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KH domain-containing, RNA-binding, signal transduction-associated protein 1 (GAP-associated tyrosine phosphoprotein p62) (Src-associated in mitosis 68 kDa protein) (Sam68) (p21 Ras GTPase-activating protein-associated p62) (p68)

 KHDR1_HUMAN             Reviewed;         443 AA.
Q07666; D3DPP3; Q6PJX7; Q8NB97; Q99760;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 179.
RecName: Full=KH domain-containing, RNA-binding, signal transduction-associated protein 1;
AltName: Full=GAP-associated tyrosine phosphoprotein p62;
AltName: Full=Src-associated in mitosis 68 kDa protein;
Short=Sam68;
AltName: Full=p21 Ras GTPase-activating protein-associated p62;
AltName: Full=p68;
Name=KHDRBS1 {ECO:0000312|HGNC:HGNC:18116};
Synonyms=SAM68 {ECO:0000303|PubMed:1374686};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAA59990.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RNA-BINDING, METHYLATION, AND INTERACTION WITH RASA1.
TISSUE=Fetal brain {ECO:0000312|EMBL:AAA59990.1};
PubMed=1374686; DOI=10.1016/0092-8674(92)90455-L;
Wong G., Muller O., Clark R., Conroy L., Moran M.F., Polakis P.,
McCormick F.;
"Molecular cloning and nucleic acid binding properties of the GAP-
associated tyrosine phosphoprotein p62.";
Cell 69:551-558(1992).
[2] {ECO:0000305, ECO:0000312|EMBL:AAB47504.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY,
AND DEVELOPMENTAL STAGE.
TISSUE=Placenta {ECO:0000269|PubMed:9013542};
PubMed=9013542; DOI=10.1074/jbc.272.6.3129;
Barlat I., Maurier F., Duchesne M., Guitard E., Tocque B.,
Schweighoffer F.;
"A role for Sam68 in cell cycle progression antagonized by a spliced
variant within the KH domain.";
J. Biol. Chem. 272:3129-3132(1997).
[3] {ECO:0000305, ECO:0000312|EMBL:BAC03643.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain {ECO:0000312|EMBL:BAC03643.1};
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4] {ECO:0000305, ECO:0000312|EMBL:CAH71945.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305, ECO:0000312|EMBL:AAH00717.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph {ECO:0000312|EMBL:AAH19109.1}, and
Placenta {ECO:0000312|EMBL:AAH00717.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 18-31; 57-96; 103-131; 139-152; 176-185; 292-302
AND 316-340, METHYLATION AT ARG-320; ARG-331 AND ARG-340, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[8] {ECO:0000305}
PROTEIN SEQUENCE OF 102-110 AND 169-175 (ISOFORMS 1/2), FUNCTION,
PHOSPHORYLATION, AND INTERACTION WITH LCK; FYN; PTPN6; PLCG1; GRB2;
CBL; JAK3 AND PIK3R1.
PubMed=9045636; DOI=10.1074/jbc.272.10.6214;
Fusaki N., Iwamatsu A., Iwashima M., Fujisawa J.;
"Interaction between Sam68 and Src family tyrosine kinases, Fyn and
Lck, in T cell receptor signaling.";
J. Biol. Chem. 272:6214-6219(1997).
[9] {ECO:0000305}
INTERACTION WITH KHDRBS3.
TISSUE=Testis {ECO:0000269|PubMed:10332027};
PubMed=10332027; DOI=10.1093/hmg/8.6.959;
Venables J.P., Vernet C., Chew S.L., Elliott D.J., Cowmeadow R.B.,
Wu J., Cooke H.J., Artzt K., Eperon I.C.;
"T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-
binding protein implicated in spermatogenesis.";
Hum. Mol. Genet. 8:959-969(1999).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH PTK6.
PubMed=10913193; DOI=10.1128/MCB.20.16.6114-6126.2000;
Derry J.J., Richard S., Valderrama Carvajal H., Ye X., Vasioukhin V.,
Cochrane A.W., Chen T., Tyner A.L.;
"Sik (BRK) phosphorylates Sam68 in the nucleus and negatively
regulates its RNA binding ability.";
Mol. Cell. Biol. 20:6114-6126(2000).
[11] {ECO:0000305}
FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH STAT3.
PubMed=11585385; DOI=10.1006/cimm.2001.1815;
Sanchez-Margalet V., Martin-Romero C.;
"Human leptin signaling in human peripheral blood mononuclear cells:
activation of the JAK-STAT pathway.";
Cell. Immunol. 211:30-36(2001).
[12] {ECO:0000305}
METHYLATION AT ARG-45; ARG-52; ARG-304; ARG-310; ARG-315; ARG-320 AND
ARG-325, AND SUBCELLULAR LOCATION.
PubMed=12529443; DOI=10.1091/mbc.E02-08-0484;
Cote J., Boisvert F.-M., Boulanger M.-C., Bedford M.T., Richard S.;
"Sam68 RNA binding protein is an in vivo substrate for protein
arginine N-methyltransferase 1.";
Mol. Biol. Cell 14:274-287(2003).
[13]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-340, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=15782174; DOI=10.1038/nmeth715;
Ong S.E., Mittler G., Mann M.;
"Identifying and quantifying in vivo methylation sites by heavy methyl
SILAC.";
Nat. Methods 1:119-126(2004).
[14] {ECO:0000305}
ACETYLATION, AND INTERACTION WITH RNA.
PubMed=15021911; DOI=10.1038/sj.onc.1207484;
Babic I., Jakymiw A., Fujita D.J.;
"The RNA binding protein Sam68 is acetylated in tumor cell lines, and
its acetylation correlates with enhanced RNA binding activity.";
Oncogene 23:3781-3789(2004).
[15]
PHOSPHORYLATION AT TYR-435; TYR-440 AND TYR-443, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF TYR-435; TYR-440 AND TYR-443.
PubMed=16179349; DOI=10.1074/jbc.M505802200;
Lukong K.E., Larocque D., Tyner A.L., Richard S.;
"Tyrosine phosphorylation of sam68 by breast tumor kinase regulates
intranuclear localization and cell cycle progression.";
J. Biol. Chem. 280:38639-38647(2005).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[17]
IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; RBMX; NCOA5 AND
PPP1CA.
PubMed=17890166; DOI=10.1016/j.bbapap.2007.07.015;
Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K.,
Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.;
"The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative
nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-
G.";
Biochim. Biophys. Acta 1774:1339-1350(2007).
[18]
FUNCTION, INTERACTION WITH HNRNPA1, PHOSPHORYLATION, AND MUTAGENESIS
OF VAL-229.
PubMed=17371836; DOI=10.1083/jcb.200701005;
Paronetto M.P., Achsel T., Massiello A., Chalfant C.E., Sette C.;
"The RNA-binding protein Sam68 modulates the alternative splicing of
Bcl-x.";
J. Cell Biol. 176:929-939(2007).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-29, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-175, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[25]
FUNCTION.
PubMed=20186123; DOI=10.1038/emboj.2010.19;
Pedrotti S., Bielli P., Paronetto M.P., Ciccosanti F., Fimia G.M.,
Stamm S., Manley J.L., Sette C.;
"The splicing regulator Sam68 binds to a novel exonic splicing
silencer and functions in SMN2 alternative splicing in spinal muscular
atrophy.";
EMBO J. 29:1235-1247(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
FUNCTION.
PubMed=21613532; DOI=10.1261/rna.2616111;
Coyle J.H., Bor Y.C., Rekosh D., Hammarskjold M.L.;
"The Tpr protein regulates export of mRNAs with retained introns that
traffic through the Nxf1 pathway.";
RNA 17:1344-1356(2011).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[30]
LACK OF FUNCTION IN UNSPLICED RNA EXPORT, AND LACK OF INTERACTION WITH
TPR.
PubMed=22253824; DOI=10.1371/journal.pone.0029921;
Rajanala K., Nandicoori V.K.;
"Localization of nucleoporin Tpr to the nuclear pore complex is
essential for Tpr mediated regulation of the export of unspliced
RNA.";
PLoS ONE 7:E29921-E29921(2012).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-20; SER-29;
THR-33; SER-150 AND THR-183, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-58 AND SER-390,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[33]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-282; ARG-284; ARG-331 AND
ARG-340, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[34]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[35]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[36]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[37]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[39]
RNA-BINDING, FUNCTION, SELF-ASSOCIATION, AND MUTAGENESIS OF TYR-241.
