DYL1_HUMAN
ID DYL1_HUMAN Reviewed; 89 AA.
AC P63167; Q15701;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Dynein light chain 1, cytoplasmic;
DE AltName: Full=8 kDa dynein light chain;
DE Short=DLC8;
DE AltName: Full=Dynein light chain LC8-type 1;
DE AltName: Full=Protein inhibitor of neuronal nitric oxide synthase;
DE Short=PIN;
GN Name=DYNLL1; Synonyms=DLC1, DNCL1, DNCLC1, HDLC1;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8628263; DOI=10.1128/mcb.16.5.1966;
RA Dick T., Ray K., Salz H.K., Chia W.;
RT "Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and
RT apoptotic cell death in Drosophila melanogaster.";
RL Mol. Cell. Biol. 16:1966-1977(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION IN REGULATION OF APOPTOSIS, AND INTERACTION WITH BCL2L11 AND BCL2.
RX PubMed=10198631; DOI=10.1016/s1097-2765(00)80456-6;
RA Puthalakath H., Huang D.C., O'Reilly L.A., King S.M., Strasser A.;
RT "The proapoptotic activity of the Bcl-2 family member Bim is regulated by
RT interaction with the dynein motor complex.";
RL Mol. Cell 3:287-296(1999).
RN [4]
RP INTERACTION WITH HUMAN SPUMARETROVIRUS GAG (MICROBIAL INFECTION).
RX PubMed=12857789; DOI=10.1242/jcs.00613;
RA Petit C., Giron M.L., Tobaly-Tapiero J., Bittoun P., Real E., Jacob Y.,
RA Tordo N., De The H., Saib A.;
RT "Targeting of incoming retroviral Gag to the centrosome involves a direct
RT interaction with the dynein light chain 8.";
RL J. Cell Sci. 116:3433-3442(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
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 FUNCTION IN REGULATION OF BCL2L11, INTERACTION WITH PAK1 AND BCL2L11,
RP PHOSPHORYLATION AT SER-88, AND MUTAGENESIS OF SER-88.
RX PubMed=15193260; DOI=10.1016/j.ccr.2004.05.022;
RA Vadlamudi R.K., Bagheri-Yarmand R., Yang Z., Balasenthil S., Nguyen D.,
RA Sahin A.A., den Hollander P., Kumar R.;
RT "Dynein light chain 1, a p21-activated kinase 1-interacting substrate,
RT promotes cancerous phenotypes.";
RL Cancer Cell 5:575-585(2004).
RN [7]
RP INTERACTION WITH TXNDC17.
RX PubMed=14607843; DOI=10.1074/jbc.m307959200;
RA Jeong W., Chang T.-S., Boja E.S., Fales H.M., Rhee S.G.;
RT "Roles of TRP14, a thioredoxin-related protein in tumor necrosis factor-
RT alpha signaling pathways.";
RL J. Biol. Chem. 279:3151-3159(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH ESR1.
RX PubMed=15891768; DOI=10.1038/sj.embor.7400417;
RA Rayala S.K., den Hollander P., Balasenthil S., Yang Z., Broaddus R.R.,
RA Kumar R.;
RT "Functional regulation of oestrogen receptor pathway by the dynein light
RT chain 1.";
RL EMBO Rep. 6:538-544(2005).
RN [9]
RP ERRATUM OF PUBMED:15891768.
RA Rayala S.K., den Hollander P., Balasenthil S., Yang Z., Broaddus R.R.,
RA Kumar R.;
RL EMBO Rep. 6:1101-1101(2005).
RN [10]
RP FUNCTION, AND INTERACTION WITH WWC1.
RX PubMed=16684779; DOI=10.1074/jbc.m600021200;
RA Rayala S.K., den Hollander P., Manavathi B., Talukder A.H., Song C.,
RA Peng S., Barnekow A., Kremerskothen J., Kumar R.;
RT "Essential role of KIBRA in co-activator function of dynein light chain 1
RT in mammalian cells.";
RL J. Biol. Chem. 281:19092-19099(2006).
