Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q14203

- DCTN1_HUMAN

UniProt

Q14203 - DCTN1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dynactin subunit 1

Gene

DCTN1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. motor activity Source: UniProtKB-KW

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  3. cell death Source: UniProtKB-KW
  4. cellular protein metabolic process Source: Reactome
  5. endoplasmic reticulum unfolded protein response Source: Reactome
  6. G2/M transition of mitotic cell cycle Source: Reactome
  7. melanosome transport Source: Ensembl
  8. microtubule-based transport Source: InterPro
  9. mitotic cell cycle Source: Reactome
  10. mitotic nuclear division Source: ProtInc
  11. nervous system development Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_18273. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Dynactin subunit 1
Alternative name(s):
150 kDa dynein-associated polypeptide
DAP-150
Short name:
DP-150
p135
p150-glued
Gene namesi
Name:DCTN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:2711. DCTN1.

Subcellular locationi

Cytoplasm 1 Publication. Cytoplasmcytoskeleton 1 Publication
Note: Colocalizes with microtubules.

GO - Cellular componenti

  1. cell leading edge Source: Ensembl
  2. centrosome Source: UniProtKB
  3. cytoplasm Source: ProtInc
  4. cytosol Source: Reactome
  5. dynactin complex Source: InterPro
  6. dynein complex Source: UniProtKB-KW
  7. kinetochore Source: UniProtKB
  8. membrane Source: UniProtKB
  9. microtubule Source: UniProtKB
  10. spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591G → 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. 1 Publication
VAR_015850
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.2 Publications
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti571 – 5711M → T in ALS; associated with disease susceptibility. 1 Publication
VAR_063872
Natural varianti785 – 7851R → W in ALS; associated with disease susceptibility. 1 Publication
VAR_063873
Natural varianti1101 – 11011R → K in ALS; associated with disease susceptibility. 1 Publication
VAR_063874
Natural varianti1249 – 12491T → I in ALS; unknown pathological significance. 2 Publications
Corresponds to variant rs72466496 [ dbSNP | Ensembl ].
VAR_063875
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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521F → L in PERRYS; mutation carriers either do not develop depression or they do develop it late in the disease course. 1 Publication
VAR_071452
Natural varianti71 – 711G → A in PERRYS. 1 Publication
VAR_063867
Natural varianti71 – 711G → E in PERRYS. 1 Publication
VAR_063868
Natural varianti71 – 711G → R in PERRYS; reduced microtubule binding; results in the accumulation of intracytoplasmic inclusions. 2 Publications
VAR_063869
Natural varianti72 – 721T → P in PERRYS. 1 Publication
VAR_063870
Natural varianti74 – 741Q → P in PERRYS; diminishes microtubule binding and lead to intracytoplasmic inclusions. 1 Publication
VAR_063871
Natural varianti78 – 781Y → C in PERRYS; significantly reduced microtubule binding. 1 Publication
VAR_071453

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi68 – 681K → A: Abolishes interaction with CLIP1. 1 Publication
Mutagenesisi90 – 901R → E: Abolishes interaction with CLIP1. 1 Publication

Keywords - Diseasei

Amyotrophic lateral sclerosis, Neurodegeneration, Parkinsonism

Organism-specific databases

MIMi105400. phenotype.
168605. phenotype.
607641. phenotype.
Orphaneti803. Amyotrophic lateral sclerosis.
139589. Distal hereditary motor neuropathy type 7.
178509. Perry syndrome.
PharmGKBiPA27180.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12781278Dynactin subunit 1PRO_0000083518Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081Phosphothreonine1 Publication

Post-translational modificationi

Ubiquitinated by a SCF complex containing FBXL5, leading to its degradation by the proteasome.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ14203.
PaxDbiQ14203.
PRIDEiQ14203.

2D gel databases

OGPiQ14203.

PTM databases

PhosphoSiteiQ14203.

Miscellaneous databases

PMAP-CutDBQ14203.

Expressioni

Tissue specificityi

Brain.

Gene expression databases

BgeeiQ14203.
CleanExiHS_DCTN1.
ExpressionAtlasiQ14203. baseline and differential.
GenevestigatoriQ14203.

