Q9UBP0 (SPAST_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Spastin
EC=3.6.4.3

Alternative name(s):
Spastic paraplegia 4 protein

Gene names

Name:	SPAST
Synonyms:	ADPSP, FSP2, KIAA1083, SPG4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	616 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and for completion of the abscission stage of cytokinesis. May also play a role in axon growth and the formation of axonal branches. Ref.5 Ref.6 Ref.11 Ref.12 Ref.18 Ref.23
Catalytic activity	ATP + H2O = ADP + phosphate. Ref.11 Ref.12 Ref.17 Ref.18 Ref.20
Subunit structure	Homohexamer. Binding to ATP stabilizes the homohexameric form. Binds to microtubules at least in part via the alpha-tubulin and beta-tubulin tails. The hexamer may adopt a ring conformation through which microtubules pass prior to being severed. Does not interact strongly with tubulin heterodimers. Interacts (via MIT domain) with CHMP1B; the interaction is direct. Interacts with ATL1, RTN1, SSNA1 and ZFYVE27. Ref.8 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.24
Subcellular location	Membrane; Single-pass membrane protein Potential. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton. Cytoplasm › perinuclear region. Endoplasmic reticulum. Endosome. Nucleus. Cytoplasm › cytoskeleton › spindle. Note: Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B. Enriched in the distal axons and branches of postmitotic neurons. Isoform 3 is the main endosomal form. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.23 Ref.24
Tissue specificity	Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. The short isoforms may predominate in brain and spinal cord. Ref.1
Developmental stage	Expressed in fetal brain, heart, kidney, liver, lung, skeletal muscle, spleen and thymus. Ref.1
Involvement in disease	Defects in SPAST are the cause of spastic paraplegia autosomal dominant type 4 (SPG4) [MIM:182601]. Spastic paraplegia is 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. SPG4 is the most common form of autosomal dominant spastic paraplegias. Ref.1 Ref.5 Ref.11 Ref.13 Ref.15 Ref.18 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46
Sequence similarities	Belongs to the AAA ATPase family. Spastin subfamily. Contains 1 MIT domain.
Biophysicochemical properties	Kinetic parameters: Kinetic parameters shown are for full length enzyme. KM=0.45 mM for ATP Ref.11 Ref.18 Vmax=1.2 nmol/min/µg enzyme

Ontologies

Keywords
Biological process	Cell cycle Cell division Differentiation Neurogenesis
Cellular component	Cytoplasm Cytoskeleton Endoplasmic reticulum Endosome Membrane Microtubule Nucleus
Coding sequence diversity	Alternative initiation Alternative promoter usage Alternative splicing Polymorphism
Disease	Hereditary spastic paraplegia Neurodegeneration
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ER to Golgi vesicle-mediated transport Inferred from mutant phenotype Ref.23. Source: UniProtKB cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell death Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW cytokinesis, completion of separation Inferred from mutant phenotype Ref.23. Source: UniProtKB microtubule bundle formation Inferred from direct assay Ref.12. Source: UniProtKB microtubule severing Inferred from direct assay Ref.11Ref.12Ref.18. Source: UniProtKB nervous system development Inferred from electronic annotation. Source: UniProtKB-KW protein hexamerization Inferred from direct assay Ref.18. Source: UniProtKB protein homooligomerization Inferred from direct assay Ref.18. Source: UniProtKB
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell endosome Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.9Ref.23. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW alpha-tubulin binding Inferred from physical interaction Ref.18. Source: UniProtKB beta-tubulin binding Inferred from physical interaction Ref.18. Source: UniProtKB microtubule binding Inferred from direct assay Ref.11Ref.12Ref.18. Source: UniProtKB microtubule-severing ATPase activity Inferred from direct assay Ref.11Ref.12Ref.18. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative promoter usage, alternative splicing and alternative initiation. [Align] [Select]

Note: Alternative promoter usage of a cryptic promoter in exon 1 can direct the synthesis of N-terminally truncated isoforms, which may also arise from alternative initiation.

Isoform 1 (identifier: Q9UBP0-1)

Also known as: Long; Long variant 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: Q9UBP0-2)

Also known as: Long variant 2;

The sequence of this isoform differs from the canonical sequence as follows:
     197-228: Missing.

Isoform 3 (identifier: Q9UBP0-3)

Also known as: Short; Short variant 1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-86: Missing.

Note: Produced by alternative promoter usage. May also be produced by alternative initiation at Met-87 of isoform 1. Major isoform.

Isoform 4 (identifier: Q9UBP0-4)

Also known as: Short variant 2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-86: Missing.
     197-228: Missing.

