Reviewed, UniProtKB/Swiss-Prot Q8I0P1 (SPAST_DROME)

Names and origin

Protein names

Recommended name:
    Spastin
    EC=3.6.4.3
Alternative name(s):
    D-Spastin
    Dm-Spastin
    Dspastin

Gene names

Name:	spas
ORF Names:	CG5977

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	758 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13
Catalytic activity	ATP + H2O = ADP + phosphate. Ref.8 Ref.13
Subunit structure	Homohexamer. The homohexamer is stabilized by ATP-binding. The homohexamer may adopt a ring conformation through which microtubules pass prior to being severed. Interacts with microtubules. Interacts with atl; may be involved in microtubule dynamics. Ref.8 Ref.12 Ref.13
Subcellular location	Membrane; Single-pass membrane protein Potential. Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Note: Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles.
Developmental stage	Maternally expressed in early embryogenesis with high expression until blastoderm. At the cell formation stage, strongly expressed near the basal part of the cell layer underlying the surface. During germband extension and stomodeal plate formation, expressed in the ventral head and trunk ectoderm, as well as in cells near the cephalic furrow and in the invaginating hindgut and midgut primordia. After germband retraction and delamination of neuroblasts at stage 13, expressed in subsets of cells in all neuromeres of the CNS including those of the supraesophageal and subesophageal ganglia. In later embryonic stages expressed in cell clusters throughout the supraesophageal ganglion, with pronounced expression also seen in the subesophageal ganglion. In the ventral nerve cord (VNC), expressed in two broad longitudinal stripes located laterally, and weakly expressed in some midline cells. Also expressed in some sensory head organs of the peripheral nervous system (PNS), most probably the Bolwigs organs and/or the dorsal organs. Expressed in the developing larval neuromusculature, muscles and neuronal axons. Enriched in neuromuscular junctions throughout the muscles of the body wall. Enriched in punctate domains of synaptic boutons and excluded from interbouton axonal connections. Colocalizes with the synaptic vesicle pools. Ref.6 Ref.5
Disruption phenotype	Loss of protein expression throughout the embryo leads to pupal lethality. Loss of protein expression specifically in the nervous system causes synaptic undergrowth and a reduction in total synaptic area. Neuromuscular junction boutons are smaller and more numerous. Microtubule stability appears to be enhanced within neuronal axons and at neuromuscular junctions and synaptic currents are increased. Older flies exhibit numerous vacuoles in the neuropil and cortex. Adult coordination and locomotory behavior are compromised and lifespan is reduced. Ref.6 Ref.7 Ref.9
Sequence similarities	Belongs to the AAA ATPase family. Spastin subfamily. Contains 1 MIT domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Differentiation Mitosis Neurogenesis
Cellular component	Cytoplasm Cytoskeleton Membrane Microtubule
Domain	Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW locomotory behavior Ref.7 Inferred from mutant phenotype. Source: FlyBase microtubule cytoskeleton organization Ref.7 Inferred from mutant phenotype. Source: FlyBase microtubule severing Ref.13 Inferred from direct assay. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW nervous system development Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of microtubule depolymerization Ref.6 Ref.8 Ref.10 Ref.13 Inferred from direct assay. Source: UniProtKB
Cellular component	centrosome Ref.10 Inferred from direct assay. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW terminal button Ref.6 Inferred from direct assay. Source: FlyBase
Molecular function	ATP binding Inferred by curator. Source: UniProtKB alpha-tubulin binding Ref.13 Non-traceable author statement. Source: UniProtKB microtubule binding Ref.13 Inferred from direct assay. Source: UniProtKB microtubule-severing ATPase activity Ref.13 Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 758

758

Spastin

PRO_0000367144

Regions

Transmembrane

115 – 134

20

Potential

Domain

232 – 308

77

MIT

Nucleotide binding

523 – 530

8

ATP Probable

Region

1 – 210

210

Required for localization to punctate cytoplasmic foci

Region

1 – 159

159

Interaction with atl

Region

208 – 758

551

Sufficient for interaction with microtubules and microtubule severing

Region

443 – 455

13

Required for interaction with microtubules

Amino acid modifications

Modified residue

439

1

Phosphothreonine By similarity

Experimental info

Mutagenesis

465

1

L → A: Strongly impairs microtubule severing and weakly impairs ATPase activity; when associated with A-471 and A-472. Ref.13

