KHDR1_HUMAN
ID KHDR1_HUMAN Reviewed; 443 AA.
AC Q07666; D3DPP3; Q6PJX7; Q8NB97; Q99760;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 213.
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|HGNC:HGNC:18116};
GN Synonyms=SAM68 {ECO:0000303|PubMed:1374686};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA59990.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, RNA-BINDING,
RP METHYLATION, AND INTERACTION WITH RASA1.
RC TISSUE=Fetal brain {ECO:0000312|EMBL:AAA59990.1};
RX PubMed=1374686; DOI=10.1016/0092-8674(92)90455-l;
RA Wong G., Muller O., Clark R., Conroy L., Moran M.F., Polakis P.,
RA McCormick F.;
RT "Molecular cloning and nucleic acid binding properties of the GAP-
RT associated tyrosine phosphoprotein p62.";
RL Cell 69:551-558(1992).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAB47504.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Placenta {ECO:0000269|PubMed:9013542};
RX PubMed=9013542; DOI=10.1074/jbc.272.6.3129;
RA Barlat I., Maurier F., Duchesne M., Guitard E., Tocque B.,
RA Schweighoffer F.;
RT "A role for Sam68 in cell cycle progression antagonized by a spliced
RT variant within the KH domain.";
RL J. Biol. Chem. 272:3129-3132(1997).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAC03643.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain {ECO:0000312|EMBL:BAC03643.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AL139249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAH00717.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph {ECO:0000312|EMBL:AAH19109.1}, and
RC Placenta {ECO:0000312|EMBL:AAH00717.1};
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 [7]
RP PROTEIN SEQUENCE OF 18-31; 57-96; 103-131; 139-152; 176-185; 292-302 AND
RP 316-340, METHYLATION AT ARG-320; ARG-331 AND ARG-340, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8] {ECO:0000305}
RP PROTEIN SEQUENCE OF 102-110 AND 169-175 (ISOFORMS 1/2), FUNCTION,
RP PHOSPHORYLATION, AND INTERACTION WITH LCK; FYN; PTPN6; PLCG1; GRB2; CBL;
RP JAK3 AND PIK3R1.
RX PubMed=9045636; DOI=10.1074/jbc.272.10.6214;
RA Fusaki N., Iwamatsu A., Iwashima M., Fujisawa J.;
RT "Interaction between Sam68 and Src family tyrosine kinases, Fyn and Lck, in
RT T cell receptor signaling.";
RL J. Biol. Chem. 272:6214-6219(1997).
RN [9] {ECO:0000305}
RP INTERACTION WITH KHDRBS3.
RC TISSUE=Testis {ECO:0000269|PubMed:10332027};
RX PubMed=10332027; DOI=10.1093/hmg/8.6.959;
RA Venables J.P., Vernet C., Chew S.L., Elliott D.J., Cowmeadow R.B., Wu J.,
RA Cooke H.J., Artzt K., Eperon I.C.;
RT "T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-
RT binding protein implicated in spermatogenesis.";
RL Hum. Mol. Genet. 8:959-969(1999).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PTK6.
RX PubMed=10913193; DOI=10.1128/mcb.20.16.6114-6126.2000;
RA Derry J.J., Richard S., Valderrama Carvajal H., Ye X., Vasioukhin V.,
RA Cochrane A.W., Chen T., Tyner A.L.;
RT "Sik (BRK) phosphorylates Sam68 in the nucleus and negatively regulates its
RT RNA binding ability.";
RL Mol. Cell. Biol. 20:6114-6126(2000).
RN [11] {ECO:0000305}
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH STAT3.
RX PubMed=11585385; DOI=10.1006/cimm.2001.1815;
RA Sanchez-Margalet V., Martin-Romero C.;
RT "Human leptin signaling in human peripheral blood mononuclear cells:
RT activation of the JAK-STAT pathway.";
RL Cell. Immunol. 211:30-36(2001).
RN [12] {ECO:0000305}
RP METHYLATION AT ARG-45; ARG-52; ARG-304; ARG-310; ARG-315; ARG-320 AND
RP ARG-325, AND SUBCELLULAR LOCATION.
