KHDR1_MOUSE
ID KHDR1_MOUSE Reviewed; 443 AA.
AC Q60749; A2ACH3; B2KG38; Q3U8T3; Q60735; Q7M4N5; Q99M33;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=KH domain-containing, RNA-binding, signal transduction-associated protein 1;
DE AltName: Full=GAP-associated tyrosine phosphoprotein p62;
DE AltName: Full=Src-associated in mitosis 68 kDa protein;
DE Short=Sam68;
DE AltName: Full=p21 Ras GTPase-activating protein-associated p62;
DE AltName: Full=p68;
GN Name=Khdrbs1 {ECO:0000312|MGI:MGI:893579};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA86693.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 103-120 AND 139-150.
RC STRAIN=BALB/c X DBA/2 {ECO:0000312|EMBL:AAA86693.1};
RC TISSUE=Dendritic cell {ECO:0000269|PubMed:7541765};
RX PubMed=7541765; DOI=10.1016/0378-1119(95)00040-d;
RA Agger R., Freimuth P.;
RT "Purification and cDNA sequence of a murine protein homologous to the human
RT p62 tyrosine phosphoprotein that associates with the Ras GTPase-activating
RT protein p120 GAP.";
RL Gene 158:307-308(1995).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAA64997.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH FYN; GRB2 AND PLCG1.
RC TISSUE=Thymus {ECO:0000312|EMBL:AAA64997.1};
RX PubMed=7799925; DOI=10.1128/mcb.15.1.186;
RA Richard S., Yu D., Blumer K.J., Hausladen D., Olszowy M.W., Connelly P.A.,
RA Shaw A.S.;
RT "Association of p62, a multifunctional SH2- and SH3-domain-binding protein,
RT with src family tyrosine kinases, Grb2, and phospholipase C gamma-1.";
RL Mol. Cell. Biol. 15:186-197(1995).
RN [3] {ECO:0000312|EMBL:BAC34303.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC34303.1};
RC TISSUE=Bone marrow, and Pancreas {ECO:0000312|EMBL:BAC34303.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5] {ECO:0000312|EMBL:AAH02051.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH02051.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH02051.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6] {ECO:0000305}
RP PROTEIN SEQUENCE OF 57-71; 103-131; 139-152; 158-165; 222-230; 273-282 AND
RP 433-443, FUNCTION, PHOSPHORYLATION AT SER-113, AND INTERACTION WITH SRC.
RX PubMed=7512695; DOI=10.1038/368871a0;
RA Fumagalli S., Totty N.F., Hsuan J.J., Courtneidge S.A.;
RT "A target for Src in mitosis.";
RL Nature 368:871-874(1994).
RN [7] {ECO:0000305}
RP FUNCTION, RNA-BINDING, AND HOMOOLIGOMERIZATION.
RX PubMed=9315629; DOI=10.1128/mcb.17.10.5707;
RA Chen T., Damaj B.B., Herrera C., Lasko P., Richard S.;
RT "Self-association of the single-KH-domain family members Sam68, GRP33, GLD-
RT 1, and Qk1: role of the KH domain.";
RL Mol. Cell. Biol. 17:5707-5718(1997).
RN [8]
RP INTERACTION WITH FYN; PLCG1; GRB2; RASA1; KHDRBS2 AND KHDRBS3.
RC TISSUE=Brain;
RX PubMed=10077576; DOI=10.1073/pnas.96.6.2710;
RA Di Fruscio M., Chen T., Richard S.;
RT "Characterization of Sam68-like mammalian proteins SLM-1 and SLM-2: SLM-1
RT is a Src substrate during mitosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2710-2715(1999).
RN [9]
RP INTERACTION WITH RBMY1A1.
RX PubMed=10823932; DOI=10.1073/pnas.97.11.5717;
RA Elliott D.J., Bourgeois C.F., Klink A., Stevenin J., Cooke H.J.;
RT "A mammalian germ cell-specific RNA-binding protein interacts with
RT ubiquitously expressed proteins involved in splice site selection.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5717-5722(2000).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CBP.