Organism-specific databases

HPAiCAB009108.
HPA034635.

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 (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. Interacts with CEP131.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BBS4Q96RK43EBI-724352,EBI-1805814
Hap1P542564EBI-724352,EBI-994539From a different organism.
MAPTP10636-88EBI-724352,EBI-366233

Protein-protein interaction databases

BioGridi108007. 64 interactions.
DIPiDIP-31365N.
IntActiQ14203. 42 interactions.
MINTiMINT-5004548.
STRINGi9606.ENSP00000354791.

Structurei

Secondary structure

1
1278
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 193Combined sources
Beta strandi32 – 354Combined sources
Turni36 – 383Combined sources
Beta strandi41 – 488Combined sources
Beta strandi51 – 555Combined sources
Beta strandi57 – 659Combined sources
Beta strandi67 – 737Combined sources
Beta strandi76 – 783Combined sources
Turni83 – 853Combined sources
Beta strandi86 – 894Combined sources
Helixi91 – 933Combined sources
Beta strandi94 – 963Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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/D18-111[»]
3TQ7X-ray2.30P/Q27-97[»]
ProteinModelPortaliQ14203.
SMRiQ14203. Positions 25-98.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14203.

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 coili213 – 547335Sequence AnalysisAdd
BLAST
Coiled coili943 – 1049107Sequence AnalysisAdd
BLAST
Coiled coili1182 – 121130Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi164 – 19128Ser-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.
InParanoidiQ14203.
KOiK04648.
OMAiPEDSTMQ.
OrthoDBiEOG79W94B.
PhylomeDBiQ14203.
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 (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform p150 (identifier: Q14203-1) [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
MAQSKRHVYS RTPSGSRMSA EASARPLRVG SRVEVIGKGH RGTVAYVGAT
60 70 80 90 100
LFATGKWVGV ILDEAKGKND GTVQGRKYFT CDEGHGIFVR QSQIQVFEDG
110 120 130 140 150
ADTTSPETPD SSASKVLKRE GTDTTAKTSK LRGLKPKKAP TARKTTTRRP
160 170 180 190 200
KPTRPASTGV AGASSSLGPS GSASAGELSS SEPSTPAQTP LAAPIIPTPV
210 220 230 240 250
LTSPGAVPPL PSPSKEEEGL RAQVRDLEEK LETLRLKRAE 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 ELSENCSERP GLRGAAGEQL
660 670 680 690 700
SFAAGLVYSL SLLQATLHRY EHALSQCSVD VYKKVGSLYP EMSAHERSLD
710 720 730 740 750
FLIELLHKDQ LDETVNVEPL TKAIKYYQHL YSIHLAEQPE DCTMQLADHI
760 770 780 790 800
KFTQSALDCM SVEVGRLRAF LQGGQEATDI ALLLRDLETS CSDIRQFCKK
810 820 830 840 850
IRRRMPGTDA PGIPAALAFG PQVSDTLLDC RKHLTWVVAV LQEVAAAAAQ
860 870 880 890 900
LIAPLAENEG LLVAALEELA FKASEQIYGT PSSSPYECLR QSCNILISTM
910 920 930 940 950
NKLATAMQEG EYDAERPPSK PPPVELRAAA LRAEITDAEG LGLKLEDRET
960 970 980 990 1000
VIKELKKSLK IKGEELSEAN VRLSLLEKKL DSAAKDADER IEKVQTRLEE
1010 1020 1030 1040 1050
TQALLRKKEK EFEETMDALQ ADIDQLEAEK AELKQRLNSQ SKRTIEGLRG
1060 1070 1080 1090 1100
PPPSGIATLV SGIAGEEQQR GAIPGQAPGS VPGPGLVKDS PLLLQQISAM
1110 1120 1130 1140 1150
RLHISQLQHE NSILKGAQMK ASLASLPPLH VAKLSHEGPG SELPAGALYR
1160 1170 1180 1190 1200
KTSQLLETLN QLSTHTHVVD ITRTSPAAKS PSAQLMEQVA QLKSLSDTVE
1210 1220 1230 1240 1250
KLKDEVLKET VSQRPGATVP TDFATFPSSA FLRAKEEQQD DTVYMGKVTF
1260 1270
SCAAGFGQRH RLVLTQEQLH QLHSRLIS
Length:1,278
Mass (Da):141,695
Last modified:October 18, 2001 - v3
Checksum:i6DCEA5E67856E4BC
GO
Isoform p135 (identifier: Q14203-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: MAQSKRHVYS...SKLRGLKPKK → MMRQ

Show »
Length:1,144
Mass (Da):127,404
Checksum:iD4011CF3E4BF06F6
GO
Isoform 3 (identifier: Q14203-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,236
Mass (Da):136,820
Checksum:iF4374391D7DF0F04
GO
Isoform 4 (identifier: Q14203-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     132-151: Missing.
     1066-1070: Missing.

Note: No experimental confirmation available.

Show »
Length:1,253
Mass (Da):138,750
Checksum:i9871FA03C07751DE
GO
Isoform 5 (identifier: Q14203-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,139
Mass (Da):126,733
Checksum:i1997342C3ADA9F82
GO
Isoform 6 (identifier: Q14203-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     132-138: Missing.

Note: No experimental confirmation available.

Show »
Length:1,271
Mass (Da):140,887
Checksum:i7BCE4BF282947485
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101S → N in CAA67333. (PubMed:8856662)Curated
Sequence conflicti257 – 2571Q → R in BAG59757. (PubMed:14702039)Curated
Sequence conflicti349 – 3491K → R in AK314352. (PubMed:14702039)Curated
Sequence conflicti368 – 3681A → V in AK314352. (PubMed:14702039)Curated
Sequence conflicti526 – 5261H → N in AAH71583. (PubMed:15489334)Curated
Sequence conflicti618 – 6181K → R in AAH71583. (PubMed:15489334)Curated
Sequence conflicti712 – 7121D → V in CAA67333. (PubMed:8856662)Curated
Sequence conflicti1081 – 10811V → M in AAP35404. 1 PublicationCurated
Sequence conflicti1261 – 12611R → Q in BAG59757. (PubMed:14702039)Curated
Sequence conflicti1274 – 12741S → I in AAH71583. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521F → L in PERRYS; mutation carriers either do not develop depression or they do develop it late in the disease course. 1 Publication
VAR_071452
Natural varianti59 – 591G → 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. 1 Publication
VAR_015850
Natural varianti71 – 711G → A in PERRYS. 1 Publication
VAR_063867
Natural varianti71 – 711G → E in PERRYS. 1 Publication
VAR_063868
Natural varianti71 – 711G → R in PERRYS; reduced microtubule binding; results in the accumulation of intracytoplasmic inclusions. 2 Publications
VAR_063869
Natural varianti72 – 721T → P in PERRYS. 1 Publication
VAR_063870
Natural varianti74 – 741Q → P in PERRYS; diminishes microtubule binding and lead to intracytoplasmic inclusions. 1 Publication
VAR_063871
Natural varianti78 – 781Y → C in PERRYS; significantly reduced microtubule binding. 1 Publication
VAR_071453
Natural varianti163 – 1631A → P.
VAR_001373
Natural varianti287 – 2871L → M.
Corresponds to variant rs13420401 [ dbSNP | Ensembl ].
VAR_048677
Natural varianti495 – 4951R → Q.
Corresponds to variant rs17721059 [ dbSNP | Ensembl ].
VAR_048678
Natural varianti571 – 5711M → T in ALS; associated with disease susceptibility. 1 Publication
VAR_063872
Natural varianti785 – 7851R → W in ALS; associated with disease susceptibility. 1 Publication
VAR_063873
Natural varianti1101 – 11011R → K in ALS; associated with disease susceptibility. 1 Publication
VAR_063874
Natural varianti1249 – 12491T → I in ALS; unknown pathological significance. 2 Publications
Corresponds to variant rs72466496 [ dbSNP | Ensembl ].
VAR_063875

