Q14203 (DCTN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1278 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.10 Ref.12 Ref.14 Ref.16 Ref.17 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Note: Colocalizes with microtubules. Ref.23
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	Distal hereditary motor neuronopathy 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.25 Ref.28 Ref.29 Ref.31 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.26 Ref.27 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.29
Sequence similarities	Belongs to the dynactin 150 kDa subunit family. Contains 1 CAP-Gly domain.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm Cytoskeleton Dynein Microtubule
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Amyotrophic lateral sclerosis Neurodegeneration Parkinsonism
Domain	Coiled coil
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/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 mitosis Non-traceable author statement PubMed 1828535. Source: ProtInc nervous system development Non-traceable author statement PubMed 17360970. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell leading edge Inferred from electronic annotation. Source: Compara centrosome Inferred from direct assay PubMed 21399614. Source: UniProtKB cytosol Traceable author statement. Source: Reactome 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_function	motor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BBS4	Q96RK4	3	EBI-724352,EBI-1805814

Alternative products

This entry describes 5 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1278

1278

Dynactin subunit 1

PRO_0000083518

Regions

Domain

48 – 90

43

CAP-Gly

Coiled coil

213 – 547

335

Potential

Coiled coil

943 – 1049

107

Potential

Coiled coil

1182 – 1211

30

Potential

Compositional bias

164 – 191

28

Ser-rich

Amino acid modifications

Modified residue

108

1

Phosphothreonine Ref.15

Modified residue

541

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 138

138

MAQSK…LKPKK → MMRQ in isoform p135 and isoform 5.

VSP_000760

Alternative sequence

1 – 17

17

Missing in isoform 3.

VSP_045392

Alternative sequence

132 – 151

20

Missing in isoform 3 and isoform 4.

VSP_045393

Alternative sequence

1066 – 1070

5

Missing in isoform 3, isoform 4 and isoform 5.

VSP_045394

Natural variant

59

1

G → 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.25 Ref.28 Ref.29 Ref.31

VAR_015850

Natural variant

71

1

G → A in PERRYS. Ref.29

VAR_063867

Natural variant

71

1

G → E in PERRYS. Ref.29

VAR_063868

Natural variant

71

1

G → R in PERRYS; diminishes microtubule binding and lead to intracytoplasmic inclusions. Ref.29

VAR_063869

Natural variant

72

1

T → P in PERRYS. Ref.29

VAR_063870

Natural variant

74

1

Q → P in PERRYS; diminishes microtubule binding and lead to intracytoplasmic inclusions. Ref.29

VAR_063871

Natural variant

163

1

A → P.

VAR_001373

Natural variant

287

1

L → M.
Corresponds to variant rs13420401 [ dbSNP | Ensembl ].

VAR_048677

Natural variant

495

1

R → Q.
Corresponds to variant rs17721059 [ dbSNP | Ensembl ].

VAR_048678

Natural variant

571

1

M → T in susceptibility to amyotrophic lateral sclerosis. Ref.26

VAR_063872

Natural variant

785

1

R → W in susceptibility to amyotrophic lateral sclerosis. Ref.26

VAR_063873

Natural variant

1101

1

R → K in susceptibility to amyotrophic lateral sclerosis. Ref.27

VAR_063874

Natural variant

1249

1

T → I in susceptibility to amyotrophic lateral sclerosis; uncertain pathogenicity. Ref.26 Ref.30

VAR_063875

Experimental info

Mutagenesis

68

1

K → A: Abolishes interaction with CLIP1. Ref.24

Mutagenesis

90

1

R → E: Abolishes interaction with CLIP1. Ref.24

Sequence conflict

10

1

S → N no nucleotide entry Ref.3

Sequence conflict

10

1

S → N in CAA67333. Ref.7

Sequence conflict

132 – 138

7

Missing no nucleotide entry Ref.3

Sequence conflict

132 – 138

7

Missing in CAA67333. Ref.7

Sequence conflict

257

1

Q → R in BAG59757. Ref.2

Sequence conflict

349

1

K → R in AK314352. Ref.2

Sequence conflict

368

1

A → V in AK314352. Ref.2

Sequence conflict

526

1

H → N in AAH71583. Ref.5

Sequence conflict

618

1

K → R in AAH71583. Ref.5

Sequence conflict

712

1

D → V no nucleotide entry Ref.3

Sequence conflict

712

1

D → V in CAA67333. Ref.7

Sequence conflict

1081

1

V → M in AAP35404. Ref.9

Sequence conflict

1261

1

R → Q in BAG59757. Ref.2

Sequence conflict

1274

1

S → I in AAH71583. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1278

Helix Strand Turn

Details...