PubMed=26758068; DOI=10.1038/ncomms10355;
Feracci M., Foot J.N., Grellscheid S.N., Danilenko M., Stehle R.,
Gonchar O., Kang H.S., Dalgliesh C., Meyer N.H., Liu Y., Lahat A.,
Sattler M., Eperon I.C., Elliott D.J., Dominguez C.;
"Structural basis of RNA recognition and dimerization by the STAR
proteins T-STAR and Sam68.";
Nat. Commun. 7:10355-10355(2016).
[40]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-96; LYS-102; LYS-139;
LYS-175 AND LYS-432, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[41]
STRUCTURE BY NMR OF 97-135, FUNCTION, SUBUNIT, AND MUTAGENESIS OF
TYR-103; GLU-110 AND PHE-118.
PubMed=20610388; DOI=10.1074/jbc.M110.126185;
Meyer N.H., Tripsianes K., Vincendeau M., Madl T., Kateb F.,
Brack-Werner R., Sattler M.;
"Structural basis for homodimerization of the Src-associated during
mitosis, 68-kDa protein (Sam68) Qua1 domain.";
J. Biol. Chem. 285:28893-28901(2010).
[42]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 365-419 IN COMPLEX WITH APC,
PHOSPHORYLATION AT TYR-387, AND MUTAGENESIS OF GLU-381; TYR-383 AND
GLU-384.
PubMed=22000517; DOI=10.1016/j.str.2011.07.013;
Morishita E.C., Murayama K., Kato-Murayama M., Ishizuka-Katsura Y.,
Tomabechi Y., Hayashi T., Terada T., Handa N., Shirouzu M.,
Akiyama T., Yokoyama S.;
"Crystal structures of the armadillo repeat domain of adenomatous
polyposis coli and its complex with the tyrosine-rich domain of
Sam68.";
Structure 19:1496-1508(2011).
-!- FUNCTION: 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 (By similarity). 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).
{ECO:0000250|UniProtKB:Q60749, ECO:0000269|PubMed:15021911,
ECO:0000269|PubMed:17371836, ECO:0000269|PubMed:20186123,
ECO:0000269|PubMed:20610388, ECO:0000269|PubMed:22253824,
ECO:0000269|PubMed:26758068}.
-!- FUNCTION: Isoform 3, which is expressed in growth-arrested cells
only, inhibits S phase. {ECO:0000269|PubMed:9013542}.
-!- SUBUNIT: Self-associates to form homooligomers when bound to RNA,
oligomerization appears to be limited when binding to proteins;
dimerization increases RNA affinity (PubMed:26758068,
PubMed:20610388). 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:1374686,
PubMed:9045636, PubMed:10332027, PubMed:11585385, PubMed:17371836,
PubMed:22000517). 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 RBMY1A1, 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).
{ECO:0000250|UniProtKB:Q60749, ECO:0000250|UniProtKB:Q91V33,
ECO:0000269|PubMed:10332027, ECO:0000269|PubMed:10913193,
ECO:0000269|PubMed:11585385, ECO:0000269|PubMed:1374686,
ECO:0000269|PubMed:17371836, ECO:0000269|PubMed:17890166,
ECO:0000269|PubMed:22000517, ECO:0000269|PubMed:9045636}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-1364, EBI-1364;
P25054:APC; NbExp=3; IntAct=EBI-1364, EBI-727707;
P06241:FYN; NbExp=4; IntAct=EBI-1364, EBI-515315;
P62993:GRB2; NbExp=8; IntAct=EBI-1364, EBI-401755;
P08631:HCK; NbExp=4; IntAct=EBI-1364, EBI-346340;
P09651:HNRNPA1; NbExp=9; IntAct=EBI-1364, EBI-352662;
P52333:JAK3; NbExp=2; IntAct=EBI-1364, EBI-518246;
P06239:LCK; NbExp=5; IntAct=EBI-1364, EBI-1348;
P06240:Lck (xeno); NbExp=2; IntAct=EBI-1364, EBI-1401;
P23727:PIK3R1 (xeno); NbExp=2; IntAct=EBI-1364, EBI-520244;
P19174:PLCG1; NbExp=2; IntAct=EBI-1364, EBI-79387;
P51531:SMARCA2; NbExp=2; IntAct=EBI-1364, EBI-679562;
P12931:SRC; NbExp=3; IntAct=EBI-1364, EBI-621482;
P40763:STAT3; NbExp=2; IntAct=EBI-1364, EBI-518675;
P15498:VAV1; NbExp=3; IntAct=EBI-1364, EBI-625518;
O95365:ZBTB7A; NbExp=9; IntAct=EBI-1364, EBI-2795384;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1374686}.
