Gene DYNC1H1 - ENSG00000197102 | NCBI Gene ID: 1778

Details for: DYNC1H1

Gene ID: 1778

Symbol: DYNC1H1

Ensembl ID: ENSG00000197102

Description: dynein cytoplasmic 1 heavy chain 1

Associated with

Adaptive immune system
(R-HSA-1280218)
Aggrephagy
(R-HSA-9646399)
Amplification of signal from the kinetochores
(R-HSA-141424)
Amplification of signal from unattached kinetochores via a mad2 inhibitory signal
(R-HSA-141444)
Anchoring of the basal body to the plasma membrane
(R-HSA-5620912)
Asparagine n-linked glycosylation
(R-HSA-446203)
Aurka activation by tpx2
(R-HSA-8854518)
Autophagy
(R-HSA-9612973)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
Cell cycle checkpoints
(R-HSA-69620)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Centrosome maturation
(R-HSA-380287)
Cilium assembly
(R-HSA-5617833)
Copi-independent golgi-to-er retrograde traffic
(R-HSA-6811436)
Copi-mediated anterograde transport
(R-HSA-6807878)
Disease
(R-HSA-1643685)
Eml4 and nudc in mitotic spindle formation
(R-HSA-9648025)
Er to golgi anterograde transport
(R-HSA-199977)
G2/m transition
(R-HSA-69275)
Golgi-to-er retrograde transport
(R-HSA-8856688)
Hcmv early events
(R-HSA-9609690)
Hcmv infection
(R-HSA-9609646)
Hsp90 chaperone cycle for steroid hormone receptors (shr) in the presence of ligand
(R-HSA-3371497)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Innate immune system
(R-HSA-168249)
Intra-golgi and retrograde golgi-to-er traffic
(R-HSA-6811442)
Loss of nlp from mitotic centrosomes
(R-HSA-380259)
Loss of proteins required for interphase microtubule organization from the centrosome
(R-HSA-380284)
Macroautophagy
(R-HSA-1632852)
Membrane trafficking
(R-HSA-199991)
Metabolism of proteins
(R-HSA-392499)
Mhc class ii antigen presentation
(R-HSA-2132295)
Mitotic anaphase
(R-HSA-68882)
Mitotic g2-g2/m phases
(R-HSA-453274)
Mitotic metaphase and anaphase
(R-HSA-2555396)
Mitotic prometaphase
(R-HSA-68877)
Mitotic spindle checkpoint
(R-HSA-69618)
M phase
(R-HSA-68886)
Neutrophil degranulation
(R-HSA-6798695)
Organelle biogenesis and maintenance
(R-HSA-1852241)
Post-translational protein modification
(R-HSA-597592)
Recruitment of mitotic centrosome proteins and complexes
(R-HSA-380270)
Recruitment of numa to mitotic centrosomes
(R-HSA-380320)
Regulation of plk1 activity at g2/m transition
(R-HSA-2565942)
Resolution of sister chromatid cohesion
(R-HSA-2500257)
Rho gtpase effectors
(R-HSA-195258)
Rho gtpases activate formins
(R-HSA-5663220)
Selective autophagy
(R-HSA-9663891)
Separation of sister chromatids
(R-HSA-2467813)
Signaling by rho gtpases
(R-HSA-194315)
Signaling by rho gtpases, miro gtpases and rhobtb3
(R-HSA-9716542)
Signal transduction
(R-HSA-162582)
Transport to the golgi and subsequent modification
(R-HSA-948021)
Vesicle-mediated transport
(R-HSA-5653656)
Viral infection pathways
(R-HSA-9824446)
Atp binding
(GO:0005524)
Atp hydrolysis activity
(GO:0016887)
Axon cytoplasm
(GO:1904115)
Azurophil granule lumen
(GO:0035578)
Cell cortex
(GO:0005938)
Cell division
(GO:0051301)
Centrosome
(GO:0005813)
Cytoplasmic dynein complex
(GO:0005868)
Cytoplasmic microtubule
(GO:0005881)
Cytoplasmic microtubule organization
(GO:0031122)
Cytosol
(GO:0005829)
Dynein complex
(GO:0030286)
Dynein intermediate chain binding
(GO:0045505)
Dynein light intermediate chain binding
(GO:0051959)
Establishment of spindle localization
(GO:0051293)
Extracellular exosome
(GO:0070062)
Extracellular region
(GO:0005576)
Filopodium
(GO:0030175)
Membrane
(GO:0016020)
Microtubule
(GO:0005874)
Minus-end-directed microtubule motor activity
(GO:0008569)
Mitotic spindle organization
(GO:0007052)
Nuclear migration
(GO:0007097)
P-body assembly
(GO:0033962)
Positive regulation of cold-induced thermogenesis
(GO:0120162)
Positive regulation of intracellular transport
(GO:0032388)
Positive regulation of spindle assembly
(GO:1905832)
Protein binding
(GO:0005515)
Regulation of metaphase plate congression
(GO:0090235)
Regulation of mitotic spindle organization
(GO:0060236)
Retrograde axonal transport
(GO:0008090)
Rna binding
(GO:0003723)
Stress granule assembly
(GO:0034063)

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: GABAergic neuron (CL0000617)
Fold Change: 3.5
Marker Score: 14600
Cell Name: inhibitory interneuron (CL0000498)
Fold Change: 2.78
Marker Score: 12853
Cell Name: neuron associated cell (sensu Vertebrata) (CL0000123)
Fold Change: 2.57
Marker Score: 13485
Cell Name: nasal mucosa goblet cell (CL0002480)
Fold Change: 2.51
Marker Score: 1678
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 2.43
Marker Score: 21338
Cell Name: Purkinje cell (CL0000121)
Fold Change: 2.34
Marker Score: 79078
Cell Name: sst GABAergic cortical interneuron (CL4023017)
Fold Change: 2.28
Marker Score: 45293
Cell Name: OFF retinal ganglion cell (CL4023033)
Fold Change: 2.25
Marker Score: 942
Cell Name: vip GABAergic cortical interneuron (CL4023016)
Fold Change: 2.24
Marker Score: 85082
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 2.23
Marker Score: 1307
Cell Name: corneal endothelial cell (CL0000132)
Fold Change: 2.22
Marker Score: 1293
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 2.21
Marker Score: 75355
Cell Name: sncg GABAergic cortical interneuron (CL4023015)
Fold Change: 2.19
Marker Score: 16794
Cell Name: lamp5 GABAergic cortical interneuron (CL4023011)
Fold Change: 2.19
Marker Score: 32699
Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
Fold Change: 2.16
Marker Score: 79512
Cell Name: chandelier pvalb GABAergic cortical interneuron (CL4023036)
Fold Change: 2.13
Marker Score: 8849
Cell Name: basal cell of epithelium of trachea (CL1000348)
Fold Change: 2.13
Marker Score: 15879
Cell Name: ciliated cell (CL0000064)
Fold Change: 2.13
Marker Score: 7313
Cell Name: astrocyte of the cerebral cortex (CL0002605)
Fold Change: 2.02
Marker Score: 43205
Cell Name: pyramidal neuron (CL0000598)
Fold Change: 2.02
Marker Score: 3399
Cell Name: skeletal muscle satellite stem cell (CL0008011)
Fold Change: 2.02
Marker Score: 2154
Cell Name: myoepithelial cell of mammary gland (CL0002324)
Fold Change: 2.01
Marker Score: 9864
Cell Name: near-projecting glutamatergic cortical neuron (CL4023012)
Fold Change: 2.01
Marker Score: 18887
Cell Name: caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 2
Marker Score: 7722
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: 1.99
Marker Score: 2096
Cell Name: primary sensory neuron (sensu Teleostei) (CL0000531)
Fold Change: 1.98
Marker Score: 666
Cell Name: vascular leptomeningeal cell (CL4023051)
Fold Change: 1.98
Marker Score: 2274
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 1.97
Marker Score: 121433
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: 1.97
Marker Score: 20377
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 1.97
Marker Score: 2903
Cell Name: brainstem motor neuron (CL2000047)
Fold Change: 1.96
Marker Score: 1140
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 1.96
Marker Score: 109726
Cell Name: luminal epithelial cell of mammary gland (CL0002326)
Fold Change: 1.91
Marker Score: 3387
Cell Name: renal interstitial pericyte (CL1001318)
Fold Change: 1.9
Marker Score: 1813
Cell Name: duct epithelial cell (CL0000068)
Fold Change: 1.88
Marker Score: 878
Cell Name: cerebellar granule cell precursor (CL0002362)
Fold Change: 1.87
Marker Score: 1050
Cell Name: Unknown (CL0002371)
Fold Change: 1.83
Marker Score: 1946
Cell Name: CNS interneuron (CL0000402)
Fold Change: 1.82
Marker Score: 876
Cell Name: basal cell (CL0000646)
Fold Change: 1.82
Marker Score: 2349
Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
Fold Change: 1.82
Marker Score: 17287
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 1.82
Marker Score: 434
Cell Name: CD8-positive, alpha-beta memory T cell, CD45RO-positive (CL0001203)
Fold Change: 1.81
Marker Score: 5090
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 1.81
Marker Score: 7593
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 1.81
Marker Score: 2186
Cell Name: neuron (CL0000540)
Fold Change: 1.81
Marker Score: 7354
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: 1.8
Marker Score: 11693
Cell Name: stellate neuron (CL0000122)
Fold Change: 1.8
Marker Score: 9654
Cell Name: granulosa cell (CL0000501)
Fold Change: 1.8
Marker Score: 18077
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 1.79
