PUM2_HUMAN
ID PUM2_HUMAN Reviewed; 1066 AA.
AC Q8TB72; B3KSL0; B4E2B6; D6W527; O00234; Q53TV7; Q8WY43; Q9HAN2;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Pumilio homolog 2;
DE Short=Pumilio-2;
GN Name=PUM2; Synonyms=KIAA0235, PUMH2;
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 3), AND TISSUE SPECIFICITY.
RX PubMed=12459267; DOI=10.1016/s0378-1119(02)01060-0;
RA Spassov D.S., Jurecic R.;
RT "Cloning and comparative sequence analysis of PUM1 and PUM2 genes, human
RT members of the Pumilio family of RNA-binding proteins.";
RL Gene 299:195-204(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Trachea;
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=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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 578-1066 (ISOFORM 1).
RC TISSUE=Lung, and Placenta;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 110-1066 (ISOFORM 2), TISSUE SPECIFICITY,
RP RNA-BINDING, AND INTERACTION WITH DAZ1 AND DAZL.
RX PubMed=12511597; DOI=10.1073/pnas.0234478100;
RA Moore F.L., Jaruzelska J., Fox M.S., Urano J., Firpo M.T., Turek P.J.,
RA Dorfman D.M., Reijo Pera R.A.;
RT "Human Pumilio-2 is expressed in embryonic stem cells and germ cells and
RT interacts with DAZ (Deleted in AZoospermia) and DAZ-like proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:538-543(2003).
RN [9]
RP INDUCTION.
RX PubMed=12771951; DOI=10.1038/sj.onc.1206537;
RA Dazard J.-E., Gal H., Amariglio N., Rechavi G., Domany E., Givol D.;
RT "Genome-wide comparison of human keratinocyte and squamous cell carcinoma
RT responses to UVB irradiation: implications for skin and epithelial
RT cancer.";
RL Oncogene 22:2993-3006(2003).
RN [10]
RP HOMODIMERIZATION, AND INTERACTION WITH NANOS1.
RX PubMed=12690449; DOI=10.1007/s00427-003-0303-2;
RA Jaruzelska J., Kotecki M., Kusz K., Spik A., Firpo M., Reijo Pera R.A.;
RT "Conservation of a Pumilio-Nanos complex from Drosophila germ plasm to
RT human germ cells.";
RL Dev. Genes Evol. 213:120-126(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, 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 [12]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=18776931; DOI=10.1371/journal.pone.0003164;
RA Galgano A., Forrer M., Jaskiewicz L., Kanitz A., Zavolan M., Gerber A.P.;
RT "Comparative analysis of mRNA targets for human PUF-family proteins
RT suggests extensive interaction with the miRNA regulatory system.";
RL PLoS ONE 3:E3164-E3164(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-178; SER-182; THR-184
RP AND SER-587, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP 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 [16]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH SNAPIN AND
RP NANOS1.
RX PubMed=19168546; DOI=10.1093/molehr/gap004;
RA Ginter-Matuszewska B., Spik A., Rembiszewska A., Koyias C.,
RA Kupryjanczyk J., Jaruzelska J.;
RT "The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1 proteins
RT in human male germ cells.";
RL Mol. Hum. Reprod. 15:173-179(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-184, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-182 AND SER-587, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
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 [20]
RP INTERACTION WITH DDX20.
RX PubMed=21800163; DOI=10.1007/s00418-011-0842-y;
RA Ginter-Matuszewska B., Kusz K., Spik A., Grzeszkowiak D., Rembiszewska A.,
RA Kupryjanczyk J., Jaruzelska J.;
RT "NANOS1 and PUMILIO2 bind microRNA biogenesis factor GEMIN3, within
RT chromatoid body in human germ cells.";
RL Histochem. Cell Biol. 136:279-287(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-587, 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 [22]
RP FUNCTION.
RX PubMed=22345517; DOI=10.1101/gad.182568.111;
RA Miles W.O., Tschop K., Herr A., Ji J.Y., Dyson N.J.;
RT "Pumilio facilitates miRNA regulation of the E2F3 oncogene.";
RL Genes Dev. 26:356-368(2012).
