405.40)	15	NC_000015.10 (51829653..51915725)
RS_2023_10	current	T2T-CHM13v2.0 (GCF_009914755.1)	15	NC_060939.1 (49637162..49723313)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	15	NC_000015.9 (52121850..52207922)

Chromosome 15 - NC_000015.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Tropomodulins Control the Balance between Protrusive and Contractile Structures by Stabilizing Actin-Tropomyosin Filaments.
Title: Tropomodulins Control the Balance between Protrusive and Contractile Structures by Stabilizing Actin-Tropomyosin Filaments.
These findings reveal that Tmod3 enhances aggressive behavior of hepatocellular carcinoma (HCC) both in vitro and in vivo by interacting with EFGR and by activating the PI3K-AKT signaling pathway.
Title: Tropomodulin 3 modulates EGFR-PI3K-AKT signaling to drive hepatocellular carcinoma metastasis.
TMOD3 expression was found to be elevated in liver cancer cells and tissues. In the in vitro experiments, liver cancer cell proliferation, invasion and migration were inhibited by TMOD3 knockdown and promoted by ectopic expression of TMOD3. TMOD3 overexpression activated MAPK/ERK signaling and increased the levels of other targets of this pathway.
Title: Tropomodulin 3 promotes liver cancer progression by activating the MAPK/ERK signaling pathway.
study has identified several new proteins like RHOC, DLG5, UGDH, TMOD3 in addition to known chemoresistance associated proteins in non-small cell lung carcinoma.
Title: Global proteomic profiling identifies etoposide chemoresistance markers in non-small cell lung carcinoma.
investigation of biomarkers for early diagnosis of endometriosis: Data suggest that TMOD3, tropomyosin 3, and stomatin-like protein 2 are autoantigens present in blood of women with endometriosis; immunodominant epitopes were identified.
Title: Identification and validation of novel serum markers for early diagnosis of endometriosis.
findings show that the pointed-end capping protein Tmod3 contributes to epithelial cell shape within confluent monolayers of polarized epithelial cells
Title: Tmod3 regulates polarized epithelial cell morphology.
levels of TM1, TM2 and TM3 are reduced in human transitional cell carcinoma cells, but significantly upregulated by inhibition of the mitogen-activated protein kinase-signaling pathway
Title: Alterations in tropomyosin isoform expression in human transitional cell carcinoma of the urinary bladder.
the Tmod3 isoform may regulate actin dynamics differently in cells than the previously described tropomodulin isoforms
Title: Tropomodulin 3 binds to actin monomers.
capping of actin filament pointed ends by Tmod3 inhibits cell migration and reveal a novel control mechanism for regulation of actin filaments in lamellipodia.
Title: Pointed-end capping by tropomodulin3 negatively regulates endothelial cell motility.

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Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

TMOD3_9585 (e-PCR)
- UniSTS:468765

RH71182 (e-PCR)
- UniSTS:12842

STS-N36078 (e-PCR)
- UniSTS:2109

SHGC-36394 (e-PCR)
- UniSTS:596

RH45657 (e-PCR)
- UniSTS:60772

SHGC-80857 (e-PCR)
- UniSTS:102506

D10S16 (e-PCR)
- UniSTS:155756

D1S1425 (e-PCR)
- UniSTS:149621

WI-13716 (e-PCR)
- UniSTS:21386

SGC44370 (e-PCR)
- UniSTS:27340

RH103426 (e-PCR)
- UniSTS:97751

SHGC-105181 (e-PCR)
- UniSTS:169182

D15S1203 (e-PCR)
- UniSTS:34274

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables actin binding	IEA Inferred from Electronic Annotation more info
enables cadherin binding involved in cell-cell adhesion	HDA more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables tropomyosin binding	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in actin filament organization	IBA Inferred from Biological aspect of Ancestor more info
involved_in cell-cell adhesion	IEA Inferred from Electronic Annotation more info
involved_in erythrocyte development	IEA Inferred from Electronic Annotation more info
involved_in mitotic cell cycle phase transition	IEA Inferred from Electronic Annotation more info
involved_in muscle contraction	IBA Inferred from Biological aspect of Ancestor more info
involved_in myofibril assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in pointed-end actin filament capping	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of mitotic cell cycle phase transition	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in adherens junction	HDA more info	PubMed
is_active_in cytoskeleton	IBA Inferred from Biological aspect of Ancestor more info
is_active_in myofibril	IBA Inferred from Biological aspect of Ancestor more info
is_active_in striated muscle thin filament	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: tropomodulin-3

Names: tropomodulin 3 (ubiquitous); ubiquitous tropomodulin

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_014547.5 → NP_055362.1 tropomodulin-3

See identical proteins and their annotated locations for NP_055362.1

Status: VALIDATED

Source sequence(s)

AC090971, AL137543, BC020542, BM975185

Consensus CDS

CCDS10145.1

UniProtKB/Swiss-Prot

B2R6G7, Q9NT43, Q9NYL9, Q9NZR0

UniProtKB/TrEMBL

Q5HYL6

Related

ENSP00000308753.7, ENST00000308580.12

Conserved Domains (2) summary

pfam03250
Location:5 → 146

Tropomodulin; Tropomodulin

cl26161
Location:216 → 292

LRR_RI; Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond ...