Q8WXF7 (ATLA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ATL1
Synonyms:	GBP3, SPG3A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	558 AA.
Sequence status	Complete.
Protein existence	Evidence 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.9 Ref.12 Ref.13 Ref.15
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. Interacts with REEP1. Ref.2 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Cell projection › axon 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 autosomal dominant 3 (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.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Hereditary sensory neuropathy 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.24
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 component	Cell projection Endoplasmic reticulum Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Hereditary spastic paraplegia Neurodegeneration Neuropathy
Domain	Coiled coil Transmembrane Transmembrane helix
Ligand	GTP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axonogenesis 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.15. Source: UniProtKB protein homooligomerization Inferred from direct assay Ref.9. Source: UniProtKB
Cellular_component	Golgi 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.9. Source: UniProtKB
Molecular_function	GTP binding Inferred from sequence or structural similarity. Source: UniProtKB GTPase activity Inferred from direct assay Ref.9. Source: UniProtKB identical protein binding Inferred from direct assay Ref.9. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Reep5	Q60870	2	EBI-2410266,EBI-2410304	From a different organism.
Rtn3	Q9ES97-3	3	EBI-2410266,EBI-1487798	From a different organism.
RTN4	Q9NQC3-1	2	EBI-2410266,EBI-715972
Rtn4	Q9JK11-3	2	EBI-2410266,EBI-920002	From 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 558

558

Atlastin-1

PRO_0000190971

Regions

Topological domain

1 – 449

449

Cytoplasmic Ref.9

Transmembrane

450 – 470

21

Helical; Potential

Topological domain

471

1

Lumenal Potential

Transmembrane

472 – 492

21

Helical; Potential

Topological domain

493 – 558

66

Cytoplasmic Ref.9

Nucleotide binding

74 – 81

8

GTP Potential

Nucleotide binding

146 – 150

5

GTP Potential

Region

448 – 558

111

Sufficient for membrane association

Coiled coil

412 – 439

28

Potential

Amino acid modifications

Modified residue

10

1

Phosphoserine By similarity

Modified residue

22

1

Phosphoserine By similarity

Modified residue

23

1

Phosphoserine By similarity

Natural variations

Alternative sequence

518 – 522

5

Missing in isoform 2.

VSP_044864

Natural variant

43

1

D → E. Ref.7
Corresponds to variant rs17850684 [ dbSNP | Ensembl ].

VAR_058963

Natural variant

66

1

E → Q in HSN1D; shows no significant changes in GTPase activity and no changes in endoplasmic reticulum morphology. Ref.24

VAR_065508

Natural variant

154

1

Q → E in SPG3. Ref.23

VAR_067655

Natural variant

157

1

L → W in SPG3. Ref.21

VAR_065509

Natural variant

161

1

A → P in SPG3; affects endoplasmic reticulum and Golgi morphology. Ref.12 Ref.19

VAR_019446

Natural variant

193

1

F → C. Ref.7
Corresponds to variant rs17850683 [ dbSNP | Ensembl ].

VAR_058964

Natural variant

196

1

Y → C in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.25

VAR_067656

Natural variant

217

1

R → Q in SPG3; alters endoplasmic reticulum morphology. Ref.13 Ref.17

VAR_017146

Natural variant

239

1

R → C in SPG3; affects endoplasmic reticulum and Golgi morphology. Ref.1 Ref.12 Ref.23 Ref.25

VAR_017147

Natural variant

247

1

H → P in SPG3. Ref.19

VAR_019447

Natural variant

253

1

V → I in SPG3. Ref.23 Ref.25

VAR_067657

Natural variant

258

1

H → R in SPG3. Ref.1

VAR_017148

Natural variant

259

1

S → Y in SPG3. Ref.1

VAR_017149

Natural variant

355

1

N → K in HSN1D; the mutant protein has decreased GTPase activity compared to wild-type and causes disruption of endoplasmic reticulum network morphology. Ref.24

VAR_065510

Natural variant

408

1

M → V in SPG3. Ref.18

VAR_065511

Natural variant

413

1

F → V in SPG3. Ref.23

VAR_067658

Natural variant

415

1

R → W in SPG3. Ref.20 Ref.23

VAR_065512

Natural variant

436

1

Missing 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.22

VAR_065513

Natural variant

440

1

N → T in SPG3. Ref.23

VAR_067659

Natural variant

495

1

R → W in SPG3; affects endoplasmic reticulum and Golgi morphology. Ref.12 Ref.23 Ref.25

VAR_067660

Experimental info

Mutagenesis

80

1

K → A: Alters endoplasmic reticulum morphogenesis. Ref.13

Mutagenesis

151

1

F → S: Affects endoplasmic reticulum and Golgi morphology. Ref.12

Mutagenesis

162

1

T → P: Affects endoplasmic reticulum and Golgi morphology. Ref.12

Mutagenesis

398

1

S → Y: Affects endoplasmic reticulum and Golgi morphology. Ref.12

Secondary structure

1

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558

Helix Strand Turn

Details...

Beta strand

34 – 40

7

Turn

42 – 44

3

Beta strand

46 – 48

3

Helix

50 – 57

8

Turn

60 – 64

5

Beta strand

65 – 75

11

Beta strand

76 – 79

4

Helix

80 – 92

13

Turn

93 – 95

3

Turn

97 – 100

4

Beta strand

115 – 117

3

Beta strand

122 – 128

7

Beta strand

130 – 133

4

Beta strand

135 – 137

3

Beta strand

139 – 147

9

Beta strand

152 – 156

5

Helix

157 – 170

14

Beta strand

172 – 181

10

Helix

184 – 200

17

Beta strand

208 – 217

10

Turn

222 – 224

3

Helix

229 – 240

12

Helix

248 – 260

13

Beta strand

261 – 268

8

Helix

274 – 278

5

Helix

286 – 288

3

Helix

291 – 305

15

Turn

307 – 309

3

Helix

322 – 337

16

Beta strand

338 – 341

4

Helix

347 – 375

29

Beta strand

377 – 380

4

Helix

384 – 404

21

Helix

410 – 438

29

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 68A33C39DD43504C	FASTA	558	63,544
	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
	Isoform 2 [UniParc]. Checksum: 663877DBC4B1FC67	FASTA	553	63,055
	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 AAALWDQALY KLYSAAATHR HLYHQAFPTP 550 KSESTEQSEK KKM

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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

GeneReviews

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.

IPI

IPI00103530.
IPI00479177.

RefSeq

NP_001121185.1. NM_001127713.1.
NP_056999.2. NM_015915.4.
NP_853629.2. NM_181598.3.

UniGene

Hs.584905.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q8WXF7.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-53502N.

IntAct

Q8WXF7. 7 interactions.

STRING

9606.ENSP00000351155.

PTM databases

PhosphoSite

Q8WXF7.

Polymorphism databases

DMDM

37999727.

Proteomic databases

PaxDb

Q8WXF7.

PRIDE

Q8WXF7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000354525; ENSP00000346522; ENSG00000198513.
ENST00000358385; ENSP00000351155; ENSG00000198513.
ENST00000441560; ENSP00000413675; ENSG00000198513.

GeneID

51062.

KEGG

hsa:51062.

UCSC

uc001wyf.4. human.

Organism-specific databases

CTD

51062.

GeneCards

GC14P050999.

HGNC

HGNC:11231. ATL1.

HPA

HPA027550.

MIM

182600. phenotype.
606439. gene.
613708. phenotype.

neXtProt

NX_Q8WXF7.

Orphanet

100984. Autosomal dominant spastic paraplegia type 3.
36386. Hereditary sensory and autonomic neuropathy type 1.

PharmGKB

PA36061.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG325148.

HOGENOM

HOG000234332.

HOVERGEN

HBG062891.

InParanoid

Q8WXF7.

OMA

RDRNSWG.

OrthoDB

EOG49078Q.

PhylomeDB

Q8WXF7.

Gene expression databases

ArrayExpress

Q8WXF7.

Bgee

Q8WXF7.

CleanEx

HS_ATL1.

Genevestigator

Q8WXF7.

GermOnline

ENSG00000198513. Homo sapiens.

Family and domain databases

InterPro

IPR003191. Guanylate-bd_C.
IPR015894. Guanylate-bd_N.
[Graphical view]

Pfam

PF02263. GBP. 1 hit.
[Graphical view]

SUPFAM

SSF48340. GBP. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q8WXF7.

GenomeRNAi

51062.

NextBio

53649.

SOURCE

Search...

Entry information

Entry name

ATLA1_HUMAN

Accession

Primary (citable) accession number: Q8WXF7
Secondary accession number(s): A6NND5 , A8K2C0, G5E9T1, O95890, Q69YH7, Q96FK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2003
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.