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Protein

Dynactin subunit 1

Gene

Dctn1

Organism
Mus musculus (Mouse)
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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiREACT_272448. Recruitment of mitotic centrosome proteins and complexes.
REACT_276302. Loss of Nlp from mitotic centrosomes.
REACT_286537. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_316383. MHC class II antigen presentation.
REACT_328862. Anchoring of the basal body to the plasma membrane.
REACT_345278. Regulation of PLK1 Activity at G2/M Transition.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:107745. Dctn1.

Subcellular locationi

GO - Cellular componenti

  • cell leading edge Source: MGI
  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB-SubCell
  • dynactin complex Source: InterPro
  • dynein complex Source: UniProtKB-KW
  • kinetochore Source: MGI
  • membrane Source: MGI
  • microtubule Source: MGI
  • protein complex Source: MGI
  • retromer complex Source: Ensembl
  • spindle pole Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12811281Dynactin subunit 1PRO_0000083519Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081PhosphothreonineBy similarity

Post-translational modificationi

Ubiquitinated by a SCF complex containing FBXL5, leading to its degradation by the proteasome.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO08788.
PaxDbiO08788.
PRIDEiO08788.

PTM databases

PhosphoSiteiO08788.

Expressioni

Gene expression databases

BgeeiO08788.
CleanExiMM_DCTN1.
ExpressionAtlasiO08788. baseline and differential.
GenevisibleiO08788. MM.

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 MAPRE1, MAPRE2 and MAPRE3. Interacts with FBXL5. Interacts with ECM29. 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 with SNX6 (PubMed:19935774). Interacts with CEP126 (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Kif3aP287414EBI-776180,EBI-6169413
Kif5aP331752EBI-776180,EBI-349710

Protein-protein interaction databases

BioGridi199072. 14 interactions.
DIPiDIP-32057N.
IntActiO08788. 24 interactions.
MINTiMINT-1847327.
STRINGi10090.ENSMUSP00000109552.

Structurei

3D structure databases

ProteinModelPortaliO08788.
SMRiO08788. Positions 25-98.
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 – 547334Sequence AnalysisAdd
BLAST
Coiled coili943 – 1049107Sequence AnalysisAdd
BLAST
Coiled coili1185 – 121430Sequence 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

eggNOGiCOG5244.
GeneTreeiENSGT00770000120567.
HOGENOMiHOG000015352.
HOVERGENiHBG004956.
InParanoidiO08788.
OMAiPEDSTMQ.
TreeFamiTF105246.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
InterProiIPR000938. CAP-Gly_domain.
IPR027663. DCTN1.
IPR022157. Dynactin.
[Graphical view]
PANTHERiPTHR18916:SF29. PTHR18916:SF29. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O08788-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAQSRRHMSS RTPSGSRMST EASARPLRVG SRVEVIGKGH RGTVAYVGAT
60 70 80 90 100
LFATGKWVGV ILDEAKGKND GTVQGRKYFT CDEGHGIFVR QSQIQVFEDG
110 120 130 140 150
ADTTSPETPD SSASKVLKRE GADAAAKTSK LRGLKPKKAP TARKTTTRRP
160 170 180 190 200
KPTRPASTGV AGPSSSLGPS GSASAGELSS SEPSTPAQTP LAAPIIPTPA
210 220 230 240 250
LTSPGAAPPL PSPSKEEEGL RAQVRDLEEK LETLRLKRSE DKAKLKELEK
260 270 280 290 300
HKIQLEQVQE WKSKMQEQQA DLQRRLKEAR KEAKEALEAK ERYMEEMADT
310 320 330 340 350
ADAIEMATLD KEMAEERAES LQQEVEALKE RVDELTTDLE ILKAEIEEKG
360 370 380 390 400
SDGAASSYQL KQLEEQNARL KDALVRMRDL SSSEKQEHVK LQKLMEKKNQ
410 420 430 440 450
ELEVVRQQRE RLQEELSQAE STIDELKEQV DAALGAEEMV EMLTDRNLNL
460 470 480 490 500
EEKVRELRET VGDLEAMNEM NDELQENARE TELELREQLD MAGARVREAQ
510 520 530 540 550
KRVEAAQETV ADYQQTIKKY RQLTAHLQDV NRELTNQQEA SVERQQQPPP
560 570 580 590 600
ETFDFKIKFA ETKAHAKAIE MELRQMEVAQ ANRHMSLLTA FMPDSFLRPG
610 620 630 640 650
GDHDCVLVLL LMPRLICKAE LIRKQAQEKF DLSENCSERP GLRGAAGEQL
660 670 680 690 700
SFAAGLVYSL SLLQATLHRY EHALSQCSVD VYKKVGSLYP EMSAHERSLD
710 720 730 740 750
FLIELLHKDQ LDETVNVEPL TKAIKYYQHL YSIHLAEQPE DSTMQLADHI
760 770 780 790 800
KFTQSALDCM GVEVGRLRAF LQGGQEATDI ALLLRDLETS CSDTRQFCKK
810 820 830 840 850
IRRRMPGTDA PGIPAALAFG SQVSDTLLDC RKHLTWVVAV LQEVAAAAAQ
860 870 880 890 900
LIAPLAENEG LPVAALEELA FKASEQIYGS PSSSPYECLR QSCTILISTM
910 920 930 940 950
NKLATAMQEG EYDAERPPSK PPPVELRAAA LRAEITDAEG LGLKLEDRET
960 970 980 990 1000
VIKELKKSLK IKGEELSEAN VRLSLLEKKL DSAAKDADER IEKVQTRLDE
1010 1020 1030 1040 1050
TQTLLRKKEK DFEETMDALQ ADIDQLEAEK AELKQRLNSQ SKRTIEGLRG
1060 1070 1080 1090 1100
PPPSGIATLV SGIAGEEPQR GGAPGQAPGA LPGPGLVKDS PLLLQQISAM
1110 1120 1130 1140 1150
RLHISQLQHE NSILRGAQMK ASLAALPPLH VAKLSLPPHE GPGGNLVAGA
1160 1170 1180 1190 1200
LYRKTSQLLE KLNQLSTHTH VVDITRSSPA AKSPSAQLME QVAQLKSLSD
1210 1220 1230 1240 1250
TIEKLKDEVL KETVTQRPGA TVPTDFATFP SSAFLRAKEE QQDDTVYMGK
1260 1270 1280
VTFSCAAGLG QRHRLVLTQE QLHQLHSRLI S
Length:1,281
Mass (Da):141,676
Last modified:July 27, 2011 - v3
Checksum:iA6CEDCAAA7022EB5
GO
Isoform 2 (identifier: O08788-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1049-1086: Missing.