RN [11]
RP SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH BCL2L11, AND MUTAGENESIS OF
RP SER-88.
RX PubMed=18084006; DOI=10.1074/jbc.m704512200;
RA Song C., Wen W., Rayala S.K., Chen M., Ma J., Zhang M., Kumar R.;
RT "Serine 88 phosphorylation of the 8-kDa dynein light chain 1 is a molecular
RT switch for its dimerization status and functions.";
RL J. Biol. Chem. 283:4004-4013(2008).
RN [12]
RP SUBUNIT, INTERACTION WITH PAK1, AND MUTAGENESIS OF THR-67.
RX PubMed=18650427; DOI=10.1074/jbc.m800758200;
RA Lightcap C.M., Sun S., Lear J.D., Rodeck U., Polenova T., Williams J.C.;
RT "Biochemical and structural characterization of the Pak1-LC8 interaction.";
RL J. Biol. Chem. 283:27314-27324(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP INTERACTION WITH BSN.
RX PubMed=19380881; DOI=10.1083/jcb.200807155;
RA Fejtova A., Davydova D., Bischof F., Lazarevic V., Altrock W.D.,
RA Romorini S., Schoene C., Zuschratter W., Kreutz M.R., Garner C.C.,
RA Ziv N.E., Gundelfinger E.D.;
RT "Dynein light chain regulates axonal trafficking and synaptic levels of
RT Bassoon.";
RL J. Cell Biol. 185:341-355(2009).
RN [15]
RP INTERACTION WITH MYZAP.
RX PubMed=20412299; DOI=10.1111/j.1742-4658.2010.07649.x;
RA Garcia-Mayoral M.F., Martinez-Moreno M., Albar J.P., Rodriguez-Crespo I.,
RA Bruix M.;
RT "Structural basis for the interaction between dynein light chain 1 and the
RT glutamate channel homolog GRINL1A.";
RL FEBS J. 277:2340-2350(2010).
RN [16]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH AMBRA1.
RX PubMed=20921139; DOI=10.1083/jcb.201002100;
RA Di Bartolomeo S., Corazzari M., Nazio F., Oliverio S., Lisi G.,
RA Antonioli M., Pagliarini V., Matteoni S., Fuoco C., Giunta L., D'Amelio M.,
RA Nardacci R., Romagnoli A., Piacentini M., Cecconi F., Fimia G.M.;
RT "The dynamic interaction of AMBRA1 with the dynein motor complex regulates
RT mammalian autophagy.";
RL J. Cell Biol. 191:155-168(2010).
RN [17]
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 [18]
RP IDENTIFICATION IN A COMPLEX WITH KNSTRN; SPAG5; PLK1 AND SGO2.
RX PubMed=21402792; DOI=10.1083/jcb.201008023;
RA Dunsch A.K., Linnane E., Barr F.A., Gruneberg U.;
RT "The astrin-kinastrin/SKAP complex localizes to microtubule plus ends and
RT facilitates chromosome alignment.";
RL J. Cell Biol. 192:959-968(2011).
RN [19]
RP INTERACTION WITH ATMIN, AND INDUCTION.
RX PubMed=22167198; DOI=10.1074/jbc.m111.306019;
RA Jurado S., Conlan L.A., Baker E.K., Ng J.L., Tenis N., Hoch N.C.,
RA Gleeson K., Smeets M., Izon D., Heierhorst J.;
RT "ATM substrate Chk2-interacting Zn2+ finger (ASCIZ) Is a bi-functional
RT transcriptional activator and feedback sensor in the regulation of dynein
RT light chain (DYNLL1) expression.";
RL J. Biol. Chem. 287:3156-3164(2012).
RN [20]
RP INTERACTION WITH FAM83D; HMMR; SPAG5 AND KNSTRN, AND TISSUE SPECIFICITY.