Note: Produced by alternative promoter usage and alternative splicing. May also be produced by alternative initiation at Met-87 of isoform 2.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 616

616

Spastin

PRO_0000084763

Regions

Transmembrane

57 – 77

21

Helical; Potential

Domain

119 – 195

77

MIT

Nucleotide binding

382 – 389

8

ATP Probable

Region

1 – 300

300

Required for interaction with RTN1

Region

1 – 194

194

Required for midbody localization

Region

1 – 80

80

Required for interaction with ATL1

Region

1 – 50

50

Required for nuclear localization

Region

50 – 87

38

Required for interaction with SSNA1 and microtubules

Region

112 – 196

85

Sufficient for interaction with CHMP1B

Region

114 – 200

87

Required for interaction with microtubules

Region

227 – 328

102

Sufficient for interaction with microtubules

Region

228 – 616

389

Sufficient for microtubule severing

Region

270 – 328

59

Required for interaction with microtubules and microtubule severing

Motif

4 – 11

8

Nuclear localization signal Ref.7

Motif

59 – 67

9

Nuclear export signal

Motif

309 – 312

4

Nuclear localization signal Ref.7

Amino acid modifications

Modified residue

268

1

Phosphoserine Ref.21 Ref.22

Modified residue

303

1

Phosphothreonine Ref.21

Modified residue

306

1

Phosphothreonine Ref.21

Natural variations

Alternative sequence

1 – 86

86

Missing in isoform 3 and isoform 4.

VSP_036650

Alternative sequence

197 – 228

32

Missing in isoform 2 and isoform 4.

VSP_000024

Natural variant

44

1

S → L Rare polymorphism which modifies the phenotype of SPG4 disease; may decrease the activity of the alternative promoter which directs the synthesis of isoform 3 and isoform 4. Ref.19 Ref.27 Ref.41 Ref.44

VAR_010194

Natural variant

45

1

P → Q Rare polymorphism which modifies the phenotype of SPG4 disease. Ref.41

VAR_027205

Natural variant

195

1

L → V in SPG4. Ref.45

VAR_026758

Natural variant

344

1

I → K in SPG4; abrogates ATPase activity and promotes microtubule binding. Ref.11 Ref.36

VAR_019448

Natural variant

347

1

Q → K in SPG4; promotes microtubule binding. Ref.11 Ref.33

VAR_027206

Natural variant

361

1

P → L in SPG4. Ref.44

VAR_027207

Natural variant

362

1

S → C in SPG4. Ref.1 Ref.26

VAR_010195

Natural variant

370

1

G → R in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. Ref.5 Ref.26

VAR_027208

Natural variant

378

1

L → Q in SPG4. Ref.39

VAR_019439

Natural variant

381

1

F → C in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. Ref.5 Ref.26

VAR_027209

Natural variant

386

1

N → K in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles. Ref.5 Ref.11 Ref.26

VAR_027210

Natural variant

386

1

N → S in SPG4. Ref.40

VAR_019440

Natural variant

388

1

K → R in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles and impairs traffic from the ER to Golgi. Ref.5 Ref.11 Ref.13 Ref.15 Ref.23 Ref.26 Ref.33

VAR_027211

Natural variant

390

1

M → V in SPG4. Ref.39

VAR_019441

Natural variant

399

1

S → L in SPG4. Ref.31

VAR_027212

Natural variant

404

1

Missing in SPG4.

VAR_019449

Natural variant

406

1

I → V in SPG4. Ref.45

VAR_026759

Natural variant

407

1

S → R in SPG4. Ref.32

VAR_019450

Natural variant

423

1

V → L in a breast cancer sample; somatic mutation. Ref.47

VAR_035902

Natural variant

424

1

R → G in SPG4. Ref.27

VAR_010196

Natural variant

426

1

L → V in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. Ref.5 Ref.26 Ref.31

VAR_027213

Natural variant

435

1

P → L in SPG4. Ref.46

VAR_027214

Natural variant

436

1

S → F in SPG4. Ref.28

VAR_027215

Natural variant

441

1

D → G in SPG4. Ref.25

VAR_027216

Natural variant

448

1

C → Y in SPG4; abrogates binding to the tail of beta-3-tubulin, abolishes microtubule severing and promotes the formation of thick microtubule bundles. Ref.1 Ref.5 Ref.18 Ref.26

VAR_010197

Natural variant

459

1

R → G in SPG4. Ref.42

VAR_027217

Natural variant

460

1

R → C in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. Ref.42

VAR_027218

Natural variant

460

1

R → L in SPG4. Ref.5 Ref.26

VAR_027219

Natural variant

470

1

D → V in SPG4. Ref.41
Corresponds to variant rs28939368 [ dbSNP | Ensembl ].

VAR_027220

Natural variant

485

1

A → V in SPG4. Ref.30

VAR_027221

Natural variant

489

1

P → L in SPG4. Ref.31

VAR_027222

Natural variant

493

1

D → G in SPG4. Ref.45

VAR_026760

Natural variant

499

1

R → C in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles. Ref.1 Ref.5 Ref.11 Ref.26 Ref.29 Ref.33

VAR_010198

Natural variant

499

1

R → H in SPG4. Ref.45

VAR_026761

Natural variant

503

1

R → L in SPG4. Ref.37

VAR_019442

Natural variant

503

1

R → W in SPG4. Ref.45

VAR_026762

Natural variant

512

1

E → D in SPG4. Ref.34

VAR_027223

Natural variant

515

1

Missing in SPG4.

