Sequence in raw or FASTA format:
DYNC1H1 dynein, cytoplasmic 1, heavy chain 1 [
Homo sapiens (human)]
Gene Symbol DYNC1H1
Entrez Gene ID
Full Name dynein, cytoplasmic 1, heavy chain 1
Synonyms DHC1, DHC1a, DNCH1, DNCL, DNECL, DYHC, Dnchc1, HL-3, SMALED1, p22
General protein information
cytoplasmic dynein 1 heavy chain 1
cytoplasmic dynein 1 heavy chain 1
dynein heavy chain, cytosolic
dynein, cytoplasmic, heavy polypeptide 1
Gene Type protein-coding
Homo sapiens (human)
Chromosome:14 Map Location:14q32
Summary Dyneins are a group of microtubule-activated ATPases that function as molecular motors. They are divided into two subgroups of axonemal and cytoplasmic dyneins. The cytoplasmic dyneins function in intracellular motility, including retrograde axonal transport, protein sorting, organelle movement, and spindle dynamics. Molecules of conventional cytoplasmic dynein are comprised of 2 heavy chain polypeptides and a number of intermediate and light chains.This gene encodes a member of the cytoplasmic dynein heavy chain family. [provided by RefSeq, Oct 2008].
Pathway Interaction Database
lis1pathway Lissencephaly gene (LIS1) in neuronal migration and development
Related articles in PubMed Systematic dissection of dynein regulators in mitosis. Raaijmakers JA, et al. J Cell Biol, 2013 Apr 15. PMID 23589491. DCNL1 functions as a substrate sensor and activator of cullin 2-RING ligase. Heir P, et al. Mol Cell Biol, 2013 Apr. PMID 23401859. A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity. Cloutier P, et al. PLoS Genet, 2013. PMID 23349634. Reconstitution of the human cytoplasmic dynein complex. Trokter M, et al. Proc Natl Acad Sci U S A, 2012 Dec 18. PMID 23213255. Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass. Povlsen LK, et al. Nat Cell Biol, 2012 Oct. PMID 23000965. See all (97) citations in PubMed See citations in PubMed for homologs of this gene provided by HomoloGene
GeneRIFs: Gene References Into Functions
What's a GeneRIF?
Dynein forms distinct complexes requiring specific recruiters and activators to promote orderly progression through mitosis.
Title: Systematic dissection of dynein regulators in mitosis.
this study has demonstrated that the same DYNC1H1 mutation could cause spinal muscular atrophy as well as distal neuropathy, indicating pleotropic effects of the mutation.
Title: A DYNC1H1 mutation causes a dominant spinal muscular atrophy with lower extremity predominance.
LIS1 is required for dynein-mediated transport induced by membrane tethering of BICD2-N and LIS1 contributes to dynein accumulation at microtubule plus ends and BICD2-positive cellular structures.
Title: BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment to cellular structures.
analysis of reconstitution of the human cytoplasmic dynein complex
Title: Reconstitution of the human cytoplasmic dynein complex.
study demonstrates that mutations in the tail domain of the heavy chain of cytoplasmic dynein (DYNC1H1) cause spinal muscular atrophy and provide experimental evidence that a DYNC1H1 mutation disrupts dynein complex assembly and function
Title: Mutations in the tail domain of DYNC1H1 cause dominant spinal muscular atrophy.
Mutations in DYNC1H1 can lead to a broad phenotypic spectrum, confirming the importance of DYNC1H1 in both central and peripheral neuronal functions.
Title: Mutations in DYNC1H1 cause severe intellectual disability with neuronal migration defects.
Studies indicate that binding of dynactin, LIS1 and NudEL regulate cytoplasmic dynein motor activity.
Title: Multiple modes of cytoplasmic dynein regulation.
Exome sequencing of three affected individuals separated by eight meioses identified a single shared novel heterozygous variant, c.917A>G, in DYNC1H1, which encodes the cytoplasmic dynein heavy chain 1.
Title: Exome sequencing identifies a DYNC1H1 mutation in a large pedigree with dominant axonal Charcot-Marie-Tooth disease.
In an in vitro MT gliding assay, both dynein-1 and dynein-2 showed minus-end-directed motor activities.
Title: Recombinant human cytoplasmic dynein heavy chain 1 and 2: observation of dynein-2 motor activity in vitro.
these results suggest that complexes of dynein, Lis1 and CLIP-170 crosslink and slide microtubules within the spindle, thereby producing an inward force that pulls centrosomes together.
Title: Dynein, Lis1 and CLIP-170 counteract Eg5-dependent centrosome separation during bipolar spindle assembly.
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