RX PubMed=22965910; DOI=10.1083/jcb.201202112;
RA Dunsch A.K., Hammond D., Lloyd J., Schermelleh L., Gruneberg U., Barr F.A.;
RT "Dynein light chain 1 and a spindle-associated adaptor promote dynein
RT asymmetry and spindle orientation.";
RL J. Cell Biol. 198:1039-1054(2012).
RN [21]
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).
RN [22]
RP INTERACTION WITH EBOLAVIRUS PROTEIN VP35 (MICROBIAL INFECTION).
RX PubMed=25741013; DOI=10.1128/jvi.03652-14;
RA Luthra P., Jordan D.S., Leung D.W., Amarasinghe G.K., Basler C.F.;
RT "Ebola virus VP35 interaction with dynein LC8 regulates viral RNA
RT synthesis.";
RL J. Virol. 89:5148-5153(2015).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-43, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [24]
RP INTERACTION WITH HDAC6 AND TPPP.
RX PubMed=31505170; DOI=10.1016/j.bbamcr.2019.118556;
RA Olah J., Szunyogh S., Szenasi T., Szaniszlo T., Szabo A., Lehotzky A.,
RA Berki T., Nyitray L., Ovadi J.;
RT "Interactions between two regulatory proteins of microtubule dynamics,
RT HDAC6, TPPP/p25, and the hub protein, DYNLL/LC8.";
RL Biochim. Biophys. Acta 2019:118556-118556(2019).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 5-89.
RX PubMed=10426949; DOI=10.1038/11501;
RA Liang J., Jaffrey S.R., Guo W., Snyder S.H., Clardy J.;
RT "Structure of the PIN/LC8 dimer with a bound peptide.";
RL Nat. Struct. Biol. 6:735-740(1999).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NEK9, AND INTERACTION
RP WITH NEK9.
RX PubMed=23482567; DOI=10.1074/jbc.m113.459149;
RA Gallego P., Velazquez-Campoy A., Regue L., Roig J., Reverter D.;
RT "Structural analysis of the regulation of the DYNLL/LC8 binding to Nek9 by
RT phosphorylation.";
RL J. Biol. Chem. 288:12283-12294(2013).
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 changing or maintaining the spatial distribution of
CC cytoskeletal structures.
CC -!- FUNCTION: Binds and inhibits the catalytic activity of neuronal nitric
CC oxide synthase.
CC -!- FUNCTION: Promotes transactivation functions of ESR1 and plays a role
CC in the nuclear localization of ESR1. {ECO:0000269|PubMed:15891768,
CC ECO:0000269|PubMed:16684779}.
CC -!- FUNCTION: Regulates apoptotic activities of BCL2L11 by sequestering it
CC to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex
CC dissociates from cytoplasmic dynein and translocates to mitochondria
CC and sequesters BCL2 thus neutralizing its antiapoptotic activity.
CC {ECO:0000269|PubMed:10198631, ECO:0000269|PubMed:15193260}.
CC -!- SUBUNIT: Homodimer. Monomer; the monomeric form is incapable of binding
CC to target proteins. The cytoplasmic dynein 1 complex consists of two
CC catalytic heavy chains (HCs) and a number of non-catalytic subunits
CC presented by intermediate chains (ICs), light intermediate chains
CC (LICs) and light chains (LCs); the composition seems to vary in respect
CC to the IC, LIC and LC composition. The heavy chain homodimer serves as
CC a scaffold for the probable homodimeric assembly of the respective non-
CC catalytic subunits. The ICs and LICs bind directly to the HC dimer and
CC the LCs assemble on the IC dimer. Interacts with TXNDC17. Interacts
CC with WWC1 and ESR1. The WWC1-DYNLL1 interaction is mandatory for the
CC recruitment and transactivation functions of ESR1 or DYNLL1 to the
CC target chromatin. Interacts with BCL2L11 isoform 1 and isoform 2.