VAR_019443

Natural variant

534

1

L → P in SPG4. Ref.38

VAR_019444

Natural variant

551

1

A → Y in SPG4; requires 2 nucleotide substitutions. Ref.32

VAR_019451

Natural variant

555

1

D → N in SPG4. Ref.26

VAR_027224

Natural variant

556

1

A → V in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. Ref.5 Ref.26

VAR_027225

Natural variant

559

1

G → D in SPG4. Ref.28 Ref.31

VAR_027226

Natural variant

562

1

R → G in SPG4. Ref.29 Ref.41

VAR_027227

Natural variant

562

1

R → Q in SPG4. Ref.31

VAR_027228

Natural variant

584

1

D → H in SPG4. Ref.27

VAR_010199

Natural variant

607

1

W → C in SPG4. Ref.45

VAR_026763

Natural variant

614

1

T → I in SPG4; variant form with congenital arachnoid cysts. Ref.43

VAR_019445

Natural variant

615

1

T → I in SPG4. Ref.32

VAR_019452

Experimental info

Mutagenesis

1

1

M → V: Cytoplasmic and nuclear. Ref.9

Mutagenesis

87

1

M → V: Exclusively cytoplasmic. Ref.9

Mutagenesis

120

1

H → D: Impairs binding to CHMP1B. Impairs midbody localization; when associated with D-124. Ref.24

Mutagenesis

124

1

F → A: Impairs binding to CHMP1B. Ref.24

Mutagenesis

124

1

F → D: Impairs binding to CHMP1B. Impairs midbody localization; when associated with D-120. Ref.24

Mutagenesis

388

1

K → A: Abrogates ATPase activity and abolishes microtubule severing. Ref.11

Mutagenesis

415

1

Y → A: Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing. Ref.18

Mutagenesis

442

1

E → Q: Abrogates ATP hydrolysis, abolishes microtubule severing, stabilizes the homohexameric form, and promotes microtubule binding and redistribution from the endosome to microtubules. Ref.11 Ref.17 Ref.18 Ref.20

Mutagenesis

451

1

R → G: Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing. Ref.18

Mutagenesis

457

1

A → E: Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin and abolishes microtubule severing. Ref.18

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

616

Helix Strand Turn

Details...

Helix

112 – 136

25

Helix

142 – 144

3

Helix

146 – 150

5

Helix

154 – 157

4

Helix

170 – 196

27

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) (Long variant 1) [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 75E5FC5787132B4C	FASTA	616	67,197
	10 20 30 40 50 60 MNSPGGRGKK KGSGGASNPV PPRPPPPCLA PAPPAAGPAP PPESPHKRNL YYFSYPLFVG 70 80 90 100 110 120 FALLRLVAFH LGLLFVWLCQ RFSRALMAAK RSSGAAPAPA SASAPAPVPG GEAERVRVFH 130 140 150 160 170 180 KQAFEYISIA LRIDEDEKAG QKEQAVEWYK KGIEELEKGI AVIVTGQGEQ CERARRLQAK 190 200 210 220 230 240 MMTNLVMAKD RLQLLEKMQP VLPFSKSQTD VYNDSTNLAC RNGHLQSESG AVPKRKDPLT 250 260 270 280 290 300 HTSNSLPRSK TVMKTGSAGL SGHHRAPSYS GLSMVSGVKQ GSGPAPTTHK GTPKTNRTNK 310 320 330 340 350 360 PSTPTTATRK KKDLKNFRNV DSNLANLIMN EIVDNGTAVK FDDIAGQDLA KQALQEIVIL 370 380 390 400 410 420 PSLRPELFTG LRAPARGLLL FGPPGNGKTM LAKAVAAESN ATFFNISAAS LTSKYVGEGE 430 440 450 460 470 480 KLVRALFAVA RELQPSIIFI DEVDSLLCER REGEHDASRR LKTEFLIEFD GVQSAGDDRV 490 500 510 520 530 540 LVMGATNRPQ ELDEAVLRRF IKRVYVSLPN EETRLLLLKN LLCKQGSPLT QKELAQLARM 550 560 570 580 590 600 TDGYSGSDLT ALAKDAALGP IRELKPEQVK NMSASEMRNI RLSDFTESLK KIKRSVSPQT 610 LEAYIRWNKD FGDTTV
	Isoform 2 (Long variant 2) [UniParc]. Checksum: 502F0FCB78ECED14	FASTA	584	63,606
	10 20 30 40 50 60 MNSPGGRGKK KGSGGASNPV PPRPPPPCLA PAPPAAGPAP PPESPHKRNL YYFSYPLFVG 70 80 90 100 110 120 FALLRLVAFH LGLLFVWLCQ RFSRALMAAK RSSGAAPAPA SASAPAPVPG GEAERVRVFH 130 140 150 160 170 180 KQAFEYISIA LRIDEDEKAG QKEQAVEWYK KGIEELEKGI AVIVTGQGEQ CERARRLQAK 190 200 210 220 230 240 MMTNLVMAKD RLQLLESGAV PKRKDPLTHT SNSLPRSKTV MKTGSAGLSG HHRAPSYSGL 250 260 270 280 290 300 SMVSGVKQGS GPAPTTHKGT PKTNRTNKPS TPTTATRKKK DLKNFRNVDS NLANLIMNEI 310 320 330 340 350 360 VDNGTAVKFD DIAGQDLAKQ ALQEIVILPS LRPELFTGLR APARGLLLFG PPGNGKTMLA 370 380 390 400 410 420 KAVAAESNAT FFNISAASLT SKYVGEGEKL VRALFAVARE LQPSIIFIDE VDSLLCERRE 430 440 450 460 470 480 GEHDASRRLK TEFLIEFDGV QSAGDDRVLV MGATNRPQEL DEAVLRRFIK RVYVSLPNEE 490 500 510 520 530 540 TRLLLLKNLL CKQGSPLTQK ELAQLARMTD GYSGSDLTAL AKDAALGPIR ELKPEQVKNM 550 560 570 580 SASEMRNIRL SDFTESLKKI KRSVSPQTLE AYIRWNKDFG DTTV
	Isoform 3 (Short) (Short variant 1) [UniParc]. Checksum: 0A4DB33B07801675	FASTA	530	58,009
	10 20 30 40 50 60 MAAKRSSGAA PAPASASAPA PVPGGEAERV RVFHKQAFEY ISIALRIDED EKAGQKEQAV 70 80 90 100 110 120 EWYKKGIEEL EKGIAVIVTG QGEQCERARR LQAKMMTNLV MAKDRLQLLE KMQPVLPFSK 130 140 150 160 170 180 SQTDVYNDST NLACRNGHLQ SESGAVPKRK DPLTHTSNSL PRSKTVMKTG SAGLSGHHRA 190 200 210 220 230 240 PSYSGLSMVS GVKQGSGPAP TTHKGTPKTN RTNKPSTPTT ATRKKKDLKN FRNVDSNLAN 250 260 270 280 290 300 LIMNEIVDNG TAVKFDDIAG QDLAKQALQE IVILPSLRPE LFTGLRAPAR GLLLFGPPGN 310 320 330 340 350 360 GKTMLAKAVA AESNATFFNI SAASLTSKYV GEGEKLVRAL FAVARELQPS IIFIDEVDSL 370 380 390 400 410 420 LCERREGEHD ASRRLKTEFL IEFDGVQSAG DDRVLVMGAT NRPQELDEAV LRRFIKRVYV 430 440 450 460 470 480 SLPNEETRLL LLKNLLCKQG SPLTQKELAQ LARMTDGYSG SDLTALAKDA ALGPIRELKP 490 500 510 520 530 EQVKNMSASE MRNIRLSDFT ESLKKIKRSV SPQTLEAYIR WNKDFGDTTV
	Isoform 4 (Short variant 2) [UniParc]. Checksum: F8BB32A6C8CB1D73	FASTA	498	54,418
	10 20 30 40 50 60 MAAKRSSGAA PAPASASAPA PVPGGEAERV RVFHKQAFEY ISIALRIDED EKAGQKEQAV 70 80 90 100 110 120 EWYKKGIEEL EKGIAVIVTG QGEQCERARR LQAKMMTNLV MAKDRLQLLE SGAVPKRKDP 130 140 150 160 170 180 LTHTSNSLPR SKTVMKTGSA GLSGHHRAPS YSGLSMVSGV KQGSGPAPTT HKGTPKTNRT 190 200 210 220 230 240 NKPSTPTTAT RKKKDLKNFR NVDSNLANLI MNEIVDNGTA VKFDDIAGQD LAKQALQEIV 250 260 270 280 290 300 ILPSLRPELF TGLRAPARGL LLFGPPGNGK TMLAKAVAAE SNATFFNISA ASLTSKYVGE 310 320 330 340 350 360 GEKLVRALFA VARELQPSII FIDEVDSLLC ERREGEHDAS RRLKTEFLIE FDGVQSAGDD 370 380 390 400 410 420 RVLVMGATNR PQELDEAVLR RFIKRVYVSL PNEETRLLLL KNLLCKQGSP LTQKELAQLA 430 440 450 460 470 480 RMTDGYSGSD LTALAKDAAL GPIRELKPEQ VKNMSASEMR NIRLSDFTES LKKIKRSVSP 490 QTLEAYIRWN KDFGDTTV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Spastin, a new AAA protein, is altered in the most frequent form of autosomal dominant spastic paraplegia." Hazan J., Fonknechten N., Mavel D., Paternotte C., Samson D., Artiguenave F., Davoine C.-S., Cruaud C., Durr A., Wincker P., Brottier P., Cattolico L., Barbe V., Burgunder J.-M., Prud'homme J.-F., Brice A., Fontaine B., Heilig R., Weissenbach J. Nat. Genet. 23:296-303(1999) [PubMed: 10610178] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANTS SPG4 CYS-362; TYR-448 AND CYS-499.
[2]	"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:197-205(1999) [PubMed: 10470851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[3]	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].
