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Q8WXF7

- ATLA1_HUMAN

UniProt

Q8WXF7 - ATLA1_HUMAN

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Protein

Atlastin-1

Gene

ATL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. May also regulate Golgi biogenesis. May regulate axonal development.6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi74 – 818GTP
Nucleotide bindingi118 – 1203GTP
Nucleotide bindingi217 – 2182GTP
Nucleotide bindingi276 – 2794GTP

GO - Molecular functioni

  1. GTPase activity Source: UniProtKB
  2. GTP binding Source: UniProtKB
  3. identical protein binding Source: UniProtKB

GO - Biological processi

  1. axonogenesis Source: UniProtKB
  2. cell death Source: UniProtKB-KW
  3. endoplasmic reticulum organization Source: UniProtKB
  4. GTP catabolic process Source: GOC
  5. protein homooligomerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Atlastin-1 (EC:3.6.5.-)
Alternative name(s):
Brain-specific GTP-binding protein
GTP-binding protein 3
Short name:
GBP-3
Short name:
hGBP3
Guanine nucleotide-binding protein 3
Spastic paraplegia 3 protein A
Gene namesi
Name:ATL1
Synonyms:GBP3, SPG3A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:11231. ATL1.

Subcellular locationi

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. endoplasmic reticulum Source: UniProtKB
  3. endoplasmic reticulum membrane Source: UniProtKB
  4. Golgi apparatus Source: UniProtKB
  5. Golgi cis cisterna Source: UniProtKB
  6. integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Spastic paraplegia 3, autosomal dominant (SPG3) [MIM:182600]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.11 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti154 – 1541Q → E in SPG3. 1 Publication
VAR_067655
Natural varianti157 – 1571L → W in SPG3. 1 Publication
VAR_065509
Natural varianti161 – 1611A → P in SPG3; affects endoplasmic reticulum and Golgi morphology. 1 Publication
VAR_019446
Natural varianti217 – 2171R → Q in SPG3; abolishes homodimerization and GTPase activity and alters endoplasmic reticulum morphology. 1 Publication
VAR_017146
Natural varianti239 – 2391R → C in SPG3; affects endoplasmic reticulum and Golgi morphology. 3 Publications
VAR_017147
Natural varianti247 – 2471H → P in SPG3. 1 Publication
VAR_019447
Natural varianti253 – 2531V → I in SPG3. 2 Publications
VAR_067657
Natural varianti258 – 2581H → R in SPG3. 1 Publication
VAR_017148
Natural varianti259 – 2591S → Y in SPG3. 1 Publication
VAR_017149
Natural varianti408 – 4081M → V in SPG3. 1 Publication
VAR_065511
Natural varianti413 – 4131F → V in SPG3. 1 Publication
VAR_067658
Natural varianti415 – 4151R → Q in SPG3. 1 Publication
VAR_071708
Natural varianti415 – 4151R → W in SPG3. 3 Publications
VAR_065512
Natural varianti416 – 4161R → C in SPG3. 1 Publication
VAR_071709
Natural varianti436 – 4361Missing in SPG3; does not affect GTPase activity; does not affect interaction with SPAST; patients' lymphoblasts show decreased protein levels but normal levels of mRNA. 1 Publication
VAR_065513
Natural varianti440 – 4401N → T in SPG3. 1 Publication
VAR_067659
Natural varianti495 – 4951R → W in SPG3; affects endoplasmic reticulum and Golgi morphology. 2 Publications
VAR_067660
Neuropathy, hereditary sensory, 1D (HSN1D) [MIM:613708]: A disease characterized by adult-onset distal axonal sensory neuropathy leading to mutilating ulcerations as well as hyporeflexia. Some patients may show features suggesting upper neuron involvement.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti66 – 661E → Q in HSN1D; shows no significant changes in GTPase activity and no changes in endoplasmic reticulum morphology. 1 Publication
VAR_065508
Natural varianti355 – 3551N → K in HSN1D; the mutant protein has decreased GTPase activity compared to wild-type and causes disruption of endoplasmic reticulum network morphology. 1 Publication
VAR_065510

