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Q14203 (DCTN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dynactin subunit 1
Alternative name(s):
150 kDa dynein-associated polypeptide
DAP-150
Short name=DP-150
p135
p150-glued
Gene names
Name:DCTN1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1278 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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 (via C-terminus) with SNX6. Interacts with CLIP1, CLN3, DYNAP, ECM29 and FBXL5. Interacts with MISP; this interaction regulates its distribution at the cell cortex. Ref.10 Ref.12 Ref.14 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Note: Colocalizes with microtubules. Ref.24

Tissue specificity

Brain.

Post-translational modification

Ubiquitinated by a SCF complex containing FBXL5, leading to its degradation by the proteasome. Ref.12

Involvement in disease

Neuronopathy, distal hereditary motor, 7B (HMN7B) [MIM:607641]: A neuromuscular disorder. Distal hereditary motor neuronopathies constitute 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26 Ref.29 Ref.30 Ref.32

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.27 Ref.28

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.30

Sequence similarities

Belongs to the dynactin 150 kDa subunit family.

Contains 1 CAP-Gly domain.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCytoplasm
Cytoskeleton
Dynein
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAmyotrophic lateral sclerosis
Neurodegeneration
Parkinsonism
   DomainCoiled coil
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular protein metabolic process

Traceable author statement. Source: Reactome

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

microtubule-based transport

Inferred from electronic annotation. Source: InterPro

mitosis

Non-traceable author statement PubMed 1828535. Source: ProtInc

mitotic cell cycle

Traceable author statement. Source: Reactome

nervous system development

Non-traceable author statement PubMed 17360970. Source: UniProtKB

   Cellular_componentcell leading edge

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

cytoplasm

Traceable author statement PubMed 1828535. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

dynactin complex

Inferred from electronic annotation. Source: InterPro

dynein complex

Inferred from electronic annotation. Source: UniProtKB-KW

kinetochore

Inferred from direct assay PubMed 19468067. Source: UniProtKB

microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

spindle pole

Inferred from direct assay PubMed 14718566. Source: UniProtKB

   Molecular_functionmotor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform p150 (identifier: Q14203-1)

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.
Isoform p135 (identifier: Q14203-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: MAQSKRHVYS...SKLRGLKPKK → MMRQ
Isoform 3 (identifier: Q14203-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.
     132-151: Missing.
     1066-1070: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q14203-4)

The sequence of this isoform differs from the canonical sequence as follows:
     132-151: Missing.
     1066-1070: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q14203-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: MAQSKRHVYS...SKLRGLKPKK → MMRQ
     1066-1070: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: Q14203-6)

The sequence of this isoform differs from the canonical sequence as follows:
     132-138: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12781278Dynactin subunit 1
PRO_0000083518

Regions

Domain48 – 9043CAP-Gly
Coiled coil213 – 547335 Potential
Coiled coil943 – 1049107 Potential
Coiled coil1182 – 121130 Potential
Compositional bias164 – 19128Ser-rich

Amino acid modifications

Modified residue1081Phosphothreonine Ref.15

Natural variations

Alternative sequence1 – 138138MAQSK…LKPKK → MMRQ in isoform p135 and isoform 5.
VSP_000760
Alternative sequence1 – 1717Missing in isoform 3.
VSP_045392
Alternative sequence132 – 15120Missing in isoform 3 and isoform 4.
VSP_045393
Alternative sequence132 – 1387Missing in isoform 6.
VSP_047174
Alternative sequence1066 – 10705Missing in isoform 3, isoform 4 and isoform 5.
VSP_045394
Natural variant591G → S in HMN7B; shows a modestly reduced affinity for microtubules which has been suggested to impair axonal transport; the effect is identical to that of complete loss of the CAP-Gly domain. Ref.26 Ref.29 Ref.30 Ref.32
VAR_015850
Natural variant711G → A in PERRYS. Ref.30
VAR_063867
Natural variant711G → E in PERRYS. Ref.30
VAR_063868
Natural variant711G → R in PERRYS; diminishes microtubule binding and lead to intracytoplasmic inclusions. Ref.30
VAR_063869
Natural variant721T → P in PERRYS. Ref.30
VAR_063870
Natural variant741Q → P in PERRYS; diminishes microtubule binding and lead to intracytoplasmic inclusions. Ref.30
VAR_063871
Natural variant1631A → P.
VAR_001373
Natural variant2871L → M.
Corresponds to variant rs13420401 [ dbSNP | Ensembl ].
VAR_048677
Natural variant4951R → Q.
Corresponds to variant rs17721059 [ dbSNP | Ensembl ].
VAR_048678
Natural variant5711M → T in susceptibility to amyotrophic lateral sclerosis. Ref.27
VAR_063872
Natural variant7851R → W in susceptibility to amyotrophic lateral sclerosis. Ref.27
VAR_063873
Natural variant11011R → K in susceptibility to amyotrophic lateral sclerosis. Ref.28
VAR_063874
Natural variant12491T → I in susceptibility to amyotrophic lateral sclerosis; unknown pathological significance. Ref.27 Ref.31
Corresponds to variant rs72466496 [ dbSNP | Ensembl ].
VAR_063875

