SRRT_HUMAN
ID SRRT_HUMAN Reviewed; 876 AA.
AC Q9BXP5; A4D2E5; A4D2E6; A6NK22; B4DJL4; B4DZA6; O95808; Q32MI4; Q6NT74;
AC Q8TDQ5; Q9BWP6; Q9BXP4; Q9Y4S4;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2;
GN Name=SRRT; Synonyms=ARS2, ASR2;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1 AND
RP 2).
RX PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W.,
RA Koop B.F.;
RT "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL Nucleic Acids Res. 29:1352-1365(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Yang L., Huang J., Ying K., Pan Z.M., Gu Y.Q., Wang G.Q., Lin S., Wu H.,
RA Yang Q.S., Xie Y., Mao Y.M.;
RT "Cloning and bioinformatic characterization of the full length human
RT homologous asr2 gene.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Testis, and 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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 65-876 (ISOFORM 1).
RC TISSUE=Brain, and Kidney;
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 [MRNA] OF 443-876 (ISOFORMS 2/3).
RA Hu G.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-8; SER-493 AND THR-544, AND
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=18086880; DOI=10.1128/mcb.01565-07;
RA Wilson M.D., Wang D., Wagner R., Breyssens H., Gertsenstein M., Lobe C.,
RA Lu X., Nagy A., Burke R.D., Koop B.F., Howard P.L.;
RT "ARS2 is a conserved eukaryotic gene essential for early mammalian
RT development.";
RL Mol. Cell. Biol. 28:1503-1514(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540 AND THR-544, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [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 FUNCTION.
RX PubMed=19632182; DOI=10.1016/j.cell.2009.04.046;
RA Gruber J.J., Zatechka D.S., Sabin L.R., Yong J., Lum J.J., Kong M.,
RA Zong W.-X., Zhang Z., Lau C.-K., Rawlings J., Cherry S., Ihle J.N.,
RA Dreyfuss G., Thompson C.B.;
RT "Ars2 links the nuclear cap-binding complex to RNA interference and cell
RT proliferation.";
RL Cell 138:328-339(2009).
RN [19]
RP INTERACTION WITH CASP8AP2.
RX PubMed=19546234; DOI=10.1128/mcb.00289-09;
RA Kiriyama M., Kobayashi Y., Saito M., Ishikawa F., Yonehara S.;
RT "Interaction of FLASH with arsenite resistance protein 2 is involved in
RT cell cycle progression at S phase.";
RL Mol. Cell. Biol. 29:4729-4741(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, AND IDENTIFICATION BY
RP 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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20858735; DOI=10.1158/1541-7786.mcr-10-0042;
RA Gilmore-Hebert M., Ramabhadran R., Stern D.F.;
RT "Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage
RT response pathways.";
RL Mol. Cancer Res. 8:1388-1398(2010).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4; SER-74; SER-493 AND THR-544, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [23]
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 [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4 AND THR-544, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-74; SER-136; SER-493;
RP THR-544; THR-671 AND SER-679, 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-74 AND SER-570, 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 [27]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-833; ARG-840 AND ARG-850, 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 [28]
RP INTERACTION WITH NCBP2 AND NCBP3.
RX PubMed=26382858; DOI=10.1038/ncomms9192;
RA Gebhardt A., Habjan M., Benda C., Meiler A., Haas D.A., Hein M.Y., Mann A.,
RA Mann M., Habermann B., Pichlmair A.;
RT "mRNA export through an additional cap-binding complex consisting of NCBP1
RT and NCBP3.";
RL Nat. Commun. 6:8192-8192(2015).
RN [29]
RP INTERACTION WITH LUZP4.
RX PubMed=25662211; DOI=10.1093/nar/gkv070;
RA Viphakone N., Cumberbatch M.G., Livingstone M.J., Heath P.R., Dickman M.J.,
RA Catto J.W., Wilson S.A.;
RT "Luzp4 defines a new mRNA export pathway in cancer cells.";
RL Nucleic Acids Res. 43:2353-2366(2015).
RN [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-150, 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 [31]
RP INTERACTION WITH MTREX.
RX PubMed=30842217; DOI=10.1101/gad.322602.118;
RA Wang J., Chen J., Wu G., Zhang H., Du X., Chen S., Zhang L., Wang K.,
RA Fan J., Gao S., Wu X., Zhang S., Kuai B., Zhao P., Chi B., Wang L., Li G.,
RA Wong C.C.L., Zhou Y., Li J., Yun C., Cheng H.;
RT "NRDE2 negatively regulates exosome functions by inhibiting MTR4
RT recruitment and exosome interaction.";
RL Genes Dev. 33:536-549(2019).