Membrane {ECO:0000269|PubMed:1374686}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1 {ECO:0000269|PubMed:1374686};
IsoId=Q07666-1; Sequence=Displayed;
Name=2 {ECO:0000305};
IsoId=Q07666-2; Sequence=VSP_051719;
Note=No experimental confirmation available. {ECO:0000305};
Name=3 {ECO:0000269|PubMed:9013542}; Synonyms=DeltaKH
{ECO:0000269|PubMed:9013542};
IsoId=Q07666-3; Sequence=VSP_051720;
-!- TISSUE SPECIFICITY: 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. {ECO:0000269|PubMed:9013542}.
-!- DEVELOPMENTAL STAGE: Isoform 3 is only expressed in growth-
arrested cells. {ECO:0000269|PubMed:9013542}.
-!- DOMAIN: The KH domain is required for binding to RNA.
{ECO:0000250|UniProtKB:Q60749}.
-!- DOMAIN: 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).
{ECO:0000250}.
-!- PTM: Tyrosine phosphorylated by several non-receptor tyrosine
kinases, LCK, FYN and JAK3. 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 nulear
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.
{ECO:0000269|PubMed:11585385, ECO:0000269|PubMed:16179349,
ECO:0000269|PubMed:17371836, ECO:0000269|PubMed:22000517,
ECO:0000269|PubMed:9045636}.
-!- PTM: Acetylated. Positively correlates with ability to bind RNA.
{ECO:0000269|PubMed:15021911}.
-!- PTM: 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.
{ECO:0000269|PubMed:12529443, ECO:0000269|PubMed:1374686,
ECO:0000269|Ref.7}.
-!- SIMILARITY: Belongs to the KHDRBS family. {ECO:0000255}.
-!- SEQUENCE CAUTION:
Sequence=AAH10132.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M88108; AAA59990.1; -; mRNA.
EMBL; U78971; AAB47504.1; -; mRNA.
EMBL; AK091346; BAC03643.1; -; mRNA.
EMBL; AL139249; CAI21971.1; -; Genomic_DNA.
EMBL; AL445248; CAI21971.1; JOINED; Genomic_DNA.
EMBL; AL139249; CAI21972.1; -; Genomic_DNA.
EMBL; AL445248; CAI21972.1; JOINED; Genomic_DNA.
EMBL; AL445248; CAH71944.1; -; Genomic_DNA.
EMBL; AL139249; CAH71944.1; JOINED; Genomic_DNA.
EMBL; AL445248; CAH71945.1; -; Genomic_DNA.
EMBL; AL139249; CAH71945.1; JOINED; Genomic_DNA.
EMBL; CH471059; EAX07576.1; -; Genomic_DNA.
EMBL; CH471059; EAX07577.1; -; Genomic_DNA.
EMBL; BC000717; AAH00717.1; -; mRNA.
EMBL; BC010132; AAH10132.1; ALT_SEQ; mRNA.
EMBL; BC019109; AAH19109.1; -; mRNA.
CCDS; CCDS350.1; -. [Q07666-1]
CCDS; CCDS60067.1; -. [Q07666-3]
PIR; A38219; A38219.
RefSeq; NP_001258807.1; NM_001271878.1. [Q07666-3]
RefSeq; NP_006550.1; NM_006559.2. [Q07666-1]
UniGene; Hs.445893; -.
PDB; 2XA6; NMR; -; A/B=97-135.
PDB; 3QHE; X-ray; 2.40 A; B/D=365-419.
PDBsum; 2XA6; -.
PDBsum; 3QHE; -.
ProteinModelPortal; Q07666; -.
SMR; Q07666; -.
BioGrid; 115900; 171.
CORUM; Q07666; -.
DIP; DIP-29007N; -.
IntAct; Q07666; 81.
MINT; MINT-102826; -.
STRING; 9606.ENSP00000313829; -.
iPTMnet; Q07666; -.
PhosphoSitePlus; Q07666; -.
SwissPalm; Q07666; -.
