{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q07666","secondaryAccessions":["D3DPP3","Q6PJX7","Q8NB97","Q99760"],"uniProtkbId":"KHDR1_HUMAN","entryAudit":{"firstPublicDate":"2005-04-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-11-01","entryVersion":232,"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":"KH domain-containing, RNA-binding, signal transduction-associated protein 1"}},"alternativeNames":[{"fullName":{"value":"GAP-associated tyrosine phosphoprotein p62"}},{"fullName":{"value":"Src-associated in mitosis 68 kDa protein"},"shortNames":[{"value":"Sam68"}]},{"fullName":{"value":"p21 Ras GTPase-activating protein-associated p62"}},{"fullName":{"value":"p68"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:18116"}],"value":"KHDRBS1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1374686"}],"value":"SAM68"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60749"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15021911"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17371836"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20186123"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20610388"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22253824"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26080397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26758068"}],"value":"Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to (PubMed:22253824). RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner (PubMed:26080397). In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1 (PubMed:17371836, PubMed:20186123). Can regulate alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. In a neuronal activity-dependent manner cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3 alternative splicing at AS4 (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9013542"}],"value":"Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60749"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q91V33"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10332027"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10913193"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11585385"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1374686"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17371836"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17890166"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22000517"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24514149"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26080397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29496907"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9045636"}],"value":"Self-associates to form homooligomers when bound to RNA, oligomerization appears to be limited when binding to proteins; dimerization increases RNA affinity (PubMed:20610388, PubMed:26758068). Forms a trimeric complex in the nucleus consisting of BANP, HDAC6 and KHDRBS1/SAM68; HDAC6 keeps KHDRBS1 in a deacetylated state which inhibits the inclusion of CD44 alternate exons (PubMed:26080397). The complex is disrupted by MAPK1/MAPK3-mediated phosphorylation of BANP which results in BANP export to the cytoplasm (PubMed:26080397). This facilitates acetylation of KHDRBS1 and CD44 variant exon inclusion (PubMed:26080397). Interacts with KHDRBS3/SLIM-2 (PubMed:10332027). Interacts with KHDRBS2/SLIM-1; heterooligomer formation of KHDRBS family proteins may modulate RNA substrate specificity (By similarity). Interacts with RASA1, LCK, FYN, PTPN6, PLCG1, GRB2, CBL, JAK3, PIK3R, STAT3, APC, HNRNPA1 (PubMed:10332027, PubMed:11585385, PubMed:1374686, PubMed:17371836, PubMed:22000517, PubMed:9045636). Interacts with PTK6 (via SH3 and SH2 domains) (PubMed:10913193). Forms a complex with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA (PubMed:17890166). Does not interact with TPR (PubMed:22253824). Interacts with PRMT1 (By similarity). Binds WBP4/FBP21 (via WW domains), FNBP4/FBP30 (via WW domains). Interacts (via Arg/Gly-rich-flanked Pro-rich regions) with FYN (via the SH3 domain) (By similarity). Interacts with the non-receptor tyrosine kinase SRMS; the interaction leads to phosphorylation of KHDRBS1 (PubMed:29496907). Interacts with ZBTB7A; negatively regulates KHDRBS1 splicing activity toward BCL2L1 (PubMed:24514149)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P25054","geneName":"APC","intActId":"EBI-727707"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P06241","geneName":"FYN","intActId":"EBI-515315"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P62993","geneName":"GRB2","intActId":"EBI-401755"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P08631","geneName":"HCK","intActId":"EBI-346340"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P09651","geneName":"HNRNPA1","intActId":"EBI-352662"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P61978","geneName":"HNRNPK","intActId":"EBI-304185"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P52333","geneName":"JAK3","intActId":"EBI-518246"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"Q07666","geneName":"KHDRBS1","intActId":"EBI-1364"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"Q5VWX1","geneName":"KHDRBS2","intActId":"EBI-742808"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"O75525","geneName":"KHDRBS3","intActId":"EBI-722504"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P06239","geneName":"LCK","intActId":"EBI-1348"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P19338","geneName":"NCL","intActId":"EBI-346967"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P19174","geneName":"PLCG1","intActId":"EBI-79387"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P38159","geneName":"RBMX","intActId":"EBI-743526"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P51531","geneName":"SMARCA2","intActId":"EBI-679562"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P12931","geneName":"SRC","intActId":"EBI-621482"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P40763","geneName":"STAT3","intActId":"EBI-518675"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P15498","geneName":"VAV1","intActId":"EBI-625518"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"O95365","geneName":"ZBTB7A","intActId":"EBI-2795384"},"numberOfExperiments":9,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P06240","geneName":"Lck","intActId":"EBI-1401"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"Q07666","intActId":"EBI-1364"},"interactantTwo":{"uniProtKBAccession":"P23727","geneName":"PIK3R1","intActId":"EBI-520244"},"numberOfExperiments":2,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29496907"}],"value":"Predominantly located in the nucleus but also located partially in the cytoplasm"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1374686"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26080397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29496907"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29496907"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1374686"}],"value":"Membrane","id":"SL-0162"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1374686"}],"value":"1"},"isoformIds":["Q07666-1"],"isoformSequenceStatus":"Displayed"},{"name":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"2"},"isoformIds":["Q07666-2"],"sequenceIds":["VSP_051719"],"isoformSequenceStatus":"Described"},{"name":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9013542"}],"value":"3"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9013542"}],"value":"DeltaKH"}],"isoformIds":["Q07666-3"],"sequenceIds":["VSP_051720"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9013542"}],"value":"Ubiquitously expressed in all tissue examined. Isoform 1 is expressed at lower levels in brain, skeletal muscle, and liver whereas isoform 3 is intensified in skeletal muscle and in liver"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9013542"}],"value":"Isoform 3 is only expressed in growth-arrested cells"}],"commentType":"DEVELOPMENTAL STAGE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60749"}],"value":"The KH domain is required for binding to RNA"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"The Pro-rich domains are flanked by Arg/Gly-rich motifs which can be asymmetric dimethylated on arginine residues to give the DMA/Gly-rich regions. Selective methylation on these motifs can modulate protein-protein interactions (By similarity)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11585385"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16179349"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17371836"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22000517"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29496907"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9045636"}],"value":"Tyrosine phosphorylated by several non-receptor tyrosine kinases including LCK, FYN and JAK3. Also tyrosine phosphorylated by the non-receptor tyrosine kinase SRMS in an EGF-dependent manner (PubMed:29496907). Negatively correlates with ability to bind RNA but required for many interactions with proteins. Phosphorylation by PTK6 negatively regulates its RNA binding ability. Phosphorylation by PTK6 at Tyr-440 dictates the nuclear localization of KHDRBS1. Phosphorylation at Tyr-387 disrupts interaction with APC. Phosphorylation at tyrosine residues by FYN inverts activity on modulation of BCL2L1 alternative splicing"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15021911"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26080397"}],"value":"Acetylated (PubMed:15021911, PubMed:26080397). Positively correlates with ability to bind RNA (PubMed:15021911). Deacetylated by HDAC6; this regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons (PubMed:26080397)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12529443"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1374686"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.7"}],"value":"Arginine methylation is required for nuclear localization. Also can affect interaction with other proteins. Inhibits interaction with Src-like SH3 domains, but not interaction with WW domains of WBP4/FBP21 and FNBP4/FBP30"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Belongs to the KHDRBS family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Miscellaneous discrepancy","sequence":"AAH10132.1","note":"Intron retention.","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":443,"modifier":"EXACT"}},"description":"KH domain-containing, RNA-binding, signal transduction-associated protein 1","featureId":"PRO_0000050124"},{"type":"Domain","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"KH","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"Involved in homodimerization","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"26758068"}]},{"type":"Region","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":316,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":327,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":443,"modifier":"EXACT"}},"description":"Interaction with HNRNPA1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17371836"}]},{"type":"Region","location":{"start":{"value":400,"modifier":"EXACT"},"end":{"value":420,"modifier":"EXACT"}},"description":"Interaction with ZBTB7A","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24514149"}]},{"type":"Region","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":443,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":307,"modifier":"EXACT"},"end":{"value":316,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":434,"modifier":"EXACT"},"end":{"value":443,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Modified residue","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"24275569"}]},{"type":"Modified residue","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"18669648"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"18669648"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"Asymmetric dimethylarginine; 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