CC Interacts with BCL2; the interaction is greatly enhanced in the nucleus
CC and in mitochondria upon induction of apoptosis. Interacts with PAK1;
CC the interaction requires dimeric DYNLL1. Interacts with MYZAP. Part of
CC an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5,
CC PLK1, DYNLL1 and SGO2. Interacts with ATMIN; this interaction inhibits
CC ATMIN transcriptional activity and hence may play a role in a feedback
CC loop whereby DYNLL1 inhibits transactivation of its own promoter by
CC ATMIN. Interacts with NEK9 (not phosphorylated at 'Ser-944'). Interacts
CC with BICD2 (By similarity). Interacts with BCAS1 (By similarity).
CC Interacts with Basson/BSN. Interacts with HDAC6 (PubMed:31505170).
CC Interacts with TPPP (PubMed:31505170). Interacts with AMBRA1 (via TQT
CC motifs); tethering AMBRA1 to the cytoskeleton (PubMed:20921139).
CC Interacts with FAM83D/CHICA (via C-terminus) (PubMed:22965910).
CC Interacts with HMMR, SPAG5/Astrin and KNSTRN/Kinastrin
CC (PubMed:22965910). {ECO:0000250|UniProtKB:P63168,
CC ECO:0000250|UniProtKB:P63170, ECO:0000269|PubMed:10198631,
CC ECO:0000269|PubMed:14607843, ECO:0000269|PubMed:15193260,
CC ECO:0000269|PubMed:15891768, ECO:0000269|PubMed:16684779,
CC ECO:0000269|PubMed:18084006, ECO:0000269|PubMed:18650427,
CC ECO:0000269|PubMed:19380881, ECO:0000269|PubMed:20412299,
CC ECO:0000269|PubMed:20921139, ECO:0000269|PubMed:21402792,
CC ECO:0000269|PubMed:22167198, ECO:0000269|PubMed:22965910,
CC ECO:0000269|PubMed:23482567, ECO:0000269|PubMed:31505170}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human spumaretrovirus Gag
CC protein; this interaction is critical for intracellular microtubule-
CC dependent viral genome transport toward the centrosome.
CC {ECO:0000269|PubMed:12857789}.
CC -!- SUBUNIT: (Microbial infection) Interacts with ebolavirus protein VP35;
CC this interaction stabilizes VP35 N-terminal oligomerization domain and
CC enhances viral RNA synthesis. {ECO:0000269|PubMed:25741013}.
CC -!- INTERACTION:
CC P63167; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-349105, EBI-10187270;
CC P63167; Q96LC9: BMF; NbExp=3; IntAct=EBI-349105, EBI-3919268;
CC P63167; Q86WS4: C12orf40; NbExp=3; IntAct=EBI-349105, EBI-10286004;
CC P63167; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-349105, EBI-725606;
CC P63167; Q9H6X5-2: C19orf44; NbExp=5; IntAct=EBI-349105, EBI-12061599;
CC P63167; Q7Z6N9: CCDC28A; NbExp=5; IntAct=EBI-349105, EBI-10258115;
CC P63167; Q9BTE1: DCTN5; NbExp=3; IntAct=EBI-349105, EBI-747324;
CC P63167; O96015: DNAL4; NbExp=3; IntAct=EBI-349105, EBI-742362;
CC P63167; Q6W0C5: DPPA3; NbExp=5; IntAct=EBI-349105, EBI-12082590;
CC P63167; Q6P1L5: FAM117B; NbExp=11; IntAct=EBI-349105, EBI-3893327;
CC P63167; Q9UHL3: FAM153A; NbExp=4; IntAct=EBI-349105, EBI-2834075;
