Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Cytoplasmic dynein 1 intermediate chain 1 (Cytoplasmic dynein intermediate chain 1) (Dynein intermediate chain 1, cytosolic) (DH IC-1)

 DC1I1_HUMAN             Reviewed;         645 AA.
O14576; B4DME3; F5H050; G5E9K1; Q8TBF7; Q9Y2X1;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 2.
22-NOV-2017, entry version 163.
RecName: Full=Cytoplasmic dynein 1 intermediate chain 1;
AltName: Full=Cytoplasmic dynein intermediate chain 1;
AltName: Full=Dynein intermediate chain 1, cytosolic;
Short=DH IC-1;
Name=DYNC1I1; Synonyms=DNCI1, DNCIC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10049579; DOI=10.1006/geno.1998.5665;
Crackower M.A., Sinasac D.S., Xia J., Motoyama J., Prochazka M.,
Rommens J.M., Scherer S.W., Tsui L.-C.;
"Cloning and characterization of two cytoplasmic dynein intermediate
chain genes in mouse and human.";
Genomics 55:257-267(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Li G., Jin J., Hu S., Li W., Yuan J., Qiang B.;
"Molecular cloning of a cytoplasmic dynein gene.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
SUBCELLULAR LOCATION.
PubMed=19229290; DOI=10.1038/emboj.2009.38;
Sivaram M.V., Wadzinski T.L., Redick S.D., Manna T., Doxsey S.J.;
"Dynein light intermediate chain 1 is required for progress through
the spindle assembly checkpoint.";
EMBO J. 28:902-914(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[9]
INTERACTION WITH DYNLT1, AND MUTAGENESIS OF LEU-148; GLY-149; VAL-150;
LYS-152; VAL-153; GLN-155; VAL-156; ASP-157 AND PHE-158.
PubMed=27502274; DOI=10.1074/jbc.M116.736884;
Merino-Gracia J., Zamora-Carreras H., Bruix M., Rodriguez-Crespo I.;
"Molecular basis for the protein recognition specificity of the dynein
light chain DYNLT1/Tctex1: characterization of the interaction with
activin receptor IIB.";
J. Biol. Chem. 291:20962-20975(2016).
[10]
VARIANT LEU-373.
PubMed=21248752; DOI=10.1038/nature09639;
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
Futreal P.A.;
"Exome sequencing identifies frequent mutation of the SWI/SNF complex
gene PBRM1 in renal carcinoma.";
Nature 469:539-542(2011).
-!- FUNCTION: Acts as one of several non-catalytic accessory
components of the cytoplasmic dynein 1 complex that are thought to
be involved in linking dynein to cargos and to adapter proteins
that regulate dynein function. Cytoplasmic dynein 1 acts as a
motor for the intracellular retrograde motility of vesicles and
organelles along microtubules. The intermediate chains mediate the
binding of dynein to dynactin via its 150 kDa component (p150-
glued) DCNT1. May play a role in mediating the interaction of
cytoplasmic dynein with membranous organelles and kinetochores.
-!- SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1
complex consists of two catalytic heavy chains (HCs) and a number
of non-catalytic subunits presented by intermediate chains (ICs),
light intermediate chains (LICs) and light chains (LCs); the
composition seems to vary in respect to the IC, LIC and LC
composition. The heavy chain homodimer serves as a scaffold for
the probable homodimeric assembly of the respective non-catalytic
subunits. The ICs and LICs bind directly to the HC dimer and the
LCs assemble on the IC dimer. Interacts with DYNC1H1. Interacts
with DYNLT1 and DYNLT3. Interacts with DCNT1 (By similarity).
{ECO:0000250, ECO:0000269|PubMed:27502274}.
-!- INTERACTION:
Q9CZA6:Nde1 (xeno); NbExp=2; IntAct=EBI-366267, EBI-309934;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome,
centromere, kinetochore {ECO:0000269|PubMed:19229290}. Cytoplasm,
cytoskeleton, spindle pole {ECO:0000269|PubMed:19229290}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=O14576-1; Sequence=Displayed;
Name=2;
IsoId=O14576-2; Sequence=VSP_001332;
Name=3;
IsoId=O14576-3; Sequence=VSP_001332, VSP_001333;
Name=4;
IsoId=O14576-4; Sequence=VSP_001332, VSP_001333, VSP_054766;
Note=No experimental confirmation available.;
Name=5;
IsoId=O14576-5; Sequence=VSP_001333;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the dynein intermediate chain family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF063228; AAC33443.1; -; mRNA.