Beta strand

17 – 19

3

Beta strand

32 – 35

4

Turn

36 – 38

3

Beta strand

41 – 48

8

Beta strand

51 – 55

5

Beta strand

57 – 65

9

Beta strand

67 – 73

7

Beta strand

76 – 78

3

Turn

83 – 85

3

Beta strand

86 – 89

4

Helix

91 – 93

3

Beta strand

94 – 96

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform p150 [UniParc]. Last modified October 18, 2001. Version 3. Checksum: 6DCEA5E67856E4BC	FASTA	1,278	141,695
	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
	Isoform p135 [UniParc]. Checksum: D4011CF3E4BF06F6	FASTA	1,144	127,404
	10 20 30 40 50 60 MMRQAPTARK TTTRRPKPTR PASTGVAGAS SSLGPSGSAS AGELSSSEPS TPAQTPLAAP 70 80 90 100 110 120 IIPTPVLTSP GAVPPLPSPS KEEEGLRAQV RDLEEKLETL RLKRAEDKAK LKELEKHKIQ 130 140 150 160 170 180 LEQVQEWKSK MQEQQADLQR RLKEARKEAK EALEAKERYM EEMADTADAI EMATLDKEMA 190 200 210 220 230 240 EERAESLQQE VEALKERVDE LTTDLEILKA EIEEKGSDGA ASSYQLKQLE EQNARLKDAL 250 260 270 280 290 300 VRMRDLSSSE KQEHVKLQKL MEKKNQELEV VRQQRERLQE ELSQAESTID ELKEQVDAAL 310 320 330 340 350 360 GAEEMVEMLT DRNLNLEEKV RELRETVGDL EAMNEMNDEL QENARETELE LREQLDMAGA 370 380 390 400 410 420 RVREAQKRVE AAQETVADYQ QTIKKYRQLT AHLQDVNREL TNQQEASVER QQQPPPETFD 430 440 450 460 470 480 FKIKFAETKA HAKAIEMELR QMEVAQANRH MSLLTAFMPD SFLRPGGDHD CVLVLLLMPR 490 500 510 520 530 540 LICKAELIRK QAQEKFELSE NCSERPGLRG AAGEQLSFAA GLVYSLSLLQ ATLHRYEHAL 550 560 570 580 590 600 SQCSVDVYKK VGSLYPEMSA HERSLDFLIE LLHKDQLDET VNVEPLTKAI KYYQHLYSIH 610 620 630 640 650 660 LAEQPEDCTM QLADHIKFTQ SALDCMSVEV GRLRAFLQGG QEATDIALLL RDLETSCSDI 670 680 690 700 710 720 RQFCKKIRRR MPGTDAPGIP AALAFGPQVS DTLLDCRKHL TWVVAVLQEV AAAAAQLIAP 730 740 750 760 770 780 LAENEGLLVA ALEELAFKAS EQIYGTPSSS PYECLRQSCN ILISTMNKLA TAMQEGEYDA 790 800 810 820 830 840 ERPPSKPPPV ELRAAALRAE ITDAEGLGLK LEDRETVIKE LKKSLKIKGE ELSEANVRLS 850 860 870 880 890 900 LLEKKLDSAA KDADERIEKV QTRLEETQAL LRKKEKEFEE TMDALQADID QLEAEKAELK 910 920 930 940 950 960 QRLNSQSKRT IEGLRGPPPS GIATLVSGIA GEEQQRGAIP GQAPGSVPGP GLVKDSPLLL 970 980 990 1000 1010 1020 QQISAMRLHI SQLQHENSIL KGAQMKASLA SLPPLHVAKL SHEGPGSELP AGALYRKTSQ 1030 1040 1050 1060 1070 1080 LLETLNQLST HTHVVDITRT SPAAKSPSAQ LMEQVAQLKS LSDTVEKLKD EVLKETVSQR 1090 1100 1110 1120 1130 1140 PGATVPTDFA TFPSSAFLRA KEEQQDDTVY MGKVTFSCAA GFGQRHRLVL TQEQLHQLHS RLIS
	Isoform 3 [UniParc]. Checksum: F4374391D7DF0F04	FASTA	1,236	136,820