RN [23]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH A DEADENYLASE COMPLEX.
RX PubMed=22955276; DOI=10.1074/jbc.m112.373522;
RA Van Etten J., Schagat T.L., Hrit J., Weidmann C.A., Brumbaugh J.,
RA Coon J.J., Goldstrohm A.C.;
RT "Human Pumilio proteins recruit multiple deadenylases to efficiently
RT repress messenger RNAs.";
RL J. Biol. Chem. 287:36370-36383(2012).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-82; SER-136; SER-178;
RP SER-182; SER-587 AND SER-700, 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 [25]
RP INTERACTION WITH TRIM71.
RX PubMed=23125361; DOI=10.1093/nar/gks1032;
RA Loedige I., Gaidatzis D., Sack R., Meister G., Filipowicz W.;
RT "The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA
RT function.";
RL Nucleic Acids Res. 41:518-532(2013).
RN [26]
RP FUNCTION.
RX PubMed=25349211; DOI=10.1074/jbc.m114.585505;
RA Huang G., Stock C., Bommelje C.C., Weeda V.B., Shah K., Bains S., Buss E.,
RA Shaha M., Rechler W., Ramanathan S.Y., Singh B.;
RT "SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of
RT SCCRO (DCUN1D1).";
RL J. Biol. Chem. 289:34728-34742(2014).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND THR-396, 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 [28]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DHX58.
RX PubMed=25340845; DOI=10.1371/journal.ppat.1004417;
RA Narita R., Takahasi K., Murakami E., Hirano E., Yamamoto S.P., Yoneyama M.,
RA Kato H., Fujita T.;
RT "A novel function of human Pumilio proteins in cytoplasmic sensing of viral
RT infection.";
RL PLoS Pathog. 10:E1004417-E1004417(2014).
RN [29]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=26724866; DOI=10.1016/j.cell.2015.12.017;
RA Lee S., Kopp F., Chang T.C., Sataluri A., Chen B., Sivakumar S., Yu H.,
RA Xie Y., Mendell J.T.;
RT "Noncoding RNA NORAD regulates genomic stability by sequestering PUMILIO
RT proteins.";
RL Cell 164:69-80(2016).
RN [30]
RP FUNCTION, AND MIRNA-BINDING.
RX PubMed=28431233; DOI=10.1016/j.molcel.2017.03.014;
RA Treiber T., Treiber N., Plessmann U., Harlander S., Daiss J.L., Eichner N.,
RA Lehmann G., Schall K., Urlaub H., Meister G.;
RT "A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis.";
RL Mol. Cell 66:270-284(2017).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 706-1056 IN COMPLEX WITH CONSENSUS
RP MRNA, FUNCTION, AND PUMILIO REPEATS.
RX PubMed=21397187; DOI=10.1016/j.str.2010.12.019;
RA Lu G., Hall T.M.;
RT "Alternate modes of cognate RNA recognition by human PUMILIO proteins.";
RL Structure 19:361-367(2011).
