ID DC1L1_HUMAN Reviewed; 523 AA. AC Q9Y6G9; A2RRG7; Q53HC8; Q53HK7; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 3. DT 27-MAR-2024, entry version 182. DE RecName: Full=Cytoplasmic dynein 1 light intermediate chain 1; DE Short=LIC1; DE AltName: Full=Dynein light chain A; DE Short=DLC-A; DE AltName: Full=Dynein light intermediate chain 1, cytosolic; DE Short=DLIC-1 {ECO:0000303|PubMed:20026645}; GN Name=DYNC1LI1; Synonyms=DNCLI1; 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], AND VARIANT ARG-277. RC TISSUE=Pituitary; RA Dai M., Peng Y., Song H., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., RA Luo M., Chen J., Hu R.; RT "Human dynein light chain-A mRNA, complete cds."; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-277. RC TISSUE=Cerebellum, and Coronary artery; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [5] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-398 AND SER-487, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; THR-213; SER-419; RP SER-421; SER-510; THR-512; THR-513; THR-515 AND SER-516, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP FUNCTION IN THE SPINDLE ASSEMBLY CHECKPOINT, SUBUNIT, PHOSPHORYLATION AT RP SER-207; SER-398; SER-405 AND THR-408, AND 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 [14] RP INTERACTION WITH HUMAN ADENOVIRUS HEXON PROTEIN (MICROBIAL INFECTION). RX PubMed=20006841; DOI=10.1016/j.chom.2009.11.006; RA Bremner K.H., Scherer J., Yi J., Vershinin M., Gross S.P., Vallee R.B.; RT "Adenovirus transport via direct interaction of cytoplasmic dynein with the RT viral capsid hexon subunit."; RL Cell Host Microbe 6:523-535(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-510; THR-512; RP THR-513; THR-515 AND SER-516, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [17] RP FUNCTION, INTERACTION WITH RAB11FIP3, AND SUBCELLULAR LOCATION. RX PubMed=20026645; DOI=10.1242/jcs.052670; RA Horgan C.P., Hanscom S.R., Jolly R.S., Futter C.E., McCaffrey M.W.; RT "Rab11-FIP3 links the Rab11 GTPase and cytoplasmic dynein to mediate RT transport to the endosomal-recycling compartment."; RL J. Cell Sci. 123:181-191(2010). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-398; SER-419; RP SER-421; SER-487 AND SER-516, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-516, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-398; SER-405; RP THR-408; SER-412; SER-421; SER-427; SER-487; SER-510 AND SER-516, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-510, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). 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. May CC play a role in binding dynein to membranous organelles or chromosomes. CC Probably involved in the microtubule-dependent transport of CC pericentrin. Is required for progress through the spindle assembly CC checkpoint. The phosphorylated form appears to be involved in the CC selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores. CC Forms a functional Rab11/RAB11FIP3/dynein complex onto endosomal CC membrane that regulates the movement of peripheral sorting endosomes CC (SE) along microtubule tracks toward the microtubule organizing CC center/centrosome, generating the endosomal recycling compartment (ERC) CC (PubMed:20026645). {ECO:0000269|PubMed:19229290, CC ECO:0000269|PubMed:20026645}. 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 Self-associates. Interacts with DYNC1H1; DYNC1LI1 and DYNC1LI2 bind CC mutually exclusive to DYNC1H1. Interacts with PCNT (By similarity). CC Forms a complex with RAB11FIP3 and RAB11A1; the interaction between CC DYNC1LI1 and RAB11FIP3 is direct and induces DYNC1LI1 localization onto CC endosomal membrane; the complex regulates endocytic trafficking CC (PubMed:20026645). {ECO:0000250, ECO:0000269|PubMed:19229290, CC ECO:0000269|PubMed:20026645}. CC -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus 5 hexon CC protein; this interaction probably allows virus intracellular CC transport. {ECO:0000269|PubMed:20006841}. CC -!