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Q8WXF7

- ATLA1_HUMAN

UniProt

Q8WXF7 - ATLA1_HUMAN

Protein

Atlastin-1

Gene

ATL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    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
    4. 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

    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. axon Source: UniProtKB-SubCell
    2. endoplasmic reticulum Source: UniProtKB
    3. endoplasmic reticulum membrane Source: UniProtKB
    4. Golgi apparatus Source: UniProtKB
    5. Golgi cis cisterna Source: UniProtKB
    6. Golgi membrane Source: UniProtKB-SubCell
    7. integral component of membrane Source: UniProtKB

    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.9 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 → W in SPG3. 2 Publications
    VAR_065512
    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

    ArrayExpressiQ8WXF7.
    BgeeiQ8WXF7.
    CleanExiHS_ATL1.
    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.
    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

    MAKNRRDRNS WGGFSEKTYE WSSEEEEPVK KAGPVQVLIV KDDHSFELDE    50
    TALNRILLSE AVRDKEVVAV SVAGAFRKGK SFLMDFMLRY MYNQESVDWV 100
    GDYNEPLTGF SWRGGSERET TGIQIWSEIF LINKPDGKKV AVLLMDTQGT 150
    FDSQSTLRDS ATVFALSTMI SSIQVYNLSQ NVQEDDLQHL QLFTEYGRLA 200
    MEETFLKPFQ SLIFLVRDWS FPYEFSYGAD GGAKFLEKRL KVSGNQHEEL 250
    QNVRKHIHSC FTNISCFLLP HPGLKVATNP NFDGKLKEID DEFIKNLKIL 300
    IPWLLSPESL DIKEINGNKI TCRGLVEYFK AYIKIYQGEE LPHPKSMLQA 350
    TAEANNLAAV ATAKDTYNKK MEEICGGDKP FLAPNDLQTK HLQLKEESVK 400
    LFRGVKKMGG EEFSRRYLQQ LESEIDELYI QYIKHNDSKN IFHAARTPAT 450
    LFVVIFITYV IAGVTGFIGL DIIASLCNMI MGLTLITLCT WAYIRYSGEY 500
    RELGAVIDQV AAALWDQGST NEALYKLYSA AATHRHLYHQ AFPTPKSEST 550
    EQSEKKKM 558
    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 → W in SPG3. 2 Publications
    VAR_065512
    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.
    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

    ArrayExpressi Q8WXF7.
    Bgeei Q8WXF7.
    CleanExi HS_ATL1.
    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

    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.

    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 1, 2014
    This is version 116 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