{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q96BD8","secondaryAccessions":["B2R9Y6","B4E0P4"],"uniProtkbId":"SKA1_HUMAN","entryAudit":{"firstPublicDate":"2007-01-23","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2001-12-01","entryVersion":166,"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":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"SKA complex subunit 1"}},"alternativeNames":[{"fullName":{"value":"Spindle and kinetochore-associated protein 1"}}]},"genes":[{"geneName":{"value":"SKA1"},"synonyms":[{"value":"C18orf24"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9CPV1"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17093495"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19289083"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22371557"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22454517"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22483620"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23085020"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24413531"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26981768"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27667719"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27697923"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28479321"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28495837"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29153323"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29487209"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31804178"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36592928"}],"value":"Component of the SKA complex, a microtubule plus end-binding complex of the outer kinetochore that stabilizes spindle microtubule-kinetochore attachments, promotes alignment of chromosomes at the mitotic spindle equator (chromosome congression) and assists suppression of the spindle assembly checkpoint (PubMed:17093495, PubMed:19289083, PubMed:22371557, PubMed:22483620, PubMed:23085020, PubMed:26981768, PubMed:27697923, PubMed:29487209, PubMed:31804178). Kinetochores, consisting of a centromere-associated inner segment and a microtubule-contacting outer segment, play a crucial role in chromosome segregation by mediating the physical connection between centromeric DNA and spindle microtubules (PubMed:19289083, PubMed:22483620, PubMed:23085020, PubMed:28479321, PubMed:29487209). The outer kinetochore is made up of the ten-subunit KMN network complex, comprising the MIS12, NDC80 and KNL1 complexes, and auxiliary microtubule-associated components such as the SKA complex; together they connect the outer kinetochore with the inner kinetochore, bind microtubules, and mediate interactions with mitotic checkpoint proteins that delay anaphase until chromosomes are bioriented on the spindle (PubMed:17093495, PubMed:19289083, PubMed:23085020, PubMed:28479321, PubMed:29487209). The SKA complex is loaded onto bioriented kinetochores and it facilitates chromosome congression by stabilizing microtubules together with MAPRE1, and end-on attachment of the NDC80 complex to depolymerizing spindle microtubules, thereby assisting the poleward-moving kinetochore in withstanding microtubule pulling forces (PubMed:19289083, PubMed:22371557, PubMed:22454517, PubMed:23085020, PubMed:24413531, PubMed:27697923, PubMed:28479321, PubMed:28495837, PubMed:29487209). The complex associates with dynamic microtubule plus-ends and can track both depolymerizing and elongating microtubules (PubMed:23085020, PubMed:29153323). The complex recruits protein phosphatase 1 (PP1) to the kinetochore in prometaphase and metaphase, to oppose spindle assembly checkpoint signaling and promote the onset of anaphase (PubMed:26981768). In the complex, it mediates interactions with microtubules (PubMed:19289083, PubMed:22483620, PubMed:23085020, PubMed:24413531, PubMed:27667719, PubMed:29153323, PubMed:36592928). It also stimulates AURKB/Aurora B catalytic activity (PubMed:27697923). During meiosis the SKA complex stabilizes the meiotic spindle and is required for its migration to the cortex (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17093495"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19289083"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19387489"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22371557"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22454517"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22483620"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23085020"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26981768"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27225956"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28441529"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28535377"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29487209"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31804178"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32491969"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36592928"}],"value":"Component of the SKA complex, composed of SKA1, SKA2 and SKA3 (PubMed:17093495, PubMed:19289083, PubMed:19387489, PubMed:22483620, PubMed:23085020, PubMed:28441529, PubMed:28535377, PubMed:29487209, PubMed:31804178, PubMed:32491969). The SKA complex is a homodimer organized around a central W-shaped coiled-coil structure, formed by the interacting domains of SKA1, SKA2, and SKA3, each end of the 'W' is extended further by the C-terminal microtubule-binding domains of SKA1 and SKA3; the complex forms extended structures on microtubules (PubMed:17093495, PubMed:19289083, PubMed:22483620, PubMed:23085020, PubMed:27225956, PubMed:28441529, PubMed:29487209, PubMed:31804178). Interacts (via SXLP motif) with MAPRE1 (via C-terminus); the interaction is direct and stabilizes the kinetochore-microtubule attachment of the SKA1 complex (PubMed:27225956, PubMed:36592928). Interacts (via C-terminus) with protein phosphatase PP1 subunit PPP1CA; the interaction is direct and required for recruitment of PPP1CA to the kinetochore (PubMed:26981768). Interacts with the NDC80 complex; the interaction is required to establish kinetochore-microtubule end-on attachments (PubMed:22371557, PubMed:22454517, PubMed:27225956, PubMed:28535377, PubMed:32491969)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q96BD8","intActId":"EBI-741854"},"interactantTwo":{"uniProtKBAccession":"Q9UL45","geneName":"BLOC1S6","intActId":"EBI-465781"},"numberOfExperiments":9,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96BD8","intActId":"EBI-741854"},"interactantTwo":{"uniProtKBAccession":"A0A1B0GWI1","geneName":"CCDC196","intActId":"EBI-10181422"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96BD8","intActId":"EBI-741854"},"interactantTwo":{"uniProtKBAccession":"Q8IZT9","geneName":"FAM9C","intActId":"EBI-2870039"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96BD8","intActId":"EBI-741854"},"interactantTwo":{"uniProtKBAccession":"P62195","geneName":"PSMC5","intActId":"EBI-357745"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96BD8","intActId":"EBI-741854"},"interactantTwo":{"uniProtKBAccession":"Q8WVK7","geneName":"SKA2","intActId":"EBI-1773994"},"numberOfExperiments":15,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96BD8","intActId":"EBI-741854"},"interactantTwo":{"uniProtKBAccession":"Q8IX90","geneName":"SKA3","intActId":"EBI-1773976"},"numberOfExperiments":14,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96BD8","intActId":"EBI-741854"},"interactantTwo":{"uniProtKBAccession":"O95295","geneName":"SNAPIN","intActId":"EBI-296723"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96BD8","intActId":"EBI-741854"},"interactantTwo":{"uniProtKBAccession":"A1L4H1","geneName":"SSC5D","intActId":"EBI-10172867"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q96BD8","intActId":"EBI-741854"},"interactantTwo":{"uniProtKBAccession":"Q8N0S2","geneName":"SYCE1","intActId":"EBI-6872807"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9CPV1"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17093495"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19646878"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22371557"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27225956"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27697923"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28479321"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29487209"}],"value":"Localizes to bioriented kinetochores and spindle microtubules during metaphase in a NDC80 complex-dependent manner (PubMed:17093495, PubMed:28479321, PubMed:29487209). The SKA complex begins to concentrate at kinetochores before microtubule attachment but reaches maximum levels on bioriented metaphase chromosomes (PubMed:17093495). Localizes both to microtubule plus-ends and along the length of microtubules (PubMed:27225956). The localization of the SKA complex to kinetochores is positively regulated by protein serine/threonine kinase CDK1 (PubMed:28479321). The localization of the SKA complex to kinetochores is negatively regulated by protein serine/threonine kinase AURKB, and this action is opposed directly or indirectly by the PP1 and PP2A protein phosphatase complexes (PubMed:22371557, PubMed:27697923). Localizes at the centrosome during interphase and prophase (PubMed:19646878). Localizes to the meiotic spindle, but not to kinetochores, from the stage of germinal vesicle breakdown (GVBD) to meiosis II (MII) (By similarity)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15561729"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24413531"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26981768"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27225956"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"29487209"}],"value":"Cytoplasm, cytoskeleton, spindle","id":"SL-0251"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17093495"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22483620"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24413531"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26981768"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28479321"}],"value":"Chromosome, centromere, kinetochore","id":"SL-0149"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19646878"}],"value":"Cytoplasm, cytoskeleton, microtubule organizing center, centrosome","id":"SL-0048"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q96BD8-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q96BD8-2"],"sequenceIds":["VSP_037250"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22371557"}],"value":"Phosphorylated by AURKB at Thr-157 and Ser-242 which negatively regulates the association of the SKA complex with kinetochores to allow correction of aberrant kinetochore-microtubule interactions and promote mitotic sister chromatid biorientation"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the SKA1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"19413330"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"SKA complex subunit 1","featureId":"PRO_0000273155"},{"type":"Region","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"Flexiple loop that anchors 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