Marker Score: 690
Cell Name: CD8-positive, alpha-beta cytokine secreting effector T cell (CL0000908)
Fold Change: 1.79
Marker Score: 774
Cell Name: L6b glutamatergic cortical neuron (CL4023038)
Fold Change: 1.78
Marker Score: 15327
Cell Name: podocyte (CL0000653)
Fold Change: 1.77
Marker Score: 653
Cell Name: cerebral cortex endothelial cell (CL1001602)
Fold Change: 1.77
Marker Score: 1054
Cell Name: Sertoli cell (CL0000216)
Fold Change: 1.75
Marker Score: 10404
Cell Name: squamous epithelial cell (CL0000076)
Fold Change: 1.75
Marker Score: 1194
Cell Name: keratocyte (CL0002363)
Fold Change: 1.74
Marker Score: 401
Cell Name: astrocyte (CL0000127)
Fold Change: 1.74
Marker Score: 1507
Cell Name: adventitial cell (CL0002503)
Fold Change: 1.73
Marker Score: 427
Cell Name: ON retinal ganglion cell (CL4023032)
Fold Change: 1.73
Marker Score: 472
Cell Name: ciliated columnar cell of tracheobronchial tree (CL0002145)
Fold Change: 1.73
Marker Score: 14993.5
Cell Name: melanocyte (CL0000148)
Fold Change: 1.73
Marker Score: 699
Cell Name: early pro-B cell (CL0002046)
Fold Change: 1.72
Marker Score: 17425
Cell Name: peripheral nervous system neuron (CL2000032)
Fold Change: 1.72
Marker Score: 1929.5
Cell Name: type EC enteroendocrine cell (CL0000577)
Fold Change: 1.72
Marker Score: 1618
Cell Name: cortical thymic epithelial cell (CL0002364)
Fold Change: 1.71
Marker Score: 6347
Cell Name: fibroblast of breast (CL4006000)
Fold Change: 1.71
Marker Score: 973
Cell Name: mononuclear phagocyte (CL0000113)
Fold Change: 1.7
Marker Score: 1708
Cell Name: neuronal brush cell (CL0000555)
Fold Change: 1.7
Marker Score: 5689
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: 1.67
Marker Score: 1738
Cell Name: type I pneumocyte (CL0002062)
Fold Change: 1.67
Marker Score: 2010
Cell Name: inhibitory motor neuron (CL0008015)
Fold Change: 1.67
Marker Score: 787
Cell Name: hematopoietic cell (CL0000988)
Fold Change: 1.66
Marker Score: 1106
Cell Name: neural cell (CL0002319)
Fold Change: 1.65
Marker Score: 795
Cell Name: corneal epithelial cell (CL0000575)
Fold Change: 1.64
Marker Score: 1814
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 1.64
Marker Score: 3741
Cell Name: kidney interstitial fibroblast (CL1000692)
Fold Change: 1.64
Marker Score: 3152.5
Cell Name: kidney loop of Henle thick ascending limb epithelial cell (CL1001106)
Fold Change: 1.64
Marker Score: 4390
Cell Name: kidney loop of Henle thin descending limb epithelial cell (CL1001111)
Fold Change: 1.64
Marker Score: 1765
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 1.63
Marker Score: 405
Cell Name: epicardial adipocyte (CL1000309)
Fold Change: 1.63
Marker Score: 790
Cell Name: common lymphoid progenitor (CL0000051)
Fold Change: 1.62
Marker Score: 1107
Cell Name: capillary endothelial cell (CL0002144)
Fold Change: 1.62
Marker Score: 1747
Cell Name: type A enteroendocrine cell (CL0002067)
Fold Change: 1.62
Marker Score: 654
Cell Name: Leydig cell (CL0000178)
Fold Change: 1.62
Marker Score: 1747
Cell Name: hepatocyte (CL0000182)
Fold Change: 1.62
Marker Score: 1104.5
Cell Name: stromal cell (CL0000499)
Fold Change: 1.61
Marker Score: 1890
Cell Name: GABAergic amacrine cell (CL4030027)
Fold Change: 1.61
Marker Score: 3278
Cell Name: endothelial cell (CL0000115)
Fold Change: 1.6
Marker Score: 1434
Cell Name: Unknown (CL0000548)
Fold Change: 1.6
Marker Score: 1164
Cell Name: male germ cell (CL0000015)
Fold Change: 1.6
Marker Score: 460
Cell Name: Bergmann glial cell (CL0000644)
Fold Change: 1.59
Marker Score: 650
Cell Name: preosteoblast (CL0007010)
Fold Change: 1.59
Marker Score: 451
Cell Name: motor neuron (CL0000100)
Fold Change: 1.58
Marker Score: 940
Cell Name: neural progenitor cell (CL0011020)
Fold Change: 1.58
Marker Score: 6126
Cell Name: P/D1 enteroendocrine cell (CL0002268)
Fold Change: 1.58
Marker Score: 589
Cell Name: ependymal cell (CL0000065)
Fold Change: 1.58
Marker Score: 551
Cell Name: mature gamma-delta T cell (CL0000800)
Fold Change: 1.58
Marker Score: 4974.5
Cell Name: Schwann cell (CL0002573)
Fold Change: 1.57
Marker Score: 546
Cell Name: anterior lens cell (CL0002223)
Fold Change: 1.57
Marker Score: 2116
Cell Name: type I NK T cell (CL0000921)
Fold Change: 1.57
Marker Score: 1232