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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-340, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=15782174; DOI=10.1038/nmeth715;
RA Ong S.E., Mittler G., Mann M.;
RT "Identifying and quantifying in vivo methylation sites by heavy methyl
RT SILAC.";
RL Nat. Methods 1:119-126(2004).
RN [14] {ECO:0000305}
RP ACETYLATION, AND INTERACTION WITH RNA.
RX PubMed=15021911; DOI=10.1038/sj.onc.1207484;
RA Babic I., Jakymiw A., Fujita D.J.;
RT "The RNA binding protein Sam68 is acetylated in tumor cell lines, and its
RT acetylation correlates with enhanced RNA binding activity.";
RL Oncogene 23:3781-3789(2004).
RN [15]
RP PHOSPHORYLATION AT TYR-435; TYR-440 AND TYR-443, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF TYR-435; TYR-440 AND TYR-443.
RX PubMed=16179349; DOI=10.1074/jbc.m505802200;
RA Lukong K.E., Larocque D., Tyner A.L., Richard S.;
RT "Tyrosine phosphorylation of sam68 by breast tumor kinase regulates
RT intranuclear localization and cell cycle progression.";
RL J. Biol. Chem. 280:38639-38647(2005).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [17]
RP IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; RBMX; NCOA5 AND PPP1CA.
RX PubMed=17890166; DOI=10.1016/j.bbapap.2007.07.015;
RA Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N.,
RA Glover M., Lamond A.I., Moorhead G.B.G.;
RT "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside
RT kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G.";
RL Biochim. Biophys. Acta 1774:1339-1350(2007).
RN [18]
RP FUNCTION, INTERACTION WITH HNRNPA1, PHOSPHORYLATION, AND MUTAGENESIS OF
RP VAL-229.
RX PubMed=17371836; DOI=10.1083/jcb.200701005;
RA Paronetto M.P., Achsel T., Massiello A., Chalfant C.E., Sette C.;
RT "The RNA-binding protein Sam68 modulates the alternative splicing of Bcl-
RT x.";
RL J. Cell Biol. 176:929-939(2007).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-29, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-175, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [25]
RP FUNCTION.
RX PubMed=20186123; DOI=10.1038/emboj.2010.19;
RA Pedrotti S., Bielli P., Paronetto M.P., Ciccosanti F., Fimia G.M.,
RA Stamm S., Manley J.L., Sette C.;
RT "The splicing regulator Sam68 binds to a novel exonic splicing silencer and
RT functions in SMN2 alternative splicing in spinal muscular atrophy.";
RL EMBO J. 29:1235-1247(2010).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP FUNCTION.
RX PubMed=21613532; DOI=10.1261/rna.2616111;
RA Coyle J.H., Bor Y.C., Rekosh D., Hammarskjold M.L.;
RT "The Tpr protein regulates export of mRNAs with retained introns that
RT traffic through the Nxf1 pathway.";
RL RNA 17:1344-1356(2011).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [30]
RP LACK OF FUNCTION IN UNSPLICED RNA EXPORT, AND LACK OF INTERACTION WITH TPR.
RX PubMed=22253824; DOI=10.1371/journal.pone.0029921;
RA Rajanala K., Nandicoori V.K.;
RT "Localization of nucleoporin Tpr to the nuclear pore complex is essential
RT for Tpr mediated regulation of the export of unspliced RNA.";
RL PLoS ONE 7:E29921-E29921(2012).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-20; SER-29; THR-33;
RP SER-150 AND THR-183, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [32]
RP INTERACTION WITH ZBTB7A, AND REGION.
RX PubMed=24514149; DOI=10.1002/embr.201338241;
RA Bielli P., Busa R., Di Stasi S.M., Munoz M.J., Botti F., Kornblihtt A.R.,
RA Sette C.;
RT "The transcription factor FBI-1 inhibits SAM68-mediated BCL-X alternative
RT splicing and apoptosis.";
RL EMBO Rep. 15:419-427(2014).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-58 AND SER-390, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [34]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-282; ARG-284; ARG-331 AND
RP ARG-340, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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).
RN [35]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [36]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [37]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [39]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [40]
RP RNA-BINDING, FUNCTION, SELF-ASSOCIATION, AND MUTAGENESIS OF TYR-241.