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 138138MAQSK…LKPKK → MMRQ in isoform p135 and isoform 5. 1 PublicationVSP_000760Add
BLAST
Alternative sequencei1 – 1717Missing in isoform 3. 1 PublicationVSP_045392Add
BLAST
Alternative sequencei132 – 15120Missing in isoform 3 and isoform 4. 1 PublicationVSP_045393Add
BLAST
Alternative sequencei132 – 1387Missing in isoform 6. 1 PublicationVSP_047174
Alternative sequencei1066 – 10705Missing in isoform 3, isoform 4 and isoform 5. 2 PublicationsVSP_045394

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
, 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.
CCDSiCCDS1939.1. [Q14203-1]
CCDS46341.1. [Q14203-4]
CCDS46342.1. [Q14203-5]
CCDS54368.1. [Q14203-3]
CCDS54369.1. [Q14203-6]
RefSeqiNP_001128512.1. NM_001135040.2. [Q14203-4]
NP_001128513.1. NM_001135041.2. [Q14203-5]
NP_001177765.1. NM_001190836.1. [Q14203-3]
NP_001177766.1. NM_001190837.1. [Q14203-6]
NP_004073.2. NM_004082.4. [Q14203-1]
NP_075408.1. NM_023019.3. [Q14203-2]
UniGeneiHs.516111.

Genome annotation databases

EnsembliENST00000361874; ENSP00000354791; ENSG00000204843. [Q14203-1]
ENST00000394003; ENSP00000377571; ENSG00000204843. [Q14203-6]
ENST00000409240; ENSP00000386406; ENSG00000204843. [Q14203-3]
ENST00000409438; ENSP00000387270; ENSG00000204843. [Q14203-5]
ENST00000409567; ENSP00000386843; ENSG00000204843. [Q14203-4]
GeneIDi1639.
KEGGihsa:1639.
UCSCiuc002sku.3. human.
uc002skv.3. human. [Q14203-2]
uc002skx.3. human. [Q14203-1]

Polymorphism databases

DMDMi17375490.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
, 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 .
CCDSi CCDS1939.1. [Q14203-1 ]
CCDS46341.1. [Q14203-4 ]
CCDS46342.1. [Q14203-5 ]
CCDS54368.1. [Q14203-3 ]
CCDS54369.1. [Q14203-6 ]
RefSeqi NP_001128512.1. NM_001135040.2. [Q14203-4 ]
NP_001128513.1. NM_001135041.2. [Q14203-5 ]
NP_001177765.1. NM_001190836.1. [Q14203-3 ]
NP_001177766.1. NM_001190837.1. [Q14203-6 ]
NP_004073.2. NM_004082.4. [Q14203-1 ]
NP_075408.1. NM_023019.3. [Q14203-2 ]
UniGenei Hs.516111.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TXQ X-ray 1.80 A 15-107 [» ]
2COY NMR - A 1-99 [» ]
2HKN X-ray 1.87 A/B 18-111 [» ]
2HKQ X-ray 1.86 B 18-111 [» ]
2HL3 X-ray 2.03 A/B 18-111 [» ]
2HL5 X-ray 1.93 C/D 18-111 [» ]
2HQH X-ray 1.80 A/B/C/D 15-107 [» ]
3E2U X-ray 2.60 A/B/C/D 18-111 [» ]
3TQ7 X-ray 2.30 P/Q 27-97 [» ]
ProteinModelPortali Q14203.
SMRi Q14203. Positions 25-98.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108007. 64 interactions.
DIPi DIP-31365N.
IntActi Q14203. 42 interactions.
MINTi MINT-5004548.
STRINGi 9606.ENSP00000354791.

PTM databases

PhosphoSitei Q14203.

Polymorphism databases

DMDMi 17375490.

2D gel databases

OGPi Q14203.

Proteomic databases

MaxQBi Q14203.
PaxDbi Q14203.
PRIDEi Q14203.

