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Q8WXF7 (ATLA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. 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·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)
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-homooligomer 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.8 Ref.11 Ref.12 Ref.14

Subunit structure

Homooligomer. 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. Ref.2 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Cell projectionaxon By similarity Ref.8 Ref.9 Ref.11 Ref.14.

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.8 Ref.11 Ref.12

Involvement in disease

Defects in ATL1 are the cause of spastic paraplegia autosomal dominant type 3 (SPG3) [MIM:182600]; also known as Strumpell-Lorrain syndrome. Spastic paraplegia is a degenerative spinal cord disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Ref.1 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20

Defects in ATL1 are the cause of hereditary sensory neuropathy type 1D (HSN1D) [MIM:613708]. HSN1D is 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. Ref.21

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

Keywords
   Cellular componentCell projection
Endoplasmic reticulum
Golgi apparatus
Membrane
   DiseaseDisease mutation
Hereditary spastic paraplegia
Neurodegeneration
Neuropathy
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandGTP-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processaxonogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum organization

Inferred from direct assay Ref.14. Source: UniProtKB

protein homooligomerization

Inferred from direct assay Ref.8. Source: UniProtKB

   Cellular componentGolgi cis cisterna

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

axon

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral to membrane

Inferred from direct assay Ref.8. Source: UniProtKB

microsome

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionGTP binding

Inferred from sequence or structural similarity. Source: UniProtKB

GTPase activity

Inferred from direct assay Ref.8. Source: UniProtKB

identical protein binding

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 558558Atlastin-1
PRO_0000190971

Regions

Topological domain1 – 449449Cytoplasmic Ref.8
Transmembrane450 – 47021Helical; Potential
Topological domain4711Lumenal Potential
Transmembrane472 – 49221Helical; Potential
Topological domain493 – 55866Cytoplasmic Ref.8
Nucleotide binding74 – 818GTP Potential
Nucleotide binding146 – 1505GTP Potential
Region448 – 558111Sufficient for membrane association
Coiled coil412 – 43928 Potential

Amino acid modifications

Modified residue101Phosphoserine By similarity
Modified residue181Phosphothreonine By similarity
Modified residue221Phosphoserine Ref.13
Modified residue231Phosphoserine Ref.13

Natural variations

Natural variant431D → E. Ref.6
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.21
VAR_065508
Natural variant1571L → W in SPG3. Ref.19
VAR_065509
Natural variant1611A → P in SPG3; affects endoplasmic reticulum and Golgi morphology. Ref.11 Ref.17
VAR_019446
Natural variant1931F → C. Ref.6
Corresponds to variant rs17850683 [ dbSNP | Ensembl ].
VAR_058964
Natural variant2171R → Q in SPG3; alters endoplasmic reticulum morphology. Ref.12 Ref.15
VAR_017146
Natural variant2391R → C in SPG3; affects endoplasmic reticulum and Golgi morphology. Ref.1 Ref.11
VAR_017147
Natural variant2471H → P in SPG3. Ref.17
VAR_019447
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.21
VAR_065510
Natural variant4081M → V in SPG3. Ref.16
VAR_065511
Natural variant4151R → W in SPG3. Ref.18
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.
VAR_065513

Experimental info

Mutagenesis801K → A: Alters endoplasmic reticulum morphogenesis. Ref.12
Mutagenesis1511F → S: Affects endoplasmic reticulum and Golgi morphology. Ref.11
Mutagenesis1621T → P: Affects endoplasmic reticulum and Golgi morphology. Ref.11
Mutagenesis3981S → Y: Affects endoplasmic reticulum and Golgi morphology. Ref.11
Mutagenesis4951R → W: Affects endoplasmic reticulum and Golgi morphology. Ref.11

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8WXF7 [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

