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Dynactin subunit 1 (150 kDa dynein-associated polypeptide) (DAP-150) (DP-150) (p150-glued)

 DCTN1_MOUSE             Reviewed;        1281 AA.
O08788; E9QLJ1; Q3TZG7;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
25-OCT-2017, entry version 143.
RecName: Full=Dynactin subunit 1;
AltName: Full=150 kDa dynein-associated polypeptide;
AltName: Full=DAP-150;
Short=DP-150;
AltName: Full=p150-glued;
Name=Dctn1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
PubMed=9070275; DOI=10.1006/bbrc.1997.6095;
Jang W., Weber J.S., Tokito M.K., Holzbaur E.L., Meisler M.H.;
"Mouse p150Glued (dynactin 1) cDNA sequence and evaluation as a
candidate for the neuromuscular disease mutation mnd2.";
Biochem. Biophys. Res. Commun. 231:344-347(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Inner ear;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
INTERACTION WITH DST (ISOFORM 1).
PubMed=14581450; DOI=10.1083/jcb.200306075;
Liu J.J., Ding J., Kowal A.S., Nardine T., Allen E., Delcroix J.D.,
Wu C., Mobley W., Fuchs E., Yang Y.;
"BPAG1n4 is essential for retrograde axonal transport in sensory
neurons.";
J. Cell Biol. 163:223-229(2003).
[5]
SUBCELLULAR LOCATION, AND ASSOCIATION WITH MICROTUBULES.
PubMed=16954346; DOI=10.1083/jcb.200512058;
Peris L., Thery M., Faure J., Saoudi Y., Lafanechere L., Chilton J.K.,
Gordon-Weeks P., Galjart N., Bornens M., Wordeman L., Wehland J.,
Andrieux A., Job D.;
"Tubulin tyrosination is a major factor affecting the recruitment of
CAP-Gly proteins at microtubule plus ends.";
J. Cell Biol. 174:839-849(2006).
[6]
INTERACTION WITH SNX6.
PubMed=19935774; DOI=10.1038/cr.2009.130;
Hong Z., Yang Y., Zhang C., Niu Y., Li K., Zhao X., Liu J.J.;
"The retromer component SNX6 interacts with dynactin p150(Glued) and
mediates endosome-to-TGN transport.";
Cell Res. 19:1334-1349(2009).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
INTERACTION WITH BICD2.
PubMed=22956769; DOI=10.1091/mbc.E12-03-0210;
Splinter D., Razafsky D.S., Schlager M.A., Serra-Marques A.,
Grigoriev I., Demmers J., Keijzer N., Jiang K., Poser I., Hyman A.A.,
Hoogenraad C.C., King S.J., Akhmanova A.;
"BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment
to cellular structures.";
Mol. Biol. Cell 23:4226-4241(2012).
[9]
INTERACTION WITH KIF3A, AND SUBCELLULAR LOCATION.
PubMed=23386061; DOI=10.1038/emboj.2013.3;
Kodani A., Salome Sirerol-Piquer M., Seol A., Garcia-Verdugo J.M.,
Reiter J.F.;
"Kif3a interacts with Dynactin subunit p150 Glued to organize
centriole subdistal appendages.";
EMBO J. 32:597-607(2013).
[10]
INTERACTION WITH HPS6.
PubMed=25189619; DOI=10.1242/jcs.141978;
Li K., Yang L., Zhang C., Niu Y., Li W., Liu J.J.;
"HPS6 interacts with dynactin p150Glued to mediate retrograde
trafficking and maturation of lysosomes.";
J. Cell Sci. 127:4574-4588(2014).
-!- FUNCTION: Plays a key role in dynein-mediated retrograde transport
of vesicles and organelles along microtubules by recruiting and
tethering dynein to microtubules. Binds to both dynein and
microtubules providing a link between specific cargos,
microtubules and dynein. Essential for targeting dynein to
microtubule plus ends, recruiting dynein to membranous cargos and
enhancing dynein processivity (the ability to move along a
microtubule for a long distance without falling off the track).