[4]	"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] (ISOFORM 2).
[5]	"Spastin, the protein mutated in autosomal dominant hereditary spastic paraplegia, is involved in microtubule dynamics." Errico A., Ballabio A., Rugarli E.I. Hum. Mol. Genet. 11:153-163(2002) [PubMed: 11809724] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS SPG4 ARG-370; CYS-381; LYS-386; ARG-388; VAL-426; TYR-448; LEU-460; CYS-499 AND VAL-556.
[6]	"The identification of a conserved domain in both spartin and spastin, mutated in hereditary spastic paraplegia." Ciccarelli F.D., Proukakis C., Patel H., Cross H., Azam S., Patton M.A., Bork P., Crosby A.H. Genomics 81:437-441(2003) [PubMed: 12676568] [Abstract] Cited for: DOMAIN MIT, PROBABLE FUNCTION.
[7]	"Identification of nuclear localisation sequences in spastin (SPG4) using a novel Tetra-GFP reporter system." Beetz C., Brodhun M., Moutzouris K., Kiehntopf M., Berndt A., Lehnert D., Deufel T., Bastmeyer M., Schickel J. Biochem. Biophys. Res. Commun. 318:1079-1084(2004) [PubMed: 15147984] [Abstract] Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL.
[8]	"Spastin interacts with the centrosomal protein NA14, and is enriched in the spindle pole, the midbody and the distal axon." Errico A., Claudiani P., D'Addio M., Rugarli E.I. Hum. Mol. Genet. 13:2121-2132(2004) [PubMed: 15269182] [Abstract] Cited for: INTERACTION WITH SSNA1 AND MICROTUBULES, SUBCELLULAR LOCATION.
[9]	"Spastin subcellular localization is regulated through usage of different translation start sites and active export from the nucleus." Claudiani P., Riano E., Errico A., Andolfi G., Rugarli E.I. Exp. Cell Res. 309:358-369(2005) [PubMed: 16026783] [Abstract] Cited for: ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNALS, MUTAGENESIS OF MET-1 AND MET-87.
[10]	"The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B." Reid E., Connell J.W., Edwards T.L., Duley S., Brown S.E., Sanderson C.M. Hum. Mol. Genet. 14:19-38(2005) [PubMed: 15537668] [Abstract] Cited for: INTERACTION WITH CHMP1B, SUBCELLULAR LOCATION.
[11]	"Linking axonal degeneration to microtubule remodeling by Spastin-mediated microtubule severing." Evans K.J., Gomes E.R., Reisenweber S.M., Gundersen G.G., Lauring B.P. J. Cell Biol. 168:599-606(2005) [PubMed: 15716377] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-388 AND GLU-442, CHARACTERIZATION OF VARIANTS SPG4 LYS-344; LYS-347; LYS-386; ARG-388 AND CYS-499.
[12]	"Human spastin has multiple microtubule-related functions." Salinas S., Carazo-Salas R.E., Proukakis C., Cooper J.M., Weston A.E., Schiavo G., Warner T.T. J. Neurochem. 95:1411-1420(2005) [PubMed: 16219033] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION.
[13]	"Subcellular localization of spastin: implications for the pathogenesis of hereditary spastic paraplegia." Svenson I.K., Kloos M.T., Jacon A., Gallione C., Horton A.C., Pericak-Vance M.A., Ehlers M.D., Marchuk D.A. Neurogenetics 6:135-141(2005) [PubMed: 15891913] [Abstract] Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT SPG4 ARG-388.
[14]	"ZFYVE27 (SPG33), a novel spastin-binding protein, is mutated in hereditary spastic paraplegia." Mannan A.U., Krawen P., Sauter S.M., Boehm J., Chronowska A., Paulus W., Neesen J., Engel W. Am. J. Hum. Genet. 79:351-357(2006) [PubMed: 16826525] [Abstract] Cited for: INTERACTION WITH ZFYVE27.
[15]	"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 ATL1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT SPG4 ARG-388.
[16]	"Spastin, the most commonly mutated protein in hereditary spastic paraplegia interacts with Reticulon 1 an endoplasmic reticulum protein." Mannan A.U., Boehm J., Sauter S.M., Rauber A., Byrne P.C., Neesen J., Engel W. Neurogenetics 7:93-103(2006) [PubMed: 16602018] [Abstract] Cited for: INTERACTION WITH RTN1, SUBCELLULAR LOCATION.
[17]	"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: CATALYTIC ACTIVITY, INTERACTION WITH ATL1, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-442.
[18]	"Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing." White S.R., Evans K.J., Lary J., Cole J.L., Lauring B.P. J. Cell Biol. 176:995-1005(2007) [PubMed: 17389232] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, HOMOHEXAMERIZATION, INTERACTION WITH TUBULIN AND MICROTUBULES, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-415; GLU-442; ARG-451 AND ALA-457, CHARACTERIZATION OF VARIANT SPG4 TYR-448.