CC -!- FUNCTION: Acts as a mediator between the cap-binding complex (CBC) and
CC the primary microRNAs (miRNAs) processing machinery during cell
CC proliferation. Contributes to the stability and delivery of capped
CC primary miRNA transcripts to the primary miRNA processing complex
CC containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated
CC gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped
CC RNA); however interaction is probably mediated via its interaction with
CC NCBP1/CBP80 component of the CBC complex. Involved in cell cycle
CC progression at S phase. Does not directly confer arsenite resistance
CC but rather modulates arsenic sensitivity. Independently of its activity
CC on miRNAs, necessary and sufficient to promote neural stem cell self-
CC renewal. Does so by directly binding SOX2 promoter and positively
CC regulating its transcription (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:19632182}.
CC -!- SUBUNIT: Interacts with NCBP1 and DROSHA (By similarity). Interacts
CC with CASP8AP2 and ERBB4. Interacts with LUZP4. Interacts with
CC NCBP2/CBP20 and NCBP3 (PubMed:26382858). Interacts with MTREX
CC (PubMed:30842217). {ECO:0000250|UniProtKB:Q99MR6,
CC ECO:0000269|PubMed:19546234, ECO:0000269|PubMed:20858735,
CC ECO:0000269|PubMed:25662211, ECO:0000269|PubMed:26382858,
CC ECO:0000269|PubMed:30842217}.
CC -!- INTERACTION:
CC Q9BXP5; P42858: HTT; NbExp=3; IntAct=EBI-712721, EBI-466029;
CC Q9BXP5-3; P42858: HTT; NbExp=6; IntAct=EBI-25866384, EBI-466029;
CC Q9BXP5-4; P42858: HTT; NbExp=3; IntAct=EBI-16701991, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Note=Predominantly nuclear. Shuttles between the nucleus
CC and the cytoplasm in a CRM1-dependent way (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=A;
CC IsoId=Q9BXP5-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q9BXP5-2; Sequence=VSP_000324;
CC Name=3;
CC IsoId=Q9BXP5-3; Sequence=VSP_032502;
CC Name=4;
CC IsoId=Q9BXP5-4; Sequence=VSP_032502, VSP_000324;
CC Name=5;
CC IsoId=Q9BXP5-5; Sequence=VSP_038122, VSP_038123;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:18086880}.
CC -!- SIMILARITY: Belongs to the ARS2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD17774.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM00189.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAG58876.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAL23816.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF312032; AAK21005.1; -; Genomic_DNA.
DR EMBL; AF312032; AAK21006.1; -; Genomic_DNA.
DR EMBL; AF248955; AAM00189.1; ALT_FRAME; mRNA.
DR EMBL; AL096723; CAB46374.2; -; mRNA.
DR EMBL; AK296131; BAG58876.1; ALT_INIT; mRNA.
DR EMBL; AK302820; BAG64018.1; -; mRNA.
DR EMBL; AC011895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236956; EAL23815.1; -; Genomic_DNA.
DR EMBL; CH236956; EAL23816.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471091; EAW76467.1; -; Genomic_DNA.
DR EMBL; BC000082; AAH00082.2; -; mRNA.
DR EMBL; BC069249; AAH69249.1; -; mRNA.
DR EMBL; BC109117; AAI09118.1; -; mRNA.
DR EMBL; AF082871; AAD17774.1; ALT_INIT; mRNA.
DR CCDS; CCDS34709.1; -. [Q9BXP5-1]
DR CCDS; CCDS47665.1; -. [Q9BXP5-2]
DR CCDS; CCDS47666.1; -. [Q9BXP5-3]
DR CCDS; CCDS47667.1; -. [Q9BXP5-4]
DR PIR; T12455; T12455.
DR RefSeq; NP_001122324.1; NM_001128852.1. [Q9BXP5-3]
DR RefSeq; NP_001122325.1; NM_001128853.1. [Q9BXP5-2]
DR RefSeq; NP_001122326.1; NM_001128854.1. [Q9BXP5-4]
DR RefSeq; NP_056992.4; NM_015908.5. [Q9BXP5-1]
DR PDB; 5OO6; X-ray; 2.80 A; C/F/I/L/O/R/U/X=832-876.
DR PDB; 6F7J; X-ray; 3.22 A; A=171-270, B=409-764.
DR PDB; 6F7P; X-ray; 3.70 A; A/B=147-270, C/D=409-764.
DR PDB; 6F7S; X-ray; 3.37 A; A/B=147-270, C/D=409-568, C/D=600-764.
DR PDB; 6F8D; X-ray; 3.48 A; A/B=171-270, C/D=409-764.
DR PDBsum; 5OO6; -.
DR PDBsum; 6F7J; -.
DR PDBsum; 6F7P; -.
DR PDBsum; 6F7S; -.
DR PDBsum; 6F8D; -.
DR AlphaFoldDB; Q9BXP5; -.
DR SMR; Q9BXP5; -.
DR BioGRID; 119626; 248.
DR CORUM; Q9BXP5; -.
DR IntAct; Q9BXP5; 79.
DR MINT; Q9BXP5; -.
DR STRING; 9606.ENSP00000480421; -.
DR GlyGen; Q9BXP5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BXP5; -.
DR MetOSite; Q9BXP5; -.
DR PhosphoSitePlus; Q9BXP5; -.
DR SwissPalm; Q9BXP5; -.
DR BioMuta; SRRT; -.
DR DMDM; 20137457; -.
DR EPD; Q9BXP5; -.
DR jPOST; Q9BXP5; -.
DR MassIVE; Q9BXP5; -.
DR MaxQB; Q9BXP5; -.
DR PaxDb; Q9BXP5; -.
DR PeptideAtlas; Q9BXP5; -.
DR PRIDE; Q9BXP5; -.
DR ProteomicsDB; 79475; -. [Q9BXP5-1]
DR ProteomicsDB; 79476; -. [Q9BXP5-2]
DR ProteomicsDB; 79477; -. [Q9BXP5-3]
DR ProteomicsDB; 79478; -. [Q9BXP5-4]
DR ProteomicsDB; 79479; -. [Q9BXP5-5]
DR ABCD; Q9BXP5; 1 sequenced antibody.
DR Antibodypedia; 30897; 153 antibodies from 27 providers.
DR DNASU; 51593; -.
DR Ensembl; ENST00000611405.5; ENSP00000480421.1; ENSG00000087087.20. [Q9BXP5-1]
DR Ensembl; ENST00000614484.4; ENSP00000481173.1; ENSG00000087087.20. [Q9BXP5-3]
DR Ensembl; ENST00000618262.4; ENSP00000478341.1; ENSG00000087087.20. [Q9BXP5-2]
DR Ensembl; ENST00000618411.4; ENSP00000483556.1; ENSG00000087087.20. [Q9BXP5-4]
DR GeneID; 51593; -.
DR KEGG; hsa:51593; -.
DR MANE-Select; ENST00000611405.5; ENSP00000480421.1; NM_015908.6; NP_056992.4.
DR UCSC; uc032zzu.2; human. [Q9BXP5-1]
DR CTD; 51593; -.
DR DisGeNET; 51593; -.
DR GeneCards; SRRT; -.
DR HGNC; HGNC:24101; SRRT.
DR HPA; ENSG00000087087; Low tissue specificity.
DR MIM; 614469; gene.
DR neXtProt; NX_Q9BXP5; -.
DR OpenTargets; ENSG00000087087; -.
DR PharmGKB; PA164726295; -.
DR VEuPathDB; HostDB:ENSG00000087087; -.
DR eggNOG; KOG2295; Eukaryota.
DR GeneTree; ENSGT00390000005492; -.
DR HOGENOM; CLU_008560_0_0_1; -.
DR InParanoid; Q9BXP5; -.
DR OMA; QVGFNWF; -.
DR OrthoDB; 525905at2759; -.
DR PhylomeDB; Q9BXP5; -.
DR TreeFam; TF317609; -.
DR PathwayCommons; Q9BXP5; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9BXP5; -.
DR BioGRID-ORCS; 51593; 660 hits in 1081 CRISPR screens.
DR ChiTaRS; SRRT; human.
DR GeneWiki; ARS2; -.
DR GenomeRNAi; 51593; -.
DR Pharos; Q9BXP5; Tbio.
DR PRO; PR:Q9BXP5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9BXP5; protein.
DR Bgee; ENSG00000087087; Expressed in left testis and 206 other tissues.
DR ExpressionAtlas; Q9BXP5; baseline and differential.
DR Genevisible; Q9BXP5; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0140262; F:mRNA cap binding complex binding; IDA:FlyBase.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IEA:Ensembl.
DR GO; GO:0031053; P:primary miRNA processing; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0046685; P:response to arsenic-containing substance; NAS:UniProtKB.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR039727; SE/Ars2.
DR InterPro; IPR007042; SERRATE/Ars2_C.
DR InterPro; IPR021933; SERRATE/Ars2_N.
DR PANTHER; PTHR13165; PTHR13165; 2.
DR Pfam; PF04959; ARS2; 1.
