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 27-MAR-2024, entry version 201. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 106. DR CORUM; O14576; -. DR ELM; O14576; -. DR IntAct; O14576; 58. DR MINT; O14576; -. DR STRING; 9606.ENSP00000320130; -. DR GlyCosmos; O14576; 1 site, 1 glycan. 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; 9606-ENSP00000320130; -. DR PeptideAtlas; 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; 204 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 AGR; HGNC:2963; -. 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; MGVHFHP; -. DR OrthoDB; 654577at2759; -. 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; 8 hits in 1145 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 169 other cell types or tissues. DR ExpressionAtlas; O14576; baseline and differential. 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: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; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR025956; DYNC1I1/DYNC1I2. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR12442:SF34; CYTOPLASMIC DYNEIN 1 INTERMEDIATE CHAIN 1; 1. DR PANTHER; PTHR12442; DYNEIN INTERMEDIATE CHAIN; 1. DR Pfam; PF11540; Dynein_IC2; 1. DR Pfam; PF00400; WD40; 2. DR SMART; SM00320; WD40; 5. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; O14576; HS. 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 //