Can also act as a brake to slow the dynein motor during motility
along the microtubule. Can regulate microtubule stability by
promoting microtubule formation, nucleation and polymerization and
by inhibiting microtubule catastrophe in neurons. Inhibits
microtubule catastrophe by binding both to microtubules and to
tubulin, leading to enhanced microtubule stability along the axon.
Plays a role in metaphase spindle orientation. Plays a role in
centriole cohesion and subdistal appendage organization and
function. Its recruitement to the centriole in a KIF3A-dependent
manner is essential for the maintenance of centriole cohesion and
the formation of subdistal appendage. Also required for
microtubule anchoring at the mother centriole. Plays a role in
primary cilia formation. {ECO:0000250|UniProtKB:Q14203}.
-!- SUBUNIT: Monomer and homodimer. Dynactin is a large macromolecular
complex of at least 10 components; p150(glued) binds directly to
microtubules and to cytoplasmic dynein. Interacts with the C-
terminus of MAPRE1, MAPRE2 and MAPRE3. Interacts with FBXL5.
Interacts with ECM29. Interacts with CLIP1. Interacts with CLN3
and DYNAP. Interacts with MISP; this interaction regulates its
distribution at the cell cortex. Interacts with CEP131. Interacts
with CEP126. Interacts with dynein intermediate chain and dynein
heavy chain. Interacts with PLK1 (via POLO-box domain). Interacts
with TBCB and PARD6A (By similarity). Binds preferentially to
tyrosinated microtubules than to detyrosinated microtubules
(PubMed:16954346). Interacts with KIF3A (PubMed:23386061).
Interacts with HPS6 (PubMed:25189619). Interacts with SNX6
(PubMed:19935774). Interacts with BICD2 (PubMed:22956769).
Interacts with DST (isoform 1) (PubMed:14581450). Interacts with
BCCIP (By similarity). {ECO:0000250|UniProtKB:Q14203,
ECO:0000269|PubMed:14581450, ECO:0000269|PubMed:16954346,
ECO:0000269|PubMed:19935774, ECO:0000269|PubMed:22956769,
ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:25189619}.
-!- INTERACTION:
Q6A078:Cep290; NbExp=2; IntAct=EBI-776180, EBI-1811999;
P28741:Kif3a; NbExp=4; IntAct=EBI-776180, EBI-6169413;
P33175:Kif5a; NbExp=2; IntAct=EBI-776180, EBI-349710;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14203}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16954346}. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome, centriole
{ECO:0000269|PubMed:23386061}. Cytoplasm, cytoskeleton, spindle
{ECO:0000250|UniProtKB:Q14203}. Nucleus envelope
{ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cell cortex
{ECO:0000250|UniProtKB:Q14203}. Note=Localizes to microtubule plus
ends. Localizes preferentially to the ends of tyrosinated
microtubules (PubMed:16954346). Localization at centrosome is
regulated by SLK-dependent phosphorylation. Localizes to
centrosome in a PARKDA-dependent manner. PLK1-mediated
phosphorylation at Ser-179 is essential for its localization in
the nuclear envelope (By similarity). Localizes to the subdistal
appendage region of the centriole in a KIF3A-dependent manner
(PubMed:23386061). {ECO:0000250|UniProtKB:Q14203,
ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:23386061}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O08788-1; Sequence=Displayed;
Name=2;
IsoId=O08788-2; Sequence=VSP_029584;
Note=No experimental confirmation available.;
-!- DOMAIN: The CAP-Gly domain is essential for interactions with
microtubules and its binding partners and for its motion along the
microtubules. Essential for its preferential binding to
tyrosinated microtubules and for promoting the sustained
interaction of the dynein motor with microtubules.
{ECO:0000250|UniProtKB:Q14203}.
-!- PTM: Ubiquitinated by a SCF complex containing FBXL5, leading to
its degradation by the proteasome. {ECO:0000250|UniProtKB:Q14203}.
-!- PTM: Phosphorylation by SLK at Thr-145, Thr-146 and Thr-147
targets DCTN1 to the centrosome. It is uncertain if SLK
phosphorylates all three threonines or one or two of them. PLK1-
mediated phosphorylation at Ser-179 is essential for its
localization in the nuclear envelope and promotes its dissociation
from microtubules during early mitosis and positively regulates
nuclear envelope breakdown during prophase.
