DCTN1
entrez
1639
canonical
uniprot
Q14203
canonical
ensembl
ENSG00000204843
resolver
ensp
ENSP00000377571
resolver
ensp
ENSP00000386406
resolver
ensp
ENSP00000386843
resolver
ensp
ENSP00000387270
resolver
ensp
ENSP00000487279
resolver
ensp
ENSP00000487724
resolver
ensp
ENSP00000505612
resolver
enst
ENST00000680606
resolver
genesymbol
DCTN1
resolver
hgnc
HGNC:2711
resolver
uniprot
A0A7P0Z4C3
resolver
uniprot
A8MY36
resolver
uniprot
B4DM45
resolver
uniprot
E9PFS5
resolver
uniprot
E9PGE1
resolver
uniprot
G5E9H4
resolver
uniprot
O95296
resolver
uniprot
Q6IQ37
resolver
uniprot
Q9BRM9
resolver
uniprot
Q9UIU1
resolver
uniprot
Q9UIU2
resolver
uniprot_entry
A0A7P0Z4C3_HUMAN
resolver
uniprot_entry
DCTN1_HUMAN
resolver
uniprot_sec
A8MY36
resolver
uniprot_sec
B4DM45
resolver
uniprot_sec
E9PFS5
resolver
uniprot_sec
E9PGE1
resolver
uniprot_sec
G5E9H4
resolver
uniprot_sec
O95296
resolver
uniprot_sec
Q6IQ37
resolver
uniprot_sec
Q9BRM9
resolver
uniprot_sec
Q9UIU1
resolver
uniprot_sec
Q9UIU2
resolver
amino_acid_sequence
MAQSKRHVYSRTPSGSRMSAEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGTDTTAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGASSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPVLTSPGAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFELSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDCTMQLADHIKFTQSALDCMSVEVGRLRAFLQGGQEATDIALLLRDLETSCSDIRQFCKKIRRRMPGTDAPGIPAALAFGPQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLLVAALEELAFKASEQIYGTPSSSPYECLRQSCNILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLRGPPPSGIATLVSGIAGEEQQRGAIPGQAPGSVPGPGLVKDSPLLLQQISAMRLHISQLQHENSILKGAQMKASLASLPPLHVAKLSHEGPGSELPAGALYRKTSQLLETLNQLSTHTHVVDITRTSPAAKSPSAQLMEQVAQLKSLSDTVEKLKDEVLKETVSQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGFGQRHRLVLTQEQLHQLHSRLIS
uniprot
proteins
disease_involvement
DISEASE: Neuronopathy, distal hereditary motor, autosomal dominant 14 (HMND14) [MIM:607641]: A form of distal hereditary motor neuronopathy, a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. {ECO:0000269|PubMed:12627231, ECO:0000269|PubMed:16505168, ECO:0000269|PubMed:19136952, ECO:0000269|PubMed:19279216, ECO:0000269|PubMed:22777741}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Amyotrophic lateral sclerosis (ALS) [MIM:105400]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. {ECO:0000269|PubMed:15326253, ECO:0000269|PubMed:16240349}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Perry syndrome (PERRYS) [MIM:168605]: A neuropsychiatric disorder characterized by mental depression not responsive to antidepressant drugs or electroconvulsive therapy, sleep disturbances, exhaustion and marked weight loss. Parkinsonism develops later and respiratory failure occurred terminally. {ECO:0000269|PubMed:19136952, ECO:0000269|PubMed:23874158, ECO:0000269|PubMed:24676999, ECO:0000269|PubMed:24881494, ECO:0000269|PubMed:25185702, ECO:0000269|PubMed:26972003}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
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 (PubMed:25185702). 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 (PubMed:23874158). Plays a role in metaphase spindle orientation (PubMed:22327364). 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 (PubMed:23386061). Plays a role in primary cilia formation (PubMed:25774020). {ECO:0000250|UniProtKB:A0A287B8J2, ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:23874158, ECO:0000269|PubMed:25185702, ECO:0000269|PubMed:25774020}.
uniprot
proteins
mass_dalton
141695
uniprot
proteins
mutagenesis
MUTAGEN 68; /note="K->A: Abolishes interaction with CLIP1."; /evidence="ECO:0000269|PubMed:17828275"; MUTAGEN 90; /note="R->E: Abolishes interaction with CLIP1."; /evidence="ECO:0000269|PubMed:17828275"; MUTAGEN 145; /note="T->A: Affects centrosomal localization; when associated with A-146 and A-147."; /evidence="ECO:0000269|PubMed:23985322"; MUTAGEN 146; /note="T->A: Affects centrosomal localization; when associated with A-145 and A-147."; /evidence="ECO:0000269|PubMed:23985322"; MUTAGEN 147; /note="T->A: Affects centrosomal localization; when associated with A-145 and A-146."; /evidence="ECO:0000269|PubMed:23985322"; MUTAGEN 179; /note="S->A: Non-phosphorylatable by PLK1. Decreased nuclear envelope localization. No loss of microtubule-binding. No effect on its interaction with CLIP1."; /evidence="ECO:0000269|PubMed:20679239"; MUTAGEN 179; /note="S->D: No loss of localization to nuclear envelope. Decrease in microtubule-binding. No effect on its interaction with CLIP1."; /evidence="ECO:0000269|PubMed:20679239"; MUTAGEN 212; /note="S->A: No effect on its interaction with CLIP1 and PLK1."; /evidence="ECO:0000269|PubMed:20679239
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by a SCF complex containing FBXL5, leading to its degradation by the proteasome. {ECO:0000269|PubMed:17532294}.; PTM: Phosphorylation by SLK at Thr-145, Thr-146 and Thr-147 targets DCTN1 to the centrosome. It is uncertain if SLK phosphorylates all three threonines or one or two of them. PLK1-mediated phosphorylation at Ser-179 is essential for its localization in the nuclear envelope, promotes its dissociation from microtubules during early mitosis and positively regulates nuclear envelope breakdown during prophase. {ECO:0000269|PubMed:20679239, ECO:0000269|PubMed:23985322}.
uniprot
proteins
protein_family
Dynactin 150 kDa subunit family
uniprot
proteins
pubmed
12627231
uniprot
proteins
pubmed
14514668
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15326253
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16109370
uniprot
proteins
pubmed
16240349
uniprot
proteins
pubmed
16505168
uniprot
proteins
pubmed
16949363
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17532294
uniprot
proteins
pubmed
17824900
uniprot
proteins
pubmed
17828275
uniprot
proteins
pubmed
17828277
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19136952
uniprot
proteins
pubmed
19279216
uniprot
proteins
pubmed
19506225
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19935774
uniprot
proteins
pubmed
20679239
uniprot
proteins
pubmed
20682791
uniprot
proteins
pubmed
20719959
uniprot
proteins
pubmed
20978158
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22159412
uniprot
proteins
pubmed
22261744
uniprot
proteins
pubmed
22327364
uniprot
proteins
pubmed
22777741
uniprot
proteins
pubmed
22797915
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23386061
uniprot
proteins
pubmed
23509069
uniprot
proteins
pubmed
23874158
uniprot
proteins
pubmed
23985322
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24627108
uniprot
proteins
pubmed
24676999
uniprot
proteins
pubmed
24867236
uniprot
proteins
pubmed
24881494
uniprot
proteins
pubmed
25185702
uniprot
proteins
pubmed
25189619
uniprot
proteins
pubmed
25774020
uniprot
proteins
pubmed
26968983
uniprot
proteins
pubmed
26972003
uniprot
proteins
pubmed
28394342
uniprot
proteins
pubmed
35314674
uniprot
proteins
pubmed
8838327
uniprot
proteins
pubmed
8856662
uniprot
proteins
pubmed
9799602
uniprot
proteins
pubmed
9805007
uniprot
proteins
sequence_length
1278
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17828277}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17828277, ECO:0000269|PubMed:22777741, ECO:0000269|PubMed:25774020, ECO:0000269|PubMed:26972003}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20719959, ECO:0000269|PubMed:23985322, ECO:0000269|PubMed:25774020}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:25774020}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:25774020}. Nucleus envelope {ECO:0000269|PubMed:20679239}. Cytoplasm, cell cortex {ECO:0000269|PubMed:22327364}. Note=Localizes to microtubule plus ends (PubMed:17828277, PubMed:22777741, PubMed:25774020). Localizes preferentially to the ends of tyrosinated microtubules (PubMed:26972003). Localization at centrosome is regulated by SLK-dependent phosphorylation (PubMed:23985322). Localizes to centrosome in a PARKDA-dependent manner (PubMed:20719959). Localizes to the subdistal appendage region of the centriole in a KIF3A-dependent manner (PubMed:23386061). PLK1-mediated phosphorylation at Ser-179 is essential for its localization in the nuclear envelope (PubMed:20679239). {ECO:0000269|PubMed:17828277, ECO:0000269|PubMed:20679239, ECO:0000269|PubMed:20719959, ECO:0000269|PubMed:22777741, ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:23985322, ECO:0000269|PubMed:25774020, ECO:0000269|PubMed:26972003}.
uniprot
proteins