RX PubMed=12496368;
RA Hong W., Resnick R.J., Rakowski C., Shalloway D., Taylor S.J., Blobel G.A.;
RT "Physical and functional interaction between the transcriptional cofactor
RT CBP and the KH domain protein Sam68.";
RL Mol. Cancer Res. 1:48-55(2002).
RN [11]
RP FUNCTION, PHOSPHORYLATION AT SER-58; THR-71 AND THR-84, AND MUTAGENESIS OF
RP SER-58; THR-71 AND THR-84.
RX PubMed=12478298; DOI=10.1038/nature01153;
RA Matter N., Herrlich P., Koenig H.;
RT "Signal-dependent regulation of splicing via phosphorylation of Sam68.";
RL Nature 420:691-695(2002).
RN [12]
RP INTERACTION WITH PRMT1.
RX PubMed=12529443; DOI=10.1091/mbc.e02-08-0484;
RA Cote J., Boisvert F.-M., Boulanger M.-C., Bedford M.T., Richard S.;
RT "Sam68 RNA binding protein is an in vivo substrate for protein arginine N-
RT methyltransferase 1.";
RL Mol. Biol. Cell 14:274-287(2003).
RN [13]
RP RNA-BINDING.
RX PubMed=19457263; DOI=10.1186/1471-2199-10-47;
RA Galarneau A., Richard S.;
RT "The STAR RNA binding proteins GLD-1, QKI, SAM68 and SLM-2 bind bipartite
RT RNA motifs.";
RL BMC Mol. Biol. 10:47-47(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=22196734; DOI=10.1016/j.cell.2011.11.028;
RA Iijima T., Wu K., Witte H., Hanno-Iijima Y., Glatter T., Richard S.,
RA Scheiffele P.;
RT "SAM68 regulates neuronal activity-dependent alternative splicing of
RT neurexin-1.";
RL Cell 147:1601-1614(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [17]
RP MUTAGENESIS OF VAL-229.
RX PubMed=23637638; DOI=10.1371/journal.pgen.1003474;
RA Ehrmann I., Dalgliesh C., Liu Y., Danilenko M., Crosier M., Overman L.,
RA Arthur H.M., Lindsay S., Clowry G.J., Venables J.P., Fort P., Elliott D.J.;
RT "The tissue-specific RNA binding protein T-STAR controls regional splicing
RT patterns of neurexin pre-mRNAs in the brain.";
RL PLoS Genet. 9:E1003474-E1003474(2013).
RN [18]
RP FUNCTION, AND INTERACTION WITH KHDRBS2.
RX PubMed=24469635; DOI=10.1083/jcb.201310136;
RA Iijima T., Iijima Y., Witte H., Scheiffele P.;
RT "Neuronal cell type-specific alternative splicing is regulated by the KH
RT domain protein SLM1.";
RL J. Cell Biol. 204:331-342(2014).
RN [19]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-282; ARG-284; ARG-291 AND
RP ARG-331, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Recruited and tyrosine phosphorylated by several receptor
CC systems, for example the T-cell, leptin and insulin receptors. Once
CC phosphorylated, functions as an adapter protein in signal transduction
CC cascades by binding to SH2 and SH3 domain-containing proteins. Role in
CC G2-M progression in the cell cycle. Represses CBP-dependent
CC transcriptional activation apparently by competing with other nuclear
CC factors for binding to CBP. Also acts as a putative regulator of mRNA
CC stability and/or translation rates and mediates mRNA nuclear export.
CC Positively regulates the association of constitutive transport element
CC (CTE)-containing mRNA with large polyribosomes and translation
CC initiation. May not be involved in the nucleocytoplasmic export of
CC unspliced (CTE)-containing RNA species. RNA-binding protein that plays
CC a role in the regulation of alternative splicing and influences mRNA
CC splice site selection and exon inclusion. Binds to RNA containing 5'-
CC [AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides.
CC Binds poly(A). In cooperation with HNRNPA1 modulates alternative
CC splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and
CC of SMN1 (By similarity). Can regulate CD44 alternative splicing in a
CC Ras pathway-dependent manner. Can regulate alternative splicing of
CC NRXN1 and NRXN3 in the laminin G-like domain 6 containing the
CC evolutionary conserved neurexin alternative spliced segment 4 (AS4)
CC involved in neurexin selective targeting to postsynaptic partners. In a
CC neuronal activity-dependent manner cooperates synergistically with
CC KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The
CC cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3
CC alternative splicing at AS4 (PubMed:12478298, PubMed:22196734,
CC PubMed:24469635). {ECO:0000250|UniProtKB:O75525,
CC ECO:0000269|PubMed:12478298, ECO:0000269|PubMed:12496368,
CC ECO:0000269|PubMed:22196734, ECO:0000269|PubMed:24469635,
CC ECO:0000269|PubMed:7512695, ECO:0000269|PubMed:9315629}.
CC -!- SUBUNIT: Self-associates to form homooligomers when bound to RNA,
CC oligomerization appears to be limited when binding to proteins
CC (PubMed:9315629). Interacts with KHDRBS3/SLIM-2 and KHDRBS2/SLIM-1;
CC heterooligomer formation of KHDRBS family proteins may modulate RNA
CC substrate specificity (PubMed:10077576, PubMed:24469635). Interacts
CC with RASA1, FYN, GRB2, PLCG1, SRC, RBMY1A1, CBP, PRMT1 (PubMed:7799925,
CC PubMed:7512695, PubMed:10077576, PubMed:10823932, PubMed:12496368,
CC PubMed:12529443). Interacts with PTK6 (via SH3 and SH2 domains). Forms
CC a complex with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA. Binds
CC WBP4/FBP21 (via WW domains), FNBP4/FBP30 (via WW domains). Interacts
CC (via Arg/Gly-rich-flanked Pro-rich regions) with FYN (via the SH3
CC domain). Interacts with APC, HNRNPA1 (By similarity). Interacts with
CC the non-receptor tyrosine kinase SRMS; the interaction leads to
CC phosphorylation of KHDRBS1 (By similarity). Interacts with ZBTB7A;
CC negatively regulates KHDRBS1 splicing activity toward BCL2L1 (By
CC similarity). {ECO:0000250|UniProtKB:Q07666,
CC ECO:0000250|UniProtKB:Q91V33, ECO:0000269|PubMed:10077576,
CC ECO:0000269|PubMed:12496368, ECO:0000269|PubMed:12529443,
CC ECO:0000269|PubMed:24469635, ECO:0000269|PubMed:7512695,
CC ECO:0000269|PubMed:7799925, ECO:0000269|PubMed:9315629}.
CC -!- INTERACTION:
CC Q60749; P45481: Crebbp; NbExp=7; IntAct=EBI-519077, EBI-296306;
CC Q60749; P39688: Fyn; NbExp=15; IntAct=EBI-519077, EBI-524514;
CC Q60749; Q60631: Grb2; NbExp=2; IntAct=EBI-519077, EBI-1688;
CC Q60749; Q60749: Khdrbs1; NbExp=2; IntAct=EBI-519077, EBI-519077;
CC Q60749; Q9JIF0: Prmt1; NbExp=2; IntAct=EBI-519077, EBI-519055;
CC Q60749; P10686: Plcg1; Xeno; NbExp=2; IntAct=EBI-519077, EBI-520788;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12496368}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q07666}. Membrane {ECO:0000269|PubMed:12496368}.
CC Note=Predominantly located in the nucleus but also located partially in
CC the cytoplasm. {ECO:0000250|UniProtKB:Q07666}.
CC -!- TISSUE SPECIFICITY: In adult cerebellum expressed in most neuronal cell
CC populations, specifically in cerebellar granule cells of the internal
CC granular layer, ROR(alpha)-positive Purkinje cells, internal granular
CC layer and molecular layer interneurons (at protein level).
CC {ECO:0000269|PubMed:22196734}.
CC -!- DEVELOPMENTAL STAGE: In the developing cerebellum expression is high at
CC birth and declines over the first 3 weeks. At P7 highly expressed in
CC granule cell precursor cells in the external granular layer and mature
CC granule cells of the internal granule layer.
CC {ECO:0000269|PubMed:22196734}.
CC -!- DOMAIN: The KH domain is required for binding to RNA.
CC {ECO:0000269|PubMed:9315629}.
