P13496 · DCTN1_DROME
- ProteinDynactin subunit 1
- GeneDCTN1-p150
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1265 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity).
Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon. Plays a role in metaphase spindle orientation. Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitment to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole. Plays a role in primary cilia formation (By similarity).
Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon. Plays a role in metaphase spindle orientation. Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitment to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole. Plays a role in primary cilia formation (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDynactin subunit 1
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP13496
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000083523 | 1-1265 | Dynactin subunit 1 | |||
Sequence: MSEKNLKVGARVELTGKDLLGTVAYVGMTSFAVGKWVGVVLDEPKGKNSGSIKGQQYFQCDENCGMFVRPTQLRLLEAAPGSRRSIEDVSGATPTAAQPTKARLSSSRTSLSSSRQSLLGSRTQLTTSLSERTASSSSIGPRKSLAPQNSKDKESPSTSLAEGAPAASGGNGAASHASSKRASFVETGFLEILKPQFTPSQPLRSPSFTMPSNSGAEDKVALLEAQKTSAELQAQLADLTEKLETLKQRRNEDKERLREFDKMKIQFEQLQEFRTKIMGAQASLQKELLRAKQEAKDAIEAKEQHAQEMADLADNVEMITLDKEMAEEKADTLQLELESSKERIEELEVDLELLRSEMQNKAESAIGNISGGGDSPGLSTYEFKQLEQQNIRLKETLVRLRDLSAHDKHDIQKLSKELEMKRSEVTELERTKEKLSAKIDELEAIVADLQEQVDAALGAEEMVEQLAEKKMELEDKVKLLEEEIAQLEALEEVHEQLVESNHELELDLREELDLANGAKKEVLRERDAAIETIYDRDQTIVKFRELVQKLNDQLTELRDRNSSNEKESLQDPSLKMVTETIDYKQMFAESKAYTRAIDVQLRQIELSQANEHVQMLTAFMPESFMSRGGDHDSILVILLISRIVFKCDIVVSQTRERFPPVDAITREAVTQGHAVQQYAFKCRLLHYVHSLQCALHQILYGLNSCQPDTLLRAGSSLPEMVAQEKIVDGIIELLKSNQLDENSTTDNIEKCVAFFNAMNSVLLAGEQLLNEIQMIRDCVASLGAACESILSDTAIAKVIIQEAGATSDSVLLIQFLNENMESVRQQVKLIKRRLPSDQHVIKSGLSQHKVEAMRGLAQNISRIMSAMHQATKQSLAAIVSTIESDNAAEHTLPQEKYWALLTASCERIYEQDDRGPTQNFKTLLAQANSDLQLIAQHLLDKEYDIISAANNASNQQKSGAHSTPITQRAQLIKKQLEQKNVLAATLENREADVKQLKVAAKMKQNELSEMQIRKDLAEKKLSVLQNEYEHAVDKWKQKYEETSLQLQLKEKEFEETMDHLQSDIDALESEKSDLRDKLKLNSTTGKVQPGSESHSPHNISLSGNTSTAPGISNVSYSAPAGTAPVVAEEVELLKNAFNQERNQRLRLQAQDMRAKLSQFEPLHVPQPQDQRITALESELTRMKHAWVLSLLQVRSQDSVNSGTRIDAVALQRRNQPVPLKGEISSKASQLASDILTEYLQRKPHRATHGQFASFPTVDVKRVLQI | ||||||
Modified residue | 85 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 110 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 114 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 117 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 121 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 183 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1117 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Monomer and homodimer (By similarity).
Subunit of dynactin, a multiprotein complex part of a tripartite complex with dynein and a adapter, such as BICDL1, BICD2 or HOOK3. The dynactin complex is built around ACTR1A/ACTB filament and consists of an actin-related filament composed of a shoulder domain, a pointed end and a barbed end. Its length is defined by its flexible shoulder domain. The soulder is composed of 2 DCTN1 subunits, 4 DCTN2 and 2 DCTN3. DCTN1/p150(glued) binds directly to microtubules and to cytoplasmic dynein (By similarity).
Subunit of dynactin, a multiprotein complex part of a tripartite complex with dynein and a adapter, such as BICDL1, BICD2 or HOOK3. The dynactin complex is built around ACTR1A/ACTB filament and consists of an actin-related filament composed of a shoulder domain, a pointed end and a barbed end. Its length is defined by its flexible shoulder domain. The soulder is composed of 2 DCTN1 subunits, 4 DCTN2 and 2 DCTN3. DCTN1/p150(glued) binds directly to microtubules and to cytoplasmic dynein (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 27-69 | CAP-Gly | ||||
Sequence: GMTSFAVGKWVGVVLDEPKGKNSGSIKGQQYFQCDENCGMFVR | ||||||
Region | 81-179 | Disordered | ||||
Sequence: GSRRSIEDVSGATPTAAQPTKARLSSSRTSLSSSRQSLLGSRTQLTTSLSERTASSSSIGPRKSLAPQNSKDKESPSTSLAEGAPAASGGNGAASHASS | ||||||
Compositional bias | 88-164 | Polar residues | ||||
Sequence: DVSGATPTAAQPTKARLSSSRTSLSSSRQSLLGSRTQLTTSLSERTASSSSIGPRKSLAPQNSKDKESPSTSLAEGA | ||||||
Coiled coil | 213-570 | |||||
Sequence: NSGAEDKVALLEAQKTSAELQAQLADLTEKLETLKQRRNEDKERLREFDKMKIQFEQLQEFRTKIMGAQASLQKELLRAKQEAKDAIEAKEQHAQEMADLADNVEMITLDKEMAEEKADTLQLELESSKERIEELEVDLELLRSEMQNKAESAIGNISGGGDSPGLSTYEFKQLEQQNIRLKETLVRLRDLSAHDKHDIQKLSKELEMKRSEVTELERTKEKLSAKIDELEAIVADLQEQVDAALGAEEMVEQLAEKKMELEDKVKLLEEEIAQLEALEEVHEQLVESNHELELDLREELDLANGAKKEVLRERDAAIETIYDRDQTIVKFRELVQKLNDQLTELRDRNSSNEKESLQ | ||||||
Coiled coil | 812-836 | |||||
Sequence: LIQFLNENMESVRQQVKLIKRRLPS | ||||||
Coiled coil | 967-1084 | |||||
Sequence: QRAQLIKKQLEQKNVLAATLENREADVKQLKVAAKMKQNELSEMQIRKDLAEKKLSVLQNEYEHAVDKWKQKYEETSLQLQLKEKEFEETMDHLQSDIDALESEKSDLRDKLKLNSTT | ||||||
Region | 1082-1106 | Disordered | ||||
Sequence: STTGKVQPGSESHSPHNISLSGNTS | ||||||
Coiled coil | 1128-1160 | |||||
Sequence: EEVELLKNAFNQERNQRLRLQAQDMRAKLSQFE |
Sequence similarities
Belongs to the dynactin 150 kDa subunit family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,265
- Mass (Da)141,218
- Last updated2000-12-01 v2
- Checksum2038A200282B2755
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 88-164 | Polar residues | ||||
Sequence: DVSGATPTAAQPTKARLSSSRTSLSSSRQSLLGSRTQLTTSLSERTASSSSIGPRKSLAPQNSKDKESPSTSLAEGA | ||||||
Sequence conflict | 708 | in Ref. 1; J02932 | ||||
Sequence: D → A | ||||||
Sequence conflict | 865 | in Ref. 4; AAM48406 | ||||
Sequence: S → P | ||||||
Sequence conflict | 875 | in Ref. 1; J02932 | ||||
Sequence: L → V | ||||||
Sequence conflict | 888 | in Ref. 1; J02932 | ||||
Sequence: A → R | ||||||
Sequence conflict | 1043 | in Ref. 1; J02932 | ||||
Sequence: S → C |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J02932 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AE014296 EMBL· GenBank· DDBJ | AAF49788.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY118377 EMBL· GenBank· DDBJ | AAM48406.1 EMBL· GenBank· DDBJ | mRNA | ||
BT044559 EMBL· GenBank· DDBJ | ACI15754.1 EMBL· GenBank· DDBJ | mRNA |