{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q14204","secondaryAccessions":["B0I1R0","Q6DKQ7","Q8WU28","Q92814","Q9Y4G5"],"uniProtkbId":"DYHC1_HUMAN","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2005-01-04","entryVersion":236,"sequenceVersion":5},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Cytoplasmic dynein 1 heavy chain 1"}},"alternativeNames":[{"fullName":{"value":"Cytoplasmic dynein heavy chain 1"}},{"fullName":{"value":"Dynein heavy chain, cytosolic"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:2961"}],"value":"DYNC1H1"},"synonyms":[{"value":"DHC1"},{"value":"DNCH1"},{"value":"DNCL"},{"value":"DNECL"},{"value":"DYHC"},{"value":"KIAA0325"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27462074"}],"value":"Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Plays a role in mitotic spindle assembly and metaphase plate congression (PubMed:27462074)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P38650"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9JHU4"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25512093"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29420470"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31092558"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36071160"}],"value":"Homodimer. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and dynein LCs assemble on the IC dimer (PubMed:29420470, PubMed:36071160). Interacts with DYNC1LI1; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1. Interacts with DYNC1LI2; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1. Interacts with DYNC1I2 (By similarity). Interacts with BICD2 (PubMed:25512093). Interacts with isoform 2 of CRACR2A (PubMed:31092558). Interacts with DNALI1 (By 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The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function"}],"commentType":"DOMAIN"},{"commentType":"DISEASE","disease":{"diseaseId":"Charcot-Marie-Tooth disease, axonal, type 2O","diseaseAccession":"DI-03264","acronym":"CMT2O","description":"An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy.","diseaseCrossReference":{"database":"MIM","id":"614228"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21820100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24307404"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25512093"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Cortical dysplasia, complex, with other brain malformations 13","diseaseAccession":"DI-03425","acronym":"CDCBM13","description":"An autosomal dominant disorder characterized by global developmental delay with impaired intellectual development. Some patients show signs of peripheral neuropathy, such as abnormal gait and hyporeflexia. 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