EMBL; AF123074; AAD26852.1; -; mRNA.
EMBL; AK091339; BAC03639.1; -; mRNA.
EMBL; AK297427; BAG59855.1; -; mRNA.
EMBL; AC022261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC091779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC002452; AAB67047.2; -; Genomic_DNA.
EMBL; AC002540; AAB70113.1; -; Genomic_DNA.
EMBL; CH471091; EAW76753.1; -; Genomic_DNA.
EMBL; BC022540; AAH22540.1; -; mRNA.
CCDS; CCDS47645.1; -. [O14576-2]
CCDS; CCDS47646.1; -. [O14576-3]
CCDS; CCDS5644.1; -. [O14576-1]
CCDS; CCDS64718.1; -. [O14576-5]
CCDS; CCDS64719.1; -. [O14576-4]
RefSeq; NP_001129028.1; NM_001135556.1. [O14576-2]
RefSeq; NP_001129029.1; NM_001135557.1. [O14576-3]
RefSeq; NP_001265350.1; NM_001278421.1. [O14576-5]
RefSeq; NP_001265351.1; NM_001278422.1. [O14576-4]
RefSeq; NP_004402.1; NM_004411.4. [O14576-1]
RefSeq; XP_011514163.1; XM_011515861.1. [O14576-1]
RefSeq; XP_011514164.1; XM_011515862.1. [O14576-2]
RefSeq; XP_016867293.1; XM_017011804.1. [O14576-1]
RefSeq; XP_016867294.1; XM_017011805.1. [O14576-2]
UniGene; Hs.440364; -.
ProteinModelPortal; O14576; -.
BioGrid; 108118; 56.
CORUM; O14576; -.
ELM; O14576; -.
IntAct; O14576; 36.
MINT; MINT-156403; -.
STRING; 9606.ENSP00000320130; -.
iPTMnet; O14576; -.
PhosphoSitePlus; O14576; -.
BioMuta; DYNC1I1; -.
EPD; O14576; -.
MaxQB; O14576; -.
PaxDb; O14576; -.
PeptideAtlas; O14576; -.
PRIDE; O14576; -.
TopDownProteomics; O14576-3; -. [O14576-3]
Ensembl; ENST00000324972; ENSP00000320130; ENSG00000158560. [O14576-1]
Ensembl; ENST00000359388; ENSP00000352348; ENSG00000158560. [O14576-3]
Ensembl; ENST00000437599; ENSP00000398118; ENSG00000158560. [O14576-5]
Ensembl; ENST00000447467; ENSP00000392337; ENSG00000158560. [O14576-2]
Ensembl; ENST00000457059; ENSP00000412444; ENSG00000158560. [O14576-2]
Ensembl; ENST00000630942; ENSP00000486363; ENSG00000158560. [O14576-4]
GeneID; 1780; -.
KEGG; hsa:1780; -.
UCSC; uc003uob.4; human. [O14576-1]
CTD; 1780; -.
DisGeNET; 1780; -.
EuPathDB; HostDB:ENSG00000158560.14; -.
GeneCards; DYNC1I1; -.
HGNC; HGNC:2963; DYNC1I1.
HPA; HPA061689; -.
MIM; 603772; gene.
neXtProt; NX_O14576; -.
OpenTargets; ENSG00000158560; -.
PharmGKB; PA27434; -.
eggNOG; KOG1587; Eukaryota.
eggNOG; ENOG410XQ99; LUCA.
GeneTree; ENSGT00730000110228; -.
HOGENOM; HOG000116383; -.
HOVERGEN; HBG004083; -.
InParanoid; O14576; -.
KO; K10415; -.
OMA; VEPKVGH; -.
OrthoDB; EOG091G038G; -.
PhylomeDB; O14576; -.
TreeFam; TF300553; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
Reactome; R-HSA-68877; Mitotic Prometaphase.
SignaLink; O14576; -.
ChiTaRS; DYNC1I1; human.
GeneWiki; DYNC1I1; -.
GenomeRNAi; 1780; -.
PRO; PR:O14576; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000158560; -.