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## Summary DYNC1H1 is a protein that is involved in the regulation of the cell cycle and the maintenance of cellular homeostasis. It is a key component of the mitotic spindle apparatus, which is responsible for the proper segregation of chromosomes during cell division. DYNC1H1 is also involved in the regulation of autophagy, a process by which cells degrade and recycle their own components. ## Key characteristics * DYNC1H1 is a protein of the dynein family, which are a large family of proteins that are involved in the transport of organelles and molecules within cells. * It is a cytoplasmic protein that is found in all eukaryotic cells. * It is a highly conserved protein, with a sequence that is similar in mammals, birds, and reptiles. * It is a multi-functional protein that has been shown to have a variety of roles in cell cycle regulation, autophagy, and other cellular processes. ## Pathways and functions * **Mitotic spindle apparatus:** DYNC1H1 is a key component of the mitotic spindle apparatus, which is responsible for the proper segregation of chromosomes during cell division. It is involved in the formation of the bipolar spindle fibers, which are responsible for pulling the chromosomes apart. * **Autophagy:** DYNC1H1 is also involved in the regulation of autophagy, a process by which cells degrade and recycle their own components. It is a key regulator of autophagy, and its inhibition can lead to the accumulation of damaged proteins and organelles, which can lead to cell death. * **Cell cycle checkpoints:** DYNC1H1 is involved in the regulation of cell cycle checkpoints, which are mechanisms that prevent cells from dividing when they are not properly ready. It is a key component of the G1/S and G2/M checkpoints, which are the two main checkpoints of the cell cycle. ## Clinical significance DYNC1H1 is a gene that is involved in a number of human diseases. Mutations in DYNC1H1 have been linked to a number of neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis. These diseases are characterized by the accumulation of abnormal protein aggregates in the brain. DYNC1H1 is a key component of the mitotic spindle apparatus, and its mutations can lead to the formation of abnormal protein aggregates that are associated with these diseases. DYNC1H1 is a promising target for the treatment of neurodegenerative diseases. By targeting DYNC1H1, it may be possible to inhibit the formation of protein aggregates and prevent the development of neurodegenerative diseases.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Cytoplasmic dynein 1 heavy chain 1

