ID  P28023;
PN  Dynactin subunit 1;
GN  Dctn1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q14203}. Nucleus envelope {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q14203}. Note=Localizes to microtubule plus ends. Localizes preferentially to the ends of tyrosinated microtubules. Localization at centrosome is regulated by SLK-dependent phosphorylation. Localizes to centrosome in a PARKDA-dependent manner. PLK1-mediated phosphorylation at Ser-179 is essential for its localization in the nuclear envelope. Localizes to the subdistal appendage region of the centriole in a KIF3A-dependent manner. {ECO:0000250|UniProtKB:O08788, ECO:0000250|UniProtKB:Q14203}.
DR  UNIPROT: P28023;
DR  PDB: 2M02;
DR  PDB: 2MPX;
DR  Pfam: PF01302;
DR  Pfam: PF12455;
DR  PROSITE: PS00845;
DR  PROSITE: PS50245;
DE  Function: 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. {ECO:0000250|UniProtKB:Q14203}.
DE  Reference Proteome: Yes;
DE  Interaction: A0JNT9; IntAct: EBI-7894963; Score: 0.27
DE  Interaction: P54256; IntAct: EBI-9639028; Score: 0.49
DE  Interaction: P54645; IntAct: EBI-16399805; Score: 0.35
DE  Interaction: P80386; IntAct: EBI-16400563; Score: 0.35
DE  Interaction: P28023; IntAct: EBI-16128725; Score: 0.56
DE  Interaction: Q969Q1; IntAct: EBI-21997483; Score: 0.35
DE  Interaction: P19332; IntAct: EBI-26374040; Score: 0.35
GO  GO:0030424;
GO  GO:0005938;
GO  GO:0099738;
GO  GO:0031252;
GO  GO:0120103;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005868;
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0005874;
GO  GO:0005875;
GO  GO:0035371;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0005819;
GO  GO:0000922;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0051010;
GO  GO:0060090;
GO  GO:0019901;
GO  GO:0015631;
GO  GO:0051301;
GO  GO:0010457;
GO  GO:0031122;
GO  GO:0000132;
GO  GO:0032402;
GO  GO:0034454;
GO  GO:0061744;
GO  GO:0007528;
GO  GO:0050905;
GO  GO:0070050;
GO  GO:1990535;
GO  GO:1905515;
GO  GO:0051081;
GO  GO:0007097;
GO  GO:0090316;
GO  GO:0090063;
GO  GO:0031116;
GO  GO:1904398;
GO  GO:0060236;
GO  GO:0042147;
GO  GO:0021517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQSKRHMYNRTPSGSRMSTEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFT
SQ  CDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKILKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGV
SQ  AGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRDQVRDLEEKLETLRLKRSE
SQ  DKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEAKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESL
SQ  QQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQE
SQ  LEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARET
SQ  ELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAE
SQ  TKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERPG
SQ  LRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLT
SQ  KAIKYYQHLYSIHLAEQPEESTMQLADHIKFTQSALDCMSVEVGRLRAFLQGGQEATDIALLLRDLETSCSDIRQFCKKI
SQ  RRRMPGTDAPGIPAALAFGSQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGSP
SQ  SSSPYECLRQSCSILISTMNKLATAMQEGEYDAERPPSKPPPVEPWPAALRAEITDAEGLGLKLEDRETVIKELKKSLKI
SQ  KGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQTLLRKKEKEFEETMDALQADIDQLEAEKTELKQRLNSQS
SQ  KRTIEGLRGPPPSGIATLVSGIAGEEQQRGGTPGQAPGALPGPGPVKDSPLLLQQISAMRLHISQLQHENSILRGAQMKA
SQ  SLAALPPLHVAKFSLPPHEGPGGNLLSGALYRKTSQLLEKLNQLSTYTHVVDITRSSPACKSPSAQLMEQVAQLKSLSDT
SQ  IEKLKDEVLKETVTQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHGRLIS
//