RABAC1 Rab acceptor 1 [Homo sapiens (human)] - Gene

Summary

Official Symbol: RABAC1provided by HGNC
Official Full Name: Rab acceptor 1provided by HGNC
Primary source: HGNC:HGNC:9794
See related: Ensembl:ENSG00000105404 MIM:604925; AllianceGenome:HGNC:9794
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: PRA1; YIP3; PRAF1
Summary: Enables identical protein binding activity. Located in membrane. [provided by Alliance of Genome Resources, Apr 2022]
Expression: Ubiquitous expression in fat (RPKM 42.3), stomach (RPKM 42.2) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 19q13.2

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	GRCh38.p14 (GCF_000001405.40)	19	NC_000019.10 (41956683..41959321, complement)
RS_2023_10	current	T2T-CHM13v2.0 (GCF_009914755.1)	19	NC_060943.1 (44776066..44778704, complement)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	19	NC_000019.9 (42460835..42463473, complement)

Chromosome 19 - NC_000019.10 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?

RABAC1 caused caspase-3 activation and decreased cell proliferation, clonogenic cell survival, and cell migration and invasion.
Title: Prenylated Rab acceptor RABAC1 inhibits anti-apoptotic protein BCL2A1 and induces apoptosis.
Results suggest that NDRG2 and prenylated Rab acceptor-1 (PRA1) might act synergistically to prevent signaling of T-cell facto/beta-catenin.
Title: NDRG2 and PRA1 interact and synergistically inhibit T-cell factor/β-catenin signaling.
Prenylated Rab acceptor protein 1 (PRA1) was identified as an interacting partner of SNCA.
Title: Human α-synuclein modulates vesicle trafficking through its interaction with prenylated Rab acceptor protein 1.
These findings delineated novel roles of PRA1 in lipid transport and cell migration.
Title: Proteome-wide dysregulation by PRA1 depletion delineates a role of PRA1 in lipid transport and cell migration.
Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)
Title: Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
Observational study of gene-disease association. (HuGE Navigator)
Title: Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.
findings show Yip3 acts catalytically to dissociate complexes of endosomal Rabs bound to GDI and to deliver them onto membranes; propose that the conserved Yip proteins serve as GDI-displacement factors for the targeting of Rab GTPases in eukaryotic cells
Title: Yip3 catalyses the dissociation of endosomal Rab-GDI complexes.
in vivo modulation of PRA1 may be involved in TCF/beta-catenin signaling, as well as cellular proliferation and tumorigenesis
Title: Prenylated Rab acceptor 1 (PRA1) inhibits TCF/beta-catenin signaling by binding to beta-catenin.
Coexpression of a PRA1 export mutant or knockdown of PRA1 led to redistribution of LMP1 and its associated signaling molecules to the endoplasmic reticulum and subsequent impairment of LMP1-induced NF-kappaB activation.
Title: PRA1 promotes the intracellular trafficking and NF-kappaB signaling of EBV latent membrane protein 1.

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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 Variation Viewer (GRCh37.p13)

HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
Envelope transmembrane glycoprotein gp41	env	HIV-1 gp41 colocalizes and binds to prenylated Rab acceptor 1 (PRA1)	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

MARC_24204-24205:1032291902:1 (e-PCR)
- UniSTS:268859

RH78617 (e-PCR)
- UniSTS:42092

SHGC-64254 (e-PCR)
- UniSTS:50916

STS-N36775 (e-PCR)
- UniSTS:50917

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables GTPase binding	IEA Inferred from Electronic Annotation more info
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables proline-rich region binding	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Component	Evidence Code	Pubs
is_active_in Golgi apparatus	IBA Inferred from Biological aspect of Ancestor more info
located_in membrane	HDA more info	PubMed
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
located_in synaptic vesicle	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: prenylated Rab acceptor protein 1

Names: PRA1 domain family 1; PRA1 family protein 1; Rab acceptor 1 (prenylated); prenylated Rab acceptor 1

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.