Mutagenesis

465

1

L → F: Strongly impairs microtubule severing and weakly impairs ATPase activity. Ref.13

Mutagenesis

469

1

I → A: Strongly impairs microtubule severing and ATPase activity but does not affect interaction with microtubules; when associated with A-473 and A-474. Ref.13

Mutagenesis

471

1

D → A: Strongly impairs microtubule severing and weakly impairs ATPase activity; when associated with A-465 and A-472. Ref.13

Mutagenesis

472

1

E → A: Strongly impairs microtubule severing and weakly impairs ATPase activity; when associated with A-465 and A-471. Ref.13

Mutagenesis

473

1

I → A: Strongly impairs microtubule severing and ATPase activity but does not affect interaction with microtubules; when associated with A-469 and A-474. Ref.13

Mutagenesis

474

1

V → A: Strongly impairs microtubule severing and ATPase activity but does not affect interaction with microtubules; when associated with A-469 and A-473. Ref.13

Mutagenesis

503

1

S → C: Impairs microtubule severing and ATPase activity. Ref.8

Mutagenesis

511

1

G → R: Abrogates microtubule severing and strongly impairs ATPase activity. Ref.13

Mutagenesis

529

1

K → R: Abrogates microtubule severing and ATPase activity. Induces accumulation of hyperstable microtubules at the neuromuscular junction presynpatic terminal and reduces synaptic area. Reduces adult lifespan and impairs climbing activity. Ref.8 Ref.9

Mutagenesis

555

1

K → A: Abrogates microtubule severing. Ref.13

Mutagenesis

556

1

Y → A: Abrogates microtubule severing. Ref.13

Mutagenesis

557

1

V → A: Abrogates microtubule severing and impairs ATPase activity. Ref.13

Mutagenesis

558

1

G → A or V: Abrogates microtubule severing. Ref.13

Mutagenesis

559

1

D → A or R: Abrogates microtubule severing. Ref.13

Mutagenesis

560

1

G → A: Impairs microtubule severing. Ref.13

Mutagenesis

560

1

G → V: Abrogates microtubule severing. Ref.13

Mutagenesis

561

1

E → A or R: Abrogates microtubule severing. Ref.13

Mutagenesis

562

1

K → A or R: Abrogates microtubule severing.

Mutagenesis

583

1

E → A: Abrogates microtubule severing and ATPase activity. Ref.8 Ref.13

Mutagenesis

583

1

E → Q: Impairs interaction with microtubules and promotes hexamerization. Ref.8 Ref.13

Mutagenesis

589

1

S → Y: Impairs microtubule severing. Ref.13

Mutagenesis

591

1

R → A or E: Abrogates microtubule severing. Ref.13

Mutagenesis

595

1

E → A: Impairs microtubule severing. Ref.13

Mutagenesis

595

1

E → R: Abrogates microtubule severing. Ref.13

Mutagenesis

596

1

H → A: Impairs microtubule severing. Ref.13

Mutagenesis

596

1

H → D: Abrogates microtubule severing and impairs ATPase activity. Ref.13

Mutagenesis

596

1

H → Y: Abrogates microtubule severing. Ref.13

Mutagenesis

597

1

E → K: Impairs microtubule severing. Ref.13

Mutagenesis

598

1

A → L: Abrogates microtubule severing. Ref.13

Mutagenesis

601

1

R → E: Abrogates microtubule severing. Ref.13

Mutagenesis

601

1

R → L: Abrogates microtubule severing and strongly impairs ATPase activity. Ref.13

Mutagenesis

631

1

P → L: Abrogates microtubule severing. Ref.13

Mutagenesis

632

1

Q → A: Strongly impairs microtubule severing and weakly impairs ATPase activity. Ref.13

Mutagenesis

633

1

E → A: Weakly impairs microtubule severing and ATPase activity. Ref.13

Mutagenesis

633

1

E → R: Impairs microtubule severing. Ref.13

Mutagenesis

697

1

D → N: Weakly impairs microtubule severing and strongly impairs ATPase activity. Ref.8

Mutagenesis

704

1

R → Q: Abrogates microtubule severing. Ref.13

Mutagenesis

753

1

Y → A: Strongly impairs microtubule severing and ATPase activity. Ref.13

Sequence conflict

665

1

Q → E in AAN71010. Ref.3

Sequence conflict

665

1

Q → E in AAN71106. Ref.3

Secondary structure

1

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758

Helix Strand Turn

Details...