Note: No experimental confirmation available.
Show »
Length:1,243
Mass (Da):138,206
Checksum:i17BD5B9ED7CD2474
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti406 – 4061R → W in BAE34241 (PubMed:16141072).Curated
Sequence conflicti721 – 7233TKA → NKG in AAB57773 (PubMed:9070275).Curated
Sequence conflicti732 – 7321S → R in AAB57773 (PubMed:9070275).Curated
Sequence conflicti1202 – 12021I → V in BAE34241 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1049 – 108638Missing in isoform 2. 1 PublicationVSP_029584Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60312 mRNA. Translation: AAB57773.1.
AK157867 mRNA. Translation: BAE34241.1.
AC160400 Genomic DNA. No translation available.
CCDSiCCDS39532.1. [O08788-1]
PIRiJC5368.
RefSeqiNP_031861.2. NM_007835.2. [O08788-1]
UniGeneiMm.6919.

Genome annotation databases

EnsembliENSMUST00000113918; ENSMUSP00000109551; ENSMUSG00000031865. [O08788-2]
ENSMUST00000113919; ENSMUSP00000109552; ENSMUSG00000031865. [O08788-1]
GeneIDi13191.
UCSCiuc009cmz.2. mouse. [O08788-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60312 mRNA. Translation: AAB57773.1.
AK157867 mRNA. Translation: BAE34241.1.
AC160400 Genomic DNA. No translation available.
CCDSiCCDS39532.1. [O08788-1]
PIRiJC5368.
RefSeqiNP_031861.2. NM_007835.2. [O08788-1]
UniGeneiMm.6919.

3D structure databases

ProteinModelPortaliO08788.
SMRiO08788. Positions 25-98.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199072. 14 interactions.
DIPiDIP-32057N.
IntActiO08788. 24 interactions.
MINTiMINT-1847327.
STRINGi10090.ENSMUSP00000109552.

Chemistry

ChEMBLiCHEMBL2176787.

PTM databases

PhosphoSiteiO08788.

Proteomic databases

MaxQBiO08788.
PaxDbiO08788.
PRIDEiO08788.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000113918; ENSMUSP00000109551; ENSMUSG00000031865. [O08788-2]
ENSMUST00000113919; ENSMUSP00000109552; ENSMUSG00000031865. [O08788-1]
GeneIDi13191.
UCSCiuc009cmz.2. mouse. [O08788-1]

Organism-specific databases

CTDi1639.
MGIiMGI:107745. Dctn1.

Phylogenomic databases

eggNOGiCOG5244.
GeneTreeiENSGT00770000120567.
HOGENOMiHOG000015352.
HOVERGENiHBG004956.
InParanoidiO08788.
OMAiPEDSTMQ.
TreeFamiTF105246.

Enzyme and pathway databases

ReactomeiREACT_272448. Recruitment of mitotic centrosome proteins and complexes.
REACT_276302. Loss of Nlp from mitotic centrosomes.
REACT_286537. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_316383. MHC class II antigen presentation.
REACT_328862. Anchoring of the basal body to the plasma membrane.
REACT_345278. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

ChiTaRSiDctn1. mouse.
NextBioi283312.
PROiO08788.
SOURCEiSearch...

Gene expression databases

BgeeiO08788.
CleanExiMM_DCTN1.
ExpressionAtlasiO08788. baseline and differential.
GenevisibleiO08788. MM.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
InterProiIPR000938. CAP-Gly_domain.
IPR027663. DCTN1.
IPR022157. Dynactin.
[Graphical view]
PANTHERiPTHR18916:SF29. PTHR18916:SF29. 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. "Mouse p150Glued (dynactin 1) cDNA sequence and evaluation as a candidate for the neuromuscular disease mutation mnd2."
    Jang W., Weber J.S., Tokito M.K., Holzbaur E.L., Meisler M.H.
    Biochem. Biophys. Res. Commun. 231:344-347(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Inner ear.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The retromer component SNX6 interacts with dynactin p150(Glued) and mediates endosome-to-TGN transport."
    Hong Z., Yang Y., Zhang C., Niu Y., Li K., Zhao X., Liu J.J.
    Cell Res. 19:1334-1349(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX6.

Entry informationi

Entry nameiDCTN1_MOUSE
AccessioniPrimary (citable) accession number: O08788
Secondary accession number(s): E9QLJ1, Q3TZG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.