[19]	"A cryptic promoter in the first exon of the SPG4 gene directs the synthesis of the 60-kDa spastin isoform." Mancuso G., Rugarli E.I. BMC Biol. 6:31-31(2008) [PubMed: 18613979] [Abstract] Cited for: ALTERNATIVE PROMOTER USAGE, CHARACTERIZATION OF VARIANT LEU-44.
[20]	"Spastin oligomerizes into a hexamer and the mutant spastin (E442Q) redistribute the wild-type spastin into filamentous microtubule." Pantakani D.V.K., Swapna L.S., Srinivasan N., Mannan A.U. J. Neurochem. 106:613-624(2008) [PubMed: 18410514] [Abstract] Cited for: CATALYTIC ACTIVITY, HOMOHEXAMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-442.
[21]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268; THR-303 AND THR-306, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[23]	"Spastin couples microtubule severing to membrane traffic in completion of cytokinesis and secretion." Connell J.W., Lindon C., Luzio J.P., Reid E. Traffic 10:42-56(2009) [PubMed: 19000169] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT SPG4 ARG-388.
[24]	"Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B." Yang D., Rismanchi N., Renvoise B., Lippincott-Schwartz J., Blackstone C., Hurley J.H. Nat. Struct. Mol. Biol. 15:1278-1286(2008) [PubMed: 18997780] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 112-196 IN COMPLEX WITH CHMP1B, INTERACTION WITH CHMP1B, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-120 AND PHE-124.
[25]	"Hereditary spastic paraplegia caused by mutations in the SPG4 gene." Buerger J., Fonknechten N., Hoeltzenbein M., Neumann L., Bratanoff E., Hazan J., Reis A. Eur. J. Hum. Genet. 8:771-776(2000) [PubMed: 11039577] [Abstract] Cited for: VARIANT SPG4 GLY-441.
[26]	"Spectrum of SPG4 mutations in autosomal dominant spastic paraplegia." Fonknechten N., Mavel D., Byrne P., Davoine C.-S., Cruaud C., Bonsch D., Samson D., Coutinho P., Hutchinson M., McMonagle P., Burgunder J.-M., Tartaglione A., Heinzlef O., Feki I., Deufel T., Parfrey N., Brice A., Fontaine B. , Prud'homme J.-F., Weissenbach J., Duerr A., Hazan J. Hum. Mol. Genet. 9:637-644(2000) [PubMed: 10699187] [Abstract] Cited for: VARIANTS SPG4 CYS-362; ARG-370; CYS-381; LYS-386; ARG-388; VAL-426; TYR-448; LEU-460; CYS-499; ASN-555 AND VAL-556.
[27]	"Mutation analysis of the spastin gene (SPG4) in patients with hereditary spastic paraparesis." Lindsey J.C., Lusher M.E., McDermott C.J., White K.D., Reid E., Rubinsztein D.C., Bashir R., Hazan J., Shaw P.J., Bushby K.M.D. J. Med. Genet. 37:759-765(2000) [PubMed: 11015453] [Abstract] Cited for: VARIANTS SPG4 LEU-44; GLY-424 AND HIS-584.
[28]	"Novel mutations in spastin gene and absence of correlation with age at onset of symptoms." Hentati A., Deng H.-X., Zhai H., Chen W., Yang Y., Hung W.-Y., Azim A.C., Bohlega S., Tandan R., Warner C., Laing N.G., Cambi F., Mitsumoto H., Roos R.P., Boustany R.-M.N., Ben-Hamida M., Hentati F., Siddique T. Neurology 55:1388-1390(2000) [PubMed: 11087788] [Abstract] Cited for: VARIANTS SPG4 PHE-436 AND ASP-559.
[29]	"Identification and expression analysis of spastin gene mutations in hereditary spastic paraplegia." Svenson I.K., Ashley-Koch A.E., Gaskell P.C., Riney T.J., Cumming W.J.K., Kingston H.M., Hogan E.L., Boustany R.-M.N., Vance J.M., Nance M.A., Pericak-Vance M.A., Marchuk D.A. Am. J. Hum. Genet. 68:1077-1085(2001) [PubMed: 11309678] [Abstract] Cited for: VARIANTS SPG4 CYS-499 AND GLY-562.
[30]	"A Japanese SPG4 family with a novel missense mutation of the SPG4 gene: intrafamilial variability in age at onset and clinical severity." Namekawa M., Takiyama Y., Sakoe K., Nagaki H., Shimazaki H., Yoshimura M., Ikeguchi K., Nakano I., Nishizawa M. Acta Neurol. Scand. 106:387-391(2002) [PubMed: 12460147] [Abstract] Cited for: VARIANT SPG4 VAL-485.
[31]	"Spectrum of SPG4 mutations in a large collection of North American families with hereditary spastic paraplegia." Meijer I.A., Hand C.K., Cossette P., Figlewicz D.A., Rouleau G.A. Arch. Neurol. 59:281-286(2002) [PubMed: 11843700] [Abstract] Cited for: VARIANTS SPG4 LEU-399; VAL-426; LEU-489; ASP-559 AND GLN-562.
[32]	"Mutation analysis of the spastin gene (SPG4) in patients in Germany with autosomal dominant hereditary spastic paraplegia." Sauter S.M., Miterski B., Klimpe S., Boensch D., Schoels L., Visbeck A., Papke T., Hopf H.C., Engel W., Deufel T., Epplen J.T., Neesen J. Hum. Mutat. 20:127-132(2002) [PubMed: 12124993] [Abstract] Cited for: VARIANTS SPG4 ARG-407; TYR-551 AND ILE-615.
[33]	"Spastin gene mutation in Japanese with hereditary spastic paraplegia." Yabe I., Sasaki H., Tashiro K., Matsuura T., Takegami T., Satoh T. J. Med. Genet. 39:E46-E46(2002) [PubMed: 12161613] [Abstract] Cited for: VARIANTS SPG4 LYS-347; ARG-388 AND CYS-499.
[34]	"Missense and splice site mutations in SPG4 suggest loss-of-function in dominant spastic paraplegia." Patrono C., Casali C., Tessa A., Cricchi F., Fortini D., Carrozzo R., Siciliano G., Bertini E., Santorelli F.M. J. Neurol. 249:200-205(2002) [PubMed: 11985387] [Abstract] Cited for: VARIANT SPG4 ASP-512.
[35]	"Three novel spastin (SPG4) mutations in families with autosomal dominant hereditary spastic paraplegia." Proukakis C., Hart P.E., Cornish A., Warner T.T., Crosby A.H. J. Neurol. Sci. 201:65-69(2002) [PubMed: 12163196] [Abstract] Cited for: VARIANT SPG4 PHE-404 DEL.
[36]	"A novel missense mutation (I344K) in the SPG4gene in a Korean family with autosomal-dominant hereditary spastic paraplegia." Ki C.S., Lee W.Y., Han do H., Sung D.H., Lee K.B., Lee K.A., Cho S.S., Cho S., Hwang H., Sohn K.M., Choi Y.J., Kim J.W. J. Hum. Genet. 47:473-477(2002) [PubMed: 12202986] [Abstract] Cited for: VARIANT SPG4 LYS-344.
[37]	"Screening of patients with hereditary spastic paraplegia reveals seven novel mutations in the SPG4 (Spastin) gene." Proukakis C., Auer-Grumbach M., Wagner K., Wilkinson P.A., Reid E., Patton M.A., Warner T.T., Crosby A.H. Hum. Mutat. 21:170-170(2003) [PubMed: 12552568] [Abstract] Cited for: VARIANT SPG4 LEU-503.
[38]	"Novel spastin mutations and their expression analysis in two Italian families." Molon A., Montagna P., Angelini C., Pegoraro E. Eur. J. Hum. Genet. 11:710-713(2003) [PubMed: 12939659] [Abstract] Cited for: VARIANT SPG4 PRO-534.
[39]	"Three novel mutations of the spastin gene in Chinese patients with hereditary spastic paraplegia." Tang B., Zhao G., Xia K., Pan Q., Luo W., Shen L., Long Z., Dai H., Zi X., Jiang H. Arch. Neurol. 61:49-55(2004) [PubMed: 14732620] [Abstract] Cited for: VARIANTS SPG4 GLN-378; VAL-390 AND LEU-515 DEL.
[40]	"Hereditary spastic paraplegia: clinical genetic study of 15 families." Orlacchio A., Kawarai T., Totaro A., Errico A., St George-Hyslop P.H., Rugarli E.I., Bernardi G. Arch. Neurol. 61:849-855(2004) [PubMed: 15210521] [Abstract] Cited for: VARIANT SPG4 SER-386.
[41]	"Intragenic modifiers of hereditary spastic paraplegia due to spastin gene mutations." Svenson I.K., Kloos M.T., Gaskell P.C., Nance M.A., Garbern J.Y., Hisanaga S., Pericak-Vance M.A., Ashley-Koch A.E., Marchuk D.A. Neurogenetics 5:157-164(2004) [PubMed: 15248095] [Abstract] Cited for: VARIANTS SPG4 VAL-470 AND GLY-562, VARIANTS LEU-44 AND GLN-45.
[42]	"Two novel mutations in the spastin gene (SPG4) found by DHPLC mutation analysis." Falco M., Scuderi C., Musumeci S., Sturnio M., Neri M., Bigoni S., Caniatti L., Fichera M. Neuromuscul. Disord. 14:750-753(2004) [PubMed: 15482961] [Abstract] Cited for: VARIANTS SPG4 GLY-459 AND CYS-460.
[43]	"A new SPG4 mutation in a variant form of spastic paraplegia with congenital arachnoid cysts." Orlacchio A., Gaudiello F., Totaro A., Floris R., St George-Hyslop P.H., Bernardi G., Kawarai T. Neurology 62:1875-1878(2004) [PubMed: 15159500] [Abstract] Cited for: VARIANT SPG4 ILE-614.
[44]	"Infantile hereditary spastic paraparesis due to codominant mutations in the spastin gene." Chinnery P.F., Keers S.M., Holden M.J., Ramesh V., Dalton A. Neurology 63:710-712(2004) [PubMed: 15326248] [Abstract] Cited for: VARIANTS SPG4 LEU-44 AND LEU-361.
[45]	"Eight novel mutations in SPG4 in a large sample of patients with hereditary spastic paraplegia." Crippa F., Panzeri C., Martinuzzi A., Arnoldi A., Redaelli F., Tonelli A., Baschirotto C., Vazza G., Mostacciuolo M.L., Daga A., Orso G., Profice P., Trabacca A., D'Angelo M.G., Comi G.P., Galbiati S., Lamperti C., Bonato S. , Pandolfo M., Meola G., Musumeci O., Toscano A., Trevisan C.P., Bresolin N., Bassi M.T. Arch. Neurol. 63:750-755(2006) [PubMed: 16682546] [Abstract] Cited for: VARIANTS SPG4 VAL-195; VAL-406; GLY-493; HIS-499; TRP-503 AND CYS-607.
[46]	"Novel spastin (SPG4) mutations in Italian patients with hereditary spastic paraplegia." Magariello A., Muglia M., Patitucci A., Mazzei R., Conforti F.L., Gabriele A.L., Sprovieri T., Ungaro C., Gambardella A., Mancuso M., Siciliano G., Branca D., Aguglia U., de Angelis M.V., Longo K., Quattrone A. Neuromuscul. Disord. 16:387-390(2006) [PubMed: 16684598] [Abstract] Cited for: VARIANT SPG4 LEU-435.
[47]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-423.
+	Additional computationally mapped references.