Helix

465 – 470

6

Turn

471 – 473

3

Helix

482 – 484

3

Helix

489 – 498

10

Helix

500 – 504

5

Helix

506 – 508

3

Beta strand

520 – 522

3

Helix

530 – 539

10

Beta strand

543 – 549

7

Turn

550 – 552

3

Beta strand

553 – 555

3

Helix

562 – 573

12

Beta strand

576 – 582

7

Helix

584 – 586

3

Helix

600 – 610

11

Beta strand

622 – 627

6

Helix

631 – 633

3

Helix

636 – 641

6

Beta strand

645 – 647

3

Helix

653 – 664

12

Helix

673 – 682

10

Helix

690 – 698

9

Helix

701 – 704

4

Helix

724 – 730

7

Helix

740 – 749

10

Sequences

	Sequence		Length	Mass (Da)
	Q8I0P1-1 [UniParc]. Last modified March 24, 2009. Version 2. Checksum: 406D075DCBD2A9CD	FASTA	758	82,749
	10 20 30 40 50 60 MVRTKNQSSS SSASSSSTKS PIKSSSGAGS SGGGLGGRQS THRSSSASNV AAVVAGGSSA 70 80 90 100 110 120 AGGGSSSNRR SPGSSPDGDD DTTTTDDLTP TTCSPRSGHH HSYGGYSSSV HKQNLYVVSF 130 140 150 160 170 180 PIIFLFNVLR SLIYQLFCIF RYLYGASTKV IYRPHRRDCN IEIVVQNSSK EQQQSLNHPS 190 200 210 220 230 240 ELNREGDGQE QQLSNQPQRF RPIQPLEMAA NRPGGGYSPG PGDPLLAKQK HHHRRAFEYI 250 260 270 280 290 300 SKALKIDEEN EGHKELAIEL YRKGIKELED GIAVDCWSGR GDVWDRAQRL HDKMQTNLSM 310 320 330 340 350 360 ARDRLHFLAL REQDLQMQRL SLKEKQKEEA QSKPQKTREP MLAGMTNEPM KLRVRSSGYG 370 380 390 400 410 420 PKATTSAQPT ASGRKLTIGS KRPVNLAVAN KSQTLPRNLG SKTSVGAVQR QPAKTAATPP 430 440 450 460 470 480 AVRRQFSSGR NTPPQRSRTP INNNGPSGSG ASTPVVSVKG VEQKLVQLIL DEIVEGGAKV 490 500 510 520 530 540 EWTDIAGQDV AKQALQEMVI LPSVRPELFT GLRAPAKGLL LFGPPGNGKT LLARAVATEC 550 560 570 580 590 600 SATFLNISAA SLTSKYVGDG EKLVRALFAV ARHMQPSIIF IDEVDSLLSE RSSSEHEASR 610 620 630 640 650 660 RLKTEFLVEF DGLPGNPDGD RIVVLAATNR PQELDEAALR RFTKRVYVSL PDEQTRELLL 670 680 690 700 710 720 NRLLQKQGSP LDTEALRRLA KITDGYSGSD LTALAKDAAL EPIRELNVEQ VKCLDISAMR 730 740 750 AITEQDFHSS LKRIRRSVAP QSLNSYEKWS QDYGDITI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Testis.
[4]	Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Identification of the Drosophila melanogaster homolog of the human spastin gene." Kammermeier L., Spring J., Stierwald M., Burgunder J.-M., Reichert H. Dev. Genes Evol. 213:412-415(2003) [PubMed: 12908108] [Abstract] Cited for: IDENTIFICATION, DEVELOPMENTAL STAGE.
[6]	"The hereditary spastic paraplegia gene, spastin, regulates microtubule stability to modulate synaptic structure and function." Trotta N., Orso G., Rossetto M.G., Daga A., Broadie K. Curr. Biol. 14:1135-1147(2004) [PubMed: 15242610] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[7]	"Drosophila spastin regulates synaptic microtubule networks and is required for normal motor function." Sherwood N.T., Sun Q., Xue M., Zhang B., Zinn K. PLoS Biol. 2:E429-E429(2004) [PubMed: 15562320] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[8]	"The Drosophila homologue of the hereditary spastic paraplegia protein, spastin, severs and disassembles microtubules." Roll-Mecak A., Vale R.D. Curr. Biol. 15:650-655(2005) [PubMed: 15823537] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-503; LYS-529; GLU-583 AND ASP-697.