CC -!- DOMAIN: The Pro-rich domains are flanked by Arg/Gly-rich motifs which
CC can be asymmetric dimethylated on arginine residues to give the
CC DMA/Gly-rich regions. Selective methylation on these motifs can
CC modulate protein-protein interactions (By similarity). {ECO:0000250}.
CC -!- PTM: Tyrosine phosphorylated by several non-receptor tyrosine kinases
CC including LCK, FYN and JAK3. Also tyrosine phosphorylated by the non-
CC receptor tyrosine kinase SRMS in an EGF-dependent manner (By
CC similarity). Phosphorylation by PTK6 negatively regulates its RNA
CC binding ability. Phosphorylation by PTK6 at Tyr-440 dictates the
CC nuclear localization of KHDRBS1. Phosphorylation by MAPK1 at Ser-58,
CC Thr-71 and Thr-84 regulates CD44 alternative splicing by promoting CD44
CC exon v5 inclusion. {ECO:0000250|UniProtKB:Q07666,
CC ECO:0000269|PubMed:12478298, ECO:0000269|PubMed:7512695}.
CC -!- PTM: Acetylated. Positively correlates with ability to bind RNA (By
CC similarity). {ECO:0000250|UniProtKB:Q07666}.
CC -!- PTM: Arginine methylation is required for nuclear localization.
CC Inhibits interaction with Src-like SH3 domains, but not interaction
CC with WW domains of WBP4/FBP21 AND FNBP4/FBP30 (By similarity).
CC {ECO:0000250|UniProtKB:Q07666}.
CC -!- SIMILARITY: Belongs to the KHDRBS family. {ECO:0000255}.
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DR EMBL; U17961; AAA86693.1; -; mRNA.
DR EMBL; U17046; AAA64997.1; -; mRNA.
DR EMBL; AK050520; BAC34303.1; -; mRNA.
DR EMBL; AK152084; BAE30934.1; -; mRNA.
DR EMBL; AL669834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU210913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002051; AAH02051.1; -; mRNA.
DR CCDS; CCDS18703.1; -.
DR PIR; I49140; I49140.
DR PIR; S43974; S43974.
DR RefSeq; NP_035447.3; NM_011317.4.
DR AlphaFoldDB; Q60749; -.
DR SMR; Q60749; -.
DR BioGRID; 203068; 21.
DR CORUM; Q60749; -.
DR DIP; DIP-2861N; -.
DR IntAct; Q60749; 25.
DR MINT; Q60749; -.
DR STRING; 10090.ENSMUSP00000066516; -.
DR iPTMnet; Q60749; -.
DR PhosphoSitePlus; Q60749; -.
DR SwissPalm; Q60749; -.
DR EPD; Q60749; -.
DR MaxQB; Q60749; -.
DR PaxDb; Q60749; -.
DR PeptideAtlas; Q60749; -.
DR PRIDE; Q60749; -.
DR ProteomicsDB; 269213; -.
DR Antibodypedia; 3944; 338 antibodies from 38 providers.
DR DNASU; 20218; -.
DR Ensembl; ENSMUST00000066257; ENSMUSP00000066516; ENSMUSG00000028790.
DR Ensembl; ENSMUST00000129342; ENSMUSP00000115402; ENSMUSG00000028790.
DR GeneID; 20218; -.
DR KEGG; mmu:20218; -.
DR UCSC; uc008uyd.2; mouse.
DR CTD; 10657; -.
DR MGI; MGI:893579; Khdrbs1.
DR VEuPathDB; HostDB:ENSMUSG00000028790; -.
DR eggNOG; KOG1588; Eukaryota.
DR GeneTree; ENSGT00940000155718; -.
DR HOGENOM; CLU_034976_0_0_1; -.
DR InParanoid; Q60749; -.
DR OMA; TPYREHP; -.
DR OrthoDB; 1012406at2759; -.
DR PhylomeDB; Q60749; -.
DR TreeFam; TF314878; -.
DR Reactome; R-MMU-8849468; PTK6 Regulates Proteins Involved in RNA Processing.
DR BioGRID-ORCS; 20218; 10 hits in 76 CRISPR screens.
DR ChiTaRS; Khdrbs1; mouse.
