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Protein

Dynactin subunit 1

Gene

Dctn1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 centriole cohesion and subdistal appendage organization and function. Its recruitement 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 - Molecular functioni

  • microtubule motor activity Source: RGD
  • tubulin binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Dynactin subunit 1
Alternative name(s):
150 kDa dynein-associated polypeptide
DAP-150
Short name:
DP-150
p150-glued
Gene namesi
Name:Dctn1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi62038. Dctn1.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmcytoskeleton By similarity
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole By similarity
  • Cytoplasmcytoskeletonspindle By similarity
  • Nucleus envelope By similarity

  • 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.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000835201 – 1280Dynactin subunit 1Add BLAST1280

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei108PhosphothreonineBy similarity1
Modified residuei145PhosphothreonineBy similarity1
Modified residuei146PhosphothreonineBy similarity1
Modified residuei147PhosphothreonineBy similarity1
Modified residuei179Phosphoserine; by PLK1By similarity1
Modified residuei212Phosphoserine; by CDK1By similarity1

Post-translational modificationi

Ubiquitinated by a SCF complex containing FBXL5, leading to its degradation by the proteasome.By similarity
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 and promotes its dissociation from microtubules during early mitosis and positively regulates nuclear envelope breakdown during prophase.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP28023.
PeptideAtlasiP28023.
PRIDEiP28023.

PTM databases

iPTMnetiP28023.
PhosphoSitePlusiP28023.

Miscellaneous databases

PMAP-CutDBP28023.

Expressioni

Tissue specificityi

Ubiquitous with a high level expression observed in the brain (at protein level).1 Publication

Interactioni

Subunit structurei

Monomer and homodimer. Dynactin is a large macromolecular complex of at least 10 components; p150(glued) binds directly to microtubules and to cytoplasmic dynein. Interacts with the C-terminus of MAPRE2 and MAPRE3. Interacts with FBXL5. Interacts with ECM29 and SNX6. Interacts with CLIP1. Interacts with CLN3 and DYNAP. Interacts with MISP; this interaction regulates its distribution at the cell cortex. Interacts with CEP131 (By similarity). Interacts (via CAP-Gly domain) with the C-terminus of MAPRE1, forming a heterotetramer (PubMed:23648839). Interacts with dynein intermediate chain and dynein heavy chain. Interacts with PLK1 (via POLO-box domain). Binds preferentially to tyrosinated microtubules than to detyrosinated microtubules. Interacts with TBCB, PARD6A, HPS6, KIF3A (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi247848. 3 interactors.
DIPiDIP-44817N.
IntActiP28023. 2 interactors.
MINTiMINT-1531595.
STRINGi10116.ENSRNOP00000059076.

Structurei

Secondary structure

11280
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 38Combined sources4
Beta strandi41 – 48Combined sources8
Beta strandi53 – 55Combined sources3
Beta strandi57 – 64Combined sources8
Beta strandi78 – 80Combined sources3
Beta strandi87 – 89Combined sources3
Turni91 – 93Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M02NMR-A19-107[»]
2MPXNMR-C26-95[»]
ProteinModelPortaliP28023.
SMRiP28023.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini48 – 90CAP-GlyPROSITE-ProRule annotationAdd BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni910 – 1280Interaction with HPS6By similarityAdd BLAST371

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili214 – 513Sequence analysisAdd BLAST300
Coiled coili942 – 1048Sequence analysisAdd BLAST107
Coiled coili1184 – 1213Sequence analysisAdd BLAST30

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi157 – 184Ser-richAdd BLAST28

Domaini

The CAP-Gly domain is essential for interactions with microtubules and its binding partners and for its motion along the microtubules. Essential for its preferential binding to tyrosinated microtubules and for promoting the sustained interaction of the dynein motor with microtubules.By similarity

Sequence similaritiesi

Belongs to the dynactin 150 kDa subunit family.Curated
Contains 1 CAP-Gly domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0971. Eukaryota.
COG5244. LUCA.
HOGENOMiHOG000015352.
HOVERGENiHBG004956.
InParanoidiP28023.
KOiK04648.
PhylomeDBiP28023.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
InterProiIPR000938. CAP-Gly_domain.
IPR027663. DCTN1.
IPR022157. Dynactin.
[Graphical view]
PANTHERiPTHR18916:SF40. PTHR18916:SF40. 1 hit.
PfamiPF01302. CAP_GLY. 1 hit.
PF12455. Dynactin. 1 hit.
[Graphical view]
SMARTiSM01052. CAP_GLY. 1 hit.
[Graphical view]
SUPFAMiSSF74924. SSF74924. 1 hit.
PROSITEiPS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28023-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQSKRHMYN RTPSGSRMST EASARPLRVG SRVEVIGKGH RGTVAYVGAT
60 70 80 90 100
LFATGKWVGV ILDEAKGKND GTVQGRKYFT CDEGHGIFVR QSQIQVFEDG
110 120 130 140 150
ADTTSPETPD SSASKILKRE GADAAAKTSK LRGLKPKKAP TARKTTTRRP
160 170 180 190 200
KPTRPASTGV AGPSSSLGPS GSASAGELSS SEPSTPAQTP LAAPIIPTPA
210 220 230 240 250
LTSPGAAPPL PSPSKEEEGL RDQVRDLEEK LETLRLKRSE DKAKLKELEK
260 270 280 290 300
HKIQLEQVQE WKSKMQEQQA DLQRRLKEAK EAKEALEAKE RYMEEMADTA
310 320 330 340 350
DAIEMATLDK EMAEERAESL QQEVEALKER VDELTTDLEI LKAEIEEKGS
360 370 380 390 400
DGAASSYQLK QLEEQNARLK DALVRMRDLS SSEKQEHVKL QKLMEKKNQE
410 420 430 440 450
LEVVRQQRER LQEELSQAES TIDELKEQVD AALGAEEMVE MLTDRNLNLE
460 470 480 490 500
EKVRELRETV GDLEAMNEMN DELQENARET ELELREQLDM AGARVREAQK
510 520 530 540 550
RVEAAQETVA DYQQTIKKYR QLTAHLQDVN RELTNQQEAS VERQQQPPPE
560 570 580 590 600
TFDFKIKFAE TKAHAKAIEM ELRQMEVAQA NRHMSLLTAF MPDSFLRPGG
610 620 630 640 650
DHDCVLVLLL MPRLICKAEL IRKQAQEKFD LSENCSERPG LRGAAGEQLS
660 670 680 690 700
FAAGLVYSLS LLQATLHRYE HALSQCSVDV YKKVGSLYPE MSAHERSLDF
710 720 730 740 750
LIELLHKDQL DETVNVEPLT KAIKYYQHLY SIHLAEQPEE STMQLADHIK
760 770 780 790 800
FTQSALDCMS VEVGRLRAFL QGGQEATDIA LLLRDLETSC SDIRQFCKKI
810 820 830 840 850
RRRMPGTDAP GIPAALAFGS QVSDTLLDCR KHLTWVVAVL QEVAAAAAQL
860 870 880 890 900
IAPLAENEGL PVAALEELAF KASEQIYGSP SSSPYECLRQ SCSILISTMN
910 920 930 940 950
KLATAMQEGE YDAERPPSKP PPVEPWPAAL RAEITDAEGL GLKLEDRETV
960 970 980 990 1000
IKELKKSLKI KGEELSEANV RLSLLEKKLD SAAKDADERI EKVQTRLEET
1010 1020 1030 1040 1050
QTLLRKKEKE FEETMDALQA DIDQLEAEKT ELKQRLNSQS KRTIEGLRGP
1060 1070 1080 1090 1100
PPSGIATLVS GIAGEEQQRG GTPGQAPGAL PGPGPVKDSP LLLQQISAMR
1110 1120 1130 1140 1150
LHISQLQHEN SILRGAQMKA SLAALPPLHV AKFSLPPHEG PGGNLLSGAL
1160 1170 1180 1190 1200
YRKTSQLLEK LNQLSTYTHV VDITRSSPAC KSPSAQLMEQ VAQLKSLSDT
1210 1220 1230 1240 1250
IEKLKDEVLK ETVTQRPGAT VPTDFATFPS SAFLRAKEEQ QDDTVYMGKV
1260 1270 1280
TFSCAAGLGQ RHRLVLTQEQ LHQLHGRLIS
Length:1,280
Mass (Da):141,930
Last modified:November 1, 1997 - v2
Checksum:iC9348CF129F4FF5C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62160 mRNA. Translation: CAA44091.1.
PIRiS16129.
RefSeqiNP_077044.1. NM_024130.1.
UniGeneiRn.11284.

Genome annotation databases

GeneIDi29167.
KEGGirno:29167.
UCSCiRGD:62038. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62160 mRNA. Translation: CAA44091.1.
PIRiS16129.
RefSeqiNP_077044.1. NM_024130.1.
UniGeneiRn.11284.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M02NMR-A19-107[»]
2MPXNMR-C26-95[»]
ProteinModelPortaliP28023.
SMRiP28023.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247848. 3 interactors.
DIPiDIP-44817N.
IntActiP28023. 2 interactors.
MINTiMINT-1531595.
STRINGi10116.ENSRNOP00000059076.

PTM databases

iPTMnetiP28023.
PhosphoSitePlusiP28023.

Proteomic databases

PaxDbiP28023.
PeptideAtlasiP28023.
PRIDEiP28023.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29167.
KEGGirno:29167.
UCSCiRGD:62038. rat.

Organism-specific databases

CTDi1639.
RGDi62038. Dctn1.

Phylogenomic databases

eggNOGiKOG0971. Eukaryota.
COG5244. LUCA.
HOGENOMiHOG000015352.
HOVERGENiHBG004956.
InParanoidiP28023.
KOiK04648.
PhylomeDBiP28023.

Miscellaneous databases

PMAP-CutDBP28023.
PROiP28023.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
InterProiIPR000938. CAP-Gly_domain.
IPR027663. DCTN1.
IPR022157. Dynactin.
[Graphical view]
PANTHERiPTHR18916:SF40. PTHR18916:SF40. 1 hit.
PfamiPF01302. CAP_GLY. 1 hit.
PF12455. Dynactin. 1 hit.
[Graphical view]
SMARTiSM01052. CAP_GLY. 1 hit.
[Graphical view]
SUPFAMiSSF74924. SSF74924. 1 hit.
PROSITEiPS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDCTN1_RAT
AccessioniPrimary (citable) accession number: P28023
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.