ATL1 (atlastin GTPase 1)

2016-10-01  

Identity

HGNC
LOCATION
14q22.1
LOCUSID
ALIAS
AD-FSP,FSP1,GBP3,HSN1D,SPG3,SPG3A,atlastin1
FUSION GENES

Other Information

Locus ID:

NCBI: 51062
MIM: 606439
HGNC: 11231
Ensembl: ENSG00000198513

Variants:

dbSNP: 51062
ClinVar: 51062
TCGA: ENSG00000198513
COSMIC: ATL1

RNA/Proteins

Gene IDTranscript IDUniprot
ENSG00000198513ENST00000358385Q8WXF7
ENSG00000198513ENST00000358385A0A0S2Z5B0
ENSG00000198513ENST00000441560Q8WXF7
ENSG00000198513ENST00000441560A0A0S2Z5A2
ENSG00000198513ENST00000553509G3V321
ENSG00000198513ENST00000554886G3V4Y8
ENSG00000198513ENST00000555266H0YJ65
ENSG00000198513ENST00000555960G3V5T4
ENSG00000198513ENST00000556067H0YJA7
ENSG00000198513ENST00000557735G3V334

Expression (GTEx)

0
5
10
15
20
25
30
35
40
45

Protein levels (Protein atlas)

Not detected
Low
Medium
High

References

Pubmed IDYearTitleCitations
202004472010Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network.143
213681132011Structures of the atlastin GTPase provide insight into homotypic fusion of endoplasmic reticulum membranes.95
212202942011Structural basis for the nucleotide-dependent dimerization of the large G protein atlastin-1/SPG3A.74
145062572003Cellular localization, oligomerization, and membrane association of the hereditary spastic paraplegia 3A (SPG3A) protein atlastin.58
163392132006Spastin and atlastin, two proteins mutated in autosomal-dominant hereditary spastic paraplegia, are binding partners.58
168159772006Interaction of two hereditary spastic paraplegia gene products, spastin and atlastin, suggests a common pathway for axonal maintenance.45
236846132013A conserved role for atlastin GTPases in regulating lipid droplet size.43
211946792011Targeted high-throughput sequencing identifies mutations in atlastin-1 as a cause of hereditary sensory neuropathy type I.42
233342942013Structural basis for conformational switching and GTP loading of the large G protein atlastin.32
255559152015The Atlastin C-terminal tail is an amphipathic helix that perturbs the bilayer structure during endoplasmic reticulum homotypic fusion.23

Citation

Dessen P

ATL1 (atlastin GTPase 1)

Atlas Genet Cytogenet Oncol Haematol. 2016-10-01

Online version: http://atlasgeneticsoncology.org/gene/55983/atl1