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: 11685207] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 12387898] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thalamus.
[4]"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: 12508121] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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].
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLU-43 AND CYS-193.
Tissue: Eye.
[7]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.
Tissue: Brain.
[8]"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: 14506257] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, REGION, TOPOLOGY, SUBUNIT.
[9]"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: 16339213] [Abstract]
Cited for: INTERACTION WITH SPAST, SUBCELLULAR LOCATION.
[10]"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: 16815977] [Abstract]
Cited for: INTERACTION WITH SPAST.
[11]"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: 17321752] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS SPAG3 PRO-161 AND CYS-239, MUTAGENESIS OF PHE-151; THR-162; SER-398 AND ARG-495, INTERACTION WITH TMED2, TISSUE SPECIFICITY.
[12]"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: 18270207] [Abstract]
Cited for: FUNCTION, CHARACTERIZATION OF VARIANT SPAG3 GLN-217, MUTAGENESIS OF LYS-80, TISSUE SPECIFICITY.
[13]"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: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-23, MASS SPECTROMETRY.
Tissue: Platelet.
[14]"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: 19665976] [Abstract]
Cited for: FUNCTION, INTERACTION WITH REEP5; RTN3 AND RTN4, SUBCELLULAR LOCATION.
[15]"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: 12112092] [Abstract]
Cited for: VARIANT SPG3 GLN-217.
[16]"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: 12939451] [Abstract]
Cited for: VARIANT SPG3 VAL-408.
[17]"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: 14695538] [Abstract]
Cited for: VARIANTS SPG3 PRO-161 AND PRO-247.
[18]"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: 15184642] [Abstract]
Cited for: VARIANT SPG3 TRP-415.
[19]"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: 16533974] [Abstract]
Cited for: VARIANT SPG3 TRP-157.
[20]"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: 17427918] [Abstract]
Cited for: VARIANT SPG3 ASN-436 DEL, CHARACTERIZATION OF VARIANT SPG3 ASN-436 DEL.
[21]"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: 21194679] [Abstract]
Cited for: VARIANTS HSN1D GLN-66 AND LYS-355, CHARACTERIZATION OF VARIANTS HSN1D GLN-66 AND LYS-355.
+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.
AL118556 Genomic DNA. No translation available.
AL606834 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65706.1.
BC010708 mRNA. Translation: AAH10708.2.
AF131801 mRNA. Translation: AAD20047.1. Different initiation.
IPIIPI00103530.
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[»]
ProteinModelPortalQ8WXF7.
SMRQ8WXF7. Positions 29-438.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8WXF7. 7 interactions.
STRINGQ8WXF7.

PTM databases

PhosphoSiteQ8WXF7.

Polymorphism databases

DMDM37999727.

Proteomic databases

PRIDEQ8WXF7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358385; ENSP00000351155; ENSG00000198513.
GeneID51062.
KEGGhsa:51062.
UCSCuc001wyf.2. human.

Organism-specific databases

CTD51062.
GeneCardsGC14P050999.
H-InvDBHIX0011643.
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

GeneTreeENSGT00390000008959.
HOGENOMHBG443778.
HOVERGENHBG062891.
InParanoidQ8WXF7.
OMAATHRHLY.
OrthoDBEOG49078Q.
PhylomeDBQ8WXF7.

Gene expression databases

ArrayExpressQ8WXF7.
BgeeQ8WXF7.
CleanExHS_ATL1.
GenevestigatorQ8WXF7.
GermOnlineENSG00000198513. Homo sapiens.

Family and domain databases

InterProIPR003191. Guanylate-bd_C.
IPR015894. Guanylate-bd_N.
[Graphical view]
Gene3DG3DSA:1.20.1000.10. Guanylate-bd_C. 1 hit.
PfamPF02263. GBP. 1 hit.
[Graphical view]
SUPFAMSSF48340. GBP. 1 hit.
ProtoNetSearch...

Other

NextBio53649.
SOURCESearch...

Entry information

Entry nameATLA1_HUMAN
AccessionPrimary (citable) accession number: Q8WXF7
Secondary accession number(s): A6NND5 expand/collapse secondary AC list , A8K2C0, O95890, Q96FK0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: March 1, 2002
Last modified: January 25, 2012
This is version 90 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

Human chromosome 14

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families