[9]	"Disease-related phenotypes in a Drosophila model of hereditary spastic paraplegia are ameliorated by treatment with vinblastine." Orso G., Martinuzzi A., Rossetto M.G., Sartori E., Feany M., Daga A. J. Clin. Invest. 115:3026-3034(2005) [PubMed: 16276413] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-529.
[10]	"Three microtubule severing enzymes contribute to the 'Pacman-flux' machinery that moves chromosomes." Zhang D., Rogers G.C., Buster D.W., Sharp D.J. J. Cell Biol. 177:231-242(2007) [PubMed: 17452528] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-439, MASS SPECTROMETRY. Tissue: Embryo.
[12]	"Drosophila Atlastin regulates the stability of muscle microtubules and is required for synapse development." Lee M., Paik S.K., Lee M.-J., Kim Y.-J., Kim S., Nahm M., Oh S.-J., Kim H.-M., Yim J., Lee C.J., Bae Y.C., Lee S. Dev. Biol. 330:250-262(2009) [PubMed: 19341724] [Abstract] Cited for: FUNCTION, INTERACTION WITH ATL.
[13]	"Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin." Roll-Mecak A., Vale R.D. Nature 451:363-367(2008) [PubMed: 18202664] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 463-758, FUNCTION, CATALYTIC ACTIVITY, HOMOHEXAMERIZATION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-465; ILE-469; ASP-471; GLU-472; ILE-473; VAL-474; GLY-511; LYS-555; TYR-556; VAL-557; GLY-558; ASP-559; GLY-560; GLU-561; GLU-583; SER-589; ARG-591; GLU-595; HIS-596; GLU-597; ALA-598; ARG-601; PRO-631; GLN-632; GLU-633; ARG-704 AND TYR-753.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE014297 Genomic DNA. Translation: AAF56223.3.
AE014297 Genomic DNA. Translation: AAN13975.2.
AY069522 mRNA. Translation: AAL39667.1. Different initiation.
BT001254 mRNA. Translation: AAN71010.1.
BT001351 mRNA. Translation: AAN71106.1.
BT044258 mRNA. Translation: ACH92323.1.

RefSeq

NP_651206.3.
NP_732941.2.

UniGene

Dm.7035

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3B9P	X-ray	2.70	A	463-758	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8I0P1. 2 interactions.

STRING

Q8I0P1.

Genome annotation databases

Ensembl

FBtr0084533; FBpp0083918; FBgn0039141; Drosophila melanogaster. [Genome view]

GeneID

42846.

KEGG

dme:Dmel_CG5977.

UCSC

CG5977-RA. d. melanogaster.

Organism-specific databases

CTD

42846.

FlyBase

FBgn0039141. spas.

Phylogenomic databases

HOGENOM

Q8I0P1.

OMA

PIRELNV.

Gene expression databases

ArrayExpress

Q8I0P1.

Family and domain databases

InterPro

IPR003593. ATPase_AAA+_core.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR007330. MIT.
[Graphical view]

Pfam

PF00004. AAA. 1 hit.
PF04212. MIT. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
SM00745. MIT. 1 hit.
[Graphical view]

PROSITE

PS00674. AAA. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SPAST_DROME

Accession

Primary (citable) accession number: Q8I0P1
Secondary accession number(s): Q8IMX5, Q8T066

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	March 24, 2009
Last modified:	November 3, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project