CleanEx; HS_DYNC1I1; -.
ExpressionAtlas; O14576; baseline and differential.
Genevisible; O14576; HS.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:AgBase.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0045504; F:dynein heavy chain binding; IBA:GO_Central.
GO; GO:0045503; F:dynein light chain binding; IBA:GO_Central.
GO; GO:0008017; F:microtubule binding; ISS:HGNC.
GO; GO:0003777; F:microtubule motor activity; ISS:HGNC.
GO; GO:0003774; F:motor activity; TAS:ProtInc.
GO; GO:0030507; F:spectrin binding; IDA:MGI.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:2000582; P:positive regulation of ATP-dependent microtubule motor activity, plus-end-directed; IBA:GO_Central.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
GO; GO:0047496; P:vesicle transport along microtubule; IMP:UniProtKB.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR025956; DYNC1I1/DYNC1I2.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF11540; Dynein_IC2; 1.
Pfam; PF00400; WD40; 1.
SMART; SM00320; WD40; 5.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Alternative splicing; Centromere; Chromosome; Complete proteome;
Cytoplasm; Cytoskeleton; Dynein; Kinetochore; Microtubule;
Motor protein; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Transport; WD repeat.
CHAIN 1 645 Cytoplasmic dynein 1 intermediate chain
1.
/FTId=PRO_0000114652.
REPEAT 285 334 WD 1.
REPEAT 338 378 WD 2.
REPEAT 387 428 WD 3.
REPEAT 437 477 WD 4.
REPEAT 482 527 WD 5.
REPEAT 530 570 WD 6.
REPEAT 576 615 WD 7.
REGION 1 123 Interaction with DCTN1. {ECO:0000250}.
REGION 147 163 Interaction with DYNLT1.
{ECO:0000269|PubMed:27502274}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:O88485}.
MOD_RES 111 111 Phosphoserine.
{ECO:0000250|UniProtKB:O88485}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000250|UniProtKB:O88485}.
MOD_RES 176 176 Phosphothreonine.
{ECO:0000250|UniProtKB:O88485}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000250|UniProtKB:O88485}.
MOD_RES 197 197 Phosphoserine.
{ECO:0000250|UniProtKB:O88485}.
MOD_RES 635 635 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
VAR_SEQ 74 90 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.2}.
/FTId=VSP_001332.
VAR_SEQ 123 142 Missing (in isoform 3, isoform 4 and
isoform 5). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_001333.
VAR_SEQ 610 645 LAVPHNDEWTRFARTLVEIRANRADSEEEGTVELSA -> G
LAMLPGWSQNSWTQAILLCWPPKVLGLQT (in isoform
4). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_054766.
VARIANT 373 373 H -> L (found in a renal cell carcinoma
case; somatic mutation).
{ECO:0000269|PubMed:21248752}.
/FTId=VAR_064709.
VARIANT 582 582 N -> T (in dbSNP:rs35077523).
/FTId=VAR_048905.
MUTAGEN 148 148 L->G: Disrupts interaction with DYNLT1.
{ECO:0000269|PubMed:27502274}.
MUTAGEN 149 149 G->E: No effect on interaction with
DYNLT1. {ECO:0000269|PubMed:27502274}.
MUTAGEN 150 150 V->G: Disrupts interaction with DYNLT1.
{ECO:0000269|PubMed:27502274}.
MUTAGEN 150 150 V->W: No effect on interaction with
DYNLT1. {ECO:0000269|PubMed:27502274}.
MUTAGEN 152 152 K->A,Y: No effect on interaction with
DYNLT1. {ECO:0000269|PubMed:27502274}.
MUTAGEN 153 153 V->G: Decreases interaction with DYNLT1.
{ECO:0000269|PubMed:27502274}.
MUTAGEN 155 155 Q->H,R,T,Y: No effect on interaction with
DYNLT1. {ECO:0000269|PubMed:27502274}.
MUTAGEN 156 156 V->G: Decreases interaction with DYNLT1.
{ECO:0000269|PubMed:27502274}.
MUTAGEN 157 157 D->R: No effect on interaction with
DYNLT1. {ECO:0000269|PubMed:27502274}.
MUTAGEN 158 158 F->G: Disrupts interaction with DYNLT1.
{ECO:0000269|PubMed:27502274}.