RX PubMed=26758068; DOI=10.1038/ncomms10355;
RA Feracci M., Foot J.N., Grellscheid S.N., Danilenko M., Stehle R.,
RA Gonchar O., Kang H.S., Dalgliesh C., Meyer N.H., Liu Y., Lahat A.,
RA Sattler M., Eperon I.C., Elliott D.J., Dominguez C.;
RT "Structural basis of RNA recognition and dimerization by the STAR proteins
RT T-STAR and Sam68.";
RL Nat. Commun. 7:10355-10355(2016).
RN [41]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-96; LYS-102; LYS-139; LYS-175 AND
RP LYS-432, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [42]
RP INTERACTION WITH SRMS, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=29496907; DOI=10.1074/mcp.ra118.000643;
RA Goel R.K., Paczkowska M., Reimand J., Napper S., Lukong K.E.;
RT "Phosphoproteomics analysis identifies novel candidate substrates of the
RT non-receptor tyrosine kinase, SRMS.";
RL Mol. Cell. Proteomics 17:925-947(2018).
RN [43]
RP STRUCTURE BY NMR OF 97-135, FUNCTION, SUBUNIT, AND MUTAGENESIS OF TYR-103;
RP GLU-110 AND PHE-118.
RX PubMed=20610388; DOI=10.1074/jbc.m110.126185;
RA Meyer N.H., Tripsianes K., Vincendeau M., Madl T., Kateb F.,
RA Brack-Werner R., Sattler M.;
RT "Structural basis for homodimerization of the Src-associated during
RT mitosis, 68-kDa protein (Sam68) Qua1 domain.";
RL J. Biol. Chem. 285:28893-28901(2010).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 365-419 IN COMPLEX WITH APC,
RP PHOSPHORYLATION AT TYR-387, AND MUTAGENESIS OF GLU-381; TYR-383 AND
RP GLU-384.
RX PubMed=22000517; DOI=10.1016/j.str.2011.07.013;
RA Morishita E.C., Murayama K., Kato-Murayama M., Ishizuka-Katsura Y.,
RA Tomabechi Y., Hayashi T., Terada T., Handa N., Shirouzu M., Akiyama T.,
RA Yokoyama S.;
RT "Crystal structures of the armadillo repeat domain of adenomatous polyposis
RT coli and its complex with the tyrosine-rich domain of Sam68.";
RL Structure 19:1496-1508(2011).
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. According to some authors, is not involved in the
CC nucleocytoplasmic export of unspliced (CTE)-containing RNA species
CC according to (PubMed:22253824). RNA-binding protein that plays a role
CC in the regulation of alternative splicing and influences mRNA splice
CC site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-
CC 3' as a bipartite motif spaced by more than 15 nucleotides. Binds
CC poly(A). Can regulate CD44 alternative splicing in a Ras pathway-
CC dependent manner (By similarity). In cooperation with HNRNPA1 modulates
CC alternative splicing of BCL2L1 by promoting splicing toward isoform
CC Bcl-X(S), and of SMN1 (PubMed:17371836, PubMed:20186123). Can regulate
CC alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6
CC containing the evolutionary conserved neurexin alternative spliced
CC segment 4 (AS4) involved in neurexin selective targeting to
CC postsynaptic partners. In a neuronal activity-dependent manner
CC cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1
CC exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is
CC antagonistic for regulation of NXRN3 alternative splicing at AS4 (By
CC similarity). {ECO:0000250|UniProtKB:Q60749,
CC ECO:0000269|PubMed:15021911, ECO:0000269|PubMed:17371836,
CC ECO:0000269|PubMed:20186123, ECO:0000269|PubMed:20610388,
CC ECO:0000269|PubMed:22253824, ECO:0000269|PubMed:26758068}.
CC -!- FUNCTION: Isoform 3, which is expressed in growth-arrested cells only,
CC inhibits S phase. {ECO:0000269|PubMed:9013542}.
CC -!- SUBUNIT: Self-associates to form homooligomers when bound to RNA,
CC oligomerization appears to be limited when binding to proteins;
CC dimerization increases RNA affinity (PubMed:26758068, PubMed:20610388).