CC -!- FUNCTION: Sequence-specific RNA-binding protein that acts as a post-
CC transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds
CC to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-
CC UGUANAUA-3', that is related to the Nanos Response Element (NRE) (,
CC PubMed:21397187). Mediates post-transcriptional repression of
CC transcripts via different mechanisms: acts via direct recruitment of
CC the CCR4-POP2-NOT deadenylase leading to translational inhibition and
CC mRNA degradation (PubMed:22955276). Also mediates deadenylation-
CC independent repression by promoting accessibility of miRNAs
CC (PubMed:18776931, PubMed:22345517). Acts as a post-transcriptional
CC repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA
CC regulation (PubMed:22345517). Plays a role in cytoplasmic sensing of
CC viral infection (PubMed:25340845). Represses a program of genes
CC necessary to maintain genomic stability such as key mitotic, DNA repair
CC and DNA replication factors. Its ability to repress those target mRNAs
CC is regulated by the lncRNA NORAD (non-coding RNA activated by DNA
CC damage) which, due to its high abundance and multitude of PUMILIO
CC binding sites, is able to sequester a significant fraction of PUM1 and
CC PUM2 in the cytoplasm (PubMed:26724866). May regulate DCUN1D3 mRNA
CC levels (PubMed:25349211). May support proliferation and self-renewal of
CC stem cells. Binds specifically to miRNA MIR199A precursor, with PUM1,
CC regulates miRNA MIR199A expression at a postranscriptional level
CC (PubMed:28431233). {ECO:0000269|PubMed:18776931,
CC ECO:0000269|PubMed:21397187, ECO:0000269|PubMed:22345517,
CC ECO:0000269|PubMed:22955276, ECO:0000269|PubMed:25340845,
CC ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26724866,
CC ECO:0000269|PubMed:28431233}.
CC -!- SUBUNIT: Homodimer; homodimerizes in vitro. Interacts with DAZ1, DAZL
CC and NANOS1 via its pumilio repeats. Interacts with NANOS3 (By
CC similarity). Interacts with SNAPIN. Recruits the CCR4-POP2-NOT
CC deadenylase leading to translational inhibition and mRNA degradation.
CC Interacts with DDX20. In case of viral infection, interacts with DHX58
CC (PubMed:25340845). Interacts with TRIM71 (via NHL repeats) in an RNA-
CC dependent manner (PubMed:23125361). {ECO:0000250|UniProtKB:Q80U58,
CC ECO:0000269|PubMed:12511597, ECO:0000269|PubMed:12690449,
CC ECO:0000269|PubMed:19168546, ECO:0000269|PubMed:21397187,
CC ECO:0000269|PubMed:21800163, ECO:0000269|PubMed:22955276,
CC ECO:0000269|PubMed:23125361, ECO:0000269|PubMed:25340845}.
CC -!- INTERACTION:
CC Q8TB72; Q8N9W6: BOLL; NbExp=3; IntAct=EBI-311190, EBI-998198;
CC Q8TB72; Q9NQZ3: DAZ1; NbExp=5; IntAct=EBI-311190, EBI-997955;
CC Q8TB72; Q9Q2G4: ORF; Xeno; NbExp=3; IntAct=EBI-311190, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:19168546}.
CC Cytoplasmic granule {ECO:0000269|PubMed:25340845}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:19168546}. Note=The cytoplasmic
CC granules are stress granules which are a dense aggregation in the
CC cytosol composed of proteins and RNAs that appear when the cell is
CC under stress. Colocalizes with NANOS3 in the stress granules.
CC Colocalizes with NANOS1 and SNAPIN in the perinuclear region of germ
CC cells. {ECO:0000269|PubMed:25340845}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8TB72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TB72-2; Sequence=VSP_009319;
CC Name=3;
CC IsoId=Q8TB72-3; Sequence=VSP_009320;
CC Name=4;
CC IsoId=Q8TB72-4; Sequence=VSP_053705, VSP_009320;
CC -!- TISSUE SPECIFICITY: Expressed in male germ cells of adult testis (at
CC protein level). Highly expressed in testis and ovary. Predominantly
CC expressed in stem cells and germ cells. Expressed at lower level in
CC brain, heart, kidney, liver, muscle, placenta, intestine and stomach
CC Expressed in cerebellum, corpus callosum, caudate nucleus, hippocampus,
CC medulla oblongata and putamen. Expressed in all fetal tissues tested.
CC {ECO:0000269|PubMed:12459267, ECO:0000269|PubMed:12511597,
CC ECO:0000269|PubMed:19168546}.
CC -!- INDUCTION: Down-regulated in keratinocytes upon UVB irradiation.
CC {ECO:0000269|PubMed:12771951}.