DMDM; 62511098; -.
EPD; Q07666; -.
MaxQB; Q07666; -.
PaxDb; Q07666; -.
PeptideAtlas; Q07666; -.
PRIDE; Q07666; -.
TopDownProteomics; Q07666-1; -. [Q07666-1]
TopDownProteomics; Q07666-3; -. [Q07666-3]
DNASU; 10657; -.
Ensembl; ENST00000327300; ENSP00000313829; ENSG00000121774. [Q07666-1]
Ensembl; ENST00000492989; ENSP00000417731; ENSG00000121774. [Q07666-3]
GeneID; 10657; -.
KEGG; hsa:10657; -.
UCSC; uc001bua.3; human. [Q07666-1]
CTD; 10657; -.
DisGeNET; 10657; -.
EuPathDB; HostDB:ENSG00000121774.17; -.
GeneCards; KHDRBS1; -.
HGNC; HGNC:18116; KHDRBS1.
HPA; CAB005355; -.
HPA; HPA051280; -.
HPA; HPA056813; -.
MIM; 602489; gene.
neXtProt; NX_Q07666; -.
OpenTargets; ENSG00000121774; -.
PharmGKB; PA30092; -.
eggNOG; KOG1588; Eukaryota.
eggNOG; COG5176; LUCA.
GeneTree; ENSGT00550000074434; -.
HOGENOM; HOG000230771; -.
HOVERGEN; HBG079164; -.
InParanoid; Q07666; -.
KO; K13198; -.
OMA; FLFPDMM; -.
OrthoDB; EOG091G0EED; -.
PhylomeDB; Q07666; -.
TreeFam; TF314878; -.
Reactome; R-HSA-8849468; PTK6 Regulates Proteins Involved in RNA Processing.
SignaLink; Q07666; -.
SIGNOR; Q07666; -.
ChiTaRS; KHDRBS1; human.
EvolutionaryTrace; Q07666; -.
GeneWiki; KHDRBS1; -.
GenomeRNAi; 10657; -.
PMAP-CutDB; Q07666; -.
PRO; PR:Q07666; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000121774; -.
CleanEx; HS_KHDRBS1; -.
Genevisible; Q07666; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070618; C:Grb2-Sos complex; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0008143; F:poly(A) binding; IDA:MGI.
GO; GO:0008266; F:poly(U) RNA binding; IDA:MGI.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0005070; F:SH3/SH2 adaptor activity; IPI:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0046833; P:positive regulation of RNA export from nucleus; IDA:UniProtKB.
GO; GO:0045948; P:positive regulation of translational initiation; IDA:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB.
GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
GO; GO:0046831; P:regulation of RNA export from nucleus; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.1370.10; -; 1.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
InterPro; IPR032571; Qua1_dom.
InterPro; IPR032335; Sam68-YY.
Pfam; PF00013; KH_1; 1.
Pfam; PF16274; Qua1; 1.
Pfam; PF16568; Sam68-YY; 1.
SMART; SM00322; KH; 1.
SUPFAM; SSF54791; SSF54791; 1.
PROSITE; PS50084; KH_TYPE_1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Complete proteome; Direct protein sequencing; Isopeptide bond;
Membrane; Methylation; mRNA processing; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; SH3-binding; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 443 KH domain-containing, RNA-binding, signal
transduction-associated protein 1.
/FTId=PRO_0000050124.
DOMAIN 171 197 KH. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
REGION 100 260 Involved in homodimerization.
{ECO:0000305|PubMed:26758068}.
REGION 351 443 Interaction with HNRNPA1.
{ECO:0000269|PubMed:17371836}.
COMPBIAS 34 41 Pro-rich. {ECO:0000255}.
COMPBIAS 44 55 DMA/Gly-rich. {ECO:0000255}.
COMPBIAS 59 89 Pro-rich. {ECO:0000255}.
COMPBIAS 282 292 DMA/Gly-rich. {ECO:0000255}.
COMPBIAS 295 301 Pro-rich. {ECO:0000255}.
COMPBIAS 302 332 Arg/Gly-rich. {ECO:0000255}.
COMPBIAS 334 363 Pro-rich. {ECO:0000255}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 33 33 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 45 45 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000269|PubMed:12529443}.
MOD_RES 52 52 Asymmetric dimethylarginine; partial; by
PRMT1. {ECO:0000269|PubMed:12529443}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:24275569}.
