DYL2_HUMAN
ID DYL2_HUMAN Reviewed; 89 AA.
AC Q96FJ2; B2R5B4;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Dynein light chain 2, cytoplasmic;
DE AltName: Full=8 kDa dynein light chain b;
DE Short=DLC8b;
DE AltName: Full=Dynein light chain LC8-type 2;
GN Name=DYNLL2; Synonyms=DLC2;
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].
RA Zhang H.L., Yu L., Yang J., Fu Q., Cui Y.Y., Zhao S.Y.;
RT "Cloning and sequencing of a novel human cDNA homologous to Rattus
RT norvegicus protein inhibitor of neuronal nitric oxide synthase (PIN)
RT mRNA.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 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 [6]
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 [7]
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 [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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 (By similarity). {ECO:0000250}.
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 which present 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 (By
CC similarity). The heavy chain homodimer serves as a scaffold for the
CC probable homodimeric assembly of the respective non-catalytic subunits
CC (By similarity). Dynein ICs and LICs bind directly to the HC dimer and
CC the LCs assemble on the IC dimer (By similarity). Interacts with
CC DYNC1I1 (By similarity). Interacts with BMF (By similarity). Component
CC of the myosin V motor complex (By similarity). Interacts with BCAS1 (By
CC similarity). Interacts with Basson/BSN (PubMed:19380881). Interacts
CC with AMBRA1 (via TQT motifs); tethering AMBRA1 to the cytoskeleton
CC (PubMed:20921139). {ECO:0000250|UniProtKB:Q78P75,
CC ECO:0000250|UniProtKB:Q9D0M5, ECO:0000269|PubMed:19380881,
CC ECO:0000269|PubMed:20921139}.
CC -!- INTERACTION:
CC Q96FJ2; Q96LC9: BMF; NbExp=3; IntAct=EBI-742371, EBI-3919268;
CC Q96FJ2; Q86WS4: C12orf40; NbExp=4; IntAct=EBI-742371, EBI-10286004;
CC Q96FJ2; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-742371, EBI-725606;
CC Q96FJ2; O96015: DNAL4; NbExp=6; IntAct=EBI-742371, EBI-742362;
CC Q96FJ2; Q6W0C5: DPPA3; NbExp=3; IntAct=EBI-742371, EBI-12082590;
CC Q96FJ2; Q6P1L5: FAM117B; NbExp=7; IntAct=EBI-742371, EBI-3893327;
CC Q96FJ2; P60520: GABARAPL2; NbExp=3; IntAct=EBI-742371, EBI-720116;
CC Q96FJ2; Q6NT76: HMBOX1; NbExp=4; IntAct=EBI-742371, EBI-2549423;
CC Q96FJ2; Q9NSC5: HOMER3; NbExp=4; IntAct=EBI-742371, EBI-748420;
CC Q96FJ2; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-742371, EBI-8638439;
CC Q96FJ2; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-742371, EBI-2556193;
CC Q96FJ2; P50222: MEOX2; NbExp=3; IntAct=EBI-742371, EBI-748397;
CC Q96FJ2; Q6PF18: MORN3; NbExp=4; IntAct=EBI-742371, EBI-9675802;
CC Q96FJ2; Q7L8S5: OTUD6A; NbExp=3; IntAct=EBI-742371, EBI-11960139;
CC Q96FJ2; P61925: PKIA; NbExp=3; IntAct=EBI-742371, EBI-2682139;
CC Q96FJ2; Q9Y2B9: PKIG; NbExp=3; IntAct=EBI-742371, EBI-1052231;
CC Q96FJ2; Q8IV61: RASGRP3; NbExp=3; IntAct=EBI-742371, EBI-1047876;
CC Q96FJ2; Q93073: SECISBP2L; NbExp=3; IntAct=EBI-742371, EBI-2805647;
CC Q96FJ2; O43236: SEPTIN4; NbExp=3; IntAct=EBI-742371, EBI-1047513;
CC Q96FJ2; P49901: SMCP; NbExp=3; IntAct=EBI-742371, EBI-750494;
CC Q96FJ2; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-742371, EBI-11959123;
CC Q96FJ2; Q9UKI8: TLK1; NbExp=4; IntAct=EBI-742371, EBI-740492;
CC Q96FJ2; P98170: XIAP; NbExp=3; IntAct=EBI-742371, EBI-517127;
CC Q96FJ2; Q86SH2: ZAR1; NbExp=3; IntAct=EBI-742371, EBI-18679381;
CC Q96FJ2; P0C206; Xeno; NbExp=4; IntAct=EBI-742371, EBI-9675596;
CC Q96FJ2; Q85601; Xeno; NbExp=3; IntAct=EBI-742371, EBI-9676175;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20921139}.
CC -!- SIMILARITY: Belongs to the dynein light chain family. {ECO:0000305}.
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DR EMBL; AF112997; AAP97230.1; -; mRNA.
DR EMBL; AK312125; BAG35061.1; -; mRNA.
DR EMBL; CH471109; EAW94484.1; -; Genomic_DNA.
DR EMBL; BC010744; AAH10744.1; -; mRNA.
DR CCDS; CCDS11601.1; -.
DR RefSeq; NP_542408.1; NM_080677.2.
DR PDB; 2XQQ; X-ray; 1.31 A; A/B/C/D=1-89.
DR PDB; 3P8M; X-ray; 2.90 A; A/B=1-89.
DR PDB; 4D07; X-ray; 1.85 A; A=1-89.
DR PDB; 7CNU; X-ray; 2.00 A; A/B/E=2-89.
DR PDBsum; 2XQQ; -.
DR PDBsum; 3P8M; -.
DR PDBsum; 4D07; -.
DR PDBsum; 7CNU; -.
DR AlphaFoldDB; Q96FJ2; -.
DR SMR; Q96FJ2; -.
DR BioGRID; 126680; 227.
DR CORUM; Q96FJ2; -.
DR IntAct; Q96FJ2; 87.
DR MINT; Q96FJ2; -.
DR STRING; 9606.ENSP00000477310; -.
DR iPTMnet; Q96FJ2; -.
DR PhosphoSitePlus; Q96FJ2; -.
DR BioMuta; DYNLL2; -.
DR DMDM; 56748850; -.
DR EPD; Q96FJ2; -.
DR jPOST; Q96FJ2; -.
DR MassIVE; Q96FJ2; -.
DR MaxQB; Q96FJ2; -.
DR PaxDb; Q96FJ2; -.
DR PeptideAtlas; Q96FJ2; -.
DR PRIDE; Q96FJ2; -.
DR ProteomicsDB; 76535; -.
DR TopDownProteomics; Q96FJ2; -.
DR Antibodypedia; 71353; 156 antibodies from 27 providers.
DR DNASU; 140735; -.
DR Ensembl; ENST00000579991.3; ENSP00000477310.1; ENSG00000264364.3.
DR GeneID; 140735; -.
DR KEGG; hsa:140735; -.
DR MANE-Select; ENST00000579991.3; ENSP00000477310.1; NM_080677.3; NP_542408.1.
DR UCSC; uc010wnn.2; human.
DR CTD; 140735; -.
DR DisGeNET; 140735; -.
DR GeneCards; DYNLL2; -.
DR HGNC; HGNC:24596; DYNLL2.
DR HPA; ENSG00000264364; Low tissue specificity.
DR MIM; 608942; gene.
DR neXtProt; NX_Q96FJ2; -.
DR OpenTargets; ENSG00000264364; -.
DR PharmGKB; PA142671920; -.
DR VEuPathDB; HostDB:ENSG00000264364; -.
DR eggNOG; KOG3430; Eukaryota.
DR GeneTree; ENSGT00390000000378; -.
DR HOGENOM; CLU_070944_4_0_1; -.
DR InParanoid; Q96FJ2; -.
DR OMA; RHGATWH; -.
DR OrthoDB; 1520814at2759; -.
DR PhylomeDB; Q96FJ2; -.
DR TreeFam; TF300264; -.
DR PathwayCommons; Q96FJ2; -.
DR Reactome; R-HSA-139910; Activation of BMF 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-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
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; Q96FJ2; -.
DR SIGNOR; Q96FJ2; -.
DR BioGRID-ORCS; 140735; 20 hits in 1070 CRISPR screens.
DR ChiTaRS; DYNLL2; human.
DR EvolutionaryTrace; Q96FJ2; -.
DR GeneWiki; DYNLL2; -.
DR GenomeRNAi; 140735; -.
DR Pharos; Q96FJ2; Tbio.
DR PRO; PR:Q96FJ2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96FJ2; protein.
DR Bgee; ENSG00000264364; Expressed in medial globus pallidus and 197 other tissues.
DR Genevisible; Q96FJ2; HS.
DR GO; GO:0097731; C:9+0 non-motile cilium; IDA:GO_Central.
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:0005868; C:cytoplasmic dynein complex; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031475; C:myosin V complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
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; Cytoplasm; Cytoskeleton; Dynein; Microtubule; Motor protein;
KW Reference proteome; Transport.
FT CHAIN 1..89
FT /note="Dynein light chain 2, cytoplasmic"
FT /id="PRO_0000195132"
FT SITE 41
FT /note="Interaction with myosin V motor complex"
FT /evidence="ECO:0000250"
FT TURN 1..3
FT /evidence="ECO:0007829|PDB:4D07"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:2XQQ"
FT HELIX 15..31
FT /evidence="ECO:0007829|PDB:2XQQ"
FT HELIX 35..50
FT /evidence="ECO:0007829|PDB:2XQQ"
FT STRAND 54..66
FT /evidence="ECO:0007829|PDB:2XQQ"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:2XQQ"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:2XQQ"
SQ SEQUENCE 89 AA; 10350 MW; 45364D32C0077F8E CRC64;
MSDRKAVIKN ADMSEDMQQD AVDCATQAME KYNIEKDIAA YIKKEFDKKY NPTWHCIVGR
NFGSYVTHET KHFIYFYLGQ VAILLFKSG