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi77 – 771R → A: Abolishes GTPase activity and impairs homodimerization. 2 Publications
Mutagenesisi77 – 771R → E: Abolishes homodimerization. 2 Publications
Mutagenesisi80 – 801K → A: Alters endoplasmic reticulum morphogenesis. 1 Publication
Mutagenesisi151 – 1511F → S: Affects endoplasmic reticulum and Golgi morphology. 1 Publication
Mutagenesisi162 – 1621T → P: Affects endoplasmic reticulum and Golgi morphology. 1 Publication
Mutagenesisi191 – 1911Q → R: Abolishes homodimerization. 1 Publication
Mutagenesisi247 – 2471H → R: Impairs homodimerization and GTPase activity. 1 Publication
Mutagenesisi398 – 3981S → Y: Affects endoplasmic reticulum and Golgi morphology. 1 Publication

Keywords - Diseasei

Disease mutation, Hereditary spastic paraplegia, Neurodegeneration, Neuropathy

Organism-specific databases

MIMi182600. phenotype.
613708. phenotype.
Orphaneti100984. Autosomal dominant spastic paraplegia type 3.
36386. Hereditary sensory and autonomic neuropathy type 1.
PharmGKBiPA36061.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 558558Atlastin-1PRO_0000190971Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221PhosphoserineBy similarity
Modified residuei23 – 231PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8WXF7.
PaxDbiQ8WXF7.
PRIDEiQ8WXF7.

PTM databases

PhosphoSiteiQ8WXF7.

Expressioni

Tissue specificityi

Expressed predominantly in the adult and fetal central nervous system. Measurable expression in all tissues examined, although expression in adult brain is at least 50-fold higher than in other tissues. Detected predominantly in pyramidal neurons in the cerebral cortex and the hippocampus of the brain. Expressed in upper and lower motor neurons (at protein level).3 Publications

Gene expression databases

BgeeiQ8WXF7.
CleanExiHS_ATL1.
ExpressionAtlasiQ8WXF7. baseline and differential.
GenevestigatoriQ8WXF7.

Organism-specific databases

HPAiHPA027550.

Interactioni

Subunit structurei

Monomer as apoprotein and in the GDP-bound form. Homodimer in the GTP-bound form. Interacts (via N-terminal region) with MAP4K4 (via CNH regulatory domain). Interacts with REEP5, RTN3 and RTN4 (via the transmembrane region). Interacts with SPAST; interaction is direct. May interact with TMED2. Interacts with REEP1.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-2410266,EBI-2410266
Reep5Q608702EBI-2410266,EBI-2410304From a different organism.
Rtn3Q9ES97-33EBI-2410266,EBI-1487798From a different organism.
RTN4Q9NQC3-12EBI-2410266,EBI-715972
Rtn4Q9JK11-32EBI-2410266,EBI-920002From a different organism.

Protein-protein interaction databases

BioGridi119254. 3 interactions.
DIPiDIP-53502N.
IntActiQ8WXF7. 7 interactions.
STRINGi9606.ENSP00000351155.

Structurei

Secondary structure

1
558
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 407
Turni42 – 443
Beta strandi46 – 483
Helixi50 – 578
Turni60 – 645
Beta strandi65 – 7511
Beta strandi76 – 794
Helixi80 – 9213
Turni93 – 953
Turni97 – 1004
Beta strandi115 – 1173
Beta strandi122 – 1287
Beta strandi130 – 1334
Beta strandi135 – 1373
Beta strandi139 – 1479
Beta strandi152 – 1565
Helixi157 – 17014
Beta strandi172 – 18110
Helixi184 – 20017
Beta strandi208 – 21710
Turni222 – 2243
Helixi229 – 24012
Helixi248 – 26013
Beta strandi261 – 2688
Helixi274 – 2785
Helixi286 – 2883
Helixi291 – 30515
Turni307 – 3093
Helixi322 – 33716
Beta strandi338 – 3414
Helixi347 – 37529
Beta strandi377 – 3804
Helixi384 – 40421
Helixi410 – 43829

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q5DX-ray2.70A1-447[»]
3Q5EX-ray3.01A/C/E/G1-447[»]
3QNUX-ray2.80A18-447[»]
3QOFX-ray2.80A/B/C/D18-447[»]
4IDNX-ray2.25A/B1-446[»]
4IDOX-ray2.09A/B1-446[»]
4IDPX-ray2.59A/B/C/D1-446[»]
4IDQX-ray2.30A/B/C/D1-446[»]
ProteinModelPortaliQ8WXF7.
SMRiQ8WXF7. Positions 31-442.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WXF7.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 449449Cytoplasmic1 PublicationAdd
BLAST
Topological domaini471 – 4711LumenalSequence Analysis
Topological domaini493 – 55866Cytoplasmic1 PublicationAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei450 – 47021HelicalSequence AnalysisAdd
BLAST
Transmembranei472 – 49221HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 309246GB1/RHD3-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni448 – 558111Sufficient for membrane associationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili412 – 43928Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG325148.
GeneTreeiENSGT00390000008959.
HOGENOMiHOG000234332.
HOVERGENiHBG062891.
InParanoidiQ8WXF7.
KOiK17339.
OMAiHLYHHAF.
OrthoDBiEOG7H4DTH.
PhylomeDBiQ8WXF7.
TreeFamiTF105251.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003191. Guanylate-bd_C.
IPR015894. Guanylate-bd_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF02263. GBP. 1 hit.
[Graphical view]
SUPFAMiSSF48340. SSF48340. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51715. G_GB1_RHD3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8WXF7-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAKNRRDRNS WGGFSEKTYE WSSEEEEPVK KAGPVQVLIV KDDHSFELDE
60 70 80 90 100
TALNRILLSE AVRDKEVVAV SVAGAFRKGK SFLMDFMLRY MYNQESVDWV
110 120 130 140 150
GDYNEPLTGF SWRGGSERET TGIQIWSEIF LINKPDGKKV AVLLMDTQGT
160 170 180 190 200
FDSQSTLRDS ATVFALSTMI SSIQVYNLSQ NVQEDDLQHL QLFTEYGRLA
210 220 230 240 250
MEETFLKPFQ SLIFLVRDWS FPYEFSYGAD GGAKFLEKRL KVSGNQHEEL
260 270 280 290 300
QNVRKHIHSC FTNISCFLLP HPGLKVATNP NFDGKLKEID DEFIKNLKIL
310 320 330 340 350
IPWLLSPESL DIKEINGNKI TCRGLVEYFK AYIKIYQGEE LPHPKSMLQA
360 370 380 390 400
TAEANNLAAV ATAKDTYNKK MEEICGGDKP FLAPNDLQTK HLQLKEESVK
410 420 430 440 450
LFRGVKKMGG EEFSRRYLQQ LESEIDELYI QYIKHNDSKN IFHAARTPAT
460 470 480 490 500
LFVVIFITYV IAGVTGFIGL DIIASLCNMI MGLTLITLCT WAYIRYSGEY
510 520 530 540 550
RELGAVIDQV AAALWDQGST NEALYKLYSA AATHRHLYHQ AFPTPKSEST

EQSEKKKM
Length:558
Mass (Da):63,544
Last modified:March 1, 2002 - v1
Checksum:i68A33C39DD43504C
GO
Isoform 2 (identifier: Q8WXF7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     518-522: Missing.

Note: No experimental confirmation available.