CC -!- DOMAIN: The pumilio repeats mediate the association with RNA by packing
CC together to form a right-handed superhelix that approximates a half
CC donut. RNA-binding occurs on the concave side of the surface
CC (PubMed:21397187). PUM2 is composed of 8 pumilio repeats of 36
CC residues; each repeat binds a single nucleotide in its RNA target.
CC Residues at positions 12 and 16 of the pumilio repeat bind each RNA
CC base via hydrogen bonding or van der Waals contacts with the Watson-
CC Crick edge, while the amino acid at position 13 makes a stacking
CC interaction. The recognition of RNA by pumilio repeats is base
CC specific: cysteine and glutamine at position 12 and 16, respectively,
CC bind adenine; asparagine and glutamine bind uracil; and serine and
CC glutamate bind guanine. {ECO:0000250|UniProtKB:Q14671,
CC ECO:0000269|PubMed:21397187}.
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DR EMBL; AF315591; AAG31806.1; -; mRNA.
DR EMBL; D87078; BAA19665.3; -; mRNA.
DR EMBL; AK093847; BAG52772.1; -; mRNA.
DR EMBL; AK304198; BAG65078.1; -; mRNA.
DR EMBL; AC007041; AAY15026.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00821.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00823.1; -; Genomic_DNA.
DR EMBL; BC024218; AAH24218.2; -; mRNA.
DR EMBL; BC112046; AAI12047.1; -; mRNA.
DR EMBL; BC112048; AAI12049.1; -; mRNA.
DR EMBL; AF272350; AAL36981.1; -; mRNA.
DR CCDS; CCDS1698.1; -. [Q8TB72-3]
DR CCDS; CCDS74487.1; -. [Q8TB72-4]
DR RefSeq; NP_001269681.1; NM_001282752.1. [Q8TB72-4]
DR RefSeq; NP_056132.1; NM_015317.2. [Q8TB72-3]
DR RefSeq; XP_005262664.1; XM_005262607.1. [Q8TB72-1]
DR RefSeq; XP_005262666.1; XM_005262609.1. [Q8TB72-2]
DR RefSeq; XP_006712036.1; XM_006711973.1.
DR RefSeq; XP_006712037.1; XM_006711974.2. [Q8TB72-1]
DR RefSeq; XP_011531021.1; XM_011532719.1. [Q8TB72-1]
DR RefSeq; XP_011531022.1; XM_011532720.2. [Q8TB72-1]
DR RefSeq; XP_011531023.1; XM_011532721.2. [Q8TB72-1]
DR RefSeq; XP_016859190.1; XM_017003701.1.
DR RefSeq; XP_016859191.1; XM_017003702.1.
DR RefSeq; XP_016859196.1; XM_017003707.1.
DR RefSeq; XP_016859197.1; XM_017003708.1.
DR PDB; 3Q0Q; X-ray; 2.00 A; A=706-1056.
DR PDB; 3Q0R; X-ray; 2.00 A; A=706-1056.
DR PDB; 3Q0S; X-ray; 2.00 A; A=706-1056.
DR PDBsum; 3Q0Q; -.
DR PDBsum; 3Q0R; -.
DR PDBsum; 3Q0S; -.
DR AlphaFoldDB; Q8TB72; -.
DR SMR; Q8TB72; -.
DR BioGRID; 116949; 152.
DR IntAct; Q8TB72; 22.
DR MINT; Q8TB72; -.
DR STRING; 9606.ENSP00000338173; -.
DR GlyGen; Q8TB72; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TB72; -.
DR PhosphoSitePlus; Q8TB72; -.
DR BioMuta; PUM2; -.
DR DMDM; 41688714; -.
DR EPD; Q8TB72; -.
DR jPOST; Q8TB72; -.
DR MassIVE; Q8TB72; -.
DR MaxQB; Q8TB72; -.
DR PaxDb; Q8TB72; -.
DR PeptideAtlas; Q8TB72; -.
DR PRIDE; Q8TB72; -.
DR ProteomicsDB; 5806; -.