	10 20 30 40 50 60 MSAEASARPL RVGSRVEVIG KGHRGTVAYV GATLFATGKW VGVILDEAKG KNDGTVQGRK 70 80 90 100 110 120 YFTCDEGHGI FVRQSQIQVF EDGADTTSPE TPDSSASKVL KREGTDTTAK TSKLPTRPAS 130 140 150 160 170 180 TGVAGASSSL GPSGSASAGE LSSSEPSTPA QTPLAAPIIP TPVLTSPGAV PPLPSPSKEE 190 200 210 220 230 240 EGLRAQVRDL EEKLETLRLK RAEDKAKLKE LEKHKIQLEQ VQEWKSKMQE QQADLQRRLK 250 260 270 280 290 300 EARKEAKEAL EAKERYMEEM ADTADAIEMA TLDKEMAEER AESLQQEVEA LKERVDELTT 310 320 330 340 350 360 DLEILKAEIE EKGSDGAASS YQLKQLEEQN ARLKDALVRM RDLSSSEKQE HVKLQKLMEK 370 380 390 400 410 420 KNQELEVVRQ QRERLQEELS QAESTIDELK EQVDAALGAE EMVEMLTDRN LNLEEKVREL 430 440 450 460 470 480 RETVGDLEAM NEMNDELQEN ARETELELRE QLDMAGARVR EAQKRVEAAQ ETVADYQQTI 490 500 510 520 530 540 KKYRQLTAHL QDVNRELTNQ QEASVERQQQ PPPETFDFKI KFAETKAHAK AIEMELRQME 550 560 570 580 590 600 VAQANRHMSL LTAFMPDSFL RPGGDHDCVL VLLLMPRLIC KAELIRKQAQ EKFELSENCS 610 620 630 640 650 660 ERPGLRGAAG EQLSFAAGLV YSLSLLQATL HRYEHALSQC SVDVYKKVGS LYPEMSAHER 670 680 690 700 710 720 SLDFLIELLH KDQLDETVNV EPLTKAIKYY QHLYSIHLAE QPEDCTMQLA DHIKFTQSAL 730 740 750 760 770 780 DCMSVEVGRL RAFLQGGQEA TDIALLLRDL ETSCSDIRQF CKKIRRRMPG TDAPGIPAAL 790 800 810 820 830 840 AFGPQVSDTL LDCRKHLTWV VAVLQEVAAA AAQLIAPLAE NEGLLVAALE ELAFKASEQI 850 860 870 880 890 900 YGTPSSSPYE CLRQSCNILI STMNKLATAM QEGEYDAERP PSKPPPVELR AAALRAEITD 910 920 930 940 950 960 AEGLGLKLED RETVIKELKK SLKIKGEELS EANVRLSLLE KKLDSAAKDA DERIEKVQTR 970 980 990 1000 1010 1020 LEETQALLRK KEKEFEETMD ALQADIDQLE AEKAELKQRL NSQSKRTIEG LRGPPPSGIA 1030 1040 1050 1060 1070 1080 TLVSGIAGGA IPGQAPGSVP GPGLVKDSPL LLQQISAMRL HISQLQHENS ILKGAQMKAS 1090 1100 1110 1120 1130 1140 LASLPPLHVA KLSHEGPGSE LPAGALYRKT SQLLETLNQL STHTHVVDIT RTSPAAKSPS 1150 1160 1170 1180 1190 1200 AQLMEQVAQL KSLSDTVEKL KDEVLKETVS QRPGATVPTD FATFPSSAFL RAKEEQQDDT 1210 1220 1230 VYMGKVTFSC AAGFGQRHRL VLTQEQLHQL HSRLIS
	Isoform 4 [UniParc]. Checksum: 9871FA03C07751DE	FASTA	1,253	138,750
	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 LPTRPASTGV AGASSSLGPS GSASAGELSS SEPSTPAQTP LAAPIIPTPV 190 200 210 220 230 240 LTSPGAVPPL PSPSKEEEGL RAQVRDLEEK LETLRLKRAE DKAKLKELEK HKIQLEQVQE 250 260 270 280 290 300 WKSKMQEQQA DLQRRLKEAR KEAKEALEAK ERYMEEMADT ADAIEMATLD KEMAEERAES 310 320 330 340 350 360 LQQEVEALKE RVDELTTDLE ILKAEIEEKG SDGAASSYQL KQLEEQNARL KDALVRMRDL 370 380 390 400 410 420 SSSEKQEHVK LQKLMEKKNQ ELEVVRQQRE RLQEELSQAE STIDELKEQV DAALGAEEMV 430 440 450 460 470 480 EMLTDRNLNL EEKVRELRET VGDLEAMNEM NDELQENARE TELELREQLD MAGARVREAQ 490 500 510 520 530 540 KRVEAAQETV ADYQQTIKKY RQLTAHLQDV NRELTNQQEA SVERQQQPPP ETFDFKIKFA 550 560 570 580 590 600 ETKAHAKAIE MELRQMEVAQ ANRHMSLLTA FMPDSFLRPG GDHDCVLVLL LMPRLICKAE 610 620 630 640 650 660 LIRKQAQEKF ELSENCSERP GLRGAAGEQL SFAAGLVYSL SLLQATLHRY EHALSQCSVD 670 680 690 700 710 720 VYKKVGSLYP EMSAHERSLD FLIELLHKDQ LDETVNVEPL TKAIKYYQHL YSIHLAEQPE 