DR PRO; PR:Q60749; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q60749; protein.
DR Bgee; ENSMUSG00000028790; Expressed in frontonasal prominence and 253 other tissues.
DR Genevisible; Q60749; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0070618; C:Grb2-Sos complex; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; ISO:MGI.
DR GO; GO:0008266; F:poly(U) RNA binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0035591; F:signaling adaptor activity; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0045948; P:positive regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0046831; P:regulation of RNA export from nucleus; IDA:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISO:MGI.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR045071; BBP-like.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR032571; Qua1_dom.
DR InterPro; IPR032335; Sam68-YY.
DR PANTHER; PTHR11208; PTHR11208; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF16274; Qua1; 1.
DR Pfam; PF16568; Sam68-YY; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Membrane; Methylation; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; SH3-binding;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..443
FT /note="KH domain-containing, RNA-binding, signal
FT transduction-associated protein 1"
FT /id="PRO_0000050125"
FT DOMAIN 171..197
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..260
FT /note="Involved in homodimerization"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT REGION 280..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..443
FT /note="Interaction with HNRNPA1"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT REGION 400..420
FT /note="Interaction with ZBTB7A"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT REGION 411..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 45
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 52
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 58
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:12478298"
FT MOD_RES 71
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:12478298"
FT MOD_RES 84
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:12478298"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7512695"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 175
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 282
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 284
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 291
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 304
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 310
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 315
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 320
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 320
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 325
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 331
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 331
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 331
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 340
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 340
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 387
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 435
FT /note="Phosphotyrosine; by PTK6"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 440
FT /note="Phosphotyrosine; by PTK6"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MOD_RES 443
FT /note="Phosphotyrosine; by PTK6"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT CROSSLNK 96
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT CROSSLNK 432
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q07666"
FT MUTAGEN 58
FT /note="S->A: Abolishes phosphorylation, abolishes CD44
FT splicing regulation; when associated with A-71 and A-84."
FT /evidence="ECO:0000269|PubMed:12478298"
FT MUTAGEN 71
FT /note="T->A: Abolishes phosphorylation, abolishes CD44
FT splicing regulation; when associated with A-58 and A-84."
FT /evidence="ECO:0000269|PubMed:12478298"
FT MUTAGEN 84
FT /note="T->A: Abolishes phosphorylation, abolishes CD44
FT splicing regulation; when associated with A-58 and A-71."
FT /evidence="ECO:0000269|PubMed:12478298"
FT MUTAGEN 229
FT /note="V->F: Abolishes splicing regulation."
FT /evidence="ECO:0000269|PubMed:23637638"
FT CONFLICT 104
FT /note="L -> P (in Ref. 2; AAA64997)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="D -> N (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="G -> R (in Ref. 1; AAA86693)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="V -> VS (in Ref. 1; AAA86693)"
FT /evidence="ECO:0000305"
FT CONFLICT 225..230
FT /note="MDLHVF -> LGENGL (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="A -> S (in Ref. 1; AAA86693)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 48371 MW; D33DE960BEA9E5AA CRC64;
MQRRDDPASR LTRSSGRSCS KDPSGAHPSV RLTPSRPSPL PHRPRGGGGG PRGGARASPA
TQPPPLLPPS TPGPDATVVG SAPTPLLPPS ATAAVKMEPE NKYLPELMAE KDSLDPSFTH
AMQLLSVEIE KIQKGESKKD DEENYLDLFS HKNMKLKERV LIPVKQYPKF NFVGKILGPQ
GNTIKRLQEE TGAKISVLGK GSMRDKAKEE ELRKGGDPKY AHLNMDLHVF IEVFGPPCEA
YALMAHAMEE VKKFLVPDMM DDICQEQFLE LSYLNGVPEP SRGRGVSVRG RGAAPPPPPV
PRGRGVGPPR GALVRGTPVR GSITRGATVT RGVPPPPTVR GAPTPRARTA GIQRIPLPPT
PAPETYEDYG YDDTYAEQSY EGYEGYYSQS QGESEYYDYG HGELQDSYEA YGQDDWNGTR
PSLKAPPARP VKGAYREHPY GRY