CC P63167; Q14153-2: FAM53B; NbExp=3; IntAct=EBI-349105, EBI-12401851;
CC P63167; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-349105, EBI-746969;
CC P63167; P60520: GABARAPL2; NbExp=3; IntAct=EBI-349105, EBI-720116;
CC P63167; Q9NVN8: GNL3L; NbExp=3; IntAct=EBI-349105, EBI-746682;
CC P63167; Q9NQX3: GPHN; NbExp=2; IntAct=EBI-349105, EBI-2371891;
CC P63167; Q6NT76: HMBOX1; NbExp=5; IntAct=EBI-349105, EBI-2549423;
CC P63167; Q9NSC5: HOMER3; NbExp=5; IntAct=EBI-349105, EBI-748420;
CC P63167; P42858: HTT; NbExp=10; IntAct=EBI-349105, EBI-466029;
CC P63167; Q8IYA8: IHO1; NbExp=6; IntAct=EBI-349105, EBI-8638439;
CC P63167; Q8NA54: IQUB; NbExp=3; IntAct=EBI-349105, EBI-10220600;
CC P63167; Q63ZY3: KANK2; NbExp=6; IntAct=EBI-349105, EBI-2556193;
CC P63167; Q92876: KLK6; NbExp=3; IntAct=EBI-349105, EBI-2432309;
CC P63167; Q6PF18: MORN3; NbExp=3; IntAct=EBI-349105, EBI-9675802;
CC P63167; P0CAP1: MYZAP; NbExp=6; IntAct=EBI-349105, EBI-7929343;
CC P63167; Q8TD19: NEK9; NbExp=4; IntAct=EBI-349105, EBI-1044009;
CC P63167; Q96PU9: ODF3; NbExp=3; IntAct=EBI-349105, EBI-12002088;
CC P63167; O60412: OR7C2; NbExp=3; IntAct=EBI-349105, EBI-12173063;
CC P63167; Q7L8S5: OTUD6A; NbExp=5; IntAct=EBI-349105, EBI-11960139;
CC P63167; Q13153: PAK1; NbExp=4; IntAct=EBI-349105, EBI-1307;
CC P63167; P61925: PKIA; NbExp=3; IntAct=EBI-349105, EBI-2682139;
CC P63167; Q9Y2B9: PKIG; NbExp=5; IntAct=EBI-349105, EBI-1052231;
CC P63167; P63244: RACK1; NbExp=6; IntAct=EBI-349105, EBI-296739;
CC P63167; Q8TDF6-2: RASGRP4; NbExp=3; IntAct=EBI-349105, EBI-12816371;
CC P63167; O43236: SEPTIN4; NbExp=5; IntAct=EBI-349105, EBI-1047513;
CC P63167; P49901: SMCP; NbExp=9; IntAct=EBI-349105, EBI-750494;
CC P63167; Q9P2Z0: THAP10; NbExp=8; IntAct=EBI-349105, EBI-745404;
CC P63167; A0AVG3: TSNARE1; NbExp=3; IntAct=EBI-349105, EBI-12003468;
CC P63167; Q8N1W2: ZNF710; NbExp=4; IntAct=EBI-349105, EBI-18096911;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:20921139}. Nucleus
CC {ECO:0000269|PubMed:15891768}. Mitochondrion
CC {ECO:0000269|PubMed:18084006}. Note=Upon induction of apoptosis
CC translocates together with BCL2L11 to mitochondria.
CC {ECO:0000269|PubMed:18084006}.
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:8628263). Expressed in testis
CC (PubMed:22965910). {ECO:0000269|PubMed:22965910,
CC ECO:0000269|PubMed:8628263}.
CC -!- INDUCTION: Up-regulated by ATMIN, PAK1 and estrogen.
CC {ECO:0000269|PubMed:15891768, ECO:0000269|PubMed:22167198}.
CC -!- PTM: Phosphorylation at Ser-88 appears to control the dimer-monomer
CC transition. According to PubMed:15193260, it is phosphorylated at Ser-
CC 88 by PAK1, however, according to PubMed:18650427, the DYNLL1 dimer is
CC not accessible for PAK1 and the phosphorylation could not be
CC demonstrated in vitro. {ECO:0000269|PubMed:15193260}.