730 740 750 760 770 780 DCTMQLADHI KFTQSALDCM SVEVGRLRAF LQGGQEATDI ALLLRDLETS CSDIRQFCKK 790 800 810 820 830 840 IRRRMPGTDA PGIPAALAFG PQVSDTLLDC RKHLTWVVAV LQEVAAAAAQ LIAPLAENEG 850 860 870 880 890 900 LLVAALEELA FKASEQIYGT PSSSPYECLR QSCNILISTM NKLATAMQEG EYDAERPPSK 910 920 930 940 950 960 PPPVELRAAA LRAEITDAEG LGLKLEDRET VIKELKKSLK IKGEELSEAN VRLSLLEKKL 970 980 990 1000 1010 1020 DSAAKDADER IEKVQTRLEE TQALLRKKEK EFEETMDALQ ADIDQLEAEK AELKQRLNSQ 1030 1040 1050 1060 1070 1080 SKRTIEGLRG PPPSGIATLV SGIAGGAIPG QAPGSVPGPG LVKDSPLLLQ QISAMRLHIS 1090 1100 1110 1120 1130 1140 QLQHENSILK GAQMKASLAS LPPLHVAKLS HEGPGSELPA GALYRKTSQL LETLNQLSTH 1150 1160 1170 1180 1190 1200 THVVDITRTS PAAKSPSAQL MEQVAQLKSL SDTVEKLKDE VLKETVSQRP GATVPTDFAT 1210 1220 1230 1240 1250 FPSSAFLRAK EEQQDDTVYM GKVTFSCAAG FGQRHRLVLT QEQLHQLHSR LIS
	Isoform 5 [UniParc]. Checksum: 1997342C3ADA9F82	FASTA	1,139	126,733
	10 20 30 40 50 60 MMRQAPTARK TTTRRPKPTR PASTGVAGAS SSLGPSGSAS AGELSSSEPS TPAQTPLAAP 70 80 90 100 110 120 IIPTPVLTSP GAVPPLPSPS KEEEGLRAQV RDLEEKLETL RLKRAEDKAK LKELEKHKIQ 130 140 150 160 170 180 LEQVQEWKSK MQEQQADLQR RLKEARKEAK EALEAKERYM EEMADTADAI EMATLDKEMA 190 200 210 220 230 240 EERAESLQQE VEALKERVDE LTTDLEILKA EIEEKGSDGA ASSYQLKQLE EQNARLKDAL 250 260 270 280 290 300 VRMRDLSSSE KQEHVKLQKL MEKKNQELEV VRQQRERLQE ELSQAESTID ELKEQVDAAL 310 320 330 340 350 360 GAEEMVEMLT DRNLNLEEKV RELRETVGDL EAMNEMNDEL QENARETELE LREQLDMAGA 370 380 390 400 410 420 RVREAQKRVE AAQETVADYQ QTIKKYRQLT AHLQDVNREL TNQQEASVER QQQPPPETFD 430 440 450 460 470 480 FKIKFAETKA HAKAIEMELR QMEVAQANRH MSLLTAFMPD SFLRPGGDHD CVLVLLLMPR 490 500 510 520 530 540 LICKAELIRK QAQEKFELSE NCSERPGLRG AAGEQLSFAA GLVYSLSLLQ ATLHRYEHAL 550 560 570 580 590 600 SQCSVDVYKK VGSLYPEMSA HERSLDFLIE LLHKDQLDET VNVEPLTKAI KYYQHLYSIH 610 620 630 640 650 660 LAEQPEDCTM QLADHIKFTQ SALDCMSVEV GRLRAFLQGG QEATDIALLL RDLETSCSDI 670 680 690 700 710 720 RQFCKKIRRR MPGTDAPGIP AALAFGPQVS DTLLDCRKHL TWVVAVLQEV AAAAAQLIAP 730 740 750 760 770 780 LAENEGLLVA ALEELAFKAS EQIYGTPSSS PYECLRQSCN ILISTMNKLA TAMQEGEYDA 790 800 810 820 830 840 ERPPSKPPPV ELRAAALRAE ITDAEGLGLK LEDRETVIKE LKKSLKIKGE ELSEANVRLS 850 860 870 880 890 900 LLEKKLDSAA KDADERIEKV QTRLEETQAL LRKKEKEFEE TMDALQADID QLEAEKAELK 910 920 930 940 950 960 QRLNSQSKRT IEGLRGPPPS GIATLVSGIA GGAIPGQAPG SVPGPGLVKD SPLLLQQISA 970 980 990 1000 1010 1020 MRLHISQLQH ENSILKGAQM KASLASLPPL HVAKLSHEGP GSELPAGALY RKTSQLLETL 1030 1040 1050 1060 1070 1080 NQLSTHTHVV DITRTSPAAK SPSAQLMEQV AQLKSLSDTV EKLKDEVLKE TVSQRPGATV 1090 1100 1110 1120 1130 PTDFATFPSS AFLRAKEEQQ DDTVYMGKVT FSCAAGFGQR HRLVLTQEQL HQLHSRLIS

References

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[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]	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. , 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 P150), 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, MASS SPECTROMETRY. 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]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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. , 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.
[30]	"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. , 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.
[31]	"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 , 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.

IPI

IPI00219114.
IPI00872359.
IPI00916757.
IPI00935906.

RefSeq

NP_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.

UniGene

Hs.516111.

3D structure databases

PDBe
RCSB PDB
PDBj

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	15-111	[»]
3TQ7	X-ray	2.30	P/Q	27-97	[»]

ProteinModelPortal

Q14203.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31365N.

IntAct

Q14203. 16 interactions.

MINT

MINT-5004548.

STRING

9606.ENSP00000354791.

PTM databases

PhosphoSite

Q14203.

Polymorphism databases

DMDM

17375490.

2D gel databases

OGP

Q14203.

Proteomic databases

PaxDb

Q14203.

PRIDE

Q14203.

Protocols and materials databases

DNASU

1639.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361874; ENSP00000354791; ENSG00000204843.
ENST00000407639; ENSP00000384844; ENSG00000204843.
ENST00000409240; ENSP00000386406; ENSG00000204843.
ENST00000409438; ENSP00000387270; ENSG00000204843.
ENST00000409567; ENSP00000386843; ENSG00000204843.

GeneID

1639.

KEGG

hsa:1639.

UCSC

uc002skv.3. human.
uc002skx.3. human.

Organism-specific databases

CTD

1639.

GeneCards

GC02M074588.

H-InvDB

HIX0204314.

HGNC

HGNC:2711. DCTN1.

HPA

CAB009108.

MIM

105400. phenotype.
168605. phenotype.
601143. gene.
607641. phenotype.

neXtProt

NX_Q14203.

Orphanet

803. Amyotrophic lateral sclerosis.
139589. Distal hereditary motor neuropathy type 7.
178509. Perry syndrome.

PharmGKB

PA27180.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5244.

HOGENOM

HOG000015352.

HOVERGEN

HBG004956.

KO

K04648.

OMA

HVYSRTP.

OrthoDB

EOG43TZTR.

PhylomeDB

Q14203.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q14203.

Bgee

Q14203.

CleanEx

HS_DCTN1.

Genevestigator

Q14203.

GermOnline

ENSG00000204843. Homo sapiens.

Family and domain databases

Gene3D

2.30.30.190. 1 hit.

InterPro

IPR000938. CAP-Gly_domain.
IPR022157. Dynactin.
[Graphical view]

Pfam

PF01302. CAP_GLY. 1 hit.
PF12455. Dynactin. 1 hit.
[Graphical view]

SMART

SM01052. CAP_GLY. 1 hit.
[Graphical view]

SUPFAM

SSF74924. CAP-Gly_domain. 1 hit.

PROSITE

PS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DCTN1. human.

EvolutionaryTrace

Q14203.

GenomeRNAi

1639.

NextBio

6734.

PMAP-CutDB

Q14203.

SOURCE

Search...

Entry information

Entry name

DCTN1_HUMAN

Accession

Primary (citable) accession number: Q14203
Secondary accession number(s): 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:	May 1, 2013
This is version 130 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.