CC Interacts with KHDRBS3/SLIM-2 (PubMed:10332027). Interacts with
CC KHDRBS2/SLIM-1; heterooligomer formation of KHDRBS family proteins may
CC modulate RNA substrate specificity (By similarity). Interacts with
CC RASA1, LCK, FYN, PTPN6, PLCG1, GRB2, CBL, JAK3, PIK3R, STAT3, APC,
CC HNRNPA1 (PubMed:1374686, PubMed:9045636, PubMed:10332027,
CC PubMed:11585385, PubMed:17371836, PubMed:22000517). Interacts with PTK6
CC (via SH3 and SH2 domains) (PubMed:10913193). Forms a complex with ILF2,
CC ILF3, YLPM1, RBMX, NCOA5 and PPP1CA (PubMed:17890166). Does not
CC interact with TPR (PubMed:22253824). Interacts with RBMY1A1, PRMT1 (By
CC similarity). Binds WBP4/FBP21 (via WW domains), FNBP4/FBP30 (via WW
CC domains). Interacts (via Arg/Gly-rich-flanked Pro-rich regions) with
CC FYN (via the SH3 domain) (By similarity). Interacts with the non-
CC receptor tyrosine kinase SRMS; the interaction leads to phosphorylation
CC of KHDRBS1 (PubMed:29496907). Interacts with ZBTB7A; negatively
CC regulates KHDRBS1 splicing activity toward BCL2L1 (PubMed:24514149).
CC {ECO:0000250|UniProtKB:Q60749, ECO:0000250|UniProtKB:Q91V33,
CC ECO:0000269|PubMed:10332027, ECO:0000269|PubMed:10913193,
CC ECO:0000269|PubMed:11585385, ECO:0000269|PubMed:1374686,
CC ECO:0000269|PubMed:17371836, ECO:0000269|PubMed:17890166,
CC ECO:0000269|PubMed:22000517, ECO:0000269|PubMed:24514149,
CC ECO:0000269|PubMed:29496907, ECO:0000269|PubMed:9045636}.
CC -!- INTERACTION:
CC Q07666; P25054: APC; NbExp=4; IntAct=EBI-1364, EBI-727707;
CC Q07666; P06241: FYN; NbExp=7; IntAct=EBI-1364, EBI-515315;
CC Q07666; P62993: GRB2; NbExp=8; IntAct=EBI-1364, EBI-401755;
CC Q07666; P08631: HCK; NbExp=4; IntAct=EBI-1364, EBI-346340;
CC Q07666; P09651: HNRNPA1; NbExp=9; IntAct=EBI-1364, EBI-352662;
CC Q07666; P61978: HNRNPK; NbExp=3; IntAct=EBI-1364, EBI-304185;
CC Q07666; P52333: JAK3; NbExp=2; IntAct=EBI-1364, EBI-518246;
CC Q07666; Q07666: KHDRBS1; NbExp=4; IntAct=EBI-1364, EBI-1364;
CC Q07666; P06239: LCK; NbExp=5; IntAct=EBI-1364, EBI-1348;
CC Q07666; P19174: PLCG1; NbExp=3; IntAct=EBI-1364, EBI-79387;
CC Q07666; P51531: SMARCA2; NbExp=2; IntAct=EBI-1364, EBI-679562;
CC Q07666; P12931: SRC; NbExp=3; IntAct=EBI-1364, EBI-621482;
CC Q07666; P40763: STAT3; NbExp=2; IntAct=EBI-1364, EBI-518675;
CC Q07666; P15498: VAV1; NbExp=3; IntAct=EBI-1364, EBI-625518;
CC Q07666; O95365: ZBTB7A; NbExp=9; IntAct=EBI-1364, EBI-2795384;
CC Q07666; P06240: Lck; Xeno; NbExp=2; IntAct=EBI-1364, EBI-1401;
CC Q07666; P23727: PIK3R1; Xeno; NbExp=2; IntAct=EBI-1364, EBI-520244;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1374686,
CC ECO:0000269|PubMed:29496907}. Cytoplasm {ECO:0000269|PubMed:29496907}.
CC Membrane {ECO:0000269|PubMed:1374686}. Note=Predominantly located in
CC the nucleus but also located partially in the cytoplasm.
CC {ECO:0000269|PubMed:29496907}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:1374686};
CC IsoId=Q07666-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q07666-2; Sequence=VSP_051719;
CC Name=3 {ECO:0000269|PubMed:9013542}; Synonyms=DeltaKH
CC {ECO:0000269|PubMed:9013542};
CC IsoId=Q07666-3; Sequence=VSP_051720;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissue examined.
CC Isoform 1 is expressed at lower levels in brain, skeletal muscle, and
CC liver whereas isoform 3 is intensified in skeletal muscle and in liver.
CC {ECO:0000269|PubMed:9013542}.
CC -!- DEVELOPMENTAL STAGE: Isoform 3 is only expressed in growth-arrested
CC cells. {ECO:0000269|PubMed:9013542}.
CC -!- DOMAIN: The KH domain is required for binding to RNA.
CC {ECO:0000250|UniProtKB:Q60749}.
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
CC (PubMed:29496907). Negatively correlates with ability to bind RNA but
CC required for many interactions with proteins. Phosphorylation by PTK6
CC negatively regulates its RNA binding ability. Phosphorylation by PTK6
CC at Tyr-440 dictates the nuclear localization of KHDRBS1.
CC Phosphorylation at Tyr-387 disrupts interaction with APC.
CC Phosphorylation at tyrosine residues by FYN inverts activity on
CC modulation of BCL2L1 alternative splicing.
CC {ECO:0000269|PubMed:11585385, ECO:0000269|PubMed:16179349,
CC ECO:0000269|PubMed:17371836, ECO:0000269|PubMed:22000517,
CC ECO:0000269|PubMed:29496907, ECO:0000269|PubMed:9045636}.
CC -!- PTM: Acetylated. Positively correlates with ability to bind RNA.
CC {ECO:0000269|PubMed:15021911}.
CC -!- PTM: Arginine methylation is required for nuclear localization. Also
CC can affect interaction with other proteins. Inhibits interaction with
CC Src-like SH3 domains, but not interaction with WW domains of WBP4/FBP21
CC AND FNBP4/FBP30. {ECO:0000269|PubMed:12529443,
CC ECO:0000269|PubMed:1374686, ECO:0000269|Ref.7}.
CC -!- SIMILARITY: Belongs to the KHDRBS family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10132.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; M88108; AAA59990.1; -; mRNA.
DR EMBL; U78971; AAB47504.1; -; mRNA.
DR EMBL; AK091346; BAC03643.1; -; mRNA.
DR EMBL; AL139249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07576.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07577.1; -; Genomic_DNA.
DR EMBL; BC000717; AAH00717.1; -; mRNA.
DR EMBL; BC010132; AAH10132.1; ALT_SEQ; mRNA.
DR EMBL; BC019109; AAH19109.1; -; mRNA.
DR CCDS; CCDS350.1; -. [Q07666-1]
DR CCDS; CCDS60067.1; -. [Q07666-3]
DR PIR; A38219; A38219.
DR RefSeq; NP_001258807.1; NM_001271878.1. [Q07666-3]
DR RefSeq; NP_006550.1; NM_006559.2. [Q07666-1]
DR PDB; 2XA6; NMR; -; A/B=97-135.
DR PDB; 3QHE; X-ray; 2.40 A; B/D=365-419.
DR PDBsum; 2XA6; -.
DR PDBsum; 3QHE; -.
DR AlphaFoldDB; Q07666; -.
DR BMRB; Q07666; -.
DR SMR; Q07666; -.
DR BioGRID; 115900; 284.
DR CORUM; Q07666; -.
DR DIP; DIP-29007N; -.
DR IntAct; Q07666; 152.
DR MINT; Q07666; -.
DR STRING; 9606.ENSP00000313829; -.
DR GlyGen; Q07666; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q07666; -.
DR MetOSite; Q07666; -.
DR PhosphoSitePlus; Q07666; -.
DR SwissPalm; Q07666; -.
DR BioMuta; KHDRBS1; -.
DR DMDM; 62511098; -.
DR EPD; Q07666; -.
DR jPOST; Q07666; -.
DR MassIVE; Q07666; -.
DR MaxQB; Q07666; -.
DR PaxDb; Q07666; -.
DR PeptideAtlas; Q07666; -.
DR PRIDE; Q07666; -.
DR ProteomicsDB; 58523; -. [Q07666-1]
DR ProteomicsDB; 58524; -. [Q07666-2]
DR ProteomicsDB; 58525; -. [Q07666-3]
DR TopDownProteomics; Q07666-1; -. [Q07666-1]
DR TopDownProteomics; Q07666-3; -. [Q07666-3]
DR Antibodypedia; 3944; 338 antibodies from 38 providers.
DR DNASU; 10657; -.
DR Ensembl; ENST00000327300.12; ENSP00000313829.7; ENSG00000121774.18. [Q07666-1]
DR Ensembl; ENST00000492989.1; ENSP00000417731.1; ENSG00000121774.18. [Q07666-3]
DR GeneID; 10657; -.
DR KEGG; hsa:10657; -.
DR MANE-Select; ENST00000327300.12; ENSP00000313829.7; NM_006559.3; NP_006550.1.
DR UCSC; uc001bua.3; human. [Q07666-1]
DR CTD; 10657; -.
DR DisGeNET; 10657; -.
DR GeneCards; KHDRBS1; -.
DR HGNC; HGNC:18116; KHDRBS1.
DR HPA; ENSG00000121774; Low tissue specificity.
DR MIM; 602489; gene.
DR neXtProt; NX_Q07666; -.
DR OpenTargets; ENSG00000121774; -.
DR PharmGKB; PA30092; -.
DR VEuPathDB; HostDB:ENSG00000121774; -.
DR eggNOG; KOG1588; Eukaryota.
DR GeneTree; ENSGT00940000155718; -.
DR HOGENOM; CLU_034976_0_0_1; -.
DR InParanoid; Q07666; -.
DR OMA; TPYREHP; -.
DR OrthoDB; 1012406at2759; -.
DR PhylomeDB; Q07666; -.
DR TreeFam; TF314878; -.
DR PathwayCommons; Q07666; -.
DR Reactome; R-HSA-8849468; PTK6 Regulates Proteins Involved in RNA Processing.
DR SignaLink; Q07666; -.
DR SIGNOR; Q07666; -.
DR BioGRID-ORCS; 10657; 48 hits in 1085 CRISPR screens.
DR ChiTaRS; KHDRBS1; human.
DR EvolutionaryTrace; Q07666; -.
DR GeneWiki; KHDRBS1; -.
DR GenomeRNAi; 10657; -.
DR Pharos; Q07666; Tbio.
DR PRO; PR:Q07666; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q07666; protein.
DR Bgee; ENSG00000121774; Expressed in germinal epithelium of ovary and 206 other tissues.
DR Genevisible; Q07666; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070618; C:Grb2-Sos complex; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IDA:MGI.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IDA:UniProtKB.
DR GO; GO:0035591; F:signaling adaptor activity; IDA:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:GO_Central.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0045948; P:positive regulation of translational initiation; IDA:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0046831; P:regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
DR DisProt; DP01705; -.
DR Gene3D; 3.30.1370.10; -; 1.
DR IDEAL; IID00619; -.
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 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Membrane; Methylation;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW SH3-binding; 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_0000050124"
FT DOMAIN 171..197
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..260
FT /note="Involved in homodimerization"
FT /evidence="ECO:0000305|PubMed:26758068"
FT REGION 280..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..443
FT /note="Interaction with HNRNPA1"
FT /evidence="ECO:0000269|PubMed:17371836"
FT REGION 400..420
FT /note="Interaction with ZBTB7A"
FT /evidence="ECO:0000269|PubMed:24514149"
FT REGION 411..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 45
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:12529443"
FT MOD_RES 52
FT /note="Asymmetric dimethylarginine; partial; by PRMT1"
FT /evidence="ECO:0000269|PubMed:12529443"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 84
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q60749"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60749"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 175
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
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:0000250|UniProtKB:Q60749"
FT MOD_RES 304
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:12529443"
FT MOD_RES 310
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:12529443"
FT MOD_RES 315
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:12529443"
FT MOD_RES 320
FT /note="Dimethylated arginine; in A2780 ovarian carcinoma
FT cell line"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 320
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:12529443"
FT MOD_RES 325
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:12529443"
FT MOD_RES 331
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60749"
FT MOD_RES 331
FT /note="Dimethylated arginine; in A2780 ovarian carcinoma
FT cell line"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 331
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:24129315"
FT MOD_RES 340
FT /note="Dimethylated arginine; in A2780 ovarian carcinoma
FT cell line"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 340
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0007744|PubMed:15782174,
FT ECO:0007744|PubMed:24129315"
FT MOD_RES 387
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:22000517"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 435
FT /note="Phosphotyrosine; by PTK6"
FT /evidence="ECO:0000269|PubMed:16179349"
FT MOD_RES 440
FT /note="Phosphotyrosine; by PTK6"
FT /evidence="ECO:0000269|PubMed:16179349"
FT MOD_RES 443
FT /note="Phosphotyrosine; by PTK6"
FT /evidence="ECO:0000269|PubMed:16179349"
FT CROSSLNK 96
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 432
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 37..61
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_051719"
FT VAR_SEQ 169..207
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9013542"
FT /id="VSP_051720"
FT MUTAGEN 103
FT /note="Y->S: Impairs homodimerization."
