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Q8WXF7 (ATLA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ATL1
Synonyms:GBP3, SPG3A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.12 Ref.13 Ref.15 Ref.17 Ref.19

Subunit structure

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. Ref.2 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Cell projectionaxon By similarity Ref.9 Ref.10 Ref.12 Ref.15.

Tissue specificity

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). Ref.9 Ref.12 Ref.13

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.12 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.27

Sequence similarities

Belongs to the GBP family. Atlastin subfamily.

Sequence caution

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.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WXF7-1)

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.
Isoform 2 (identifier: Q8WXF7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     518-522: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 558558Atlastin-1
PRO_0000190971

Regions

Topological domain1 – 449449Cytoplasmic Ref.9
Transmembrane450 – 47021Helical; Potential
Topological domain4711Lumenal Potential
Transmembrane472 – 49221Helical; Potential
Topological domain493 – 55866Cytoplasmic Ref.9
Nucleotide binding74 – 818GTP
Nucleotide binding118 – 1203GTP
Nucleotide binding217 – 2182GTP
Nucleotide binding276 – 2794GTP
Region448 – 558111Sufficient for membrane association
Coiled coil412 – 43928 Potential

Amino acid modifications

Modified residue221Phosphoserine By similarity
Modified residue231Phosphoserine By similarity

Natural variations

Alternative sequence518 – 5225Missing in isoform 2.
VSP_044864
Natural variant431D → E. Ref.7
Corresponds to variant rs17850684 [ dbSNP | Ensembl ].
VAR_058963
Natural variant661E → Q in HSN1D; shows no significant changes in GTPase activity and no changes in endoplasmic reticulum morphology. Ref.27
VAR_065508
Natural variant1541Q → E in SPG3. Ref.26
VAR_067655
Natural variant1571L → W in SPG3. Ref.24
VAR_065509
Natural variant1611A → P in SPG3; affects endoplasmic reticulum and Golgi morphology. Ref.12 Ref.22
VAR_019446
Natural variant1931F → C. Ref.7
Corresponds to variant rs17850683 [ dbSNP | Ensembl ].
VAR_058964
Natural variant1961Y → C in a patient with hereditary spastic paraplegia; unknown pathological significance; no effect on homodimerization and GTPase activity. Ref.17 Ref.28
VAR_067656
Natural variant2171R → Q in SPG3; abolishes homodimerization and GTPase activity and alters endoplasmic reticulum morphology. Ref.13 Ref.17 Ref.20
VAR_017146
Natural variant2391R → C in SPG3; affects endoplasmic reticulum and Golgi morphology. Ref.1 Ref.12 Ref.26 Ref.28
VAR_017147
Natural variant2471H → P in SPG3. Ref.22
VAR_019447
Natural variant2531V → I in SPG3. Ref.26 Ref.28
VAR_067657
Natural variant2581H → R in SPG3. Ref.1
VAR_017148
Natural variant2591S → Y in SPG3. Ref.1
VAR_017149
Natural variant3551N → K in HSN1D; the mutant protein has decreased GTPase activity compared to wild-type and causes disruption of endoplasmic reticulum network morphology. Ref.27
VAR_065510
Natural variant4081M → V in SPG3. Ref.21
VAR_065511
Natural variant4131F → V in SPG3. Ref.26
VAR_067658
Natural variant4151R → W in SPG3. Ref.23 Ref.26
VAR_065512
Natural variant4361Missing in SPG3; does not affect GTPase activity; does not affect interaction with SPAST; patients' lymphoblasts show decreased protein levels but normal levels of mRNA. Ref.25
VAR_065513
Natural variant4401N → T in SPG3. Ref.26
VAR_067659
Natural variant4951R → W in SPG3; affects endoplasmic reticulum and Golgi morphology. Ref.12 Ref.26 Ref.28
VAR_067660

Experimental info

Mutagenesis771R → A: Abolishes GTPase activity and impairs homodimerization. Ref.17 Ref.19
Mutagenesis771R → E: Abolishes homodimerization. Ref.17 Ref.19
Mutagenesis801K → A: Alters endoplasmic reticulum morphogenesis. Ref.13
Mutagenesis1511F → S: Affects endoplasmic reticulum and Golgi morphology. Ref.12
Mutagenesis1621T → P: Affects endoplasmic reticulum and Golgi morphology. Ref.12
Mutagenesis1911Q → R: Abolishes homodimerization. Ref.17
Mutagenesis2471H → R: Impairs homodimerization and GTPase activity. Ref.17
Mutagenesis3981S → Y: Affects endoplasmic reticulum and Golgi morphology. Ref.12

Secondary structure

.............................................................. 558
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 68A33C39DD43504C

FASTA55863,544
        10         20         30         40         50         60 
MAKNRRDRNS WGGFSEKTYE WSSEEEEPVK KAGPVQVLIV KDDHSFELDE TALNRILLSE 

        70         80         90        100        110        120 
AVRDKEVVAV SVAGAFRKGK SFLMDFMLRY MYNQESVDWV GDYNEPLTGF SWRGGSERET 

       130        140        150        160        170        180 
TGIQIWSEIF LINKPDGKKV AVLLMDTQGT FDSQSTLRDS ATVFALSTMI SSIQVYNLSQ 

       190        200        210        220        230        240 
NVQEDDLQHL QLFTEYGRLA MEETFLKPFQ SLIFLVRDWS FPYEFSYGAD GGAKFLEKRL 

       250        260        270        280        290        300 
KVSGNQHEEL QNVRKHIHSC FTNISCFLLP HPGLKVATNP NFDGKLKEID DEFIKNLKIL 

       310        320        330        340        350        360 
IPWLLSPESL DIKEINGNKI TCRGLVEYFK AYIKIYQGEE LPHPKSMLQA TAEANNLAAV 

       370        380        390        400        410        420 
ATAKDTYNKK MEEICGGDKP FLAPNDLQTK HLQLKEESVK LFRGVKKMGG EEFSRRYLQQ 

       430        440        450        460        470        480 
LESEIDELYI QYIKHNDSKN IFHAARTPAT LFVVIFITYV IAGVTGFIGL DIIASLCNMI 

       490        500        510        520        530        540 
MGLTLITLCT WAYIRYSGEY RELGAVIDQV AAALWDQGST NEALYKLYSA AATHRHLYHQ 

       550 
AFPTPKSEST EQSEKKKM 

« Hide

Isoform 2 [UniParc].