Show »
Length:553
Mass (Da):63,055
Checksum:i663877DBC4B1FC67
GO

Sequence cautioni

The sequence AAD20047.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAK51160.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431D → E.1 Publication
Corresponds to variant rs17850684 [ dbSNP | Ensembl ].
VAR_058963
Natural varianti66 – 661E → Q in HSN1D; shows no significant changes in GTPase activity and no changes in endoplasmic reticulum morphology. 1 Publication
VAR_065508
Natural varianti154 – 1541Q → E in SPG3. 1 Publication
VAR_067655
Natural varianti157 – 1571L → W in SPG3. 1 Publication
VAR_065509
Natural varianti161 – 1611A → P in SPG3; affects endoplasmic reticulum and Golgi morphology. 1 Publication
VAR_019446
Natural varianti193 – 1931F → C.1 Publication
Corresponds to variant rs17850683 [ dbSNP | Ensembl ].
VAR_058964
Natural varianti196 – 1961Y → C in a patient with hereditary spastic paraplegia; unknown pathological significance; no effect on homodimerization and GTPase activity. 1 Publication
VAR_067656
Natural varianti217 – 2171R → Q in SPG3; abolishes homodimerization and GTPase activity and alters endoplasmic reticulum morphology. 1 Publication
VAR_017146
Natural varianti239 – 2391R → C in SPG3; affects endoplasmic reticulum and Golgi morphology. 3 Publications
VAR_017147
Natural varianti247 – 2471H → P in SPG3. 1 Publication
VAR_019447
Natural varianti253 – 2531V → I in SPG3. 2 Publications
VAR_067657
Natural varianti258 – 2581H → R in SPG3. 1 Publication
VAR_017148
Natural varianti259 – 2591S → Y in SPG3. 1 Publication
VAR_017149
Natural varianti355 – 3551N → K in HSN1D; the mutant protein has decreased GTPase activity compared to wild-type and causes disruption of endoplasmic reticulum network morphology. 1 Publication
VAR_065510
Natural varianti408 – 4081M → V in SPG3. 1 Publication
VAR_065511
Natural varianti413 – 4131F → V in SPG3. 1 Publication
VAR_067658
Natural varianti415 – 4151R → Q in SPG3. 1 Publication
VAR_071708
Natural varianti415 – 4151R → W in SPG3. 3 Publications
VAR_065512
Natural varianti416 – 4161R → C in SPG3. 1 Publication
VAR_071709
Natural varianti436 – 4361Missing in SPG3; does not affect GTPase activity; does not affect interaction with SPAST; patients' lymphoblasts show decreased protein levels but normal levels of mRNA. 1 Publication
VAR_065513
Natural varianti440 – 4401N → T in SPG3. 1 Publication
VAR_067659
Natural varianti495 – 4951R → W in SPG3; affects endoplasmic reticulum and Golgi morphology. 2 Publications
VAR_067660

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei518 – 5225Missing in isoform 2. 1 PublicationVSP_044864

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY032844 mRNA. Translation: AAK51160.1. Different initiation.
AF444143 mRNA. Translation: AAL37898.1.
AK290185 mRNA. Translation: BAF82874.1.
AL833591 mRNA. Translation: CAH10392.1.
AL118556 Genomic DNA. No translation available.
AL606834 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65705.1.
CH471078 Genomic DNA. Translation: EAW65706.1.
BC010708 mRNA. Translation: AAH10708.2.
AF131801 mRNA. Translation: AAD20047.1. Different initiation.
CCDSiCCDS32077.1. [Q8WXF7-2]
CCDS9700.1. [Q8WXF7-1]
RefSeqiNP_001121185.1. NM_001127713.1. [Q8WXF7-2]
NP_056999.2. NM_015915.4. [Q8WXF7-1]
NP_853629.2. NM_181598.3. [Q8WXF7-2]
UniGeneiHs.584905.