Genular Protein ID: 2796938496

Symbol: DYHC1_HUMAN

Name: Cytoplasmic dynein 1 heavy chain 1

UniProtKB Accession Codes:

Q14204 B0I1R0 Q6DKQ7 Q8WU28 Q92814 Q9Y4G5

Database IDs:

Citations:

PubMed ID: 9205841

Title: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro.

PubMed ID: 9205841

DOI: 10.1093/dnares/4.2.141

PubMed ID: 8666668

Title: Mammalian cells express three distinct dynein heavy chains that are localized to different cytoplasmic organelles.

PubMed ID: 8666668

DOI: 10.1083/jcb.133.4.831

PubMed ID: 8227145

Title: Cytoplasmic dynein plays a role in mammalian mitotic spindle formation.

PubMed ID: 8227145

DOI: 10.1083/jcb.123.4.849

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 14654843

Title: Proteomic characterization of the human centrosome by protein correlation profiling.

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 27462074

Title: Nuclear mitotic apparatus (NuMA) interacts with and regulates astrin at the mitotic spindle.

PubMed ID: 27462074

DOI: 10.1074/jbc.m116.724831

PubMed ID: 31092558

Title: Rab46 integrates Ca2+ and histamine signaling to regulate selective cargo release from Weibel-Palade bodies.

PubMed ID: 31092558

DOI: 10.1083/jcb.201810118

PubMed ID: 29420470

Title: Cryo-EM shows how dynactin recruits two dyneins for faster movement.

PubMed ID: 29420470

DOI: 10.1038/nature25462

PubMed ID: 36071160

Title: Structure of dynein-dynactin on microtubules shows tandem adaptor binding.

PubMed ID: 36071160

DOI: 10.1038/s41586-022-05186-y

PubMed ID: 21076407

Title: A de novo paradigm for mental retardation.

PubMed ID: 21076407

DOI: 10.1038/ng.712

PubMed ID: 21820100

Title: Exome sequencing identifies a DYNC1H1 mutation in a large pedigree with dominant axonal Charcot-Marie-Tooth disease.

PubMed ID: 21820100

DOI: 10.1016/j.ajhg.2011.07.002

PubMed ID: 22368300

Title: Mutations in DYNC1H1 cause severe intellectual disability with neuronal migration defects.

PubMed ID: 22368300

DOI: 10.1136/jmedgenet-2011-100542

PubMed ID: 22847149

Title: A DYNC1H1 mutation causes a dominant spinal muscular atrophy with lower extremity predominance.

PubMed ID: 22847149

DOI: 10.1007/s10048-012-0337-6

PubMed ID: 22459677

Title: Mutations in the tail domain of DYNC1H1 cause dominant spinal muscular atrophy.

PubMed ID: 22459677

DOI: 10.1212/wnl.0b013e3182556c05

PubMed ID: 23033978

Title: Diagnostic exome sequencing in persons with severe intellectual disability.

PubMed ID: 23033978

DOI: 10.1056/nejmoa1206524

PubMed ID: 23603762

Title: Mutations in TUBG1, DYNC1H1, KIF5C and KIF2A cause malformations of cortical development and microcephaly.

PubMed ID: 23603762

DOI: 10.1038/ng.2613

PubMed ID: 25512093

Title: Novel mutations in the DYNC1H1 tail domain refine the genetic and clinical spectrum of dyneinopathies.

PubMed ID: 25512093

DOI: 10.1002/humu.22744

PubMed ID: 24307404

Title: Novel dynein DYNC1H1 neck and motor domain mutations link distal spinal muscular atrophy and abnormal cortical development.

PubMed ID: 24307404

DOI: 10.1002/humu.22491

PubMed ID: 25484024

Title: Exome Sequencing Identifies DYNC1H1 Variant Associated With Vertebral Abnormality and Spinal Muscular Atrophy With Lower Extremity Predominance.

PubMed ID: 25484024

DOI: 10.1016/j.pediatrneurol.2014.09.003

PubMed ID: 26846447

Title: Identification of a de novo DYNC1H1 mutation via WES according to published guidelines.

PubMed ID: 26846447

DOI: 10.1038/srep20423

PubMed ID: 28193117

Title: Exome Sequencing Identifies De Novo DYNC1H1 Mutations Associated With Distal Spinal Muscular Atrophy and Malformations of Cortical Development.

PubMed ID: 28193117

DOI: 10.1177/0883073816683083

Sequence Information:

Length: 4646
Mass: 532408
Checksum: D4D4E15DFBDE4797
Sequence:

MSEPGGGGGE DGSAGLEVSA VQNVADVSVL QKHLRKLVPL LLEDGGEAPA ALEAALEEKS 
ALEQMRKFLS DPQVHTVLVE RSTLKEDVGD EGEEEKEFIS YNINIDIHYG VKSNSLAFIK 
RTPVIDADKP VSSQLRVLTL SEDSPYETLH SFISNAVAPF FKSYIRESGK ADRDGDKMAP 
SVEKKIAELE MGLLHLQQNI EIPEISLPIH PMITNVAKQC YERGEKPKVT DFGDKVEDPT 
FLNQLQSGVN RWIREIQKVT KLDRDPASGT ALQEISFWLN LERALYRIQE KRESPEVLLT 
LDILKHGKRF HATVSFDTDT GLKQALETVN DYNPLMKDFP LNDLLSATEL DKIRQALVAI 
FTHLRKIRNT KYPIQRALRL VEAISRDLSS QLLKVLGTRK LMHVAYEEFE KVMVACFEVF 
QTWDDEYEKL QVLLRDIVKR KREENLKMVW RINPAHRKLQ ARLDQMRKFR RQHEQLRAVI 
VRVLRPQVTA VAQQNQGEVP EPQDMKVAEV LFDAADANAI EEVNLAYENV KEVDGLDVSK 
EGTEAWEAAM KRYDERIDRV ETRITARLRD QLGTAKNANE MFRIFSRFNA LFVRPHIRGA 
IREYQTQLIQ RVKDDIESLH DKFKVQYPQS QACKMSHVRD LPPVSGSIIW AKQIDRQLTA 
YMKRVEDVLG KGWENHVEGQ KLKQDGDSFR MKLNTQEIFD DWARKVQQRN LGVSGRIFTI 
ESTRVRGRTG NVLKLKVNFL PEIITLSKEV RNLKWLGFRV PLAIVNKAHQ ANQLYPFAIS 
LIESVRTYER TCEKVEERNT ISLLVAGLKK EVQALIAEGI ALVWESYKLD PYVQRLAETV 
FNFQEKVDDL LIIEEKIDLE VRSLETCMYD HKTFSEILNR VQKAVDDLNL HSYSNLPIWV 
NKLDMEIERI LGVRLQAGLR AWTQVLLGQA EDKAEVDMDT DAPQVSHKPG GEPKIKNVVH 
ELRITNQVIY LNPPIEECRY KLYQEMFAWK MVVLSLPRIQ SQRYQVGVHY ELTEEEKFYR 
NALTRMPDGP VALEESYSAV MGIVSEVEQY VKVWLQYQCL WDMQAENIYN RLGEDLNKWQ 
ALLVQIRKAR GTFDNAETKK EFGPVVIDYG KVQSKVNLKY DSWHKEVLSK FGQMLGSNMT 
EFHSQISKSR QELEQHSVDT ASTSDAVTFI TYVQSLKRKI KQFEKQVELY RNGQRLLEKQ 
RFQFPPSWLY IDNIEGEWGA FNDIMRRKDS AIQQQVANLQ MKIVQEDRAV ESRTTDLLTD 
WEKTKPVTGN LRPEEALQAL TIYEGKFGRL KDDREKCAKA KEALELTDTG LLSGSEERVQ 
VALEELQDLK GVWSELSKVW EQIDQMKEQP WVSVQPRKLR QNLDALLNQL KSFPARLRQY 
ASYEFVQRLL KGYMKINMLV IELKSEALKD RHWKQLMKRL HVNWVVSELT LGQIWDVDLQ 
KNEAIVKDVL LVAQGEMALE EFLKQIREVW NTYELDLVNY QNKCRLIRGW DDLFNKVKEH 
INSVSAMKLS PYYKVFEEDA LSWEDKLNRI MALFDVWIDV QRRWVYLEGI FTGSADIKHL 
LPVETQRFQS ISTEFLALMK KVSKSPLVMD VLNIQGVQRS LERLADLLGK IQKALGEYLE 
RERSSFPRFY FVGDEDLLEI IGNSKNVAKL QKHFKKMFAG VSSIILNEDN SVVLGISSRE 
GEEVMFKTPV SITEHPKINE WLTLVEKEMR VTLAKLLAES VTEVEIFGKA TSIDPNTYIT 
WIDKYQAQLV VLSAQIAWSE NVETALSSMG GGGDAAPLHS VLSNVEVTLN VLADSVLMEQ 
PPLRRRKLEH LITELVHQRD VTRSLIKSKI DNAKSFEWLS QMRFYFDPKQ TDVLQQLSIQ 
MANAKFNYGF EYLGVQDKLV QTPLTDRCYL TMTQALEARL GGSPFGPAGT GKTESVKALG 
HQLGRFVLVF NCDETFDFQA MGRIFVGLCQ VGAWGCFDEF NRLEERMLSA VSQQVQCIQE 
ALREHSNPNY DKTSAPITCE LLNKQVKVSP DMAIFITMNP GYAGRSNLPD NLKKLFRSLA 
MTKPDRQLIA QVMLYSQGFR TAEVLANKIV PFFKLCDEQL SSQSHYDFGL RALKSVLVSA 
GNVKRERIQK IKREKEERGE AVDEGEIAEN LPEQEILIQS VCETMVPKLV AEDIPLLFSL 
LSDVFPGVQY HRGEMTALRE ELKKVCQEMY LTYGDGEEVG GMWVEKVLQL YQITQINHGL 
MMVGPSGSGK SMAWRVLLKA LERLEGVEGV AHIIDPKAIS KDHLYGTLDP NTREWTDGLF 
THVLRKIIDS VRGELQKRQW IVFDGDVDPE WVENLNSVLD DNKLLTLPNG ERLSLPPNVR 