FT /evidence="ECO:0000269|PubMed:20610388"
FT MUTAGEN 110
FT /note="E->A: Impairs homodimerization."
FT /evidence="ECO:0000269|PubMed:20610388"
FT MUTAGEN 118
FT /note="F->S: Disrupts homodimerization, impairs influence
FT on alternative splicing."
FT /evidence="ECO:0000269|PubMed:20610388"
FT MUTAGEN 229
FT /note="V->F: Disrupts binding to poly(A). Decreased binding
FT to the BCL2L1 mRNA. Loss of function in BCL2L1 splicing.
FT Changed nuclear localization."
FT /evidence="ECO:0000269|PubMed:17371836"
FT MUTAGEN 241
FT /note="Y->E: Fails to influence alternative splicing of
FT CD44, NRXN2 and NRXN3."
FT /evidence="ECO:0000269|PubMed:26758068"
FT MUTAGEN 381
FT /note="E->K: Disrupts interaction with APC."
FT /evidence="ECO:0000269|PubMed:22000517"
FT MUTAGEN 383
FT /note="Y->K: Impairs interaction with APC."
FT /evidence="ECO:0000269|PubMed:22000517"
FT MUTAGEN 384
FT /note="E->K: Disrupts interaction with APC."
FT /evidence="ECO:0000269|PubMed:22000517"
FT MUTAGEN 435
FT /note="Y->F: No effect on the nuclear localization."
FT /evidence="ECO:0000269|PubMed:16179349"
FT MUTAGEN 440
FT /note="Y->F: Completely blocks nuclear localization."
FT /evidence="ECO:0000269|PubMed:16179349"
FT MUTAGEN 443
FT /note="Y->F: No effect on the nuclear localization."
FT /evidence="ECO:0000269|PubMed:16179349"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:2XA6"
FT HELIX 119..134
FT /evidence="ECO:0007829|PDB:2XA6"
SQ SEQUENCE 443 AA; 48227 MW; 59FB4DB6FB4DBE98 CRC64;
MQRRDDPAAR MSRSSGRSGS MDPSGAHPSV RQTPSRQPPL PHRSRGGGGG SRGGARASPA
TQPPPLLPPS ATGPDATVGG PAPTPLLPPS ATASVKMEPE NKYLPELMAE KDSLDPSFTH
AMQLLTAEIE KIQKGDSKKD DEENYLDLFS HKNMKLKERV LIPVKQYPKF NFVGKILGPQ
GNTIKRLQEE TGAKISVLGK GSMRDKAKEE ELRKGGDPKY AHLNMDLHVF IEVFGPPCEA
YALMAHAMEE VKKFLVPDMM DDICQEQFLE LSYLNGVPEP SRGRGVPVRG RGAAPPPPPV
PRGRGVGPPR GALVRGTPVR GAITRGATVT RGVPPPPTVR GAPAPRARTA GIQRIPLPPP
PAPETYEEYG YDDTYAEQSY EGYEGYYSQS QGDSEYYDYG HGEVQDSYEA YGQDDWNGTR
PSLKAPPARP VKGAYREHPY GRY