CC -!- SIMILARITY: Belongs to the dynein light chain family. {ECO:0000305}.
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DR EMBL; U32944; AAB04149.1; -; mRNA.
DR EMBL; CR407672; CAG28600.1; -; mRNA.
DR CCDS; CCDS9200.1; -.
DR RefSeq; NP_001032583.1; NM_001037494.1.
DR RefSeq; NP_001032584.1; NM_001037495.1.
DR RefSeq; NP_003737.1; NM_003746.2.
DR PDB; 1CMI; X-ray; 2.50 A; A/B=5-89.
DR PDB; 3ZKE; X-ray; 2.20 A; A/C/E/G/I/K=1-89.
DR PDB; 3ZKF; X-ray; 2.60 A; A/C/E/G/I/K=1-89.
DR PDB; 6GZJ; X-ray; 1.98 A; A=1-89.
DR PDB; 6GZL; X-ray; 1.95 A; A=1-89.
DR PDB; 6RLB; EM; 4.50 A; I/J/K/L/M/N=1-89.
DR PDB; 6SC2; EM; 3.90 A; I/J/K/L/M/N=1-89.
DR PDB; 7D35; X-ray; 2.40 A; A=1-89.
DR PDBsum; 1CMI; -.
DR PDBsum; 3ZKE; -.
DR PDBsum; 3ZKF; -.
DR PDBsum; 6GZJ; -.
DR PDBsum; 6GZL; -.
DR PDBsum; 6RLB; -.
DR PDBsum; 6SC2; -.
DR PDBsum; 7D35; -.
DR AlphaFoldDB; P63167; -.
DR BMRB; P63167; -.
DR SMR; P63167; -.
DR BioGRID; 114206; 431.
DR ComplexPortal; CPX-5025; Cytoplasmic dynein complex, variant 1.
DR CORUM; P63167; -.
DR DIP; DIP-33150N; -.
DR IntAct; P63167; 230.
DR MINT; P63167; -.
DR STRING; 9606.ENSP00000376297; -.
DR GlyGen; P63167; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P63167; -.
DR MetOSite; P63167; -.
DR PhosphoSitePlus; P63167; -.
DR SwissPalm; P63167; -.
DR BioMuta; DYNLL1; -.
DR DMDM; 52783578; -.
DR EPD; P63167; -.
DR jPOST; P63167; -.
DR MassIVE; P63167; -.
DR PaxDb; P63167; -.
DR PeptideAtlas; P63167; -.
DR PRIDE; P63167; -.
DR ProteomicsDB; 57501; -.
DR TopDownProteomics; P63167; -.
DR Antibodypedia; 31481; 306 antibodies from 30 providers.
DR DNASU; 8655; -.
DR Ensembl; ENST00000242577.11; ENSP00000242577.6; ENSG00000088986.11.
DR Ensembl; ENST00000392508.2; ENSP00000376296.2; ENSG00000088986.11.
DR Ensembl; ENST00000392509.6; ENSP00000376297.2; ENSG00000088986.11.
DR Ensembl; ENST00000548342.5; ENSP00000447907.1; ENSG00000088986.11.
DR Ensembl; ENST00000549989.1; ENSP00000446614.1; ENSG00000088986.11.
DR GeneID; 8655; -.
DR KEGG; hsa:8655; -.
DR MANE-Select; ENST00000242577.11; ENSP00000242577.6; NM_003746.3; NP_003737.1.
DR CTD; 8655; -.
DR DisGeNET; 8655; -.
DR GeneCards; DYNLL1; -.
DR HGNC; HGNC:15476; DYNLL1.
DR HPA; ENSG00000088986; Low tissue specificity.
DR MIM; 601562; gene.
DR neXtProt; NX_P63167; -.
DR OpenTargets; ENSG00000088986; -.
DR PharmGKB; PA134972261; -.
DR VEuPathDB; HostDB:ENSG00000088986; -.
DR eggNOG; KOG3430; Eukaryota.
DR GeneTree; ENSGT00390000000378; -.
DR HOGENOM; CLU_070944_4_0_1; -.
DR InParanoid; P63167; -.
DR OMA; KHSPTWH; -.
DR OrthoDB; 1520814at2759; -.
DR PhylomeDB; P63167; -.
DR TreeFam; TF300264; -.
DR PathwayCommons; P63167; -.
DR Reactome; R-HSA-111446; Activation of BIM and translocation to mitochondria.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-1632852; Macroautophagy.
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-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
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-8854518; AURKA Activation by TPX2.
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; P63167; -.
DR SIGNOR; P63167; -.
DR BioGRID-ORCS; 8655; 335 hits in 1064 CRISPR screens.
DR ChiTaRS; DYNLL1; human.
DR EvolutionaryTrace; P63167; -.
DR GeneWiki; DYNLL1; -.
DR GenomeRNAi; 8655; -.
DR Pharos; P63167; Tbio.
DR PRO; PR:P63167; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P63167; protein.
DR Bgee; ENSG00000088986; Expressed in prefrontal cortex and 206 other tissues.
DR ExpressionAtlas; P63167; baseline and differential.
DR Genevisible; P63167; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0005929; C:cilium; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030286; C:dynein complex; IPI:ComplexPortal.
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:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0035721; P:intraciliary retrograde transport; IBA:GO_Central.
DR GO; GO:0044458; P:motile cilium assembly; IBA:GO_Central.
DR GO; GO:0042326; P:negative regulation of phosphorylation; IDA:UniProtKB.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR Gene3D; 3.30.740.10; -; 1.
DR InterPro; IPR037177; DLC_sf.
DR InterPro; IPR019763; Dynein_light_1/2_CS.
DR InterPro; IPR001372; Dynein_light_chain_typ-1/2.
DR PANTHER; PTHR11886; PTHR11886; 1.
DR Pfam; PF01221; Dynein_light; 1.
DR SMART; SM01375; Dynein_light; 1.
DR SUPFAM; SSF54648; SSF54648; 1.
DR PROSITE; PS01239; DYNEIN_LIGHT_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Apoptosis; Cytoplasm; Cytoskeleton;
KW Dynein; Host-virus interaction; Isopeptide bond; Microtubule;
KW Mitochondrion; Motor protein; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Transport; Ubl conjugation.
FT CHAIN 1..89
FT /note="Dynein light chain 1, cytoplasmic"
FT /id="PRO_0000195125"
FT REGION 67..89
FT /note="Interaction with ESR1"
FT /evidence="ECO:0000269|PubMed:15891768"
FT MOD_RES 36
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15193260"
FT CROSSLNK 43
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 67
FT /note="T->A: Abolishes interaction with PAK1."
FT /evidence="ECO:0000269|PubMed:18650427"
FT MUTAGEN 88
FT /note="S->A: Abolishes growth factor-mediated
FT phosphorylation. Increases BCL2L11 protein level and
FT promotes apoptosis."
FT /evidence="ECO:0000269|PubMed:15193260,
FT ECO:0000269|PubMed:18084006"
FT MUTAGEN 88
FT /note="S->E: Abolishes homodimerization. Abolishes
FT interaction with BCL2L11 isoform 1 and isoform 2."
FT /evidence="ECO:0000269|PubMed:15193260,
FT ECO:0000269|PubMed:18084006"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:6GZL"
FT HELIX 15..31
FT /evidence="ECO:0007829|PDB:6GZL"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1CMI"
FT HELIX 35..50
FT /evidence="ECO:0007829|PDB:6GZL"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:6GZL"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:6GZL"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:6GZL"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:6GZL"
SQ SEQUENCE 89 AA; 10366 MW; F5E7647D092BEB3A CRC64;
MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY NPTWHCIVGR
NFGSYVTHET KHFIYFYLGQ VAILLFKSG