CONFLICT 254 254 D -> G (in Ref. 3; BAG59855).
{ECO:0000305}.
CONFLICT 517 517 W -> C (in Ref. 6; AAH22540).
{ECO:0000305}.
SEQUENCE 645 AA; 72955 MW; 55A6FF971E632DA0 CRC64;
MSDKSDLKAE LERKKQRLAQ IREEKKRKEE ERKKKEADMQ QKKEPVQDDS DLDRKRRETE
ALLQSIGISP EPPLVQPLHF LTWDTCYFHY LVPTPMSPSS KSVSTPSEAG SQDSGDLGPL
TRTLQWDTDP SVLQLQSDSE LGRRLHKLGV SKVTQVDFLP REVVSYSKET QTPLATHQSE
EDEEDEEMVE SKVGQDSELE NQDKKQEVKE APPRELTEEE KQQILHSEEF LIFFDRTIRV
IERALAEDSD IFFDYSGREL EEKDGDVQAG ANLSFNRQFY DEHWSKHRVV TCMDWSLQYP
ELMVASYNNN EDAPHEPDGV ALVWNMKFKK TTPEYVFHCQ SSVMSVCFAR FHPNLVVGGT
YSGQIVLWDN RSHRRTPVQR TPLSAAAHTH PVYCVNVVGT QNAHNLITVS TDGKMCSWSL
DMLSTPQESM ELVYNKSKPV AVTGMAFPTG DVNNFVVGSE EGTVYTACRH GSKAGIGEVF
EGHQGPVTGI NCHMAVGPID FSHLFVTSSF DWTVKLWTTK HNKPLYSFED NADYVYDVMW
SPVHPALFAC VDGMGRLDLW NLNNDTEVPT ASVAIEGASA LNRVRWAQAG KEVAVGDSEG
RIWVYDVGEL AVPHNDEWTR FARTLVEIRA NRADSEEEGT VELSA


Related products :

Catalog number Product name Quantity
EIAAB10509 Cytoplasmic dynein 1 intermediate chain 1,Cytoplasmic dynein intermediate chain 1,DH IC-1,DNCI1,DNCIC1,DYNC1I1,Dynein intermediate chain 1, cytosolic,Homo sapiens,Human
EIAAB10513 Cytoplasmic dynein 1 intermediate chain 2,Cytoplasmic dynein intermediate chain 2,DH IC-2,DNCI2,DNCIC2,DYNC1I2,Dynein intermediate chain 2, cytosolic,Homo sapiens,Human
EIAAB10516 Cytoplasmic dynein 1 intermediate chain 2,Cytoplasmic dynein intermediate chain 2,DH IC-2,Dnci2,Dncic2,Dync1i2,Dynein intermediate chain 2, cytosolic,Rat,Rattus norvegicus
EIAAB10510 Cytoplasmic dynein 1 intermediate chain 1,Cytoplasmic dynein intermediate chain 1,DH IC-1,Dnci1,Dncic1,Dync1i1,Dynein intermediate chain 1, cytosolic,Mouse,Mus musculus
EIAAB10515 Cytoplasmic dynein 1 intermediate chain 2,Cytoplasmic dynein intermediate chain 2,DH IC-2,Dnci2,Dncic2,Dync1i2,Dynein intermediate chain 2, cytosolic,Mouse,Mus musculus
EIAAB10512 Cytoplasmic dynein 1 intermediate chain 1,Cytoplasmic dynein intermediate chain 1,DH IC-1,Dnci1,Dncic1,Dync1i1,Dynein intermediate chain 1, cytosolic,Rat,Rattus norvegicus
EIAAB10514 Bos taurus,Bovine,Cytoplasmic dynein 1 intermediate chain 2,Cytoplasmic dynein intermediate chain 2,DH IC-2,DYNC1I2,Dynein intermediate chain 2, cytosolic
EIAAB10511 Bos taurus,Bovine,Cytoplasmic dynein 1 intermediate chain 1,Cytoplasmic dynein intermediate chain 1,DH IC-1,DYNC1I1,Dynein intermediate chain 1, cytosolic
20-783-72856 MOUSE ANTI BOVINE DYNEIN CYTOPLASMIC 74kDa - Dynein intermediate chain 1. cytosolic; DH IC-1; Cytoplasmic dynein intermediate chain 1 Monoclonal 0.1 mg
EIAAB10520 Cytoplasmic dynein 1 light intermediate chain 1,DLC-A,DNCLI1,DYNC1LI1,Dynein light chain A,Dynein light intermediate chain 1, cytosolic,Homo sapiens,Human,LIC1
