DC1I1_HUMAN
ID DC1I1_HUMAN Reviewed; 645 AA.
AC O14576; B4DME3; F5H050; G5E9K1; Q8TBF7; Q9Y2X1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Cytoplasmic dynein 1 intermediate chain 1;
DE AltName: Full=Cytoplasmic dynein intermediate chain 1;
DE AltName: Full=Dynein intermediate chain 1, cytosolic;
DE Short=DH IC-1;
GN Name=DYNC1I1; Synonyms=DNCI1, DNCIC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10049579; DOI=10.1006/geno.1998.5665;
RA Crackower M.A., Sinasac D.S., Xia J., Motoyama J., Prochazka M.,
RA Rommens J.M., Scherer S.W., Tsui L.-C.;
RT "Cloning and characterization of two cytoplasmic dynein intermediate chain
RT genes in mouse and human.";
RL Genomics 55:257-267(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Li G., Jin J., Hu S., Li W., Yuan J., Qiang B.;
RT "Molecular cloning of a cytoplasmic dynein gene.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=19229290; DOI=10.1038/emboj.2009.38;
RA Sivaram M.V., Wadzinski T.L., Redick S.D., Manna T., Doxsey S.J.;
RT "Dynein light intermediate chain 1 is required for progress through the
RT spindle assembly checkpoint.";
RL EMBO J. 28:902-914(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP INTERACTION WITH DYNLT1, AND MUTAGENESIS OF LEU-148; GLY-149; VAL-150;
RP LYS-152; VAL-153; GLN-155; VAL-156; ASP-157 AND PHE-158.
RX PubMed=27502274; DOI=10.1074/jbc.m116.736884;
RA Merino-Gracia J., Zamora-Carreras H., Bruix M., Rodriguez-Crespo I.;
RT "Molecular basis for the protein recognition specificity of the dynein
RT light chain DYNLT1/Tctex1: characterization of the interaction with activin
RT receptor IIB.";
RL J. Biol. Chem. 291:20962-20975(2016).
RN [10]
RP VARIANT LEU-373.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Acts as one of several non-catalytic accessory components of
CC the cytoplasmic dynein 1 complex that are thought to be involved in
CC linking dynein to cargos and to adapter proteins that regulate dynein
CC function. Cytoplasmic dynein 1 acts as a motor for the intracellular
CC retrograde motility of vesicles and organelles along microtubules. The
CC intermediate chains mediate the binding of dynein to dynactin via its
CC 150 kDa component (p150-glued) DCTN1. May play a role in mediating the
CC interaction of cytoplasmic dynein with membranous organelles and
CC kinetochores.
CC -!- SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1 complex
CC consists of two catalytic heavy chains (HCs) and a number of non-
CC catalytic subunits presented by intermediate chains (ICs), light
CC intermediate chains (LICs) and light chains (LCs); the composition
CC seems to vary in respect to the IC, LIC and LC composition. The heavy
CC chain homodimer serves as a scaffold for the probable homodimeric
CC assembly of the respective non-catalytic subunits. The ICs and LICs
CC bind directly to the HC dimer and the LCs assemble on the IC dimer.
CC Interacts with DYNC1H1. Interacts with DYNLT1 and DYNLT3. Interacts
CC with DCTN1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:27502274}.
CC -!- INTERACTION:
CC O14576; Q8TD16: BICD2; NbExp=2; IntAct=EBI-366267, EBI-2372628;
CC O14576; Q9CZA6: Nde1; Xeno; NbExp=2; IntAct=EBI-366267, EBI-309934;
CC O14576-2; P05067: APP; NbExp=3; IntAct=EBI-25840445, EBI-77613;
CC O14576-2; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-25840445, EBI-25840379;
CC O14576-2; Q9GZQ8: MAP1LC3B; NbExp=3; IntAct=EBI-25840445, EBI-373144;
CC O14576-2; P00491: PNP; NbExp=3; IntAct=EBI-25840445, EBI-712238;
CC O14576-2; P04271: S100B; NbExp=3; IntAct=EBI-25840445, EBI-458391;
CC O14576-2; Q13501: SQSTM1; NbExp=3; IntAct=EBI-25840445, EBI-307104;
CC O14576-2; P43405-2: SYK; NbExp=3; IntAct=EBI-25840445, EBI-25892332;
CC O14576-2; Q9BVJ6: UTP14A; NbExp=3; IntAct=EBI-25840445, EBI-473284;
CC O14576-2; Q9UBQ0-2: VPS29; NbExp=3; IntAct=EBI-25840445, EBI-11141397;
CC O14576-5; P05067: APP; NbExp=3; IntAct=EBI-25936079, EBI-77613;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome, centromere,
CC kinetochore {ECO:0000269|PubMed:19229290}. Cytoplasm, cytoskeleton,
CC spindle pole {ECO:0000269|PubMed:19229290}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=O14576-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14576-2; Sequence=VSP_001332;
CC Name=3;
CC IsoId=O14576-3; Sequence=VSP_001332, VSP_001333;
CC Name=4;
CC IsoId=O14576-4; Sequence=VSP_001332, VSP_001333, VSP_054766;
CC Name=5;
CC IsoId=O14576-5; Sequence=VSP_001333;
CC -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC {ECO:0000305}.