{ECO:0000250|UniProtKB:Q14203}.
-!- SIMILARITY: Belongs to the dynactin 150 kDa subunit family.
{ECO:0000305}.
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EMBL; U60312; AAB57773.1; -; mRNA.
EMBL; AK157867; BAE34241.1; -; mRNA.
EMBL; AC160400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS39532.1; -. [O08788-1]
PIR; JC5368; JC5368.
RefSeq; NP_031861.2; NM_007835.2. [O08788-1]
UniGene; Mm.6919; -.
ProteinModelPortal; O08788; -.
SMR; O08788; -.
BioGrid; 199072; 29.
CORUM; O08788; -.
DIP; DIP-32057N; -.
IntAct; O08788; 40.
MINT; MINT-1847327; -.
STRING; 10090.ENSMUSP00000109552; -.
ChEMBL; CHEMBL2176787; -.
iPTMnet; O08788; -.
PhosphoSitePlus; O08788; -.
SwissPalm; O08788; -.
MaxQB; O08788; -.
PaxDb; O08788; -.
PeptideAtlas; O08788; -.
PRIDE; O08788; -.
Ensembl; ENSMUST00000113918; ENSMUSP00000109551; ENSMUSG00000031865. [O08788-2]
Ensembl; ENSMUST00000113919; ENSMUSP00000109552; ENSMUSG00000031865. [O08788-1]
GeneID; 13191; -.
KEGG; mmu:13191; -.
UCSC; uc009cmz.2; mouse. [O08788-1]
CTD; 1639; -.
MGI; MGI:107745; Dctn1.
eggNOG; KOG0971; Eukaryota.
eggNOG; COG5244; LUCA.
GeneTree; ENSGT00760000119173; -.
HOGENOM; HOG000015352; -.
HOVERGEN; HBG004956; -.
InParanoid; O08788; -.
KO; K04648; -.
OMA; CLRQSCN; -.
OrthoDB; EOG091G0WO0; -.
TreeFam; TF105246; -.
Reactome; R-MMU-2132295; MHC class II antigen presentation.
Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
Reactome; R-MMU-8854518; AURKA Activation by TPX2.
ChiTaRS; Dctn1; mouse.
PRO; PR:O08788; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000031865; -.
CleanEx; MM_DCTN1; -.
ExpressionAtlas; O08788; baseline and differential.
Genevisible; O08788; MM.
GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
GO; GO:0099738; C:cell cortex region; ISS:UniProtKB.
GO; GO:0031252; C:cell leading edge; IDA:MGI.
GO; GO:0005814; C:centriole; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005869; C:dynactin complex; IEA:InterPro.
GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005874; C:microtubule; ISO:MGI.
GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0030904; C:retromer complex; IEA:Ensembl.
GO; GO:0005819; C:spindle; ISS:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0070840; F:dynein complex binding; IEA:InterPro.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
GO; GO:0015631; F:tubulin binding; ISO:MGI.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0010457; P:centriole-centriole cohesion; ISS:UniProtKB.
GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:UniProtKB.
GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
GO; GO:0032402; P:melanosome transport; IMP:MGI.
GO; GO:0034454; P:microtubule anchoring at centrosome; ISS:UniProtKB.
GO; GO:1905515; P:non-motile cilium assembly; ISS:UniProtKB.
GO; GO:0051081; P:nuclear envelope disassembly; ISS:UniProtKB.
GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
GO; GO:0090063; P:positive regulation of microtubule nucleation; ISS:UniProtKB.
GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
GO; GO:0010970; P:transport along microtubule; IEA:InterPro.
Gene3D; 2.30.30.190; -; 1.
InterPro; IPR036859; CAP-Gly_dom_sf.
InterPro; IPR000938; CAP-Gly_domain.
InterPro; IPR027663; DCTN1.
InterPro; IPR022157; Dynactin.
PANTHER; PTHR18916:SF40; PTHR18916:SF40; 1.
Pfam; PF01302; CAP_GLY; 1.
Pfam; PF12455; Dynactin; 1.
SMART; SM01052; CAP_GLY; 1.