Experimental info

Mutagenesis681K → A: Abolishes interaction with CLIP1. Ref.25
Mutagenesis901R → E: Abolishes interaction with CLIP1. Ref.25
Sequence conflict101S → N in CAA67333. Ref.7
Sequence conflict2571Q → R in BAG59757. Ref.2
Sequence conflict3491K → R in AK314352. Ref.2
Sequence conflict3681A → V in AK314352. Ref.2
Sequence conflict5261H → N in AAH71583. Ref.5
Sequence conflict6181K → R in AAH71583. Ref.5
Sequence conflict7121D → V in CAA67333. Ref.7
Sequence conflict10811V → M in AAP35404. Ref.9
Sequence conflict12611R → Q in BAG59757. Ref.2
Sequence conflict12741S → I in AAH71583. Ref.5

Secondary structure

...................... 1278
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform p150 [UniParc].

Last modified October 18, 2001. Version 3.
Checksum: 6DCEA5E67856E4BC

FASTA1,278141,695
        10         20         30         40         50         60 
MAQSKRHVYS RTPSGSRMSA EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV 

        70         80         90        100        110        120 
ILDEAKGKND GTVQGRKYFT CDEGHGIFVR QSQIQVFEDG ADTTSPETPD SSASKVLKRE 

       130        140        150        160        170        180 
GTDTTAKTSK LRGLKPKKAP TARKTTTRRP KPTRPASTGV AGASSSLGPS GSASAGELSS 

       190        200        210        220        230        240 
SEPSTPAQTP LAAPIIPTPV LTSPGAVPPL PSPSKEEEGL RAQVRDLEEK LETLRLKRAE 

       250        260        270        280        290        300 
DKAKLKELEK HKIQLEQVQE WKSKMQEQQA DLQRRLKEAR KEAKEALEAK ERYMEEMADT 

       310        320        330        340        350        360 
ADAIEMATLD KEMAEERAES LQQEVEALKE RVDELTTDLE ILKAEIEEKG SDGAASSYQL 

       370        380        390        400        410        420 
KQLEEQNARL KDALVRMRDL SSSEKQEHVK LQKLMEKKNQ ELEVVRQQRE RLQEELSQAE 

       430        440        450        460        470        480 
STIDELKEQV DAALGAEEMV EMLTDRNLNL EEKVRELRET VGDLEAMNEM NDELQENARE 

       490        500        510        520        530        540 
TELELREQLD MAGARVREAQ KRVEAAQETV ADYQQTIKKY RQLTAHLQDV NRELTNQQEA 

       550        560        570        580        590        600 
SVERQQQPPP ETFDFKIKFA ETKAHAKAIE MELRQMEVAQ ANRHMSLLTA FMPDSFLRPG 

       610        620        630        640        650        660 
GDHDCVLVLL LMPRLICKAE LIRKQAQEKF ELSENCSERP GLRGAAGEQL SFAAGLVYSL 

       670        680        690        700        710        720 
SLLQATLHRY EHALSQCSVD VYKKVGSLYP EMSAHERSLD FLIELLHKDQ LDETVNVEPL 

       730        740        750        760        770        780 
TKAIKYYQHL YSIHLAEQPE DCTMQLADHI KFTQSALDCM SVEVGRLRAF LQGGQEATDI 

       790        800        810        820        830        840 
ALLLRDLETS CSDIRQFCKK IRRRMPGTDA PGIPAALAFG PQVSDTLLDC RKHLTWVVAV 

       850        860        870        880        890        900 
LQEVAAAAAQ LIAPLAENEG LLVAALEELA FKASEQIYGT PSSSPYECLR QSCNILISTM 

       910        920        930        940        950        960 
NKLATAMQEG EYDAERPPSK PPPVELRAAA LRAEITDAEG LGLKLEDRET VIKELKKSLK 

       970        980        990       1000       1010       1020 
IKGEELSEAN VRLSLLEKKL DSAAKDADER IEKVQTRLEE TQALLRKKEK EFEETMDALQ 