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DR EMBL; AF063228; AAC33443.1; -; mRNA.
DR EMBL; AF123074; AAD26852.1; -; mRNA.
DR EMBL; AK091339; BAC03639.1; -; mRNA.
DR EMBL; AK297427; BAG59855.1; -; mRNA.
DR EMBL; AC022261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002452; AAB67047.2; -; Genomic_DNA.
DR EMBL; AC002540; AAB70113.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76753.1; -; Genomic_DNA.
DR EMBL; BC022540; AAH22540.1; -; mRNA.
DR CCDS; CCDS47645.1; -. [O14576-2]
DR CCDS; CCDS47646.1; -. [O14576-3]
DR CCDS; CCDS5644.1; -. [O14576-1]
DR CCDS; CCDS64718.1; -. [O14576-5]
DR CCDS; CCDS64719.1; -. [O14576-4]
DR RefSeq; NP_001129028.1; NM_001135556.1. [O14576-2]
DR RefSeq; NP_001129029.1; NM_001135557.1. [O14576-3]
DR RefSeq; NP_001265350.1; NM_001278421.1. [O14576-5]
DR RefSeq; NP_001265351.1; NM_001278422.1. [O14576-4]
DR RefSeq; NP_004402.1; NM_004411.4. [O14576-1]
DR RefSeq; XP_011514163.1; XM_011515861.1.
DR RefSeq; XP_011514164.1; XM_011515862.1.
DR RefSeq; XP_016867293.1; XM_017011804.1.
DR RefSeq; XP_016867294.1; XM_017011805.1.
DR AlphaFoldDB; O14576; -.
DR SMR; O14576; -.
DR BioGRID; 108118; 105.
DR CORUM; O14576; -.
DR ELM; O14576; -.
DR IntAct; O14576; 57.
DR MINT; O14576; -.
DR STRING; 9606.ENSP00000320130; -.
DR GlyGen; O14576; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14576; -.
DR PhosphoSitePlus; O14576; -.
DR BioMuta; DYNC1I1; -.
DR EPD; O14576; -.
DR jPOST; O14576; -.
DR MassIVE; O14576; -.
DR MaxQB; O14576; -.
DR PaxDb; O14576; -.
DR PeptideAtlas; O14576; -.
DR PRIDE; O14576; -.
DR ProteomicsDB; 25229; -.
DR ProteomicsDB; 33962; -.
DR ProteomicsDB; 48091; -. [O14576-1]
DR ProteomicsDB; 48092; -. [O14576-2]
DR ProteomicsDB; 48093; -. [O14576-3]
DR TopDownProteomics; O14576-3; -. [O14576-3]
DR Antibodypedia; 15905; 160 antibodies from 26 providers.
DR DNASU; 1780; -.
DR Ensembl; ENST00000324972.10; ENSP00000320130.6; ENSG00000158560.14. [O14576-1]
DR Ensembl; ENST00000359388.8; ENSP00000352348.4; ENSG00000158560.14. [O14576-3]
DR Ensembl; ENST00000437599.5; ENSP00000398118.1; ENSG00000158560.14. [O14576-5]
DR Ensembl; ENST00000447467.6; ENSP00000392337.2; ENSG00000158560.14. [O14576-2]
DR Ensembl; ENST00000457059.2; ENSP00000412444.1; ENSG00000158560.14. [O14576-2]
DR Ensembl; ENST00000630942.2; ENSP00000486363.1; ENSG00000158560.14. [O14576-4]
DR GeneID; 1780; -.
DR KEGG; hsa:1780; -.
DR MANE-Select; ENST00000447467.6; ENSP00000392337.2; NM_001135556.2; NP_001129028.1. [O14576-2]
DR UCSC; uc003uob.4; human. [O14576-1]
DR CTD; 1780; -.
DR DisGeNET; 1780; -.
DR GeneCards; DYNC1I1; -.
DR HGNC; HGNC:2963; DYNC1I1.
DR HPA; ENSG00000158560; Tissue enhanced (brain).
DR MIM; 603772; gene.
DR neXtProt; NX_O14576; -.
DR OpenTargets; ENSG00000158560; -.
DR PharmGKB; PA27434; -.
DR VEuPathDB; HostDB:ENSG00000158560; -.
DR eggNOG; KOG1587; Eukaryota.
DR GeneTree; ENSGT00940000156032; -.