SUPFAM; SSF74924; SSF74924; 1.
PROSITE; PS00845; CAP_GLY_1; 1.
PROSITE; PS50245; CAP_GLY_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell division; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Dynein; Microtubule;
Mitosis; Nucleus; Phosphoprotein; Reference proteome; Transport;
Ubl conjugation.
CHAIN 1 1281 Dynactin subunit 1.
/FTId=PRO_0000083519.
DOMAIN 48 90 CAP-Gly. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
REGION 911 1281 Interaction with HPS6.
{ECO:0000269|PubMed:25189619}.
COILED 214 547 {ECO:0000255}.
COILED 943 1049 {ECO:0000255}.
COILED 1185 1214 {ECO:0000255}.
COMPBIAS 157 184 Ser-rich.
MOD_RES 108 108 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14203}.
MOD_RES 145 145 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14203}.
MOD_RES 146 146 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14203}.
MOD_RES 147 147 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14203}.
MOD_RES 179 179 Phosphoserine; by PLK1.
{ECO:0000250|UniProtKB:Q14203}.
MOD_RES 212 212 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:Q14203}.
VAR_SEQ 1049 1086 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_029584.
CONFLICT 406 406 R -> W (in Ref. 2; BAE34241).
{ECO:0000305}.
CONFLICT 721 723 TKA -> NKG (in Ref. 1; AAB57773).
{ECO:0000305}.
CONFLICT 732 732 S -> R (in Ref. 1; AAB57773).
{ECO:0000305}.
CONFLICT 1202 1202 I -> V (in Ref. 2; BAE34241).
{ECO:0000305}.
SEQUENCE 1281 AA; 141676 MW; A6CEDCAAA7022EB5 CRC64;
MAQSRRHMSS RTPSGSRMST EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV
ILDEAKGKND GTVQGRKYFT CDEGHGIFVR QSQIQVFEDG ADTTSPETPD SSASKVLKRE
GADAAAKTSK LRGLKPKKAP TARKTTTRRP KPTRPASTGV AGPSSSLGPS GSASAGELSS
SEPSTPAQTP LAAPIIPTPA LTSPGAAPPL PSPSKEEEGL RAQVRDLEEK LETLRLKRSE
DKAKLKELEK HKIQLEQVQE WKSKMQEQQA DLQRRLKEAR KEAKEALEAK ERYMEEMADT
ADAIEMATLD KEMAEERAES LQQEVEALKE RVDELTTDLE ILKAEIEEKG SDGAASSYQL
KQLEEQNARL KDALVRMRDL SSSEKQEHVK LQKLMEKKNQ ELEVVRQQRE RLQEELSQAE
STIDELKEQV DAALGAEEMV EMLTDRNLNL EEKVRELRET VGDLEAMNEM NDELQENARE
TELELREQLD MAGARVREAQ KRVEAAQETV ADYQQTIKKY RQLTAHLQDV NRELTNQQEA
SVERQQQPPP ETFDFKIKFA ETKAHAKAIE MELRQMEVAQ ANRHMSLLTA FMPDSFLRPG
GDHDCVLVLL LMPRLICKAE LIRKQAQEKF DLSENCSERP GLRGAAGEQL SFAAGLVYSL
SLLQATLHRY EHALSQCSVD VYKKVGSLYP EMSAHERSLD FLIELLHKDQ LDETVNVEPL
TKAIKYYQHL YSIHLAEQPE DSTMQLADHI KFTQSALDCM GVEVGRLRAF LQGGQEATDI
ALLLRDLETS CSDTRQFCKK IRRRMPGTDA PGIPAALAFG SQVSDTLLDC RKHLTWVVAV
LQEVAAAAAQ LIAPLAENEG LPVAALEELA FKASEQIYGS PSSSPYECLR QSCTILISTM
NKLATAMQEG EYDAERPPSK PPPVELRAAA LRAEITDAEG LGLKLEDRET VIKELKKSLK
IKGEELSEAN VRLSLLEKKL DSAAKDADER IEKVQTRLDE TQTLLRKKEK DFEETMDALQ
ADIDQLEAEK AELKQRLNSQ SKRTIEGLRG PPPSGIATLV SGIAGEEPQR GGAPGQAPGA
LPGPGLVKDS PLLLQQISAM RLHISQLQHE NSILRGAQMK ASLAALPPLH VAKLSLPPHE
GPGGNLVAGA LYRKTSQLLE KLNQLSTHTH VVDITRSSPA AKSPSAQLME QVAQLKSLSD
TIEKLKDEVL KETVTQRPGA TVPTDFATFP SSAFLRAKEE QQDDTVYMGK VTFSCAAGLG