      1030       1040       1050       1060       1070       1080 
ADIDQLEAEK AELKQRLNSQ SKRTIEGLRG PPPSGIATLV SGIAGEEQQR GAIPGQAPGS 

      1090       1100       1110       1120       1130       1140 
VPGPGLVKDS PLLLQQISAM RLHISQLQHE NSILKGAQMK ASLASLPPLH VAKLSHEGPG 

      1150       1160       1170       1180       1190       1200 
SELPAGALYR KTSQLLETLN QLSTHTHVVD ITRTSPAAKS PSAQLMEQVA QLKSLSDTVE 

      1210       1220       1230       1240       1250       1260 
KLKDEVLKET VSQRPGATVP TDFATFPSSA FLRAKEEQQD DTVYMGKVTF SCAAGFGQRH 

      1270 
RLVLTQEQLH QLHSRLIS 

« Hide

Isoform p135 [UniParc].

Checksum: D4011CF3E4BF06F6
Show »

FASTA1,144127,404
Isoform 3 [UniParc].

Checksum: F4374391D7DF0F04
Show »

FASTA1,236136,820
Isoform 4 [UniParc].

Checksum: 9871FA03C07751DE
Show »

FASTA1,253138,750
Isoform 5 [UniParc].

Checksum: 1997342C3ADA9F82
Show »

FASTA1,139126,733
Isoform 6 [UniParc].

Checksum: 7BCE4BF282947485
Show »

