HNRPD_HUMAN
ID HNRPD_HUMAN Reviewed; 355 AA.
AC Q14103; A8K9J2; P07029; Q01858; Q14100; Q14101; Q14102; Q4W5A1; Q9UCE8;
AC Q9UCE9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 237.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein D0;
DE Short=hnRNP D0;
DE AltName: Full=AU-rich element RNA-binding protein 1;
GN Name=HNRNPD; Synonyms=AUF1, HNRPD;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 70-355 (ISOFORM 2).
RC TISSUE=Cervix carcinoma;
RX PubMed=7673195; DOI=10.1074/jbc.270.38.22167;
RA Kajita Y., Nakayama J., Aizawa M., Ishikawa F.;
RT "The UUAG-specific RNA binding protein, heterogeneous nuclear
RT ribonucleoprotein D0. Common modular structure and binding properties of
RT the 2xRBD-Gly family.";
RL J. Biol. Chem. 270:22167-22175(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=9615222; DOI=10.1006/geno.1998.5237;
RA Dempsey L.A., Li M.-J., DePace A., Bray-Ward P., Maizels N.;
RT "The human HNRPD locus maps to 4q21 and encodes a highly conserved
RT protein.";
RL Genomics 49:378-384(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Lung;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 6-235.
RX PubMed=3754960; DOI=10.1093/nar/14.10.4077;
RA Lahiri D.K., Thomas J.O.;
RT "A cDNA clone of the hnRNP C proteins and its homology with the single-
RT stranded DNA binding protein UP2.";
RL Nucleic Acids Res. 14:4077-4094(1986).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-355 (ISOFORM 3), AND CHARACTERIZATION.
RC TISSUE=Blood;
RX PubMed=10024518; DOI=10.1042/bj3380417;
RA Tolnay M., Vereshchagina L.A., Tsokos G.C.;
RT "Heterogeneous nuclear ribonucleoprotein D0B is a sequence-specific DNA-
RT binding protein.";
RL Biochem. J. 338:417-425(1999).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-355 (ISOFORM 3).
RX PubMed=1433497; DOI=10.1128/jvi.66.12.6841-6848.1992;
RA Tay N., Chan S.-H., Ren E.-C.;
RT "Identification and cloning of a novel heterogeneous nuclear
RT ribonucleoprotein C-like protein that functions as a transcriptional
RT activator of the hepatitis B virus enhancer II.";
RL J. Virol. 66:6841-6848(1992).
RN [10]
RP PROTEIN SEQUENCE OF 68-85; 99-110; 112-129; 139-158; 184-218; 224-231 AND
RP 261-272, METHYLATION AT LYS-119, AND IDENTIFICATION BY 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 [11]
RP PROTEIN SEQUENCE OF 139-157; 184-203 AND 224-237, AND NUCLEOTIDE-BINDING.
RC TISSUE=Cervix carcinoma;
RX PubMed=8321232; DOI=10.1128/mcb.13.7.4301-4310.1993;
RA Ishikawa F., Matunis M.J., Dreyfuss G., Cech T.R.;
RT "Nuclear proteins that bind the pre-mRNA 3' splice site sequence r(UUAG/G)
RT and the human telomeric DNA sequence d(TTAGGG)n.";
RL Mol. Cell. Biol. 13:4301-4310(1993).
RN [12]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4).
RX PubMed=9521873; DOI=10.1006/geno.1997.5142;
RA Wagner B.J., DeMaria C.T., Sun Y., Wilson G.M., Brewer G.;
RT "Structure and genomic organization of the human AUF1 gene: alternative
RT pre-mRNA splicing generates four protein isoforms.";
RL Genomics 48:195-202(1998).
RN [13]
RP FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, AND IDENTIFICATION IN A
RP COMPLEX WITH SYNCRIP; PABPC1; PAIP1 AND CSDE1.
RC TISSUE=Placenta;
RX PubMed=11051545; DOI=10.1016/s0092-8674(00)00102-1;
RA Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H.,
RA Shyu A.-B.;
RT "A mechanism for translationally coupled mRNA turnover: interaction between
RT the poly(A) tail and a c-fos RNA coding determinant via a protein
RT complex.";
RL Cell 103:29-40(2000).
RN [14]
RP INTERACTION WITH IGF2BP2.
RX PubMed=12674497; DOI=10.1515/bc.2003.004;
RA Moraes K.C., Quaresma A.J., Maehnss K., Kobarg J.;
RT "Identification and characterization of proteins that selectively interact
RT with isoforms of the mRNA binding protein AUF1 (hnRNP D).";
RL Biol. Chem. 384:25-37(2003).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [16]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-345, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND IDENTIFICATION BY
RP 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 [18]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-193, 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-83; SER-190 AND
RP THR-193, AND 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 [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-190 AND THR-193, AND
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 [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165 AND LYS-251, ACETYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-292 (ISOFORM 3), ACETYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-273 (ISOFORM 4), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-80; SER-83; SER-190
RP AND THR-193, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [28]
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 [29]
RP INTERACTION WITH GTPBP1.
RX PubMed=21515746; DOI=10.1096/fj.10-178715;
RA Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J.,
RA Chung S.J., Senju S., Nishimura Y., Kim K.T.;
RT "Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding
RT protein 1 (GTPBP1) with its target mRNAs.";
RL FASEB J. 25:2757-2769(2011).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-83 AND SER-190, AND
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 [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-83; THR-91; THR-127;
RP SER-190; THR-193 AND SER-271, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-127 AND SER-190, 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 [33]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-272; ARG-278; ARG-280 AND
RP ARG-345, METHYLATION [LARGE SCALE ANALYSIS] AT ARG-282 (ISOFORM 3),
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-263 (ISOFORM 4), AND
RP 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 [34]
RP FUNCTION IN CIRCADIAN CLOCK, INTERACTION WITH EIF3B; EIF4G1 AND RPS3,
RP SUBCELLULAR LOCATION, AND RNA-BINDING.
RX PubMed=24423872; DOI=10.1093/nar/gkt1379;
RA Lee K.H., Kim S.H., Kim H.J., Kim W., Lee H.R., Jung Y., Choi J.H.,
RA Hong K.Y., Jang S.K., Kim K.T.;
RT "AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic
RT translation.";
RL Nucleic Acids Res. 42:3590-3606(2014).
RN [35]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-197, 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 [36]
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 [37]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-72; LYS-129 AND LYS-197, AND
RP 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 [38]
RP STRUCTURE BY NMR OF 98-172, AND FUNCTION.
RX PubMed=10080887; DOI=10.1006/jmbi.1999.2616;
RA Nagata T., Kurihara Y., Matsuda G., Saeki J., Kohno T., Yanagida Y.,
RA Ishikawa F., Uesugi S., Katahira M.;
RT "Structure and interactions with RNA of the N-terminal UUAG-specific RNA-
RT binding domain of hnRNP D0.";
RL J. Mol. Biol. 287:221-237(1999).
CC -!- FUNCTION: Binds with high affinity to RNA molecules that contain AU-
CC rich elements (AREs) found within the 3'-UTR of many proto-oncogenes
CC and cytokine mRNAs. Also binds to double- and single-stranded DNA
CC sequences in a specific manner and functions a transcription factor.
CC Each of the RNA-binding domains specifically can bind solely to a
CC single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to
CC the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA
CC oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the
CC telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Binding of RRM1 to
CC DNA inhibits the formation of DNA quadruplex structure which may play a
CC role in telomere elongation. May be involved in translationally coupled
CC mRNA turnover. Implicated with other RNA-binding proteins in the
CC cytoplasmic deadenylation/translational and decay interplay of the FOS
CC mRNA mediated by the major coding-region determinant of instability
CC (mCRD) domain. May play a role in the regulation of the rhythmic
CC expression of circadian clock core genes. Directly binds to the 3'UTR
CC of CRY1 mRNA and induces CRY1 rhythmic translation. May also be
CC involved in the regulation of PER2 translation.
CC {ECO:0000269|PubMed:10080887, ECO:0000269|PubMed:11051545,
CC ECO:0000269|PubMed:24423872}.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Part of a complex associated with the
CC FOS mCRD domain and consisting of PABPC1, PAIP1, CSDE1/UNR and SYNCRIP.
CC Interacts with IGF2BP2. Interacts with GTPBP1. Interacts with EIF4G1;
CC the interaction requires RNA. Interacts with EIF3B and RPS3.
CC {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:12674497,
CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:21515746,
CC ECO:0000269|PubMed:24423872}.
CC -!- INTERACTION:
CC Q14103; P22626: HNRNPA2B1; NbExp=2; IntAct=EBI-299674, EBI-299649;
CC Q14103; Q00839: HNRNPU; NbExp=3; IntAct=EBI-299674, EBI-351126;
CC Q14103; Q9UNL4: ING4; NbExp=9; IntAct=EBI-299674, EBI-2866661;
CC Q14103; Q9BYZ2: LDHAL6B; NbExp=2; IntAct=EBI-299674, EBI-1108377;
CC Q14103-4; Q04637: EIF4G1; NbExp=3; IntAct=EBI-432545, EBI-73711;
CC Q14103-4; Q9Y6M1: IGF2BP2; NbExp=4; IntAct=EBI-432545, EBI-1024419;
CC Q14103-4; Q9UNL4: ING4; NbExp=2; IntAct=EBI-432545, EBI-2866661;
CC Q14103-4; P11940: PABPC1; NbExp=2; IntAct=EBI-432545, EBI-81531;
CC Q14103-4; P31947: SFN; NbExp=7; IntAct=EBI-432545, EBI-476295;
CC Q14103-4; O60506: SYNCRIP; NbExp=3; IntAct=EBI-432545, EBI-1024357;
CC Q14103-4; P67809: YBX1; NbExp=3; IntAct=EBI-432545, EBI-354065;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in cytoplasmic
CC mRNP granules containing untranslated mRNAs. Component of
CC ribonucleosomes. Cytoplasmic localization oscillates diurnally.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=p45, Dx9;
CC IsoId=Q14103-1; Sequence=Displayed;
CC Name=2; Synonyms=p42, Dx4;
CC IsoId=Q14103-2; Sequence=VSP_005834;
CC Name=3; Synonyms=p40, Dx7;
CC IsoId=Q14103-3; Sequence=VSP_005835;
CC Name=4; Synonyms=p37;
CC IsoId=Q14103-4; Sequence=VSP_005834, VSP_005835;
CC -!- PTM: Arg-345 is dimethylated, probably to asymmetric dimethylarginine.
CC -!- PTM: Methylated by PRMT1, in an insulin-dependent manner. The PRMT1-
CC mediated methylation regulates tyrosine phosphorylation (By
CC similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35781.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA35781.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=CAA27544.1; Type=Miscellaneous discrepancy; Note=Several sequence conflicts.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/HNRNPDID40840ch4q21.html";
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DR EMBL; D55671; BAA09522.1; -; mRNA.
DR EMBL; D55672; BAA09523.1; -; mRNA.
DR EMBL; D55673; BAA09524.1; -; mRNA.
DR EMBL; D55674; BAA09525.1; -; mRNA.
DR EMBL; AF026126; AAC23474.1; -; Genomic_DNA.
DR EMBL; AF026126; AAC23475.1; -; Genomic_DNA.
DR EMBL; AF026126; AAC23476.1; -; Genomic_DNA.
DR EMBL; AK292707; BAF85396.1; -; mRNA.
DR EMBL; AC124016; AAY40913.1; -; Genomic_DNA.
DR EMBL; CH471057; EAX05874.1; -; Genomic_DNA.
DR EMBL; BC002401; AAH02401.1; -; mRNA.
DR EMBL; BC023977; AAH23977.1; -; mRNA.
DR EMBL; BC026015; AAH26015.1; -; mRNA.
DR EMBL; X03910; CAA27544.1; ALT_SEQ; mRNA.
DR EMBL; AF039575; AAB96683.1; -; mRNA.
DR EMBL; M94630; AAA35781.1; ALT_SEQ; mRNA.
DR CCDS; CCDS3590.1; -. [Q14103-3]
DR CCDS; CCDS3591.1; -. [Q14103-2]
DR CCDS; CCDS3592.1; -. [Q14103-1]
DR PIR; A24016; A24016.
DR PIR; A44192; A44192.
DR PIR; B48138; B48138.
DR RefSeq; NP_001003810.1; NM_001003810.1. [Q14103-4]
DR RefSeq; NP_002129.2; NM_002138.3. [Q14103-3]
DR RefSeq; NP_112737.1; NM_031369.2. [Q14103-2]
DR RefSeq; NP_112738.1; NM_031370.2. [Q14103-1]
DR PDB; 1HD0; NMR; -; A=98-172.
DR PDB; 1HD1; NMR; -; A=98-172.
DR PDB; 1IQT; NMR; -; A=183-257.
DR PDB; 1WTB; NMR; -; A=181-259.
DR PDB; 1X0F; NMR; -; A=181-259.
DR PDB; 2Z5N; X-ray; 3.20 A; B=332-355.
DR PDB; 5IM0; X-ray; 1.70 A; A=71-175, B=96-175.
DR PDBsum; 1HD0; -.
DR PDBsum; 1HD1; -.
DR PDBsum; 1IQT; -.
DR PDBsum; 1WTB; -.
DR PDBsum; 1X0F; -.
DR PDBsum; 2Z5N; -.
DR PDBsum; 5IM0; -.
DR AlphaFoldDB; Q14103; -.
DR SMR; Q14103; -.
DR BioGRID; 109425; 506.
DR ComplexPortal; CPX-1076; mCRD-poly(A)-bridging complex.
DR CORUM; Q14103; -.
DR DIP; DIP-31163N; -.
DR IntAct; Q14103; 199.
DR MINT; Q14103; -.
DR STRING; 9606.ENSP00000313199; -.
DR ChEMBL; CHEMBL4296009; -.
DR DrugBank; DB11638; Artenimol.
DR MoonDB; Q14103; Predicted.
DR GlyGen; Q14103; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14103; -.
DR MetOSite; Q14103; -.
DR PhosphoSitePlus; Q14103; -.
DR SwissPalm; Q14103; -.
DR BioMuta; HNRNPD; -.
DR DMDM; 13124489; -.
DR SWISS-2DPAGE; Q14103; -.
DR EPD; Q14103; -.
DR jPOST; Q14103; -.
DR MassIVE; Q14103; -.
DR MaxQB; Q14103; -.
DR PaxDb; Q14103; -.
DR PeptideAtlas; Q14103; -.
DR PRIDE; Q14103; -.
DR ProteomicsDB; 59811; -. [Q14103-1]
DR ProteomicsDB; 59812; -. [Q14103-2]
DR ProteomicsDB; 59813; -. [Q14103-3]
DR ProteomicsDB; 59814; -. [Q14103-4]
DR TopDownProteomics; Q14103-1; -. [Q14103-1]
DR TopDownProteomics; Q14103-2; -. [Q14103-2]
DR TopDownProteomics; Q14103-3; -. [Q14103-3]
DR Antibodypedia; 1448; 455 antibodies from 33 providers.
DR DNASU; 3184; -.
DR Ensembl; ENST00000313899.12; ENSP00000313199.7; ENSG00000138668.19. [Q14103-1]
DR Ensembl; ENST00000352301.8; ENSP00000305860.6; ENSG00000138668.19. [Q14103-2]
DR Ensembl; ENST00000353341.8; ENSP00000313327.6; ENSG00000138668.19. [Q14103-3]
DR GeneID; 3184; -.
DR KEGG; hsa:3184; -.
DR MANE-Select; ENST00000313899.12; ENSP00000313199.7; NM_031370.3; NP_112738.1.
DR UCSC; uc003hmm.2; human. [Q14103-1]
DR CTD; 3184; -.
DR DisGeNET; 3184; -.
DR GeneCards; HNRNPD; -.
DR HGNC; HGNC:5036; HNRNPD.
DR HPA; ENSG00000138668; Low tissue specificity.
DR MIM; 601324; gene.
DR neXtProt; NX_Q14103; -.
DR OpenTargets; ENSG00000138668; -.
DR PharmGKB; PA29361; -.
DR VEuPathDB; HostDB:ENSG00000138668; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000158010; -.
DR InParanoid; Q14103; -.
DR OMA; GPNQSWN; -.
DR PhylomeDB; Q14103; -.
DR TreeFam; TF314808; -.
DR PathwayCommons; Q14103; -.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR SignaLink; Q14103; -.
DR SIGNOR; Q14103; -.
DR BioGRID-ORCS; 3184; 64 hits in 1088 CRISPR screens.
DR ChiTaRS; HNRNPD; human.
DR EvolutionaryTrace; Q14103; -.
DR GeneWiki; HNRPD; -.
DR GenomeRNAi; 3184; -.
DR Pharos; Q14103; Tbio.
DR PRO; PR:Q14103; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q14103; protein.
DR Bgee; ENSG00000138668; Expressed in ganglionic eminence and 206 other tissues.
DR ExpressionAtlas; Q14103; baseline and differential.
DR Genevisible; Q14103; HS.
DR GO; GO:0005829; C:cytosol; IDA:ComplexPortal.
DR GO; GO:0106002; C:mCRD-mediated mRNA stability complex; IPI:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IEA:Ensembl.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0071732; P:cellular response to nitric oxide; IEA:Ensembl.
DR GO; GO:1904586; P:cellular response to putrescine; IEA:Ensembl.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0097167; P:circadian regulation of translation; IMP:UniProtKB.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IDA:ComplexPortal.
DR GO; GO:1990828; P:hepatocyte dedifferentiation; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:ComplexPortal.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IDA:ComplexPortal.
DR GO; GO:1905663; P:positive regulation of telomerase RNA reverse transcriptase activity; ISS:BHF-UCL.
DR GO; GO:1904355; P:positive regulation of telomere capping; ISS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0032204; P:regulation of telomere maintenance; ISS:BHF-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR GO; GO:1901355; P:response to rapamycin; IEA:Ensembl.
DR GO; GO:1904383; P:response to sodium phosphate; IEA:Ensembl.
DR GO; GO:0006401; P:RNA catabolic process; TAS:ProtInc.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR Gene3D; 3.30.70.330; -; 2.
DR IDEAL; IID00075; -.
DR InterPro; IPR012956; CARG-binding_factor_N.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF08143; CBFNT; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Biological rhythms;
KW Cytoplasm; Direct protein sequencing; DNA-binding; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; RNA-binding; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..355
FT /note="Heterogeneous nuclear ribonucleoprotein D0"
FT /id="PRO_0000081849"
FT DOMAIN 97..179
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 182..261
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 119
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|Ref.10"
FT MOD_RES 127
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 193
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 243
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60668"
FT MOD_RES 251
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 272
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 278
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 280
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 282
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q60668"
FT MOD_RES 345
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60668"
FT MOD_RES 345
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0007744|PubMed:15782174"
FT MOD_RES 345
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 72
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 79..97
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:7673195"
FT /id="VSP_005834"
FT VAR_SEQ 285..334
FT /note="GPSQNWNQGYSNYWNQGYGNYGYNSQGYGGYGGYDYTGYNNYYGYGDYSN
FT -> D (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10024518,
FT ECO:0000303|PubMed:1433497, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7673195"
FT /id="VSP_005835"
FT CONFLICT 150
FT /note="S -> R (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="F -> L (in Ref. 9; AAA35781)"
FT /evidence="ECO:0000305"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:5IM0"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:5IM0"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:5IM0"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:5IM0"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:5IM0"
FT STRAND 137..147
FT /evidence="ECO:0007829|PDB:5IM0"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:5IM0"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:5IM0"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:5IM0"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:5IM0"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:1IQT"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:1IQT"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1IQT"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:1X0F"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1IQT"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:1IQT"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:1IQT"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:1IQT"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1WTB"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:1WTB"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1IQT"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:2Z5N"
FT MOD_RES Q14103-3:282
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q14103-3:292
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES Q14103-4:263
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q14103-4:273
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
SQ SEQUENCE 355 AA; 38434 MW; D0B6EA177BEF789E CRC64;
MSEEQFGGDG AAAAATAAVG GSAGEQEGAM VAATQGAAAA AGSGAGTGGG TASGGTEGGS
AESEGAKIDA SKNEEDEGHS NSSPRHSEAA TAQREEWKMF IGGLSWDTTK KDLKDYFSKF
GEVVDCTLKL DPITGRSRGF GFVLFKESES VDKVMDQKEH KLNGKVIDPK RAKAMKTKEP
VKKIFVGGLS PDTPEEKIRE YFGGFGEVES IELPMDNKTN KRRGFCFITF KEEEPVKKIM
EKKYHNVGLS KCEIKVAMSK EQYQQQQQWG SRGGFAGRAR GRGGGPSQNW NQGYSNYWNQ
GYGNYGYNSQ GYGGYGGYDY TGYNNYYGYG DYSNQQSGYG KVSRRGGHQN SYKPY