QRHRLVLTQE QLHQLHSRLI S


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EIAAB10663 150 kDa dynein-associated polypeptide,Chicken,DAP-150,DCTN1,DP-150,Dynactin subunit 1,Gallus gallus,p150-glued
EIAAB10666 50 kDa dynein-associated polypeptide,DCTN2,DCTN50,DCTN-50,Dynactin complex 50 kDa subunit,Dynactin subunit 2,Homo sapiens,Human,p50 dynamitin
EIAAB10665 50 kDa dynein-associated polypeptide,Dctn2,DCTN-50,Dynactin complex 50 kDa subunit,Dynactin subunit 2,GMP23-48K,Growth cone membrane protein 23-48K,Mouse,Mus musculus,p50 dynamitin
GWB-42BC6F Dynactin 1 (p150 Glued Homolog) (DCTN1) Goat anti-Human Polyclonal (C-Terminus) Antibody
CSB-EL006564RA Rat dynactin 1 (p150, glued homolog, Drosophila) (DCTN1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL006564HU Human dynactin 1 (p150, glued homolog, Drosophila) (DCTN1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL006564CH Chicken dynactin 1 (p150, glued homolog, Drosophila) (DCTN1) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
CSB-EL006564MO Mouse dynactin 1 (p150, glued homolog, Drosophila) (DCTN1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-PA006564GA01HU Rabbit anti-human dynactin 1 (p150, glued homolog, Drosophila) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
CSB-PA006564GA01HU Rabbit anti-human dynactin 1 (p150, glued homolog, Drosophila) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
30-794 ACTR1B is a 42.3 kD subunit of dynactin, a macromolecular complex consisting of 10 subunits ranging in size from 22 to 150 kD. Dynactin binds to both microtubules and cytoplasmic dynein and is involve 0.05 mg
27-161 ACTR1A is a 42.6 kD subunit of dynactin, a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kD. Dynactin binds to both microtubules and cytoplasmic dynein. It is invo 0.05 mg
EIAAB10669 DCTN22,DCTN3,Dynactin complex subunit 22 kDa subunit,Dynactin subunit 3,Homo sapiens,Human,p22
EIAAB10677 DCTN6,Dynactin subunit 6,Dynactin subunit p27,Homo sapiens,Human,Protein WS-3,WS3
EIAAB05135 CAF,CAF-1 subunit A,CAF1P150,CAF-I 150 kDa subunit,CAF-I p150,CHAF1A,Chromatin assembly factor 1 subunit A,Chromatin assembly factor I p150 subunit,Homo sapiens,hp150,Human
EIAAB10676 DCTN5,Dynactin subunit 5,Dynactin subunit p25,Homo sapiens,Human
EIAAB10679 Dctn6,Dynactin subunit 6,Dynactin subunit p27,Mouse,Mus musculus,Protein WS-3,Ws3
EIAAB10674 DCTN4,Dynactin subunit 4,Dynactin subunit p62,Homo sapiens,Human
EIAAB10675 Dctn5,Dynactin subunit 5,Dynactin subunit p25,Mouse,Mus musculus
EIAAB10673 Dctn4,Dynactin subunit 4,Dynactin subunit p62,Mouse,Mus musculus
EIAAB10672 Dctn4,Dynactin subunit 4,Dynactin subunit p62,Rat,Rattus norvegicus
EIAAB05136 Bos taurus,Bovine,CAF,CAF-1 subunit A,CAF1P150,CAF-I 150 kDa subunit,CAF-I p150,CHAF1A,Chromatin assembly factor 1 subunit A,Chromatin assembly factor I p150 subunit


 

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