{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P60709","secondaryAccessions":["P02570","P70514","P99021","Q11211","Q64316","Q75MN2","Q96B34","Q96HG5"],"uniProtkbId":"ACTB_HUMAN","entryAudit":{"firstPublicDate":"1986-07-21","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1988-04-01","entryVersion":219,"sequenceVersion":1},"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":"Actin, cytoplasmic 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P68137"}],"value":"3.6.4.-"}]},"alternativeNames":[{"fullName":{"value":"Beta-actin"}}],"contains":[{"recommendedName":{"fullName":{"value":"Actin, cytoplasmic 1, N-terminally processed"}}}]},"genes":[{"geneName":{"value":"ACTB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6QAQ1"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25255767"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29581253"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29925947"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38609661"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39321809"}],"value":"Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (PubMed:25255767, PubMed:29581253). Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (PubMed:29581253). In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA (PubMed:29925947). Plays a role in the assembly of the gamma-tubulin ring complex (gTuRC), which regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments (PubMed:39321809, PubMed:38609661). Part of the ACTR1A/ACTB filament around which the dynactin complex is built (By similarity). The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25255767"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O18840"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P60710"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6QAQ1"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10411937"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11687588"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14592989"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15328537"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16685646"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17289661"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17823310"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18765789"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21555369"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21969592"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25255767"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28604741"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38609661"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39321809"}],"value":"Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix (PubMed:16685646, PubMed:28604741). Each actin can bind to 4 others (PubMed:16685646, PubMed:28604741). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57 SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (PubMed:18765789). In muscle cells, the BAF complex also contains DPF3 (PubMed:18765789). Found in a complex with XPO6, Ran, ACTB and PFN1 (PubMed:14592989). Interacts with PFN1 (PubMed:10411937, PubMed:25255767). Interacts with XPO6 and EMD (PubMed:15328537). Interacts with ERBB2 (PubMed:21555369). Interacts with GCSAM (PubMed:17823310). Interacts with TBC1D21 (By similarity). Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity). Interacts with DHX9 (via C-terminus); this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes (PubMed:11687588). Interacts with FAM107A (PubMed:21969592, PubMed:28604741). Associates with the gamma-tubulin ring complex (gTuRC) consisting of TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6 and gamma-tubulin TUBG1 or TUBG2; within the complex, interacts with TUBGCP3 and TUBGCP6 to form a luminal bridge with MZT1 that stabilizes the initial structure during complex assembly (PubMed:39321809, PubMed:38609661). Part of the ACTR1A/ACTB filament around which the dynactin complex is built (By similarity). The filament contains 8 copies of ACTR1A and 1 ACTB (By similarity). Interacts with TPRN which forms ring-like structures in the stereocilium taper region; the interaction may stabilize stereocilia in inner ear hair cells (By similarity). Interacts with AMOTL2 (via N-terminus), the interaction facilitates binding of cell junction complexes to actin fibers in endothelial cells (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P60709","geneName":"ACTB","intActId":"EBI-353944"},"numberOfExperiments":16,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P63261","geneName":"ACTG1","intActId":"EBI-351292"},"numberOfExperiments":16,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P05067","geneName":"APP","intActId":"EBI-77613"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"Q9UQB8","geneName":"BAIAP2","intActId":"EBI-525456"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P40123","geneName":"CAP2","intActId":"EBI-1051165"},"numberOfExperiments":9,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"Q16543","geneName":"CDC37","intActId":"EBI-295634"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P23528","geneName":"CFL1","intActId":"EBI-352733"},"numberOfExperiments":11,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"Q549N0","geneName":"CFL2","intActId":"EBI-10201319"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"Q9Y281","geneName":"CFL2","intActId":"EBI-351218"},"numberOfExperiments":11,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P13569","geneName":"CFTR","intActId":"EBI-349854"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P60981","geneName":"DSTN","intActId":"EBI-745191"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"Q8WTR2","geneName":"DUSP19","intActId":"EBI-8654968"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"Q08426","geneName":"EHHADH","intActId":"EBI-2339219"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P50402","geneName":"EMD","intActId":"EBI-489887"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P04626","geneName":"ERBB2","intActId":"EBI-641062"},"numberOfExperiments":11,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"Q8TCJ0-2","geneName":"FBXO25","intActId":"EBI-6264551"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P11142","geneName":"HSPA8","intActId":"EBI-351896"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P83110","geneName":"HTRA3","intActId":"EBI-2867394"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P42858","geneName":"HTT","intActId":"EBI-466029"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"O14950","geneName":"MYL12B","intActId":"EBI-1642165"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P14598","geneName":"NCF1","intActId":"EBI-395044"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P29474","geneName":"NOS3","intActId":"EBI-1391623"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"Q92636","geneName":"NSMAF","intActId":"EBI-2947053"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"Q96HA8","geneName":"NTAQ1","intActId":"EBI-741158"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P07737","geneName":"PFN1","intActId":"EBI-713780"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P78317","geneName":"RNF4","intActId":"EBI-2340927"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P37802","geneName":"TAGLN2","intActId":"EBI-1056740"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"Q9BSI4","geneName":"TINF2","intActId":"EBI-717399"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P13693","geneName":"TPT1","intActId":"EBI-1783169"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"Q7KZS0","geneName":"UBE2I","intActId":"EBI-10180829"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"Q9UBQ0-2","geneName":"VPS29","intActId":"EBI-11141397"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"O75083","geneName":"WDR1","intActId":"EBI-351917"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P63104","geneName":"YWHAZ","intActId":"EBI-347088"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"P08413","geneName":"Camk2b","intActId":"EBI-916155"},"numberOfExperiments":4,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P60709","intActId":"EBI-353944"},"interactantTwo":{"uniProtKBAccession":"Q8K4J6","geneName":"Mrtfa","intActId":"EBI-8291665"},"numberOfExperiments":3,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17289661"}],"value":"Localized in cytoplasmic mRNP granules containing untranslated mRNAs"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11687588"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17289661"}],"value":"Cytoplasm, cytoskeleton","id":"SL-0090"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11687588"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29925947"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16139798"}],"value":"ISGylated"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29343822"}],"value":"Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23673617"}],"value":"Monomethylation at Lys-84 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes (PubMed:23673617). Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (PubMed:23673617)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P60710"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30526847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30626964"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30785395"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31388018"}],"value":"Methylated at His-73 by SETD3 (PubMed:30526847, PubMed:30626964, PubMed:30785395, PubMed:31388018). Methylation at His-73 is required for smooth muscle contraction of the laboring uterus during delivery (By similarity)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36173861"}],"value":"N-terminal cleavage of acetylated methionine of immature cytoplasmic actin by ACTMAP"}],"commentType":"PTM","molecule":"Actin, cytoplasmic 1"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29581253"}],"value":"N-terminal acetylation by NAA80 affects actin filament depolymerization and elongation, including elongation driven by formins (PubMed:29581253). In contrast, filament nucleation by the Arp2/3 complex is not affected (PubMed:29581253)"}],"commentType":"PTM","molecule":"Actin, cytoplasmic 1, N-terminally processed"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19015515"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"26228148"}],"value":"(Microbial infection) Monomeric actin is cross-linked by V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial toxins mediate the cross-link between Lys-50 of one monomer and Glu-270 of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding (PubMed:19015515). The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners (PubMed:26228148)"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Dystonia-deafness syndrome 1","diseaseAccession":"DI-00412","acronym":"DDS1","description":"An autosomal dominant form of dystonia with juvenile onset, associated with congenital or childhood-onset sensorineural deafness. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. Some DDS1 patients have dysmorphic features, skeletal anomalies, and/or mild developmental delay with impaired intellectual development.","diseaseCrossReference":{"database":"MIM","id":"607371"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16685646"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25255767"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28487785"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29788902"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35005077"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Baraitser-Winter syndrome 1","diseaseAccession":"DI-03416","acronym":"BRWS1","description":"A rare developmental disorder characterized by the combination of congenital ptosis, high-arched eyebrows, hypertelorism, ocular colobomata, and a brain malformation consisting of anterior-predominant lissencephaly. Other typical features include postnatal short stature and microcephaly, intellectual disability, seizures, and hearing loss.","diseaseCrossReference":{"database":"MIM","id":"243310"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22366783"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30733661"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Thrombocytopenia 8, with dysmorphic features and developmental delay","diseaseAccession":"DI-06744","acronym":"THC8","description":"A form of thrombocytopenia, a hematologic disorder defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting. THC8 is an autosomal dominant form characterized by early-childhood onset of thrombocytopenia with platelet anisotropy. Affected individuals also have dysmorphic facial features and variable developmental delay with speech delay and mildly impaired intellectual development.","diseaseCrossReference":{"database":"MIM","id":"620475"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10411937"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25255767"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30315159"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30733661"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Becker nevus syndrome","diseaseAccession":"DI-06747","acronym":"BNS","description":"A syndrome characterized by the association of Becker nevi with musculoskeletal abnormalities, unilateral breast hypoplasia, intellectual disability, developmental delay, and cardiomyopathy. Becker nevus is a cutaneous hamartoma that appears in childhood as a unilateral tan patch and increases in thickness, pigmentation, and hair growth during adolescence. Histologically, epidermal acanthosis is accompanied by irregularly dispersed ectopic smooth muscle bundles and increased terminal hair follicles. Most cases are sporadic.","diseaseCrossReference":{"database":"MIM","id":"604919"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28347698"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Congenital smooth muscle hamartoma, with or without hemihypertrophy","diseaseAccession":"DI-06743","acronym":"CSMH","description":"A benign skin lesion that usually presents as an indurated, slightly pigmented or flesh-colored plaque with perifollicular papules or coarse hair. Histopathologically, there is excessive proliferation of ectopic smooth muscle within the dermis. Hair follicles are normal in number and hyperkeratosis, acanthosis and hyperpigmentation of the basal cell layer can sometimes be seen. Rarely, CSMH is associated with hemihypertrophy.","diseaseCrossReference":{"database":"MIM","id":"620470"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32170967"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"In vertebrates 3 main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the actin family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19377461"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24336203"}],"value":"Was originally thought to be part of the MLL5-L complex, at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT (PubMed:19377461). 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