DR ProteomicsDB; 73970; -. [Q8TB72-1]
DR ProteomicsDB; 73971; -. [Q8TB72-2]
DR ProteomicsDB; 73972; -. [Q8TB72-3]
DR Antibodypedia; 12999; 433 antibodies from 38 providers.
DR DNASU; 23369; -.
DR Ensembl; ENST00000338086.9; ENSP00000338173.5; ENSG00000055917.16. [Q8TB72-3]
DR Ensembl; ENST00000361078.7; ENSP00000354370.4; ENSG00000055917.16. [Q8TB72-3]
DR GeneID; 23369; -.
DR KEGG; hsa:23369; -.
DR MANE-Select; ENST00000361078.7; ENSP00000354370.4; NM_015317.5; NP_056132.1. [Q8TB72-3]
DR UCSC; uc002rdt.2; human. [Q8TB72-1]
DR CTD; 23369; -.
DR DisGeNET; 23369; -.
DR GeneCards; PUM2; -.
DR HGNC; HGNC:14958; PUM2.
DR HPA; ENSG00000055917; Low tissue specificity.
DR MIM; 607205; gene.
DR neXtProt; NX_Q8TB72; -.
DR OpenTargets; ENSG00000055917; -.
DR PharmGKB; PA34043; -.
DR VEuPathDB; HostDB:ENSG00000055917; -.
DR eggNOG; KOG1488; Eukaryota.
DR GeneTree; ENSGT00940000157575; -.
DR InParanoid; Q8TB72; -.
DR OMA; TPGHCLT; -.
DR OrthoDB; 207351at2759; -.
DR PhylomeDB; Q8TB72; -.
DR TreeFam; TF318160; -.
DR PathwayCommons; Q8TB72; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q8TB72; -.
DR SIGNOR; Q8TB72; -.
DR BioGRID-ORCS; 23369; 29 hits in 1079 CRISPR screens.
DR ChiTaRS; PUM2; human.
DR EvolutionaryTrace; Q8TB72; -.
DR GeneWiki; PUM2; -.
DR GenomeRNAi; 23369; -.
DR Pharos; Q8TB72; Tbio.
DR PRO; PR:Q8TB72; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8TB72; protein.
DR Bgee; ENSG00000055917; Expressed in colonic epithelium and 212 other tissues.
DR ExpressionAtlas; Q8TB72; baseline and differential.
DR Genevisible; Q8TB72; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0106222; F:lncRNA binding; IEA:Ensembl.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0062104; F:pumilio-response element binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0051276; P:chromosome organization; IEA:Ensembl.
DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR GO; GO:0035196; P:miRNA processing; IMP:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; IMP:UniProtKB.
DR GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; IDA:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IDA:MGI.
DR GO; GO:0051983; P:regulation of chromosome segregation; IDA:UniProtKB.
DR GO; GO:0060964; P:regulation of miRNA-mediated gene silencing; TAS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; IDA:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR GO; GO:0034063; P:stress granule assembly; IEA:Ensembl.
DR CDD; cd07920; Pumilio; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR033712; Pumilio_RNA-bd.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR Pfam; PF00806; PUF; 8.
DR SMART; SM00025; Pumilio; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50302; PUM; 8.
DR PROSITE; PS50303; PUM_HD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Translation regulation.