FASTA1,271140,887

References

« Hide 'large scale' references
[1]"Human DCTN1: genomic structure and evaluation as a candidate for Alstrom syndrome."
Collin G.B., Nishina P.M., Marshall J.D., Naggert J.K.
Genomics 53:359-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
Tissue: Brain and Trachea.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Brain.
[6]"Localization of the DCTN1 gene encoding p150Glued to human chromosome 2p13 by fluorescence in situ hybridization."
Holzbaur E.L.F., Tokito M.K.
Genomics 31:398-399(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-1278.
Tissue: Brain.
[7]"Functionally distinct isoforms of dynactin are expressed in human neurons."
Tokito M.K., Howland D.S., Lee V.M.-Y., Holzbaur E.L.F.
Mol. Biol. Cell 7:1167-1180(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-1278 (ISOFORM 6), ALTERNATIVE SPLICING.
Tissue: Brain.
[8]"The genomic structure of DCTN1, a candidate gene for limb-girdle muscular dystrophy."
Tokito M.K., Holzbaur E.L.F.
Biochim. Biophys. Acta 1442:432-436(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-1278.
[9]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1081-1278.
[10]"Characterization of functional domains of human EB1 family proteins."
Bu W., Su L.-K.
J. Biol. Chem. 278:49721-49731(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAPRE1; MAPRE2 AND MAPRE3.
[11]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"FBXL5 interacts with p150Glued and regulates its ubiquitination."
Zhang N., Liu J., Ding X., Aikhionbare F., Jin C., Yao X.
Biochem. Biophys. Res. Commun. 359:34-39(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, INTERACTION WITH FBXL5.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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.
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ECM29.
[17]"A novel human dynactin-associated protein, dynAP, promotes activation of Akt, and ergosterol-related compounds induce dynAP-dependent apoptosis of human cancer cells."
Kunoh T., Noda T., Koseki K., Sekigawa M., Takagi M., Shin-ya K., Goshima N., Iemura S., Natsume T., Wada S., Mukai Y., Ohta S., Sasaki R., Mizukami T.
Mol. Cancer Ther. 9:2934-2942(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DYNAP.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Neuronal ceroid lipofuscinosis protein CLN3 interacts with motor proteins and modifies location of late endosomal compartments."
Uusi-Rauva K., Kyttala A., van der Kant R., Vesa J., Tanhuanpaa K., Neefjes J., Olkkonen V.M., Jalanko A.
Cell. Mol. Life Sci. 69:2075-2089(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLN3.
[20]"MISP is a novel Plk1 substrate required for proper spindle orientation and mitotic progression."
Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L., Ponting C.P., Goenczy P., Hoffmann I.
J. Cell Biol. 200:773-787(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MISP.
[21]"Structural basis for the activation of microtubule assembly by the EB1 and p150Glued complex."
Hayashi I., Wilde A., Mal T.K., Ikura M.
Mol. Cell 19:449-460(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 15-107 IN COMPLEX WITH MAPRE1, INTERACTION WITH MAPRE1.
[22]"Solution structure of the CAP-Gly domain in human dynactin 1."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-99.
[23]"Key interaction modes of dynamic +TIP networks."
Honnappa S., Okhrimenko O., Jaussi R., Jawhari H., Jelesarov I., Winkler F.K., Steinmetz M.O.
Mol. Cell 23:663-671(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 18-111 IN COMPLEX WITH MAPRE1, INTERACTION WITH MAPRE1.
[24]"Structure-function relationship of CAP-Gly domains."
Weisbrich A., Honnappa S., Jaussi R., Okhrimenko O., Frey D., Jelesarov I., Akhmanova A., Steinmetz M.O.
Nat. Struct. Mol. Biol. 14:959-967(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 15-111 IN COMPLEX WITH CLIP1, SUBCELLULAR LOCATION, INTERACTION WITH CLIP1.
[25]"CLIP170 autoinhibition mimics intermolecular interactions with p150Glued or EB1."
Hayashi I., Plevin M.J., Ikura M.
Nat. Struct. Mol. Biol. 14:980-981(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 15-107 IN COMPLEX WITH CLIP1, INTERACTION WITH CLIP1, MUTAGENESIS OF LYS-68 AND ARG-90.
[26]"Mutant dynactin in motor neuron disease."
Puls I., Jonnakuty C., LaMonte B.H., Holzbaur E.L., Tokito M., Mann E., Floeter M.K., Bidus K., Drayna D., Oh S.J., Brown R.H. Jr., Ludlow C.L., Fischbeck K.H.
Nat. Genet. 33:455-456(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HMN7B SER-59.
[27]"Point mutations of the p150 subunit of dynactin (DCTN1) gene in ALS."
Muench C., Sedlmeier R., Meyer T., Homberg V., Sperfeld A.D., Kurt A., Prudlo J., Peraus G., Hanemann C.O., Stumm G., Ludolph A.C.
Neurology 63:724-726(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SUSCEPTIBILITY TO ALS THR-571; TRP-785 AND ILE-1249.
[28]"Heterozygous R1101K mutation of the DCTN1 gene in a family with ALS and FTD."
Muench C., Rosenbohm A., Sperfeld A.-D., Uttner I., Reske S., Krause B.J., Sedlmeier R., Meyer T., Hanemann C.O., Stumm G., Ludolph A.C.
Ann. Neurol. 58:777-780(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SUSCEPTIBILITY TO ALS LYS-1101.
[29]"A motor neuron disease-associated mutation in p150Glued perturbs dynactin function and induces protein aggregation."
Levy J.R., Sumner C.J., Caviston J.P., Tokito M.K., Ranganathan S., Ligon L.A., Wallace K.E., LaMonte B.H., Harmison G.G., Puls I., Fischbeck K.H., Holzbaur E.L.F.
J. Cell Biol. 172:733-745(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT HMN7B SER-59.
[30]"DCTN1 mutations in Perry syndrome."
Farrer M.J., Hulihan M.M., Kachergus J.M., Daechsel J.C., Stoessl A.J., Grantier L.L., Calne S., Calne D.B., Lechevalier B., Chapon F., Tsuboi Y., Yamada T., Gutmann L., Elibol B., Bhatia K.P., Wider C., Vilarino-Gueell C., Ross O.A. expand/collapse author list , Brown L.A., Castanedes-Casey M., Dickson D.W., Wszolek Z.K.
Nat. Genet. 41:163-165(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PERRYS ARG-71; GLU-71; ALA-71; PRO-72 AND PRO-74, CHARACTERIZATION OF VARIANTS PERRYS ARG-71 AND PRO-74, CHARACTERIZATION OF VARIANT HMN7B SER-59.
[31]"Characterization of DCTN1 genetic variability in neurodegeneration."
Vilarino-Gueell C., Wider C., Soto-Ortolaza A.I., Cobb S.A., Kachergus J.M., Keeling B.H., Dachsel J.C., Hulihan M.M., Dickson D.W., Wszolek Z.K., Uitti R.J., Graff-Radford N.R., Boeve B.F., Josephs K.A., Miller B., Boylan K.B., Gwinn K., Adler C.H. expand/collapse author list , Aasly J.O., Hentati F., Destee A., Krygowska-Wajs A., Chartier-Harlin M.-C., Ross O.A., Rademakers R., Farrer M.J.
Neurology 72:2024-2028(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ILE-1249.
[32]"Neurodegeneration mutations in dynactin impair dynein-dependent nuclear migration."
Moore J.K., Sept D., Cooper J.A.
Proc. Natl. Acad. Sci. U.S.A. 106:5147-5152(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT HMN7B SER-59.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF064205, AF064203, AF064204 Genomic DNA. Translation: AAD55811.1.
AF064205, AF064204 Genomic DNA. Translation: AAD55812.1.
AK297286 mRNA. Translation: BAG59757.1.
AK314352 mRNA. No translation available.
AC005041 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAW99684.1.
BC071583 mRNA. Translation: AAH71583.1.
X98801 mRNA. Translation: CAA67333.1.
AF086947 expand/collapse EMBL AC list , AF086927, AF086928, AF086929, AF086930, AF086931, AF086932, AF086933, AF086934, AF086935, AF086936, AF086937, AF086938, AF086939, AF086940, AF086941, AF086942, AF086943, AF086944, AF086945, AF086946 Genomic DNA. Translation: AAD03694.1.
BT006758 mRNA. Translation: AAP35404.1.
RefSeqNP_001128512.1. NM_001135040.2.
NP_001128513.1. NM_001135041.2.
NP_001177765.1. NM_001190836.1.
NP_001177766.1. NM_001190837.1.
NP_004073.2. NM_004082.4.
NP_075408.1. NM_023019.3.
UniGeneHs.516111.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TXQX-ray1.80A15-107[»]
2COYNMR-A1-99[»]
2HKNX-ray1.87A/B18-111[»]
2HKQX-ray1.86B18-111[»]
2HL3X-ray2.03A/B18-111[»]
2HL5X-ray1.93C/D18-111[»]
2HQHX-ray1.80A/B/C/D15-107[»]
3E2UX-ray2.60A/B/C/D15-111[»]
3TQ7X-ray2.30P/Q27-97[»]
ProteinModelPortalQ14203.
SMRQ14203. Positions 25-98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108007. 57 interactions.
DIPDIP-31365N.
IntActQ14203. 38 interactions.
MINTMINT-5004548.
STRING9606.ENSP00000354791.