Checksum: 663877DBC4B1FC67
Show »

FASTA55363,055

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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]"Characterization of a novel SPG3A deletion in a French-Canadian family."
Meijer I.A., Dion P., Laurent S., Dupre N., Brais B., Levert A., Puymirat J., Rioux M.F., Sylvain M., Zhu P.P., Soderblom C., Stadler J., Blackstone C., Rouleau G.A.
Ann. Neurol. 61:599-603(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG3 ASN-436 DEL, CHARACTERIZATION OF VARIANT SPG3 ASN-436 DEL.
[26]"Mutational spectrum of the SPG4 (SPAST) and SPG3A (ATL1) genes in Spanish patients with hereditary spastic paraplegia."
Alvarez V., Sanchez-Ferrero E., Beetz C., Diaz M., Alonso B., Corao A.I., Gamez J., Esteban J., Gonzalo J.F., Pascual-Pascual S.I., Lopez de Munain A., Moris G., Ribacoba R., Marquez C., Rosell J., Marin R., Garcia-Barcina M.J., Del Castillo E., Benito C., Coto E.
BMC Neurol. 10:89-89(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG3 GLU-154; CYS-239; ILE-253; VAL-413; TRP-415; THR-440 AND TRP-495.
[27]"Targeted high-throughput sequencing identifies mutations in atlastin-1 as a cause of hereditary sensory neuropathy type I."
Guelly C., Zhu P.P., Leonardis L., Papic L., Zidar J., Schabhuttl M., Strohmaier H., Weis J., Strom T.M., Baets J., Willems J., De Jonghe P., Reilly M.M., Frohlich E., Hatz M., Trajanoski S., Pieber T.R., Janecke A.R., Blackstone C., Auer-Grumbach M.
Am. J. Hum. Genet. 88:99-105(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HSN1D GLN-66 AND LYS-355, CHARACTERIZATION OF VARIANTS HSN1D GLN-66 AND LYS-355.
[28]"Mutation screening of spastin, atlastin, and REEP1 in hereditary spastic paraplegia."
McCorquodale D.S. III, Ozomaro U., Huang J., Montenegro G., Kushman A., Citrigno L., Price J., Speziani F., Pericak-Vance M.A., Zuchner S.
Clin. Genet. 79:523-530(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-196, VARIANTS SPG3 CYS-239; ILE-253 AND TRP-495.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001121185.1. NM_001127713.1.
NP_056999.2. NM_015915.4.
NP_853629.2. NM_181598.3.
UniGeneHs.584905.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ8WXF7.
SMRQ8WXF7. Positions 31-442.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119254. 3 interactions.
DIPDIP-53502N.
IntActQ8WXF7. 7 interactions.
STRING9606.ENSP00000351155.

PTM databases

PhosphoSiteQ8WXF7.

Polymorphism databases

DMDM37999727.

Proteomic databases

PaxDbQ8WXF7.
PRIDEQ8WXF7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354525; ENSP00000346522; ENSG00000198513. [Q8WXF7-2]
ENST00000358385; ENSP00000351155; ENSG00000198513. [Q8WXF7-1]
ENST00000441560; ENSP00000413675; ENSG00000198513. [Q8WXF7-2]
GeneID51062.
KEGGhsa:51062.
UCSCuc001wyd.4. human.
uc001wyf.4. human. [Q8WXF7-1]

Organism-specific databases

CTD51062.
GeneCardsGC14P050999.
HGNCHGNC:11231. ATL1.
HPAHPA027550.
MIM182600. phenotype.
606439. gene.
613708. phenotype.
neXtProtNX_Q8WXF7.
Orphanet100984. Autosomal dominant spastic paraplegia type 3.
36386. Hereditary sensory and autonomic neuropathy type 1.
PharmGKBPA36061.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG325148.
HOGENOMHOG000234332.
HOVERGENHBG062891.
InParanoidQ8WXF7.
KOK17339.
OMAHLYHHAF.
OrthoDBEOG7H4DTH.
PhylomeDBQ8WXF7.
TreeFamTF105251.

Gene expression databases

ArrayExpressQ8WXF7.
BgeeQ8WXF7.
CleanExHS_ATL1.
GenevestigatorQ8WXF7.

Family and domain databases

InterProIPR003191. Guanylate-bd_C.
IPR015894. Guanylate-bd_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF02263. GBP. 1 hit.
[Graphical view]
SUPFAMSSF48340. SSF48340. 1 hit.
SSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ8WXF7.
GeneWikiAtlastin.
GenomeRNAi51062.
NextBio53649.
PROQ8WXF7.
SOURCESearch...

Entry information

Entry nameATLA1_HUMAN
AccessionPrimary (citable) accession number: Q8WXF7
Secondary accession number(s): A6NND5 expand/collapse secondary AC list , A8K2C0, G5E9T1, O95890, Q69YH7, Q96FK0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: March 1, 2002
Last modified: March 19, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM