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Protein

Spastin

Gene

SPAST

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated (PubMed:11809724, PubMed:15716377, PubMed:16219033, PubMed:17389232, PubMed:20530212, PubMed:22637577, PubMed:26875866). Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (PubMed:26875866). Severing activity is not dependent on tubulin acetylation or detyrosination (PubMed:26875866). Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex (PubMed:19000169, PubMed:21310966, PubMed:26040712). Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex (PubMed:21310966). Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase (PubMed:26040712). Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling (PubMed:23897888). Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing (PubMed:23897888). Probably plays a role in axon growth and the formation of axonal branches (PubMed:15716377).UniRule annotation11 Publications
Isoform 1: Involved in lipid metabolism by regulating the size and distribution of lipid droplets.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation6 Publications

Enzyme regulationi

Allosteric enzyme with a cooperative mechanism; at least two neighbor subunits influence each other strongly in spastin hexamers (PubMed:22637577). Microtubule binding promotes cooperative interactions among spastin subunits (PubMed:22637577). ATP-bound enzyme interacts strongly and cooperatively with microtubules; this interaction stimulates ATP hydrolysis (PubMed:23745751).UniRule annotation2 Publications

Kineticsi

Kinetic parameters shown are for full-length enzyme. N-terminally truncated spastin (residues 228-616), which has been shown to exhibit full severing activity, shows a basal ATP turnover rate of 0.78 sec(-1) in the absence of microtubules, a KM of 0.16 mM for ATP, and the ATP turnover rate is extrapolated to 3.83 sec(-1) in the presence of microtubules. ATPase activity shows non-Michaelis-Menten kinetics in the presence of microtubules, but is close to non-cooperative behavior in their absence (PubMed:22637577).1 Publication
  1. KM=0.45 mM for ATP3 Publications
  1. Vmax=1.2 nmol/min/µg enzyme3 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi382 – 389ATPUniRule annotation1 Publication8

GO - Molecular functioni

  • alpha-tubulin binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • beta-tubulin binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • microtubule-severing ATPase activity Source: UniProtKB
  • protein complex binding Source: ARUK-UCL

GO - Biological processi

  • anterograde axonal transport Source: UniProtKB
  • axonal transport of mitochondrion Source: UniProtKB
  • cell differentiation Source: UniProtKB-KW
  • cytokinetic process Source: UniProtKB
  • cytoskeleton-dependent cytokinesis Source: ARUK-UCL
  • ER to Golgi vesicle-mediated transport Source: UniProtKB
  • exit from mitosis Source: UniProtKB
  • membrane fission Source: UniProtKB
  • metabolic process Source: UniProtKB-KW
  • microtubule bundle formation Source: UniProtKB
  • microtubule severing Source: UniProtKB
  • mitotic cytokinesis Source: UniProtKB
  • mitotic spindle disassembly Source: UniProtKB
  • nervous system development Source: UniProtKB-KW
  • nuclear envelope reassembly Source: UniProtKB
  • positive regulation of cytokinesis Source: UniProtKB
  • protein hexamerization Source: UniProtKB
  • protein homooligomerization Source: UniProtKB

Keywordsi

Molecular functionDevelopmental protein, Hydrolase
Biological processCell cycle, Cell division, Differentiation, Neurogenesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.4.3. 2681.
SABIO-RKiQ9UBP0.

Names & Taxonomyi

Protein namesi
Recommended name:
Spastin1 PublicationUniRule annotation (EC:3.6.4.3UniRule annotation6 Publications)
Alternative name(s):
Spastic paraplegia 4 protein
Gene namesi
Name:SPASTUniRule annotationImported
Synonyms:ADPSP, FSP2, KIAA10831 Publication, SPG4UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000021574.11.
HGNCiHGNC:11233. SPAST.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 56CytoplasmicUniRule annotation1 PublicationAdd BLAST56
Intramembranei57 – 77HelicalUniRule annotation1 PublicationAdd BLAST21
Topological domaini78 – 616CytoplasmicUniRule annotation1 PublicationAdd BLAST539

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Endoplasmic reticulum, Endosome, Lipid droplet, Membrane, Microtubule, Nucleus

Pathology & Biotechi

Involvement in diseasei

Spastic paraplegia 4, autosomal dominant (SPG4)43 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:182601
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07582744 – 616Missing in SPG4. 1 PublicationAdd BLAST573
Natural variantiVAR_07582895A → T in SPG4. 1 Publication1
Natural variantiVAR_06762897P → T in SPG4; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs372005558Ensembl.1
Natural variantiVAR_075829112 – 616Missing in SPG4. 1 PublicationAdd BLAST505
Natural variantiVAR_075830135 – 616Missing in SPG4. 1 PublicationAdd BLAST482
Natural variantiVAR_067563162V → I in SPG4; unknown pathological significance. 2 PublicationsCorresponds to variant dbSNP:rs141944844Ensembl.1
Natural variantiVAR_026758195L → V in SPG4. 1 Publication1
Natural variantiVAR_067629201V → D in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_075831244 – 616Missing in SPG4. 1 PublicationAdd BLAST373
Natural variantiVAR_075832245 – 616Missing in SPG4. 1 PublicationAdd BLAST372
Natural variantiVAR_075833254 – 616Missing in SPG4. 1 PublicationAdd BLAST363
Natural variantiVAR_067631287Missing in SPG4. 1 Publication1
Natural variantiVAR_067632293P → L in SPG4. 1 PublicationCorresponds to variant dbSNP:rs773193617Ensembl.1
Natural variantiVAR_075834309R → H in SPG4. 1 PublicationCorresponds to variant dbSNP:rs202152835Ensembl.1
Natural variantiVAR_067633314L → S in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_079314328I → K in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_067634328I → L in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_019448344I → K in SPG4; abrogates ATPase activity and promotes microtubule binding. 2 PublicationsCorresponds to variant dbSNP:rs121908513Ensembl.1
Natural variantiVAR_027206347Q → K in SPG4; promotes microtubule binding. 2 Publications1
Natural variantiVAR_067564356E → K in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_067635360L → V in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_027207361P → L in SPG4. 1 Publication1
Natural variantiVAR_010195362S → C in SPG4. 2 PublicationsCorresponds to variant dbSNP:rs121908509Ensembl.1
Natural variantiVAR_075835363L → P in SPG4. 1 Publication1
Natural variantiVAR_075836364R → M in SPG4. 1 Publication1
Natural variantiVAR_067636364R → T in SPG4. 1 Publication1
Natural variantiVAR_067565365P → S in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_079315366E → K in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_075837368F → L in SPG4. 2 Publications1
Natural variantiVAR_079316368F → V in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_027208370G → R in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. 2 Publications1
Natural variantiVAR_075838372R → G in SPG4. 1 Publication1
Natural variantiVAR_079317372R → T in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_075839377G → E in SPG4. 1 Publication1
Natural variantiVAR_019439378L → Q in SPG4. 1 Publication1
Natural variantiVAR_067637378L → R in SPG4. 1 Publication1
Natural variantiVAR_067638380L → H in SPG4. 2 Publications1
Natural variantiVAR_027209381F → C in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. 2 Publications1
Natural variantiVAR_067566382G → R in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_027210386N → K in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles. 3 Publications1
Natural variantiVAR_019440386N → S in SPG4. 1 PublicationCorresponds to variant dbSNP:rs121908514Ensembl.1
Natural variantiVAR_079318386N → Y in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_027211388K → R in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles and impairs traffic from the ER to Golgi. 7 Publications1
Natural variantiVAR_079319390M → T in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_019441390M → V in SPG4. 1 PublicationCorresponds to variant dbSNP:rs797044850Ensembl.1
Natural variantiVAR_067639391L → P in SPG4. 1 Publication1
Natural variantiVAR_067640393 – 396Missing in SPG4. 1 Publication4
Natural variantiVAR_027212399S → L in SPG4. 4 Publications1
Natural variantiVAR_019449404Missing in SPG4. 1 Publication1
Natural variantiVAR_075840406I → R in SPG4. 1 Publication1
Natural variantiVAR_026759406I → V in SPG4. 1 PublicationCorresponds to variant dbSNP:rs587777757Ensembl.1
Natural variantiVAR_067567407S → I in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_019450407S → R in SPG4. 1 Publication1
Natural variantiVAR_067641409A → T in SPG4. 2 Publications1
Natural variantiVAR_067642410S → R in SPG4. 1 Publication1
Natural variantiVAR_067568413S → L in SPG4. 1 Publication1
Natural variantiVAR_079320418E → A in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_067569422L → F in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_010196424R → G in SPG4. 1 Publication1
Natural variantiVAR_067643426L → F in SPG4. 1 Publication1
Natural variantiVAR_027213426L → V in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. 4 Publications1
Natural variantiVAR_075841431 – 616Missing in SPG4. 1 PublicationAdd BLAST186
Natural variantiVAR_027214435P → L in SPG4. 1 Publication1
Natural variantiVAR_027215436S → F in SPG4. 1 Publication1
Natural variantiVAR_067644436S → P in SPG4. 1 Publication1
Natural variantiVAR_027216441D → G in SPG4. 1 PublicationCorresponds to variant dbSNP:rs121908512Ensembl.1
Natural variantiVAR_067645441D → N in SPG4. 1 Publication1
Natural variantiVAR_075842441D → V in SPG4. 1 Publication1
Natural variantiVAR_067570445S → N in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_010197448C → Y in SPG4; abrogates binding to the tail of beta-3-tubulin, abolishes microtubule severing and promotes the formation of thick microtubule bundles. 4 PublicationsCorresponds to variant dbSNP:rs121908510Ensembl.1
Natural variantiVAR_075843450R → S in SPG4. 1 Publication1
Natural variantiVAR_075844451Missing in SPG4. 1 Publication1
Natural variantiVAR_067571454E → K in SPG4. 1 Publication1
Natural variantiVAR_075845458S → R in SPG4. 1 Publication1
Natural variantiVAR_027217459R → G in SPG4. 1 Publication1
Natural variantiVAR_027218460R → C in SPG4. 2 PublicationsCorresponds to variant dbSNP:rs878854990Ensembl.1
Natural variantiVAR_027219460R → L in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. 2 Publications1
Natural variantiVAR_067572460R → S in SPG4. 3 Publications1
Natural variantiVAR_075846461L → P in SPG4. 1 Publication1
Natural variantiVAR_067646463T → A in SPG4. 1 Publication1
Natural variantiVAR_067647464E → A in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_027220470D → V in SPG4. 1 PublicationCorresponds to variant dbSNP:rs28939368Ensembl.1
Natural variantiVAR_079321470D → Y in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_067573482V → L in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_079322485A → T in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_027221485A → V in SPG4. 1 Publication1
Natural variantiVAR_027222489P → L in SPG4. 1 Publication1
Natural variantiVAR_075847490 – 616Missing in SPG4. 1 PublicationAdd BLAST127
Natural variantiVAR_067648492L → F in SPG4. 1 Publication1
Natural variantiVAR_026760493D → G in SPG4. 1 Publication1
Natural variantiVAR_067649498R → G in SPG4. 2 Publications1
Natural variantiVAR_079323498R → M in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_010198499R → C in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles. 6 PublicationsCorresponds to variant dbSNP:rs121908511Ensembl.1
Natural variantiVAR_026761499R → H in SPG4. 2 PublicationsCorresponds to variant dbSNP:rs878854991Ensembl.1
Natural variantiVAR_019442503R → L in SPG4. 1 Publication1
Natural variantiVAR_067650503R → RR in SPG4. 1 Publication1
Natural variantiVAR_026762503R → W in SPG4. 2 PublicationsCorresponds to variant dbSNP:rs864622162Ensembl.1
Natural variantiVAR_027223512E → D in SPG4. 1 Publication1
Natural variantiVAR_067574512Missing in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_067651514R → G in SPG4. 1 Publication1
Natural variantiVAR_019443515Missing in SPG4. 1 Publication1
Natural variantiVAR_019444534L → P in SPG4. 1 Publication1
Natural variantiVAR_067575534L → V in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_079324546 – 616Missing in SPG4. 1 PublicationAdd BLAST71
Natural variantiVAR_067652550T → I in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_019451551A → Y in SPG4; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_075848555D → G in SPG4. 1 Publication1
Natural variantiVAR_027224555D → N in SPG4. 1 Publication1
Natural variantiVAR_027225556A → V in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. 2 Publications1
Natural variantiVAR_027226559G → D in SPG4. 2 PublicationsCorresponds to variant dbSNP:rs864622179Ensembl.1
Natural variantiVAR_075849559G → R in SPG4. 1 PublicationCorresponds to variant dbSNP:rs878854992Ensembl.1
Natural variantiVAR_075850562 – 616Missing in SPG4. 1 PublicationAdd BLAST55
Natural variantiVAR_027227562R → G in SPG4. 2 PublicationsCorresponds to variant dbSNP:rs121908518Ensembl.1
Natural variantiVAR_067576562R → P in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_027228562R → Q in SPG4. 1 PublicationCorresponds to variant dbSNP:rs863224923Ensembl.1
Natural variantiVAR_067653579N → H in SPG4; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs144594804Ensembl.1
Natural variantiVAR_067654580I → T in SPG4. 1 Publication1
Natural variantiVAR_075851581 – 616Missing in SPG4. 2 PublicationsAdd BLAST36
Natural variantiVAR_010199584D → H in SPG4. 1 Publication1
Natural variantiVAR_075852595S → R in SPG4. 1 Publication1
Natural variantiVAR_026763607W → C in SPG4. 1 Publication1
Natural variantiVAR_019445614T → I in SPG4; variant form with congenital arachnoid cysts. 1 Publication1
Natural variantiVAR_019452615T → I in SPG4. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1M → V: Cytoplasmic and nuclear. 1 Publication1
Mutagenesisi65R → G: Abolishes localization to lipid droplets. 1 Publication1
Mutagenesisi81 – 84RFSR → GFSG: Does not affect localization to lipid droplets. 1 Publication4
Mutagenesisi87M → V: Exclusively cytoplasmic. 1 Publication1
Mutagenesisi120H → D: Impairs binding to CHMP1B. Impairs midbody localization; when associated with D-124. 1 Publication1
Mutagenesisi124F → A: Impairs binding to CHMP1B. 1 Publication1
Mutagenesisi124F → D: Impairs binding to CHMP1B. Impairs midbody localization; when associated with D-120. 1 Publication1
Mutagenesisi310 – 312KKK → QQQ: Loss of microtubule-binding. 1 Publication3
Mutagenesisi388K → A: Abrogates ATPase activity and abolishes microtubule severing. 1 Publication1
Mutagenesisi415Y → A: Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing. 1 Publication1
Mutagenesisi442E → Q: Abrogates ATP hydrolysis, abolishes microtubule severing, stabilizes the homohexameric form, and promotes microtubule binding and redistribution from the endosome to microtubules. 8 Publications1
Mutagenesisi448C → A or G: Abolishes ATPase activity. 1 Publication1
Mutagenesisi448C → S: Does not affect ATPase activity. 1 Publication1
Mutagenesisi451R → G: Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing. 1 Publication1
Mutagenesisi457A → E: Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin and abolishes microtubule severing. 1 Publication1

Keywords - Diseasei

Disease mutation, Hereditary spastic paraplegia, Neurodegeneration

Organism-specific databases

DisGeNETi6683.
GeneReviewsiSPAST.
MalaCardsiSPAST.
MIMi182601. phenotype.
OpenTargetsiENSG00000021574.
Orphaneti100985. Autosomal dominant spastic paraplegia type 4.
PharmGKBiPA36063.

Polymorphism and mutation databases

BioMutaiSPAST.
DMDMi12230611.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000847631 – 616SpastinAdd BLAST616

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei245PhosphoserineCombined sources1
Modified residuei268PhosphoserineCombined sources1
Modified residuei306PhosphothreonineCombined sources1
Modified residuei597PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UBP0.
PaxDbiQ9UBP0.
PeptideAtlasiQ9UBP0.
PRIDEiQ9UBP0.

PTM databases

iPTMnetiQ9UBP0.
PhosphoSitePlusiQ9UBP0.

Expressioni

Tissue specificityi

Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. The short isoforms may predominate in brain and spinal cord.1 Publication

Developmental stagei

Expressed in fetal brain, heart, kidney, liver, lung, skeletal muscle, spleen and thymus.1 Publication

Gene expression databases

BgeeiENSG00000021574.
CleanExiHS_SPAST.
ExpressionAtlasiQ9UBP0. baseline and differential.
GenevisibleiQ9UBP0. HS.

Organism-specific databases

HPAiHPA017311.

Interactioni

Subunit structurei

Homohexamer (PubMed:17389232, PubMed:22637577). Mostly monomeric, but assembles into hexameric structure for short periods of time. Oligomerization seems to be a prerequisite for catalytic activity (PubMed:17389232, PubMed:22637577). Binding to ATP in a cleft between two adjacent subunits stabilizes the homohexameric form (PubMed:17389232, PubMed:22637577). Binds to microtubules at least in part via the alpha-tubulin and beta-tubulin tails (PubMed:15269182, PubMed:15716377, PubMed:23272056). The hexamer adopts a ring conformation through which microtubules pass prior to being severed (PubMed:17389232, PubMed:22637577). Does not interact strongly with tubulin heterodimers (PubMed:15269182, PubMed:15716377, PubMed:23272056). Interacts (via MIT domain) with CHMP1B; the interaction is direct (PubMed:15537668, PubMed:18997780). Interacts with SSNA1 (PubMed:15269182). Interacts with ATL1 (PubMed:16339213, PubMed:16815977). Interacts with RTN1 (PubMed:16602018). Interacts with ZFYVE27 (PubMed:16826525, PubMed:23969831). Isoform 1 but not isoform 3 interacts with RTN2 (PubMed:22232211). Interacts with REEP1 (PubMed:20200447). Interacts (via MIT domain) with IST1 (PubMed:23897888, PubMed:26040712).UniRule annotation16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATL1Q8WXF7-14EBI-1222832,EBI-15590227

GO - Molecular functioni

  • alpha-tubulin binding Source: UniProtKB
  • beta-tubulin binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • protein complex binding Source: ARUK-UCL

Protein-protein interaction databases

BioGridi112562. 29 interactors.
CORUMiQ9UBP0.
DIPiDIP-38418N.
ELMiQ9UBP0.
IntActiQ9UBP0. 14 interactors.
STRINGi9606.ENSP00000320885.

Structurei

Secondary structure

1616
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi112 – 136Combined sources25
Beta strandi139 – 141Combined sources3
Helixi142 – 144