IMFEVQDLKY ATLATVSRCG MVWFSEDVLS TDMIFNNFLA RLRSIPLDEG EDEAQRRRKG 
KEDEGEEAAS PMLQIQRDAA TIMQPYFTSN GLVTKALEHA FQLEHIMDLT RLRCLGSLFS 
MLHQACRNVA QYNANHPDFP MQIEQLERYI QRYLVYAILW SLSGDSRLKM RAELGEYIRR 
ITTVPLPTAP NIPIIDYEVS ISGEWSPWQA KVPQIEVETH KVAAPDVVVP TLDTVRHEAL 
LYTWLAEHKP LVLCGPPGSG KTMTLFSALR ALPDMEVVGL NFSSATTPEL LLKTFDHYCE 
YRRTPNGVVL APVQLGKWLV LFCDEINLPD MDKYGTQRVI SFIRQMVEHG GFYRTSDQTW 
VKLERIQFVG ACNPPTDPGR KPLSHRFLRH VPVVYVDYPG PASLTQIYGT FNRAMLRLIP 
SLRTYAEPLT AAMVEFYTMS QERFTQDTQP HYIYSPREMT RWVRGIFEAL RPLETLPVEG 
LIRIWAHEAL RLFQDRLVED EERRWTDENI DTVALKHFPN IDREKAMSRP ILYSNWLSKD 
YIPVDQEELR DYVKARLKVF YEEELDVPLV LFNEVLDHVL RIDRIFRQPQ GHLLLIGVSG 
AGKTTLSRFV AWMNGLSVYQ IKVHRKYTGE DFDEDLRTVL RRSGCKNEKI AFIMDESNVL 
DSGFLERMNT LLANGEVPGL FEGDEYATLM TQCKEGAQKE GLMLDSHEEL YKWFTSQVIR 
NLHVVFTMNP SSEGLKDRAA TSPALFNRCV LNWFGDWSTE ALYQVGKEFT SKMDLEKPNY 
IVPDYMPVVY DKLPQPPSHR EAIVNSCVFV HQTLHQANAR LAKRGGRTMA ITPRHYLDFI 
NHYANLFHEK RSELEEQQMH LNVGLRKIKE TVDQVEELRR DLRIKSQELE VKNAAANDKL 
KKMVKDQQEA EKKKVMSQEI QEQLHKQQEV IADKQMSVKE DLDKVEPAVI EAQNAVKSIK 
KQHLVEVRSM ANPPAAVKLA LESICLLLGE STTDWKQIRS IIMRENFIPT IVNFSAEEIS 
DAIREKMKKN YMSNPSYNYE IVNRASLACG PMVKWAIAQL NYADMLKRVE PLRNELQKLE 
DDAKDNQQKA NEVEQMIRDL EASIARYKEE YAVLISEAQA IKADLAAVEA KVNRSTALLK 
SLSAERERWE KTSETFKNQM STIAGDCLLS AAFIAYAGYF DQQMRQNLFT TWSHHLQQAN 
IQFRTDIART EYLSNADERL RWQASSLPAD DLCTENAIML KRFNRYPLII DPSGQATEFI 
MNEYKDRKIT RTSFLDDAFR KNLESALRFG NPLLVQDVES YDPVLNPVLN REVRRTGGRV 
LITLGDQDID LSPSFVIFLS TRDPTVEFPP DLCSRVTFVN FTVTRSSLQS QCLNEVLKAE 
RPDVDEKRSD LLKLQGEFQL RLRQLEKSLL QALNEVKGRI LDDDTIITTL ENLKREAAEV 
TRKVEETDIV MQEVETVSQQ YLPLSTACSS IYFTMESLKQ IHFLYQYSLQ FFLDIYHNVL 
YENPNLKGVT DHTQRLSIIT KDLFQVAFNR VARGMLHQDH ITFAMLLARI KLKGTVGEPT 
YDAEFQHFLR GNEIVLSAGS TPRIQGLTVE QAEAVVRLSC LPAFKDLIAK VQADEQFGIW 
LDSSSPEQTV PYLWSEETPA TPIGQAIHRL LLIQAFRPDR LLAMAHMFVS TNLGESFMSI 
MEQPLDLTHI VGTEVKPNTP VLMCSVPGYD ASGHVEDLAA EQNTQITSIA IGSAEGFNQA 
DKAINTAVKS GRWVMLKNVH LAPGWLMQLE KKLHSLQPHA CFRLFLTMEI NPKVPVNLLR 
AGRIFVFEPP PGVKANMLRT FSSIPVSRIC KSPNERARLY FLLAWFHAII QERLRYAPLG 
WSKKYEFGES DLRSACDTVD TWLDDTAKGR QNISPDKIPW SALKTLMAQS IYGGRVDNEF 
DQRLLNTFLE RLFTTRSFDS EFKLACKVDG HKDIQMPDGI RREEFVQWVE LLPDTQTPSW 
LGLPNNAERV LLTTQGVDMI SKMLKMQMLE DEDDLAYAET EKKTRTDSTS DGRPAWMRTL 
HTTASNWLHL IPQTLSHLKR TVENIKDPLF RFFEREVKMG AKLLQDVRQD LADVVQVCEG 
KKKQTNYLRT LINELVKGIL PRSWSHYTVP AGMTVIQWVS DFSERIKQLQ NISLAAASGG 
AKELKNIHVC LGGLFVPEAY ITATRQYVAQ ANSWSLEELC LEVNVTTSQG ATLDACSFGV 
TGLKLQGATC NNNKLSLSNA ISTALPLTQL RWVKQTNTEK KASVVTLPVY LNFTRADLIF 
TVDFEIATKE DPRSFYERGV AVLCTE