- INTERACTION: CC Q9Y6G9; P15259: PGAM2; NbExp=3; IntAct=EBI-2556107, EBI-2511669; CC Q9Y6G9; Q04864: REL; NbExp=4; IntAct=EBI-2556107, EBI-307352; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome, centromere, CC kinetochore {ECO:0000269|PubMed:19229290}. Cytoplasm, cytoskeleton, CC spindle pole {ECO:0000269|PubMed:19229290}. Recycling endosome membrane CC {ECO:0000269|PubMed:20026645}. Note=During interphase, localized in CC vesicles continuously moving from peripheral sorting endosomes in the CC cell towards the pericentrosomal endosomal recycling compartment (ERC). CC {ECO:0000269|PubMed:20026645}. CC -!- PTM: Phosphorylated during mitosis but not in interphase. CC {ECO:0000269|PubMed:19229290}. CC -!- SIMILARITY: Belongs to the dynein light 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; AF078849; AAD44481.1; -; mRNA. DR EMBL; AK222573; BAD96293.1; -; mRNA. DR EMBL; AK222653; BAD96373.1; -; mRNA. DR EMBL; CH471055; EAW64433.1; -; Genomic_DNA. DR EMBL; BC131620; AAI31621.1; -; mRNA. DR CCDS; CCDS2654.1; -. DR RefSeq; NP_057225.2; NM_016141.3. DR PDB; 6B9H; X-ray; 1.50 A; B=433-458. DR PDB; 6PSD; X-ray; 2.66 A; B/D/F/H/J/L/N/P=433-457. DR PDB; 6PSE; X-ray; 2.40 A; C=433-458. DR PDBsum; 6B9H; -. DR PDBsum; 6PSD; -. DR PDBsum; 6PSE; -. DR AlphaFoldDB; Q9Y6G9; -. DR SMR; Q9Y6G9; -. DR BioGRID; 119327; 239. DR CORUM; Q9Y6G9; -. DR IntAct; Q9Y6G9; 49. DR MINT; Q9Y6G9; -. DR STRING; 9606.ENSP00000273130; -. DR GlyCosmos; Q9Y6G9; 2 sites, 1 glycan. DR GlyGen; Q9Y6G9; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q9Y6G9; -. DR MetOSite; Q9Y6G9; -. DR PhosphoSitePlus; Q9Y6G9; -. DR SwissPalm; Q9Y6G9; -. DR BioMuta; DYNC1LI1; -. DR DMDM; 134047749; -. DR CPTAC; CPTAC-965; -. DR EPD; Q9Y6G9; -. DR jPOST; Q9Y6G9; -. DR MassIVE; Q9Y6G9; -. DR MaxQB; Q9Y6G9; -. DR PaxDb; 9606-ENSP00000273130; -. DR PeptideAtlas; Q9Y6G9; -. DR ProteomicsDB; 86677; -. DR Pumba; Q9Y6G9; -. DR Antibodypedia; 27761; 296 antibodies from 24 providers. DR DNASU; 51143; -. DR Ensembl; ENST00000273130.9; ENSP00000273130.4; ENSG00000144635.9. DR GeneID; 51143; -. DR KEGG; hsa:51143; -. DR MANE-Select; ENST00000273130.9; ENSP00000273130.4; NM_016141.4; NP_057225.2. DR UCSC; uc003cfb.4; human. DR AGR; HGNC:18745; -. DR CTD; 51143; -. DR DisGeNET; 51143; -. DR GeneCards; DYNC1LI1; -. DR HGNC; HGNC:18745; DYNC1LI1. DR HPA; ENSG00000144635; Low tissue specificity. DR MIM; 615890; gene. DR neXtProt; NX_Q9Y6G9; -. DR OpenTargets; ENSG00000144635; -. DR PharmGKB; PA38670; -. DR VEuPathDB; HostDB:ENSG00000144635; -. DR eggNOG; KOG3905; Eukaryota. DR GeneTree; ENSGT00390000008295; -. DR HOGENOM; CLU_021937_2_1_1; -. DR InParanoid; Q9Y6G9; -. DR OMA; VMLEKDF; -. DR OrthoDB; 179830at2759; -. DR PhylomeDB; Q9Y6G9; -. DR TreeFam; TF352602; -. DR PathwayCommons; Q9Y6G9; -. 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-6798695; Neutrophil degranulation. 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; Q9Y6G9; -. DR SIGNOR; Q9Y6G9; -. DR BioGRID-ORCS; 51143; 51 hits in 1159 CRISPR screens. DR ChiTaRS; DYNC1LI1; human. DR GeneWiki; DYNC1LI1; -. DR GenomeRNAi; 51143; -. DR Pharos; Q9Y6G9; Tbio. DR PRO; PR:Q9Y6G9; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9Y6G9; Protein. DR Bgee; ENSG00000144635; Expressed in cortical plate and 207 other cell types or tissues. DR ExpressionAtlas; Q9Y6G9; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; IDA:UniProtKB. DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome. DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0045504; F:dynein heavy chain binding; IPI:FlyBase. DR GO; GO:0019003; F:GDP binding; IDA:FlyBase. DR GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central. DR GO; GO:0007018; P:microtubule-based movement; IMP:UniProtKB. DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IMP:UniProtKB. DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IDA:UniProtKB. DR DisProt; DP02547; -. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR008467; Dynein1_light_intermed_chain. DR InterPro; IPR022780; Dynein_light_int_chain. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR12688:SF2; CYTOPLASMIC DYNEIN 1 LIGHT INTERMEDIATE CHAIN 1; 1. DR PANTHER; PTHR12688; DYNEIN LIGHT INTERMEDIATE CHAIN; 1. DR Pfam; PF05783; DLIC; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR Genevisible; Q9Y6G9; HS. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell cycle; Cell division; Centromere; KW Chromosome; Cytoplasm; Cytoskeleton; Dynein; Endosome; KW Host-virus interaction; Kinetochore; Membrane; Microtubule; Mitosis; KW Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome; KW Transport. FT CHAIN 1..523 FT /note="Cytoplasmic dynein 1 light intermediate chain 1" FT /id="PRO_0000114666" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 387..434 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 456..523 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 405..422 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 506..523 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 74..81 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MOD_RES 207 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19229290, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 213 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 398 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19229290, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 405 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19229290, FT ECO:0007744|PubMed:23186163" FT MOD_RES 408 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:19229290, FT ECO:0007744|PubMed:23186163" FT MOD_RES 412 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 419 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 421 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 427 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 487 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 510 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 512 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 513 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 515 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 516 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT VARIANT 147 FT /note="M -> T (in dbSNP:rs34181332)" FT /id="VAR_061141" FT VARIANT 277 FT /note="Q -> R (in dbSNP:rs2303857)" FT /evidence="ECO:0000269|Ref.1, ECO:0000269|Ref.2" FT /id="VAR_023325" FT CONFLICT 186 FT /note="M -> I (in Ref. 2; BAD96293)" FT /evidence="ECO:0000305" FT CONFLICT 210 FT /note="R -> G (in Ref. 2; BAD96293)" FT /evidence="ECO:0000305" FT CONFLICT 225 FT /note="L -> V (in Ref. 1; AAD44481)" FT /evidence="ECO:0000305" FT CONFLICT 267 FT /note="I -> F (in Ref. 1; AAD44481)" FT /evidence="ECO:0000305" FT CONFLICT 351 FT /note="D -> G (in Ref. 2; BAD96293)" FT /evidence="ECO:0000305" FT HELIX 443..453 FT /evidence="ECO:0007829|PDB:6B9H" SQ SEQUENCE 523 AA; 56579 MW; 29159F560E382095 CRC64; MAAVGRVGSF GSSPPGLSST YTGGPLGNEI ASGNGGAAAG DDEDGQNLWS CILSEVSTRS RSKLPAGKNV LLLGEDGAGK TSLIRKIQGI EEYKKGRGLE YLYLNVHDED RDDQTRCNVW ILDGDLYHKG LLKFSLDAVS LKDTLVMLVV DMSKPWTALD SLQKWASVVR EHVDKLKIPP EEMKQMEQKL IRDFQEYVEP GEDFPASPQR RNTASQEDKD DSVVLPLGAD TLTHNLGIPV LVVCTKCDAI SVLEKEHDYR DEHFDFIQSH IRKFCLQYGA ALIYTSVKEN KNIDLVYKYI VQKLYGFPYK IPAVVVEKDA VFIPAGWDND KKIGILHENF QTLKAEDNFE DIITKPPVRK FVHEKEIMAE DDQVFLMKLQ SLLAKQPPTA AGRPVDASPR VPGGSPRTPN RSVSSNVASV SPIPAGSKKI DPNMKAGATS EGVLANFFNS LLSKKTGSPG GPGVSGGSPA GGAGGGSSGL PPSTKKSGQK PVLDVHAELD RITRKPVTVS PTTPTSPTEG EAS //