MOD_RES 84 84 Phosphothreonine; by MAPK1.
{ECO:0000250|UniProtKB:Q60749}.
MOD_RES 113 113 Phosphoserine.
{ECO:0000250|UniProtKB:Q60749}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 175 175 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 183 183 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 282 282 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 284 284 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 291 291 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q60749}.
MOD_RES 304 304 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000269|PubMed:12529443}.
MOD_RES 310 310 Omega-N-methylarginine; by PRMT1.
{ECO:0000269|PubMed:12529443}.
MOD_RES 315 315 Omega-N-methylarginine; by PRMT1.
{ECO:0000269|PubMed:12529443}.
MOD_RES 320 320 Dimethylated arginine; in A2780 ovarian
carcinoma cell line. {ECO:0000269|Ref.7}.
MOD_RES 320 320 Omega-N-methylarginine; by PRMT1.
{ECO:0000269|PubMed:12529443}.
MOD_RES 325 325 Omega-N-methylarginine; by PRMT1.
{ECO:0000269|PubMed:12529443}.
MOD_RES 331 331 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q60749}.
MOD_RES 331 331 Dimethylated arginine; in A2780 ovarian
carcinoma cell line. {ECO:0000269|Ref.7}.
MOD_RES 331 331 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 331 331 Omega-N-methylated arginine; by PRMT1;
alternate. {ECO:0000269|Ref.7}.
MOD_RES 340 340 Dimethylated arginine; in A2780 ovarian
carcinoma cell line. {ECO:0000269|Ref.7}.
MOD_RES 340 340 Omega-N-methylarginine; by PRMT1.
{ECO:0000244|PubMed:15782174,
ECO:0000244|PubMed:24129315}.
MOD_RES 387 387 Phosphotyrosine.
{ECO:0000305|PubMed:22000517}.
MOD_RES 390 390 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 435 435 Phosphotyrosine; by PTK6.
{ECO:0000269|PubMed:16179349}.
MOD_RES 440 440 Phosphotyrosine; by PTK6.
{ECO:0000269|PubMed:16179349}.
MOD_RES 443 443 Phosphotyrosine; by PTK6.
{ECO:0000269|PubMed:16179349}.
CROSSLNK 96 96 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 102 102 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 139 139 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 175 175 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 432 432 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 37 61 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_051719.
VAR_SEQ 169 207 Missing (in isoform 3).
{ECO:0000303|PubMed:9013542}.
/FTId=VSP_051720.
MUTAGEN 103 103 Y->S: Impairs homodimerization.
{ECO:0000269|PubMed:20610388}.
MUTAGEN 110 110 E->A: Impairs homodimerization.
{ECO:0000269|PubMed:20610388}.
MUTAGEN 118 118 F->S: Disrupts homodimerization, impairs
influence on alternative splicing.
{ECO:0000269|PubMed:20610388}.
MUTAGEN 229 229 V->F: Disrupts binding to poly(A),
impairs interaction with BCL2L1
modulation of BCL2L1 alternative
splicing. {ECO:0000269|PubMed:17371836}.
MUTAGEN 241 241 Y->E: Fails to influence alternative
splicing of CD44, NRXN2 and NRXN3.
{ECO:0000269|PubMed:26758068}.
MUTAGEN 381 381 E->K: Disrupts interaction with APC.
{ECO:0000269|PubMed:22000517}.
MUTAGEN 383 383 Y->K: Impairs interaction with APC.
{ECO:0000269|PubMed:22000517}.
MUTAGEN 384 384 E->K: Disrupts interaction with APC.
{ECO:0000269|PubMed:22000517}.
MUTAGEN 435 435 Y->F: No effect on the nuclear
localization.
{ECO:0000269|PubMed:16179349}.
MUTAGEN 440 440 Y->F: Completely blocks nuclear
localization.
{ECO:0000269|PubMed:16179349}.
MUTAGEN 443 443 Y->F: No effect on the nuclear
localization.
{ECO:0000269|PubMed:16179349}.
HELIX 100 113 {ECO:0000244|PDB:2XA6}.
HELIX 119 134 {ECO:0000244|PDB:2XA6}.
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


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18-661-15005 KH domain-containing. RNA-binding. signal transduction-associated protein 1 - p21 Ras GTPase-activating protein-associated p62; GAP-associated tyrosine phosphoprotein p62; Src-associated in mitosis 68 0.1 mg
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EIAAB34704 ARHGAP27,CAMGAP1,CIN85-associated multi-domain-containing Rho GTPase-activating protein 1,Homo sapiens,Human,PP905,Rho GTPase-activating protein 27,Rho-type GTPase-activating protein 27,SH3 domain-con
EIAAB34703 Arhgap27,Camgap1,CIN85-associated multi-domain-containing Rho GTPase-activating protein 1,Mouse,Mus musculus,Rho GTPase-activating protein 27,Rho-type GTPase-activating protein 27
EIAAB34705 Arhgap27,Camgap1,CIN85-associated multi-domain-containing Rho GTPase-activating protein 1,Rat,Rattus norvegicus,Rho GTPase-activating protein 27,Rho-type GTPase-activating protein 27
EIAAB34654 ARHGAP1,CDC42 GTPase-activating protein,CDC42GAP,GTPase-activating protein rhoOGAP,Homo sapiens,Human,p50-RhoGAP,Rho GTPase-activating protein 1,RHOGAP1,Rho-related small GTPase protein activator,Rho-
EIAAB34688 Arhgap20,Kiaa1391,Mouse,Mus musculus,RA and RhoGAP domain-containing protein,RARhoGAP,Rho GTPase-activating protein 20,Rho-type GTPase-activating protein 20
30-773 CHN2 is a protein with a phorbol-ester_DAG-type zinc finger, a Rho-GAP domain and an SH2 domain. This protein has GTPase-activating protein activity that is regulated by phospholipid binding and bindi 0.05 mg
EIAAB34670 Arhgap10,Mouse,Mus musculus,PH and SH3 domain-containing rhoGAP protein,PSGAP,PS-GAP,Rho GTPase-activating protein 10,Rho-type GTPase-activating protein 10
EIAAB34687 Arhgap20,RA and RhoGAP domain-containing protein,RARhoGAP,Rat,Rattus norvegicus,Rho GTPase-activating protein 20,Rho-type GTPase-activating protein 20
EIAAB34717 Arhgap32,Brain-specific Rho GTPase-activating protein,GAB-associated Cdc42_Rac GTPase-activating protein,GC-GAP,Grit,Kiaa0712,Mouse,Mus musculus,p200RhoGAP,p250GAP,Rho GTPase-activating protein 32,Rho
EIAAB34719 ARHGAP33,Homo sapiens,Human,Rho GTPase-activating protein 33,Rho-type GTPase-activating protein 33,SNX26,Sorting nexin-26,Tc10_CDC42 GTPase-activating protein,TCGAP
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EIAAB34718 Arhgap33,Mouse,Mus musculus,Rho GTPase-activating protein 33,Rho-type GTPase-activating protein 33,Snx26,Sorting nexin-26,Tc10_CDC42 GTPase-activating protein,Tcgap
EIAAB34690 ARHGAP10,ARHGAP21,Homo sapiens,Human,KIAA1424,Rho GTPase-activating protein 10,Rho GTPase-activating protein 21,Rho-type GTPase-activating protein 21
EIAAB34500 GAP-related-interacting partner to E12,GARNL1,GRIPE,GTPase-activating Rap_Ran-GAP domain-like 1,p240,Pig,Ral GTPase-activating protein subunit alpha-1,RALGAPA1,Sus scrofa,Tuberin-like protein 1,TULIP1
EIAAB34501 GAP-related-interacting partner to E12,Garnl1,GRIPE,GTPase-activating RapGAP domain-like 1,Kiaa0884,Mouse,Mus musculus,p240,Ral GTPase-activating protein subunit alpha-1,Ralgapa1,Tuberin-like protein
EIAAB34502 GAP-related-interacting partner to E12,Garnl1,GRIPE,GTPase-activating RapGAP domain-like 1,p240,Ral GTPase-activating protein subunit alpha-1,Ralgapa1,Rat,Rattus norvegicus,Tuberin-like protein 1,Tuli
EIAAB34689 Arhgap10,Arhgap21,Kiaa1424,Mouse,Mus musculus,Rho GTPase-activating protein 10,Rho GTPase-activating protein 21,Rho-type GTPase-activating protein 21
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