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FLASH GENE
Symbol DYNLL1 contributors: mct/npt/pgu - updated : 03-05-2010
HGNC name dynein, light chain, LC8-type 1
HGNC id 15476
Location 12q24.31      Physical location : 120.907.659 - 120.936.297
Synonym name
  • dynein, cytoplasmic, light chain (protein inhibitor of neuronal NOS)
  • protein inhibitor of neuronal nitric oxide synthase
  • dynein, cytoplasmic, light polypeptide 1
    • Synonym symbol(s) LC8, PIN, DaLC1, DLC8, hdlc1, LC8a, DNCL1, DNCLC1, DLC1, MGC126137, MGC126138
    DNA
    TYPE functioning gene
    STRUCTURE 28.64 kb     3 Exon(s)
    MAPPING cloned Y linked N status provisional
    RNA
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    3 - 820 - 89 - 2008 18579519
    3 - 747 - 89 - 2008 18579519
    3 - 733 - 89 - 2008 18579519
    EXPRESSION
    Type ubiquitous
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Digestiveliver   highly
     stomach   highly
    Endocrinepancreas   highly
    Urinarybladder   highly
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
  • three potential C2H2 zinc finger structures
  • IKAROS-like motif
  • at least 18 SQ/TQ motifs in its sequence
    • HOMOLOGY
    Homologene
    FAMILY
  • dynein light chain family
    • CATEGORY motor/contractile
    SUBCELLULAR LOCALIZATION     plasma membrane
        intracellular
    intracellular,cytoplasm,cytosolic
    intracellular,cytoplasm,cytoskeleton,microtubule
    intracellular,nucleus
    basic FUNCTION
  • dynein light chain, may be involved in some aspects of dynein-related intracellular transport and motility
  • may play a role in changing or maintaining the spatial distribution of cytoskeletal structures
  • involved in fundamental processes, including retrograde vesicular trafficking, ciliary/flagellar motility, and cell division
  • having crucial regulatory roles, in various systems potentially due to its ability to promote dimerization of partially disordered proteins
  • DYNLL1, DYNLL2 are required for outer arm dynein motor function
  • is not required for NEK9 oligomerization
  • is not absolutely required for NEK9 autoactivation, but binding to NEK9 increases the efficiency of this process
  • acts as a hub protein in several cellular events having functions unrelated to cargo transport, for instance in nuclear transport, apoptosis and cancer development
  • DYNLL1 binding to certain cellular targets interferes with ATM/ATR phosphorylation and vice versa
    • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
  • essential component of the microtubule-based molecular motor dynein
    • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • with TRPS1(suppression of transcriptional repression activity of TRPS1)
  • binding with BMF and BCL2L11
  • also interacts with proteins that are not clearly connected with dynein or microtubule-based transport, including some with roles in apoptosis, viral pathogenesis, enzyme regulation, and kidney developmen
  • binds CHUK in a redox-dependent manner and thereby prevents its phosphorylation by IKK (TXNDC17 contributes to this inhibitory activity by maintaining DYNLL1 in a reduced state)
  • interacting partner of GNB2L1 (GNB2L1 formed a complex with DYNLL1 and BCL2L11, in the presence of apoptotic agents)
  • cooperate with PAK1 in malignant transformation of breast cancer cells (facilitates nuclear import of PAK1, function indispensable during vertebrate development)
  • POLR2M is a DYNLL1 binding partner
  • NEK9 binds to DYNLL/LC8, a highly conserved protein originally described as a component of the dynein complex (binding interferes with the interaction of NEK9 with its downstream partner NEK6 as well as with NEK6 activation, thus controlling both processes)
  • ATMIN is a DYNLL1-binding partner (DYNLL1 binds to multiple SQ/TQ motifs present in the C-terminal domain of ATMIN)
  • bind to proteins with KXTQT motifs
    • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    ANIMAL & CELL MODELS