PTM databases

PhosphoSiteQ14203.

Polymorphism databases

DMDM17375490.

2D gel databases

OGPQ14203.

Proteomic databases

PaxDbQ14203.
PRIDEQ14203.

Protocols and materials databases

DNASU1639.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361874; ENSP00000354791; ENSG00000204843. [Q14203-1]
ENST00000394003; ENSP00000377571; ENSG00000204843. [Q14203-6]
ENST00000407639; ENSP00000384844; ENSG00000204843. [Q14203-2]
ENST00000409240; ENSP00000386406; ENSG00000204843. [Q14203-3]
ENST00000409438; ENSP00000387270; ENSG00000204843. [Q14203-5]
ENST00000409567; ENSP00000386843; ENSG00000204843. [Q14203-4]
GeneID1639.
KEGGhsa:1639.
UCSCuc002sku.3. human.
uc002skv.3. human. [Q14203-2]
uc002skx.3. human. [Q14203-1]

Organism-specific databases

CTD1639.
GeneCardsGC02M074588.
H-InvDBHIX0204314.
HGNCHGNC:2711. DCTN1.
HPACAB009108.
HPA034635.
MIM105400. phenotype.
168605. phenotype.
601143. gene.
607641. phenotype.
neXtProtNX_Q14203.
Orphanet803. Amyotrophic lateral sclerosis.
139589. Distal hereditary motor neuropathy type 7.
178509. Perry syndrome.
PharmGKBPA27180.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5244.
HOGENOMHOG000015352.
HOVERGENHBG004956.
KOK04648.
OMASAQLMEQ.
OrthoDBEOG79W94B.
PhylomeDBQ14203.
TreeFamTF105246.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_17015. Metabolism of proteins.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ14203.
BgeeQ14203.
CleanExHS_DCTN1.
GenevestigatorQ14203.

Family and domain databases

Gene3D2.30.30.190. 1 hit.
InterProIPR000938. CAP-Gly_domain.
IPR027663. DCTN1.
IPR022157. Dynactin.
[Graphical view]
PANTHERPTHR18916:SF26. PTHR18916:SF26. 1 hit.
PfamPF01302. CAP_GLY. 1 hit.
PF12455. Dynactin. 1 hit.
[Graphical view]
SMARTSM01052. CAP_GLY. 1 hit.
[Graphical view]
SUPFAMSSF74924. SSF74924. 1 hit.
PROSITEPS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDCTN1. human.
EvolutionaryTraceQ14203.
GeneWikiDCTN1.
GenomeRNAi1639.
NextBio6734.
PMAP-CutDBQ14203.
PROQ14203.
SOURCESearch...

Entry information

Entry nameDCTN1_HUMAN
AccessionPrimary (citable) accession number: Q14203
Secondary accession number(s): A8MY36 expand/collapse secondary AC list , B4DM45, E9PFS5, E9PGE1, G5E9H4, O95296, Q6IQ37, Q9BRM9, Q9UIU1, Q9UIU2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 18, 2001
Last modified: April 16, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM