CSDE1_HUMAN
ID CSDE1_HUMAN Reviewed; 798 AA.
AC O75534; A8K281; E9PGZ0; G5E9Q2; O94961; Q5TF04; Q5TF05; Q68DF1; Q68DI9;
AC Q9Y2S4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Cold shock domain-containing protein E1 {ECO:0000305};
DE AltName: Full=N-ras upstream gene protein;
DE AltName: Full=Protein UNR;
GN Name=CSDE1 {ECO:0000312|HGNC:HGNC:29905};
GN Synonyms=D1S155E, KIAA0885, NRU, UNR;
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] (ISOFORM 2).
RX PubMed=2052355;
RA Nicolaiew N., Triqueneaux G., Dautry F.;
RT "Organization of the human N-ras locus: characterization of a gene located
RT immediately upstream of N-ras.";
RL Oncogene 6:721-730(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Pituitary;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thalamus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cervix;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-498 (ISOFORM 2).
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 67-166, AND ALTERNATIVE SPLICING.
RX PubMed=8439573; DOI=10.1016/0167-4781(93)90270-n;
RA Boussadia O., Jacquemin-Sablon H., Dautry F.;
RT "Exon skipping in the expression of the gene immediately upstream of N-ras
RT (unr/NRU).";
RL Biochim. Biophys. Acta 1172:64-72(1993).
RN [11]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH STRAP.
RX PubMed=10049359; DOI=10.1101/gad.13.4.437;
RA Hunt S.L., Hsuan J.J., Totty N., Jackson R.J.;
RT "unr, a cellular cytoplasmic RNA-binding protein with five cold-shock
RT domains, is required for internal initiation of translation of human
RT rhinovirus RNA.";
RL Genes Dev. 13:437-448(1999).
RN [12]
RP FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, AND IDENTIFICATION IN A
RP COMPLEX WITH HNRPD; SYNCRIP; PABPC1 AND PAIP1.
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 [13]
RP FUNCTION, AND INTERACTION WITH PABPC1.
RX PubMed=15314026; DOI=10.1101/gad.1219104;
RA Chang T.-C., Yamashita A., Chen C.-Y.A., Yamashita Y., Zhu W., Durdan S.,
RA Kahvejian A., Sonenberg N., Shyu A.-B.;
RT "UNR, a new partner of poly(A)-binding protein, plays a key role in
RT translationally coupled mRNA turnover mediated by the c-fos major coding-
RT region determinant.";
RL Genes Dev. 18:2010-2023(2004).
RN [14]
RP IDENTIFICATION IN A MRNP COMPLEX WITH IGF2BP1 AND PABPC1.
RX PubMed=16356927; DOI=10.1093/nar/gki1014;
RA Patel G.P., Ma S., Bag J.;
RT "The autoregulatory translational control element of poly(A)-binding
RT protein mRNA forms a heteromeric ribonucleoprotein complex.";
RL Nucleic Acids Res. 33:7074-7089(2005).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND IDENTIFICATION BY
RP 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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, AND IDENTIFICATION BY
RP 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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, AND IDENTIFICATION BY
RP 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 [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-276; SER-584 AND
RP THR-761, AND IDENTIFICATION BY MASS SPECTROMETRY [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 [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-91, 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 [25]
RP INTERACTION WITH EIF4ENIF1.
RX PubMed=27342281; DOI=10.1093/nar/gkw565;
RA Kamenska A., Simpson C., Vindry C., Broomhead H., Benard M.,
RA Ernoult-Lange M., Lee B.P., Harries L.W., Weil D., Standart N.;
RT "The DDX6-4E-T interaction mediates translational repression and P-body
RT assembly.";
RL Nucleic Acids Res. 44:6318-6334(2016).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-91, AND IDENTIFICATION BY MASS
RP 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 [27]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29395067; DOI=10.1016/j.molcel.2017.12.020;
RA Youn J.Y., Dunham W.H., Hong S.J., Knight J.D.R., Bashkurov M., Chen G.I.,
RA Bagci H., Rathod B., MacLeod G., Eng S.W.M., Angers S., Morris Q.,
RA Fabian M., Cote J.F., Gingras A.C.;
RT "High-Density Proximity Mapping Reveals the Subcellular Organization of
RT mRNA-Associated Granules and Bodies.";
RL Mol. Cell 69:517.e11-532.e11(2018).
RN [28]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH EIF4ENIF1.
RX PubMed=32354837; DOI=10.1101/gad.336073.119;
RA Raesch F., Weber R., Izaurralde E., Igreja C.;
RT "4E-T-bound mRNAs are stored in a silenced and deadenylated form.";
RL Genes Dev. 34:847-860(2020).
RN [29]
RP STRUCTURE BY NMR OF 15-90; 175-259; 348-424; 508-582 AND 673-738.
RX PubMed=20213426; DOI=10.1007/s10969-010-9081-z;
RA Goroncy A.K., Koshiba S., Tochio N., Tomizawa T., Inoue M., Watanabe S.,
RA Harada T., Tanaka A., Ohara O., Kigawa T., Yokoyama S.;
RT "The NMR solution structures of the five constituent cold-shock domains
RT (CSD) of the human UNR (upstream of N-ras) protein.";
RL J. Struct. Funct. Genomics 11:181-188(2010).
CC -!- FUNCTION: RNA-binding protein involved in translationally coupled mRNA
CC turnover (PubMed:11051545, PubMed:15314026). Implicated with other RNA-
CC binding proteins in the cytoplasmic deadenylation/translational and
CC decay interplay of the FOS mRNA mediated by the major coding-region
CC determinant of instability (mCRD) domain (PubMed:11051545,
CC PubMed:15314026). Required for efficient formation of stress granules
CC (PubMed:29395067). {ECO:0000269|PubMed:11051545,
CC ECO:0000269|PubMed:15314026, ECO:0000269|PubMed:29395067}.
CC -!- FUNCTION: (Microbial infection) Required for internal initiation of
CC translation of human rhinovirus RNA. {ECO:0000269|PubMed:10049359}.
CC -!- SUBUNIT: Component of a multi subunit autoregulatory ribonucleoprotein
CC complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1
CC (PubMed:16356927). Interacts with STRAP (PubMed:10049359). Part of a
CC complex associated with the FOS mCRD domain and consisting of PABPC1,
CC PAIP1, HNRPD and SYNCRIP (PubMed:11051545). The interaction with PABPC1
CC is direct and RNA-independent (PubMed:11051545, PubMed:15314026).
CC Interacts with EIF4ENIF1/4E-T (PubMed:27342281, PubMed:32354837).
CC {ECO:0000269|PubMed:10049359, ECO:0000269|PubMed:11051545,
CC ECO:0000269|PubMed:15314026, ECO:0000269|PubMed:16356927,
CC ECO:0000269|PubMed:27342281, ECO:0000269|PubMed:32354837}.
CC -!- INTERACTION:
CC O75534; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-719186, EBI-10175124;
CC O75534; Q8IV36: HID1; NbExp=3; IntAct=EBI-719186, EBI-743438;
CC O75534-3; Q8IV36: HID1; NbExp=3; IntAct=EBI-12397458, EBI-743438;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, Stress granule
CC {ECO:0000305|PubMed:29395067}. Cytoplasm, P-body
CC {ECO:0000269|PubMed:32354837}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O75534-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75534-2; Sequence=VSP_001138;
CC Name=3;
CC IsoId=O75534-3; Sequence=VSP_045615, VSP_001138;
CC Name=4;
CC IsoId=O75534-4; Sequence=VSP_045615;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74908.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF077054; AAD27787.1; -; mRNA.
DR EMBL; AB020692; BAA74908.2; ALT_INIT; mRNA.
DR EMBL; AK290146; BAF82835.1; -; mRNA.
DR EMBL; CR749378; CAH18231.1; -; mRNA.
DR EMBL; CR749431; CAH18269.1; -; mRNA.
DR EMBL; AL096773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56612.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56616.1; -; Genomic_DNA.
DR EMBL; BC032446; AAH32446.1; -; mRNA.
DR EMBL; AF070542; AAC28634.1; -; mRNA.
DR CCDS; CCDS30811.1; -. [O75534-2]
DR CCDS; CCDS30812.1; -. [O75534-1]
DR CCDS; CCDS44197.1; -. [O75534-3]
DR CCDS; CCDS55626.1; -. [O75534-4]
DR PIR; S29815; S29815.
DR RefSeq; NP_001007554.1; NM_001007553.2. [O75534-1]
DR RefSeq; NP_001123995.1; NM_001130523.2. [O75534-3]
DR RefSeq; NP_001229820.1; NM_001242891.1. [O75534-4]
DR RefSeq; NP_001229821.1; NM_001242892.1. [O75534-1]
DR RefSeq; NP_001229822.1; NM_001242893.1. [O75534-2]
DR RefSeq; NP_009089.4; NM_007158.5. [O75534-2]
DR PDB; 1WFQ; NMR; -; A=15-90.
DR PDB; 1X65; NMR; -; A=348-423.
DR PDB; 2YTV; NMR; -; A=673-738.
DR PDB; 2YTX; NMR; -; A=175-258.
DR PDB; 2YTY; NMR; -; A=508-582.
DR PDBsum; 1WFQ; -.
DR PDBsum; 1X65; -.
DR PDBsum; 2YTV; -.
DR PDBsum; 2YTX; -.
DR PDBsum; 2YTY; -.
DR AlphaFoldDB; O75534; -.
DR SMR; O75534; -.
DR BioGRID; 113583; 162.
DR ComplexPortal; CPX-1076; mCRD-poly(A)-bridging complex.
DR CORUM; O75534; -.
DR IntAct; O75534; 43.
DR MINT; O75534; -.
DR STRING; 9606.ENSP00000481762; -.
DR GlyGen; O75534; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75534; -.
DR MetOSite; O75534; -.
DR PhosphoSitePlus; O75534; -.
DR SwissPalm; O75534; -.
DR BioMuta; CSDE1; -.
DR EPD; O75534; -.
DR jPOST; O75534; -.
DR MassIVE; O75534; -.
DR MaxQB; O75534; -.
DR PaxDb; O75534; -.
DR PeptideAtlas; O75534; -.
DR PRIDE; O75534; -.
DR ProteomicsDB; 20422; -.
DR ProteomicsDB; 34008; -.
DR ProteomicsDB; 50073; -. [O75534-1]
DR ProteomicsDB; 50074; -. [O75534-2]
DR Antibodypedia; 20164; 218 antibodies from 29 providers.
DR DNASU; 7812; -.
DR Ensembl; ENST00000261443.9; ENSP00000261443.5; ENSG00000009307.17. [O75534-2]
DR Ensembl; ENST00000339438.10; ENSP00000342408.6; ENSG00000009307.17. [O75534-2]
DR Ensembl; ENST00000358528.9; ENSP00000351329.4; ENSG00000009307.17. [O75534-1]
DR Ensembl; ENST00000369530.5; ENSP00000358543.1; ENSG00000009307.17. [O75534-3]
DR Ensembl; ENST00000438362.7; ENSP00000407724.3; ENSG00000009307.17. [O75534-1]
DR Ensembl; ENST00000534699.5; ENSP00000432958.1; ENSG00000009307.17. [O75534-1]
DR Ensembl; ENST00000610726.5; ENSP00000481762.1; ENSG00000009307.17. [O75534-4]
DR Ensembl; ENST00000684913.1; ENSP00000510656.1; ENSG00000009307.17. [O75534-2]
DR Ensembl; ENST00000686025.1; ENSP00000508776.1; ENSG00000009307.17. [O75534-2]
DR Ensembl; ENST00000686235.1; ENSP00000509507.1; ENSG00000009307.17. [O75534-2]
DR Ensembl; ENST00000688211.1; ENSP00000508995.1; ENSG00000009307.17. [O75534-4]
DR Ensembl; ENST00000689217.1; ENSP00000508874.1; ENSG00000009307.17. [O75534-1]
DR Ensembl; ENST00000689732.1; ENSP00000510376.1; ENSG00000009307.17. [O75534-2]
DR Ensembl; ENST00000689989.1; ENSP00000509808.1; ENSG00000009307.17. [O75534-1]
DR Ensembl; ENST00000692719.1; ENSP00000510208.1; ENSG00000009307.17. [O75534-1]
DR Ensembl; ENST00000693467.1; ENSP00000510042.1; ENSG00000009307.17. [O75534-2]
DR GeneID; 7812; -.
DR KEGG; hsa:7812; -.
DR MANE-Select; ENST00000358528.9; ENSP00000351329.4; NM_001007553.3; NP_001007554.1.
DR UCSC; uc001efi.4; human. [O75534-1]
DR CTD; 7812; -.
DR DisGeNET; 7812; -.
DR GeneCards; CSDE1; -.
DR HGNC; HGNC:29905; CSDE1.
DR HPA; ENSG00000009307; Tissue enhanced (skeletal).
DR MIM; 191510; gene.
DR neXtProt; NX_O75534; -.
DR OpenTargets; ENSG00000009307; -.
DR PharmGKB; PA142672072; -.
DR VEuPathDB; HostDB:ENSG00000009307; -.
DR eggNOG; ENOG502QSJ1; Eukaryota.
DR GeneTree; ENSGT00390000016950; -.
DR HOGENOM; CLU_012335_1_0_1; -.
DR InParanoid; O75534; -.
DR OMA; PPIMNSD; -.
DR OrthoDB; 136290at2759; -.
DR PhylomeDB; O75534; -.
DR TreeFam; TF324707; -.
DR PathwayCommons; O75534; -.
DR SignaLink; O75534; -.
DR SIGNOR; O75534; -.
DR BioGRID-ORCS; 7812; 196 hits in 1116 CRISPR screens.
DR ChiTaRS; CSDE1; human.
DR EvolutionaryTrace; O75534; -.
DR GeneWiki; CSDE1; -.
DR GenomeRNAi; 7812; -.
DR Pharos; O75534; Tbio.
DR PRO; PR:O75534; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75534; protein.
DR Bgee; ENSG00000009307; Expressed in calcaneal tendon and 206 other tissues.
DR ExpressionAtlas; O75534; baseline and differential.
DR Genevisible; O75534; HS.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0106002; C:mCRD-mediated mRNA stability complex; IPI:ComplexPortal.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0035613; F:RNA stem-loop binding; IDA:FlyBase.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IDA:ComplexPortal.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:FlyBase.
DR GO; GO:0008584; P:male gonad development; TAS:ProtInc.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:ComplexPortal.
DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IMP:UniProtKB.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IDA:ComplexPortal.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:FlyBase.
DR GO; GO:0034063; P:stress granule assembly; IMP:UniProtKB.
DR CDD; cd04458; CSP_CDS; 2.
DR Gene3D; 2.40.50.140; -; 6.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR019844; CSD_1.
DR InterPro; IPR002059; CSP_DNA-bd.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR024642; SUZ-C.
DR Pfam; PF00313; CSD; 5.
DR Pfam; PF12901; SUZ-C; 1.
DR SMART; SM00357; CSP; 5.
DR SUPFAM; SSF50249; SSF50249; 5.
DR PROSITE; PS00352; CSD_1; 4.
DR PROSITE; PS51857; CSD_2; 9.
DR PROSITE; PS51938; SUZ_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..798
FT /note="Cold shock domain-containing protein E1"
FT /id="PRO_0000100348"
FT DOMAIN 26..87
FT /note="CSD 1"
FT DOMAIN 136..179
FT /note="CSD 2; truncated"
FT DOMAIN 186..245
FT /note="CSD 3"
FT DOMAIN 297..337
FT /note="CSD 4; truncated"
FT DOMAIN 349..410
FT /note="CSD 5"
FT DOMAIN 447..507
FT /note="CSD 6"
FT DOMAIN 519..579
FT /note="CSD 7"
FT DOMAIN 610..670
FT /note="CSD 8"
FT DOMAIN 674..735
FT /note="CSD 9"
FT DOMAIN 748..789
FT /note="SUZ-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01287"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 761
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MENVFTVSSDPHPSPAAPPSLSLPLSSSSTSSGTKKQKRTPTYQRSM
FT (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_045615"
FT VAR_SEQ 104..134
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10931946,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:2052355, ECO:0000303|Ref.9"
FT /id="VSP_001138"
FT CONFLICT 31
FT /note="E -> G (in Ref. 2; AAD27787)"
FT /evidence="ECO:0000305"
FT CONFLICT 92..95
FT /note="QEIL -> TRNP (in Ref. 2; AAD27787)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="L -> P (in Ref. 5; CAH18231)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="T -> P (in Ref. 2; AAD27787)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="S -> G (in Ref. 5; CAH18269)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="F -> L (in Ref. 5; CAH18269)"
FT /evidence="ECO:0000305"
FT CONFLICT 363..385
FT /note="IKCVDRDVRMFFHFSEILDGNQL -> HPSVWIRECSVCSFPLPVKFWMGTS
FT S (in Ref. 2; AAD27787)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="V -> I (in Ref. 5; CAH18269)"
FT /evidence="ECO:0000305"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1WFQ"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:1WFQ"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:1WFQ"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:1WFQ"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1WFQ"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1WFQ"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1WFQ"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:1WFQ"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1WFQ"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:1WFQ"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:2YTX"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:2YTX"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2YTX"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:2YTX"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:2YTX"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:2YTX"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:2YTX"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:2YTX"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:1X65"
FT STRAND 362..370
FT /evidence="ECO:0007829|PDB:1X65"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:1X65"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:1X65"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:1X65"
FT STRAND 519..526
FT /evidence="ECO:0007829|PDB:2YTY"
FT STRAND 528..534
FT /evidence="ECO:0007829|PDB:2YTY"
FT STRAND 536..539
FT /evidence="ECO:0007829|PDB:2YTY"
FT STRAND 541..545
FT /evidence="ECO:0007829|PDB:2YTY"
FT TURN 546..548
FT /evidence="ECO:0007829|PDB:2YTY"
FT TURN 553..555
FT /evidence="ECO:0007829|PDB:2YTY"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:2YTY"
FT STRAND 676..680
FT /evidence="ECO:0007829|PDB:2YTV"
FT STRAND 683..689
FT /evidence="ECO:0007829|PDB:2YTV"
FT STRAND 693..701
FT /evidence="ECO:0007829|PDB:2YTV"
FT TURN 702..704
FT /evidence="ECO:0007829|PDB:2YTV"
FT STRAND 716..718
FT /evidence="ECO:0007829|PDB:2YTV"
FT STRAND 725..727
FT /evidence="ECO:0007829|PDB:2YTV"
SQ SEQUENCE 798 AA; 88885 MW; 2BD0B32F33D454DA CRC64;
MSFDPNLLHN NGHNGYPNGT SAALRETGVI EKLLTSYGFI QCSERQARLF FHCSQYNGNL
QDLKVGDDVE FEVSSDRRTG KPIAVKLVKI KQEILPEERM NGQVVCAVPH NLESKSPAAP
GQSPTGSVCY ERNGEVFYLT YTPEDVEGNV QLETGDKINF VIDNNKHTGA VSARNIMLLK
KKQARCQGVV CAMKEAFGFI ERGDVVKEIF FHYSEFKGDL ETLQPGDDVE FTIKDRNGKE
VATDVRLLPQ GTVIFEDISI EHFEGTVTKV IPKVPSKNQN DPLPGRIKVD FVIPKELPFG
DKDTKSKVTL LEGDHVRFNI STDRRDKLER ATNIEVLSNT FQFTNEAREM GVIAAMRDGF
GFIKCVDRDV RMFFHFSEIL DGNQLHIADE VEFTVVPDML SAQRNHAIRI KKLPKGTVSF
HSHSDHRFLG TVEKEATFSN PKTTSPNKGK EKEAEDGIIA YDDCGVKLTI AFQAKDVEGS
TSPQIGDKVE FSISDKQRPG QQVATCVRLL GRNSNSKRLL GYVATLKDNF GFIETANHDK
EIFFHYSEFS GDVDSLELGD MVEYSLSKGK GNKVSAEKVN KTHSVNGITE EADPTIYSGK
VIRPLRSVDP TQTEYQGMIE IVEEGDMKGE VYPFGIVGMA NKGDCLQKGE SVKFQLCVLG
QNAQTMAYNI TPLRRATVEC VKDQFGFINY EVGDSKKLFF HVKEVQDGIE LQAGDEVEFS
VILNQRTGKC SACNVWRVCE GPKAVAAPRP DRLVNRLKNI TLDDASAPRL MVLRQPRGPD
NSMGFGAERK IRQAGVID