Genome annotation databases

EnsembliENST00000358385; ENSP00000351155; ENSG00000198513. [Q8WXF7-1]
ENST00000441560; ENSP00000413675; ENSG00000198513. [Q8WXF7-2]
GeneIDi51062.
KEGGihsa:51062.
UCSCiuc001wyd.4. human.
uc001wyf.4. human. [Q8WXF7-1]

Polymorphism databases

DMDMi37999727.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY032844 mRNA. Translation: AAK51160.1 . Different initiation.
AF444143 mRNA. Translation: AAL37898.1 .
AK290185 mRNA. Translation: BAF82874.1 .
AL833591 mRNA. Translation: CAH10392.1 .
AL118556 Genomic DNA. No translation available.
AL606834 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65705.1 .
CH471078 Genomic DNA. Translation: EAW65706.1 .
BC010708 mRNA. Translation: AAH10708.2 .
AF131801 mRNA. Translation: AAD20047.1 . Different initiation.
CCDSi CCDS32077.1. [Q8WXF7-2 ]
CCDS9700.1. [Q8WXF7-1 ]
RefSeqi NP_001121185.1. NM_001127713.1. [Q8WXF7-2 ]
NP_056999.2. NM_015915.4. [Q8WXF7-1 ]
NP_853629.2. NM_181598.3. [Q8WXF7-2 ]
UniGenei Hs.584905.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3Q5D X-ray 2.70 A 1-447 [» ]
3Q5E X-ray 3.01 A/C/E/G 1-447 [» ]
3QNU X-ray 2.80 A 18-447 [» ]
3QOF X-ray 2.80 A/B/C/D 18-447 [» ]
4IDN X-ray 2.25 A/B 1-446 [» ]
4IDO X-ray 2.09 A/B 1-446 [» ]
4IDP X-ray 2.59 A/B/C/D 1-446 [» ]
4IDQ X-ray 2.30 A/B/C/D 1-446 [» ]
ProteinModelPortali Q8WXF7.
SMRi Q8WXF7. Positions 31-442.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119254. 3 interactions.
DIPi DIP-53502N.
IntActi Q8WXF7. 7 interactions.
STRINGi 9606.ENSP00000351155.

PTM databases

PhosphoSitei Q8WXF7.

Polymorphism databases

DMDMi 37999727.

Proteomic databases

MaxQBi Q8WXF7.
PaxDbi Q8WXF7.
PRIDEi Q8WXF7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358385 ; ENSP00000351155 ; ENSG00000198513 . [Q8WXF7-1 ]
ENST00000441560 ; ENSP00000413675 ; ENSG00000198513 . [Q8WXF7-2 ]
GeneIDi 51062.
KEGGi hsa:51062.
UCSCi uc001wyd.4. human.
uc001wyf.4. human. [Q8WXF7-1 ]

Organism-specific databases

CTDi 51062.
GeneCardsi GC14P050999.
GeneReviewsi ATL1.
HGNCi HGNC:11231. ATL1.
HPAi HPA027550.
MIMi 182600. phenotype.
606439. gene.
613708. phenotype.
neXtProti NX_Q8WXF7.
Orphaneti 100984. Autosomal dominant spastic paraplegia type 3.
36386. Hereditary sensory and autonomic neuropathy type 1.
PharmGKBi PA36061.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG325148.
GeneTreei ENSGT00390000008959.
HOGENOMi HOG000234332.
HOVERGENi HBG062891.
InParanoidi Q8WXF7.
KOi K17339.
OMAi HLYHHAF.
OrthoDBi EOG7H4DTH.
PhylomeDBi Q8WXF7.
TreeFami TF105251.

Miscellaneous databases

EvolutionaryTracei Q8WXF7.
GeneWikii Atlastin.
GenomeRNAii 51062.
NextBioi 53649.
PROi Q8WXF7.
SOURCEi Search...