DR HOGENOM; CLU_012999_1_1_1; -.
DR InParanoid; O14576; -.
DR OMA; YVRDYTI; -.
DR PhylomeDB; O14576; -.
DR TreeFam; TF300553; -.
DR PathwayCommons; O14576; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; O14576; -.
DR BioGRID-ORCS; 1780; 7 hits in 1066 CRISPR screens.
DR ChiTaRS; DYNC1I1; human.
DR GeneWiki; DYNC1I1; -.
DR GenomeRNAi; 1780; -.
DR Pharos; O14576; Tbio.
DR PRO; PR:O14576; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O14576; protein.
DR Bgee; ENSG00000158560; Expressed in endothelial cell and 167 other tissues.
DR ExpressionAtlas; O14576; baseline and differential.
DR Genevisible; O14576; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0003774; F:cytoskeletal motor activity; TAS:ProtInc.
DR GO; GO:0045504; F:dynein heavy chain binding; IBA:GO_Central.
DR GO; GO:0045503; F:dynein light chain binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; ISS:HGNC-UCL.
DR GO; GO:0003777; F:microtubule motor activity; ISS:HGNC-UCL.
DR GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0010970; P:transport along microtubule; IBA:GO_Central.
DR GO; GO:0047496; P:vesicle transport along microtubule; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR025956; DYNC1I1/DYNC1I2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF11540; Dynein_IC2; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Centromere; Chromosome; Cytoplasm;
KW Cytoskeleton; Dynein; Kinetochore; Microtubule; Motor protein;
KW Phosphoprotein; Reference proteome; Repeat; Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT CHAIN 2..645
FT /note="Cytoplasmic dynein 1 intermediate chain 1"
FT /id="PRO_0000114652"
FT REPEAT 285..334
FT /note="WD 1"
FT REPEAT 338..378
FT /note="WD 2"
FT REPEAT 387..428
FT /note="WD 3"
FT REPEAT 437..477
FT /note="WD 4"
FT REPEAT 482..527
FT /note="WD 5"
FT REPEAT 530..570
FT /note="WD 6"
FT REPEAT 576..615
FT /note="WD 7"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..123
FT /note="Interaction with DCTN1"
FT /evidence="ECO:0000250"
FT REGION 95..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..163
FT /note="Interaction with DYNLT1"
FT /evidence="ECO:0000269|PubMed:27502274"
FT REGION 169..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88485"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62871"
FT MOD_RES 105
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88485"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88485"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88485"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88485"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88485"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 74..90
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_001332"
FT VAR_SEQ 123..142
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_001333"
FT VAR_SEQ 610..645
FT /note="LAVPHNDEWTRFARTLVEIRANRADSEEEGTVELSA -> GLAMLPGWSQNS
FT WTQAILLCWPPKVLGLQT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054766"
FT VARIANT 373
FT /note="H -> L (found in a renal cell carcinoma case;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064709"
FT VARIANT 582
FT /note="N -> T (in dbSNP:rs35077523)"
FT /id="VAR_048905"
FT MUTAGEN 148
FT /note="L->G: Disrupts interaction with DYNLT1."
FT /evidence="ECO:0000269|PubMed:27502274"
FT MUTAGEN 149
FT /note="G->E: No effect on interaction with DYNLT1."
FT /evidence="ECO:0000269|PubMed:27502274"
FT MUTAGEN 150
FT /note="V->G: Disrupts interaction with DYNLT1."
FT /evidence="ECO:0000269|PubMed:27502274"
FT MUTAGEN 150
FT /note="V->W: No effect on interaction with DYNLT1."
FT /evidence="ECO:0000269|PubMed:27502274"
FT MUTAGEN 152
FT /note="K->A,Y: No effect on interaction with DYNLT1."
FT /evidence="ECO:0000269|PubMed:27502274"
FT MUTAGEN 153
FT /note="V->G: Decreases interaction with DYNLT1."
FT /evidence="ECO:0000269|PubMed:27502274"
FT MUTAGEN 155
FT /note="Q->H,R,T,Y: No effect on interaction with DYNLT1."
FT /evidence="ECO:0000269|PubMed:27502274"
FT MUTAGEN 156
FT /note="V->G: Decreases interaction with DYNLT1."
FT /evidence="ECO:0000269|PubMed:27502274"
FT MUTAGEN 157
FT /note="D->R: No effect on interaction with DYNLT1."
FT /evidence="ECO:0000269|PubMed:27502274"
FT MUTAGEN 158
FT /note="F->G: Disrupts interaction with DYNLT1."
FT /evidence="ECO:0000269|PubMed:27502274"
FT CONFLICT 254
FT /note="D -> G (in Ref. 3; BAG59855)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="W -> C (in Ref. 6; AAH22540)"
FT /evidence="ECO:0000305"
SQ 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
