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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

Required for the cytoplasmic dynein-driven retrograde movement of vesicles and organelles along microtubules. Dynein-dynactin interaction is a key component of the mechanism of axonal transport of vesicles and organelles.

GO - Molecular functioni

  • microtubule motor activity Source: RGD

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

  • Note: Colocalizes with microtubules. Localization at centrosome is regulated by SLK-dependent phosphorylation.By similarity

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB-SubCell
  • cytoplasmic dynein complex Source: RGD
  • dynactin complex Source: InterPro
  • microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12801280Dynactin subunit 1PRO_0000083520Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081PhosphothreonineBy similarity
Modified residuei145 – 1451PhosphothreonineBy similarity
Modified residuei146 – 1461PhosphothreonineBy similarity
Modified residuei147 – 1471PhosphothreonineBy similarity

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.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP28023.
PeptideAtlasiP28023.
PRIDEiP28023.

PTM databases

iPTMnetiP28023.
PhosphoSiteiP28023.

Miscellaneous databases

PMAP-CutDBP28023.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

1
1280
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 384Combined sources
Beta strandi41 – 488Combined sources
Beta strandi53 – 553Combined sources
Beta strandi57 – 648Combined sources
Beta strandi78 – 803Combined sources
Beta strandi87 – 893Combined sources
Turni91 – 933Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M02NMR-A19-107[»]
2MPXNMR-C26-95[»]
ProteinModelPortaliP28023.
SMRiP28023. Positions 1-104.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 9043CAP-GlyPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili214 – 513300Sequence analysisAdd
BLAST
Coiled coili942 – 1048107Sequence analysisAdd
BLAST
Coiled coili1184 – 121330Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi157 – 18428Ser-richAdd
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2M02NMR-A19-107[»]
2MPXNMR-C26-95[»]
ProteinModelPortaliP28023.
SMRiP28023. Positions 1-104.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP28023.
PhosphoSiteiP28023.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Homology of a 150K cytoplasmic dynein-associated polypeptide with the Drosophila gene Glued."
    Holzbaur E.L.F., Hammarback J.A., Paschal B.M., Kravit N.G., Pfister K.K., Vallee R.B.
    Nature 351:579-583(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. Holzbaur E.L.F., Hammarback J.A., Paschal B.M., Kravit N.G., Pfister K.K., Vallee R.B.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Three-dimensional structure of CAP-Gly domain of mammalian dynactin determined by magic angle spinning NMR spectroscopy: conformational plasticity and interactions with end-binding protein EB1."
    Yan S., Hou G., Schwieters C.D., Ahmed S., Williams J.C., Polenova T.
    J. Mol. Biol. 425:4249-4266(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 19-107, INTERACTION WITH MAPRE1, SUBUNIT.

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: July 6, 2016
This is version 131 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.