FT CHAIN 1..1066
FT /note="Pumilio homolog 2"
FT /id="PRO_0000075919"
FT DOMAIN 706..1048
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 726..761
FT /note="Pumilio 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REPEAT 762..797
FT /note="Pumilio 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REPEAT 798..835
FT /note="Pumilio 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REPEAT 836..871
FT /note="Pumilio 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REPEAT 872..907
FT /note="Pumilio 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REPEAT 908..943
FT /note="Pumilio 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REPEAT 944..979
FT /note="Pumilio 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REPEAT 983..1022
FT /note="Pumilio 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REGION 1..260
FT /note="Interaction with SNAPIN"
FT /evidence="ECO:0000269|PubMed:19168546"
FT REGION 106..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..745
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 777..781
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 813..817
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 851..855
FT /note="Non-specific-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 887..891
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 923..927
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 959..963
FT /note="Guanine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1002..1006
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT COMPBIAS 106..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 184
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 587
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 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 674
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053705"
FT VAR_SEQ 574..652
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12511597"
FT /id="VSP_009319"
FT VAR_SEQ 829..830
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12459267,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9039502"
FT /id="VSP_009320"
FT VARIANT 367
FT /note="N -> S (in dbSNP:rs34032508)"
FT /id="VAR_057100"
FT HELIX 709..715
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 724..727
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT TURN 728..730
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 731..735
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 738..748
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 753..765
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 767..771
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT TURN 774..776
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 777..786
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 789..799
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 803..808
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 812..822
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 828..835
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT TURN 836..839
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 841..846
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 850..860
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 863..866
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 867..872
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT TURN 873..876
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 877..881
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 886..896
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 899..911
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 913..916
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 922..932
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 935..945
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 949..953
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 958..968
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 971..982
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT STRAND 987..989
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 991..996
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 1001..1011
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 1014..1024
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 1025..1027
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 1028..1033
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 1035..1037
FT /evidence="ECO:0007829|PDB:3Q0Q"
FT HELIX 1040..1045
FT /evidence="ECO:0007829|PDB:3Q0Q"
SQ SEQUENCE 1066 AA; 114216 MW; CF6F9D7998CD5D9E CRC64;
MNHDFQALAL ESRGMGELLP TKKFWEPDDS TKDGQKGIFL GDDEWRETAW GASHHSMSQP
IMVQRRSGQG FHGNSEVNAI LSPRSESGGL GVSMVEYVLS SSPADKLDSR FRKGNFGTRD
AETDGPEKGD QKGKASPFEE DQNRDLKQGD DDDSKINGRG LPNGMDADCK DFNRTPGSRQ
ASPTEVVERL GPNTNPSEGL GPLPNPTANK PLVEEFSNPE TQNLDAMEQV GLESLQFDYP
GNQVPMDSSG ATVGLFDYNS QQQLFQRTNA LTVQQLTAAQ QQQYALAAAQ QPHIAGVFSA
GLAPAAFVPN PYIISAAPPG TDPYTAAGLA AAATLAGPAV VPPQYYGVPW GVYPANLFQQ
QAAAAANNTA SQQAASQAQP GQQQVLRAGA GQRPLTPNQG QQGQQAESLA AAAAANPTLA
FGQGLATGMP GYQVLAPTAY YDQTGALVVG PGARTGLGAP VRLMAPTPVL ISSAAAQAAA
AAAAGGTASS LTGSTNGLFR PIGTQPPQQQ QQQPSTNLQS NSFYGSSSLT NSSQSSSLFS
HGPGQPGSTS LGFGSGNSLG AAIGSALSGF GSSVGSSASS SATRRESLST SSDLYKRSSS
SLAPIGQPFY NSLGFSSSPS PIGMPLPSQT PGHSLTPPPS LSSHGSSSSL HLGGLTNGSG
RYISAAPGAE AKYRSASSTS SLFSSSSQLF PPSRLRYNRS DIMPSGRSRL LEDFRNNRFP
NLQLRDLIGH IVEFSQDQHG SRFIQQKLER ATPAERQMVF NEILQAAYQL MTDVFGNYVI
QKFFEFGSLD QKLALATRIR GHVLPLALQM YGCRVIQKAL ESISSDQQVI SEMVKELDGH
VLKCVKDQNG NHVVQKCIEC VQPQSLQFII DAFKGQVFVL STHPYGCRVI QRILEHCTAE
QTLPILEELH QHTEQLVQDQ YGNYVIQHVL EHGRPEDKSK IVSEIRGKVL ALSQHKFASN
VVEKCVTHAS RAERALLIDE VCCQNDGPHS ALYTMMKDQY ANYVVQKMID MAEPAQRKII
MHKIRPHITT LRKYTYGKHI LAKLEKYYLK NSPDLGPIGG PPNGML