Protocols and materials databases

DNASUi 1639.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361874 ; ENSP00000354791 ; ENSG00000204843 . [Q14203-1 ]
ENST00000394003 ; ENSP00000377571 ; ENSG00000204843 . [Q14203-6 ]
ENST00000409240 ; ENSP00000386406 ; ENSG00000204843 . [Q14203-3 ]
ENST00000409438 ; ENSP00000387270 ; ENSG00000204843 . [Q14203-5 ]
ENST00000409567 ; ENSP00000386843 ; ENSG00000204843 . [Q14203-4 ]
GeneIDi 1639.
KEGGi hsa:1639.
UCSCi uc002sku.3. human.
uc002skv.3. human. [Q14203-2 ]
uc002skx.3. human. [Q14203-1 ]

Organism-specific databases

CTDi 1639.
GeneCardsi GC02M074588.
GeneReviewsi DCTN1.
H-InvDB HIX0204314.
HGNCi HGNC:2711. DCTN1.
HPAi CAB009108.
HPA034635.
MIMi 105400. phenotype.
168605. phenotype.
601143. gene.
607641. phenotype.
neXtProti NX_Q14203.
Orphaneti 803. Amyotrophic lateral sclerosis.
139589. Distal hereditary motor neuropathy type 7.
178509. Perry syndrome.
PharmGKBi PA27180.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5244.
GeneTreei ENSGT00770000120567.
HOGENOMi HOG000015352.
HOVERGENi HBG004956.
InParanoidi Q14203.
KOi K04648.
OMAi PEDSTMQ.
OrthoDBi EOG79W94B.
PhylomeDBi Q14203.
TreeFami TF105246.

Enzyme and pathway databases

Reactomei REACT_121399. MHC class II antigen presentation.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_18273. XBP1(S) activates chaperone genes.

Miscellaneous databases

ChiTaRSi DCTN1. human.
EvolutionaryTracei Q14203.
GeneWikii DCTN1.
GenomeRNAii 1639.
NextBioi 6734.
PMAP-CutDB Q14203.
PROi Q14203.
SOURCEi Search...

Gene expression databases

Bgeei Q14203.
CleanExi HS_DCTN1.
ExpressionAtlasi Q14203. baseline and differential.
Genevestigatori Q14203.

Family and domain databases

Gene3Di 2.30.30.190. 1 hit.
InterProi IPR000938. CAP-Gly_domain.
IPR027663. DCTN1.
IPR022157. Dynactin.
[Graphical view ]
PANTHERi PTHR18916:SF29. PTHR18916:SF29. 1 hit.
Pfami PF01302. CAP_GLY. 1 hit.
PF12455. Dynactin. 1 hit.
[Graphical view ]
SMARTi SM01052. CAP_GLY. 1 hit.
[Graphical view ]
SUPFAMi SSF74924. SSF74924. 1 hit.
PROSITEi PS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. Cited for: INTERACTION WITH CEP131.
  21. "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.
  22. "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.
  23. "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.
  24. Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 18-111 IN COMPLEX WITH MAPRE1, INTERACTION WITH MAPRE1.
  25. Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 15-111 IN COMPLEX WITH CLIP1, SUBCELLULAR LOCATION, INTERACTION WITH CLIP1.
  26. "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.
  27. Cited for: VARIANT HMN7B SER-59.
  28. Cited for: INVOLVEMENT IN ALS, VARIANTS ALS THR-571; TRP-785 AND ILE-1249.
  29. Cited for: VARIANT ALS LYS-1101.
  30. "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.
  31. 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.
  32. Cited for: VARIANT ILE-1249.
  33. "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.
  34. "A Novel DCTN1 mutation with late-onset parkinsonism and frontotemporal atrophy."
    Araki E., Tsuboi Y., Daechsel J., Milnerwood A., Vilarino-Guell C., Fujii N., Mishima T., Oka T., Hara H., Fukae J., Farrer M.J.
    Mov. Disord. 29:1201-1204(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PERRYS LEU-52.
  35. Cited for: VARIANTS PERRYS ARG-71 AND CYS-78, CHARACTERIZATION OF VARIANTS PERRYS ARG-71 AND CYS-78.

Entry informationi

Entry nameiDCTN1_HUMAN
AccessioniPrimary (citable) accession number: Q14203
Secondary accession number(s): A8MY36
, B4DM45, E9PFS5, E9PGE1, G5E9H4, O95296, Q6IQ37, Q9BRM9, Q9UIU1, Q9UIU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 18, 2001
Last modified: November 26, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3