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. For the full schema, download it here.

Details for: DYNC1H1

Associated with

Cells (max top 100)

Other Information

Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. PubMed ID: 9205841

Mammalian cells express three distinct dynein heavy chains that are localized to different cytoplasmic organelles. PubMed ID: 8666668

Cytoplasmic dynein plays a role in mammalian mitotic spindle formation. PubMed ID: 8227145

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Proteomic characterization of the human centrosome by protein correlation profiling. PubMed ID: 14654843

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. PubMed ID: 22223895

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

Nuclear mitotic apparatus (NuMA) interacts with and regulates astrin at the mitotic spindle. PubMed ID: 27462074

Rab46 integrates Ca2+ and histamine signaling to regulate selective cargo release from Weibel-Palade bodies. PubMed ID: 31092558

Cryo-EM shows how dynactin recruits two dyneins for faster movement. PubMed ID: 29420470

Structure of dynein-dynactin on microtubules shows tandem adaptor binding. PubMed ID: 36071160

A de novo paradigm for mental retardation. PubMed ID: 21076407

Exome sequencing identifies a DYNC1H1 mutation in a large pedigree with dominant axonal Charcot-Marie-Tooth disease. PubMed ID: 21820100

Mutations in DYNC1H1 cause severe intellectual disability with neuronal migration defects. PubMed ID: 22368300

A DYNC1H1 mutation causes a dominant spinal muscular atrophy with lower extremity predominance. PubMed ID: 22847149

Mutations in the tail domain of DYNC1H1 cause dominant spinal muscular atrophy. PubMed ID: 22459677

Diagnostic exome sequencing in persons with severe intellectual disability. PubMed ID: 23033978

Mutations in TUBG1, DYNC1H1, KIF5C and KIF2A cause malformations of cortical development and microcephaly. PubMed ID: 23603762

Novel mutations in the DYNC1H1 tail domain refine the genetic and clinical spectrum of dyneinopathies. PubMed ID: 25512093

Novel dynein DYNC1H1 neck and motor domain mutations link distal spinal muscular atrophy and abnormal cortical development. PubMed ID: 24307404

Exome Sequencing Identifies DYNC1H1 Variant Associated With Vertebral Abnormality and Spinal Muscular Atrophy With Lower Extremity Predominance. PubMed ID: 25484024

Identification of a de novo DYNC1H1 mutation via WES according to published guidelines. PubMed ID: 26846447

Exome Sequencing Identifies De Novo DYNC1H1 Mutations Associated With Distal Spinal Muscular Atrophy and Malformations of Cortical Development. PubMed ID: 28193117