DR Pfam; PF12066; SERRATE_Ars2_N; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Cytoplasm;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-mediated gene silencing; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CHAIN 2..876
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000220965"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..383
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 8
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 544
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 671
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 833
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 840
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 850
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 150
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 196..231
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038122"
FT VAR_SEQ 387
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038123"
FT VAR_SEQ 388
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032502"
FT VAR_SEQ 776..780
FT /note="ILPPG -> S (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_000324"
FT CONFLICT 106
FT /note="G -> GG (in Ref. 3; CAB46374)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="D -> E (in Ref. 2; AAM00189)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="N -> Y (in Ref. 2; AAM00189)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="D -> Y (in Ref. 4; BAG64018)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="R -> K (in Ref. 4; BAG64018)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="R -> W (in Ref. 3; CAB46374)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="V -> A (in Ref. 3; CAB46374)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="K -> R (in Ref. 3; CAB46374)"
FT /evidence="ECO:0000305"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:6F7S"
FT HELIX 175..190
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 203..230
FT /evidence="ECO:0007829|PDB:6F7J"
FT TURN 231..235
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 243..257
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:6F7J"
FT STRAND 422..428
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 434..442
FT /evidence="ECO:0007829|PDB:6F7J"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:6F7J"
FT STRAND 463..469
FT /evidence="ECO:0007829|PDB:6F7J"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:6F7S"
FT HELIX 475..481
FT /evidence="ECO:0007829|PDB:6F7J"
FT TURN 482..484
FT /evidence="ECO:0007829|PDB:6F7J"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:6F8D"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:6F7J"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 509..512
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 514..535
FT /evidence="ECO:0007829|PDB:6F7J"
FT STRAND 540..544
FT /evidence="ECO:0007829|PDB:6F7S"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 562..565
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 571..577
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 603..618
FT /evidence="ECO:0007829|PDB:6F7J"
FT TURN 624..627
FT /evidence="ECO:0007829|PDB:6F7J"
FT TURN 631..635
FT /evidence="ECO:0007829|PDB:6F7J"
FT STRAND 636..638
FT /evidence="ECO:0007829|PDB:6F7J"
FT STRAND 643..646
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 658..670
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 671..674
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 682..688
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 693..704
FT /evidence="ECO:0007829|PDB:6F7J"
FT STRAND 706..709
FT /evidence="ECO:0007829|PDB:6F7S"
FT STRAND 712..714
FT /evidence="ECO:0007829|PDB:6F7S"
FT TURN 716..719
FT /evidence="ECO:0007829|PDB:6F7J"
FT STRAND 721..724
FT /evidence="ECO:0007829|PDB:6F7S"
FT HELIX 725..734
FT /evidence="ECO:0007829|PDB:6F7J"
FT HELIX 737..755
FT /evidence="ECO:0007829|PDB:6F7J"
FT STRAND 756..758
FT /evidence="ECO:0007829|PDB:6F7J"
SQ SEQUENCE 876 AA; 100666 MW; EB3ABD1325EA98D9 CRC64;
MGDSDDEYDR RRRDKFRRER SDYDRSRERD ERRRGDDWND REWDRGRERR SRGEYRDYDR
NRRERFSPPR HELSPPQKRM RRDWDEHSSD PYHSGYEMPY AGGGGGPTYG PPQPWGHPDV
HIMQHHVLPI QARLGSIAEI DLGVPPPVMK TFKEFLLSLD DSVDETEAVK RYNDYKLDFR
RQQMQDFFLA HKDEEWFRSK YHPDEVGKRR QEARGALQNR LRVFLSLMET GWFDNLLLDI
DKADAIVKML DAAVIKMEGG TENDLRILEQ EEEEEQAGKP GEPSKKEEGR AGAGLGDGER
KTNDKDEKKE DGKQAENDSS NDDKTKKSEG DGDKEEKKED SEKEAKKSSK KRNRKHSGDD
SFDEGSVSES ESESESGQAE EEKEEAEEAL KEKEKPKEEE WEKPKDAAGL ECKPRPLHKT
CSLFMRNIAP NISRAEIISL CKRYPGFMRV ALSEPQPERR FFRRGWVTFD RSVNIKEICW
NLQNIRLREC ELSPGVNRDL TRRVRNINGI TQHKQIVRND IKLAAKLIHT LDDRTQLWAS
EPGTPPLPTS LPSQNPILKN ITDYLIEEVS AEEEELLGSS GGAPPEEPPK EGNPAEINVE
RDEKLIKVLD KLLLYLRIVH SLDYYNTCEY PNEDEMPNRC GIIHVRGPMP PNRISHGEVL
EWQKTFEEKL TPLLSVRESL SEEEAQKMGR KDPEQEVEKF VTSNTQELGK DKWLCPLSGK
KFKGPEFVRK HIFNKHAEKI EEVKKEVAFF NNFLTDAKRP ALPEIKPAQP PGPAQILPPG
LTPGLPYPHQ TPQGLMPYGQ PRPPILGYGA GAVRPAVPTG GPPYPHAPYG AGRGNYDAFR
GQGGYPGKPR NRMVRGDPRA IVEYRDLDAP DDVDFF