Web resources

GeneReviews

Protein Spotlight

The making of crooked - Issue 104 of April 2009

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ246001 mRNA. Translation: CAB60141.1.
AJ246003 Genomic DNA. Translation: CAB60208.1.
AB029006 mRNA. Translation: BAA83035.1.
CH471053 Genomic DNA. Translation: EAX00462.1.
BC150260 mRNA. Translation: AAI50261.1.

IPI

IPI00002707.
IPI00219816.
IPI00923524.
IPI00923553.

RefSeq

NP_055761.2. NM_014946.3.
NP_955468.1. NM_199436.1.

UniGene

Hs.468091.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3EAB	X-ray	2.50	A/B/C/D/E/F	112-196	[»]

ProteinModelPortal

Q9UBP0.

SMR

Q9UBP0. Positions 112-196, 324-608.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UBP0. 2 interactions.

STRING

Q9UBP0.

PTM databases

PhosphoSite

Q9UBP0.

Polymorphism databases

DMDM

12230611.

Proteomic databases

PeptideAtlas

Q9UBP0.

PRIDE

Q9UBP0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000315285; ENSP00000320885; ENSG00000021574.

GeneID

6683.

KEGG

hsa:6683.

UCSC

uc002roc.1. human.
uc002rod.1. human.

Organism-specific databases

CTD

6683.

GeneCards

GC02P032288.

H-InvDB

HIX0001953.

HGNC

HGNC:11233. SPAST.

HPA

HPA017311.

MIM

182601. phenotype.
604277. gene.

neXtProt

NX_Q9UBP0.

Orphanet

100985. Autosomal dominant spastic paraplegia type 4.

PharmGKB

PA36063.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13108.

GeneTree

ENSGT00570000078874.

HOGENOM

HBG724153.

HOVERGEN

HBG108502.

InParanoid

Q9UBP0.

OMA

THKSTPK.

OrthoDB

EOG4NZTTF.

PhylomeDB

Q9UBP0.

Gene expression databases

ArrayExpress

Q9UBP0.

Bgee

Q9UBP0.

CleanEx

HS_SPAST.

Genevestigator

Q9UBP0.

Family and domain databases

InterPro

IPR003593. ATPase_AAA+_core.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR007330. MIT.
IPR017179. Spastin.
[Graphical view]

KO

K13254.

Pfam

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

PIRSF

PIRSF037338. Spastin. 1 hit.

SMART

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

PROSITE

PS00674. AAA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

26047.

SOURCE

Search...

Entry information

Entry name

SPAST_HUMAN

Accession

Primary (citable) accession number: Q9UBP0
Secondary accession number(s): A7E2A7, Q9UPR9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 110 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.