Gene expression databases

Bgeei Q8WXF7.
CleanExi HS_ATL1.
ExpressionAtlasi Q8WXF7. baseline and differential.
Genevestigatori Q8WXF7.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR003191. Guanylate-bd_C.
IPR015894. Guanylate-bd_N.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF02263. GBP. 1 hit.
[Graphical view ]
SUPFAMi SSF48340. SSF48340. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS51715. G_GB1_RHD3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations in a newly identified GTPase gene cause autosomal dominant hereditary spastic paraplegia."
    Zhao X., Alvarado D., Rainier S., Lemons R., Hedera P., Weber C.H., Tukel T., Apak M., Heiman-Patterson T., Ming L., Bui M., Fink J.K.
    Nat. Genet. 29:326-331(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SPG3 CYS-239; ARG-258 AND TYR-259.
  2. "A novel GTP-binding protein hGBP3 interacts with NIK/HGK."
    Luan Z., Zhang Y., Liu A., Man Y., Cheng L., Hu G.
    FEBS Lett. 530:233-238(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH MAP4K4.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Thalamus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Endometrium.
  5. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLU-43 AND CYS-193.
    Tissue: Eye.
  8. Mei G., Yu W., Gibbs R.A.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-558 (ISOFORM 1).
    Tissue: Brain.
  9. "Cellular localization, oligomerization, and membrane association of the hereditary spastic paraplegia 3A (SPG3A) protein atlastin."
    Zhu P.-P., Patterson A., Lavoie B., Stadler J., Shoeb M., Patel R., Blackstone C.
    J. Biol. Chem. 278:49063-49071(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, REGION, TOPOLOGY, SUBUNIT.
  10. "Spastin and atlastin, two proteins mutated in autosomal-dominant hereditary spastic paraplegia, are binding partners."
    Sanderson C.M., Connell J.W., Edwards T.L., Bright N.A., Duley S., Thompson A., Luzio J.P., Reid E.
    Hum. Mol. Genet. 15:307-318(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPAST, SUBCELLULAR LOCATION.
  11. "Interaction of two hereditary spastic paraplegia gene products, spastin and atlastin, suggests a common pathway for axonal maintenance."
    Evans K.J., Keller C., Pavur K., Glasgow K., Conn B., Lauring B.P.
    Proc. Natl. Acad. Sci. U.S.A. 103:10666-10671(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPAST.
  12. "Mutations in the SPG3A gene encoding the GTPase atlastin interfere with vesicle trafficking in the ER/Golgi interface and Golgi morphogenesis."
    Namekawa M., Muriel M.-P., Janer A., Latouche M., Dauphin A., Debeir T., Martin E., Duyckaerts C., Prigent A., Depienne C., Sittler A., Brice A., Ruberg M.
    Mol. Cell. Neurosci. 35:1-13(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS SPG3 PRO-161; CYS-239 AND TRP-495, MUTAGENESIS OF PHE-151; THR-162 AND SER-398, INTERACTION WITH TMED2, TISSUE SPECIFICITY.
  13. "Atlastin GTPases are required for Golgi apparatus and ER morphogenesis."
    Rismanchi N., Soderblom C., Stadler J., Zhu P.-P., Blackstone C.
    Hum. Mol. Genet. 17:1591-1604(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION OF VARIANT SPAG3 GLN-217, MUTAGENESIS OF LYS-80, TISSUE SPECIFICITY.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  15. "A class of dynamin-like GTPases involved in the generation of the tubular ER network."
    Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A., Rapoport T.A., Blackstone C.
    Cell 138:549-561(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH REEP5; RTN3 AND RTN4, SUBCELLULAR LOCATION.
  16. "Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network."
    Park S.H., Zhu P.P., Parker R.L., Blackstone C.
    J. Clin. Invest. 120:1097-1110(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH REEP1.
  17. "Structural basis for the nucleotide-dependent dimerization of the large G protein atlastin-1/SPG3A."
    Byrnes L.J., Sondermann H.
    Proc. Natl. Acad. Sci. U.S.A. 108:2216-2221(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-447 IN COMPLEX WITH GDP, FUNCTION, CHARACTERIZATION OF VARIANT CYS-196, CHARACTERIZATION OF VARIANT SPAG3 GLN-217, MUTAGENESIS OF ARG-77; GLN-191 AND HIS-247, SUBUNIT.
  18. "Structures of the atlastin GTPase provide insight into homotypic fusion of endoplasmic reticulum membranes."
    Bian X., Klemm R.W., Liu T.Y., Zhang M., Sun S., Sui X., Liu X., Rapoport T.A., Hu J.
    Proc. Natl. Acad. Sci. U.S.A. 108:3976-3981(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 18-447IN COMPLEX WITH GDP, SUBUNIT.
  19. "Structural basis for conformational switching and GTP loading of the large G protein atlastin."
    Byrnes L.J., Singh A., Szeto K., Benvin N.M., O'Donnell J.P., Zipfel W.R., Sondermann H.
    EMBO J. 32:369-384(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 1-446 IN COMPLEX WITH GTP ANALOG, FUNCTION, SUBUNIT, MUTAGENESIS OF ARG-77.
  20. "Further evidence that SPG3A gene mutations cause autosomal dominant hereditary spastic paraplegia."
    Muglia M., Magariello A., Nicoletti G., Patitucci A., Gabriele A.L., Conforti F.L., Mazzei R., Caracciolo M., Ardito B., Lastilla M., Tedeschi G., Quattrone A.
    Ann. Neurol. 51:794-795(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SPG3 GLN-217.
  21. "Infancy onset hereditary spastic paraplegia associated with a novel atlastin mutation."
    Dalpozzo F., Rossetto M.G., Boaretto F., Sartori E., Mostacciuolo M.L., Daga A., Bassi M.T., Martinuzzi A.
    Neurology 61:580-581(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SPG3 VAL-408.
  22. "Novel mutations in the Atlastin gene (SPG3A) in families with autosomal dominant hereditary spastic paraplegia and evidence for late onset forms of HSP linked to the SPG3A locus."
    Sauter S.M., Engel W., Neumann L.M., Kunze J., Neesen J.
    Hum. Mutat. 23:98-98(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SPG3 PRO-161 AND PRO-247.
  23. "Incomplete penetrance in an SPG3A-linked family with a new mutation in the atlastin gene."
    D'Amico A., Tessa A., Sabino A., Bertini E., Santorelli F.M., Servidei S.
    Neurology 62:2138-2139(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SPG3 TRP-415.
  24. "De novo occurrence of novel SPG3A/atlastin mutation presenting as cerebral palsy."
    Rainier S., Sher C., Reish O., Thomas D., Fink J.K.
    Arch. Neurol. 63:445-447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SPG3 TRP-157.
  25. Cited for: VARIANT SPG3 ASN-436 DEL, CHARACTERIZATION OF VARIANT SPG3 ASN-436 DEL.
  26. Cited for: VARIANTS SPG3 GLU-154; CYS-239; ILE-253; VAL-413; TRP-415; THR-440 AND TRP-495.
  27. Cited for: VARIANTS HSN1D GLN-66 AND LYS-355, CHARACTERIZATION OF VARIANTS HSN1D GLN-66 AND LYS-355.
  28. Cited for: VARIANT CYS-196, VARIANTS SPG3 CYS-239; ILE-253 AND TRP-495.
  29. "Late-onset hereditary spastic paraplegia with thin corpus callosum caused by a new SPG3A mutation."
    Orlacchio A., Montieri P., Babalini C., Gaudiello F., Bernardi G., Kawarai T.
    J. Neurol. 258:1361-1363(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SPG3 CYS-416.
  30. "Do not trust the pedigree: reduced and sex-dependent penetrance at a novel mutation hotspot in ATL1 blurs autosomal dominant inheritance of spastic paraplegia."
    Varga R.E., Schuele R., Fadel H., Valenzuela I., Speziani F., Gonzalez M., Rudenskaia G., Nuernberg G., Thiele H., Altmueller J., Alvarez V., Gamez J., Garbern J.Y., Nuernberg P., Zuchner S., Beetz C.
    Hum. Mutat. 34:860-863(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SPG3 GLN-415 AND TRP-415.

Entry informationi

Entry nameiATLA1_HUMAN
AccessioniPrimary (citable) accession number: Q8WXF7
Secondary accession number(s): A6NND5
, A8K2C0, G5E9T1, O95890, Q69YH7, Q96FK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: March 1, 2002
Last modified: October 29, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3