EIAAB10517 Cytoplasmic dynein 1 light intermediate chain 1,DLC-A,Dncli1,Dnclic1,Dync1li1,Dynein light chain A,Dynein light intermediate chain 1, cytosolic,Mouse,Mus musculus
EIAAB10519 Cytoplasmic dynein 1 light intermediate chain 1,DLC-A,Dncli1,Dync1li1,Dynein light chain A,Dynein light intermediate chain 1, cytosolic,Rat,Rattus norvegicus
EIAAB10523 Cytoplasmic dynein 1 light intermediate chain 2,DNCLI2,DYNC1LI2,Dynein light intermediate chain 2, cytosolic,Homo sapiens,Human,LIC2,LIC-2,LIC53_55
EIAAB10521 Cytoplasmic dynein 1 light intermediate chain 2,Dncli2,Dync1li2,Dynein light intermediate chain 2, cytosolic,LIC-2,LIC53_55,Rat,Rattus norvegicus
EIAAB10522 Cytoplasmic dynein 1 light intermediate chain 2,Dncli2,Dnclic2,Dync1li2,Dynein light intermediate chain 2, cytosolic,Mouse,Mus musculus
EIAAB10518 Chicken,Cytoplasmic dynein 1 light intermediate chain 1,DLC-A,DNCLI1,DYNC1LI1,Dynein light chain A,Dynein light intermediate chain 1, cytosolic,Gallus gallus,LIC57_59
EIAAB10527 CGI-60,Cytoplasmic dynein 2 light intermediate chain 1,D2LIC,DYNC2LI1,Dynein 2 light intermediate chain,Homo sapiens,Human,LIC3
EIAAB12175 Cytoplasmic dynein 2 heavy chain,Cytoplasmic dynein 2 heavy chain 1,DHC1B,DHC2,DNCH2,DYH1B,DYNC2H1,Dynein cytoplasmic heavy chain 2,Dynein heavy chain 11,Dynein heavy chain isotype 1B,hDHC11,Homo sapi
EIAAB12173 Cytoplasmic dynein 2 heavy chain,Cytoplasmic dynein 2 heavy chain 1,Dhc1b,Dlp4,Dnch2,Dnchc2,Dync2h1,Dynein cytoplasmic heavy chain 2,Dynein heavy chain isotype 1B,Dynein-like protein 4,Rat,Rattus norv
EIAAB12174 Cytoplasmic dynein 2 heavy chain,Cytoplasmic dynein 2 heavy chain 1,Dhc1b,Dnchc2,Dync2h1,Dynein cytoplasmic heavy chain 2,Dynein heavy chain 11,Dynein heavy chain isotype 1B,Kiaa1997,mDHC11,Mouse,Mus
EIAAB12170 Cytoplasmic dynein 1 heavy chain 1,Cytoplasmic dynein heavy chain 1,DHC1,DNCH1,DNCL,DNECL,DYHC,DYNC1H1,Dynein heavy chain, cytosolic,Homo sapiens,Human,KIAA0325
EIAAB12171 Cytoplasmic dynein 1 heavy chain 1,Cytoplasmic dynein heavy chain 1,Dhc1,Dnch1,Dnchc1,Dnec1,Dyhc,Dync1h1,Dynein heavy chain, cytosolic,MAP 1C,Map1c,Rat,Rattus norvegicus
EIAAB12172 Cytoplasmic dynein 1 heavy chain 1,Cytoplasmic dynein heavy chain 1,Dhc1,Dnch1,Dnchc1,Dyhc,Dync1h1,Dynein heavy chain, cytosolic,Mouse,Mus musculus
EIAAB11505 Axonemal dynein intermediate chain 1,Dnai1,Dnaic1,Dynein intermediate chain 1, axonemal,Mouse,Mus musculus
EIAAB11504 Axonemal dynein intermediate chain 1,DNAI1,Dynein intermediate chain 1, axonemal,Homo sapiens,Human


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur