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Pumilio homolog 1 (HsPUM) (Pumilio-1)

 PUM1_HUMAN              Reviewed;        1186 AA.
Q14671; A8K6W4; B4DG92; D3DPN3; E9PCJ0; Q53HH5; Q5VXY7; Q9HAN1;
02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
02-FEB-2004, sequence version 3.
25-OCT-2017, entry version 160.
RecName: Full=Pumilio homolog 1 {ECO:0000305};
Short=HsPUM;
Short=Pumilio-1;
Name=PUM1 {ECO:0000312|HGNC:HGNC:14957};
Synonyms=KIAA0099 {ECO:0000303|PubMed:7788527}, PUMH1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=12459267; DOI=10.1016/S0378-1119(02)01060-0;
Spassov D.S., Jurecic R.;
"Cloning and comparative sequence analysis of PUM1 and PUM2 genes,
human members of the Pumilio family of RNA-binding proteins.";
Gene 299:195-204(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Bone marrow;
PubMed=7788527; DOI=10.1093/dnares/2.1.37;
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. III.
The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:37-43(1995).
[3]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R., Nomura N.;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Coronary artery;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
TISSUE=Amygdala, and Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INDUCTION.
PubMed=12771951; DOI=10.1038/sj.onc.1206537;
Dazard J.-E., Gal H., Amariglio N., Rechavi G., Domany E., Givol D.;
"Genome-wide comparison of human keratinocyte and squamous cell
carcinoma responses to UVB irradiation: implications for skin and
epithelial cancer.";
Oncogene 22:2993-3006(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
FUNCTION, AND RNA-BINDING.
PubMed=18776931; DOI=10.1371/journal.pone.0003164;
Galgano A., Forrer M., Jaskiewicz L., Kanitz A., Zavolan M.,
Gerber A.P.;
"Comparative analysis of mRNA targets for human PUF-family proteins
suggests extensive interaction with the miRNA regulatory system.";
PLoS ONE 3:E3164-E3164(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-75; SER-209 AND
SER-709, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-209; SER-709 AND
SER-806, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, PHOSPHORYLATION AT
SER-209 AND SER-714, AND MUTAGENESIS OF SER-209 AND SER-714.
PubMed=20818387; DOI=10.1038/ncb2105;
Kedde M., van Kouwenhove M., Zwart W., Oude Vrielink J.A., Elkon R.,
Agami R.;
"A Pumilio-induced RNA structure switch in p27-3' UTR controls miR-221
and miR-222 accessibility.";
Nat. Cell Biol. 12:1014-1020(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-106; SER-209 AND
SER-709, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
FUNCTION.
PubMed=20860814; DOI=10.1186/1758-907X-1-17;
Leibovich L., Mandel-Gutfreund Y., Yakhini Z.;
"A structural-based statistical approach suggests a cooperative
activity of PUM1 and miR-410 in human 3'-untranslated regions.";
Silence 1:17-17(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
DOMAIN, FUNCTION, AND MUTAGENESIS OF 863-SER--GLN-867;
899-ASN--GLN-903; 935-CYS--GLN-939; 971-ASN--GLN-975; CYS-1007;
1007-CYS--GLN-1011; 1043-ASN--GLN-1047; 1079-SER--GLU-1083 AND
1122-ASN--GLN-1126.
PubMed=21572425; DOI=10.1038/nchembio.577;
Filipovska A., Razif M.F., Nygaard K.K., Rackham O.;
"A universal code for RNA recognition by PUF proteins.";
Nat. Chem. Biol. 7:425-427(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-709, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
FUNCTION.
PubMed=22345517; DOI=10.1101/gad.182568.111;
Miles W.O., Tschop K., Herr A., Ji J.Y., Dyson N.J.;
"Pumilio facilitates miRNA regulation of the E2F3 oncogene.";
Genes Dev. 26:356-368(2012).
[22]
FUNCTION, SUBUNIT, AND INTERACTION WITH A DEADENYLASE COMPLEX.
PubMed=22955276; DOI=10.1074/jbc.M112.373522;
Van Etten J., Schagat T.L., Hrit J., Weidmann C.A., Brumbaugh J.,
Coon J.J., Goldstrohm A.C.;
"Human Pumilio proteins recruit multiple deadenylases to efficiently
repress messenger RNAs.";
J. Biol. Chem. 287:36370-36383(2012).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; THR-112; SER-124;
SER-159; SER-197; SER-209; SER-709; SER-806 AND SER-822, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
INTERACTION WITH TRIM71.
PubMed=23125361; DOI=10.1093/nar/gks1032;
Loedige I., Gaidatzis D., Sack R., Meister G., Filipowicz W.;
"The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA
function.";
Nucleic Acids Res. 41:518-532(2013).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-229, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-796, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[28]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DHX58.
PubMed=25340845; DOI=10.1371/journal.ppat.1004417;
Narita R., Takahasi K., Murakami E., Hirano E., Yamamoto S.P.,
Yoneyama M., Kato H., Fujita T.;
"A novel function of human Pumilio proteins in cytoplasmic sensing of
viral infection.";
PLoS Pathog. 10:E1004417-E1004417(2014).
[29]
FUNCTION.
PubMed=25768905; DOI=10.1016/j.cell.2015.02.012;
Gennarino V.A., Singh R.K., White J.J., De Maio A., Han K., Kim J.Y.,
Jafar-Nejad P., di Ronza A., Kang H., Sayegh L.S., Cooper T.A.,
Orr H.T., Sillitoe R.V., Zoghbi H.Y.;
"Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
increasing wild-type Ataxin1 levels.";
Cell 160:1087-1098(2015).
[30]
FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=26724866; DOI=10.1016/j.cell.2015.12.017;
Lee S., Kopp F., Chang T.C., Sataluri A., Chen B., Sivakumar S.,
Yu H., Xie Y., Mendell J.T.;
"Noncoding RNA NORAD regulates genomic stability by sequestering
PUMILIO proteins.";
Cell 164:69-80(2016).
[31]
FUNCTION, AND MIRNA-BINDING.
PubMed=28431233; DOI=10.1016/j.molcel.2017.03.014;
Treiber T., Treiber N., Plessmann U., Harlander S., Daiss J.L.,
Eichner N., Lehmann G., Schall K., Urlaub H., Meister G.;
"A Compendium of RNA-Binding Proteins that Regulate MicroRNA
Biogenesis.";
Mol. Cell 66:270-284(2017).
[32]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 828-1166.
PubMed=11336708; DOI=10.1016/S1097-2765(01)00229-5;
Wang X., Zamore P.D., Hall T.M.T.;
"Crystal structure of a Pumilio homology domain.";
Mol. Cell 7:855-865(2001).
[33]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 828-1176 IN COMPLEX WITH RNA,
AND MUTAGENESIS OF 1043-ASN-TYR-1044 AND GLN-1047.
PubMed=12202039; DOI=10.1016/S0092-8674(02)00873-5;
Wang X., McLachlan J., Zamore P.D., Hall T.M.T.;
"Modular recognition of RNA by a human pumilio-homology domain.";
Cell 110:501-512(2002).
[34]
X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 828-1170 IN COMPLEX WITH
CONSENSUS MRNA, FUNCTION, RNA-BINDING, AND DOMAIN.
PubMed=18328718; DOI=10.1016/j.str.2008.01.006;
Gupta Y.K., Nair D.T., Wharton R.P., Aggarwal A.K.;
"Structures of human Pumilio with noncognate RNAs reveal molecular
mechanisms for binding promiscuity.";
Structure 16:549-557(2008).
[35]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 828-1176, FUNCTION,
RNA-BINDING, AND DOMAIN.
PubMed=21653694; DOI=10.1074/jbc.M111.244889;
Dong S., Wang Y., Cassidy-Amstutz C., Lu G., Bigler R., Jezyk M.R.,
Li C., Hall T.M., Wang Z.;
"Specific and modular binding code for cytosine recognition in
Pumilio/FBF (PUF) RNA-binding domains.";
J. Biol. Chem. 286:26732-26742(2011).
[36]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 828-1176 IN COMPLEX WITH
CONSENSUS MRNA, FUNCTION, RNA-BINDING, AND DOMAIN.
PubMed=21397187; DOI=10.1016/j.str.2010.12.019;
Lu G., Hall T.M.;
"Alternate modes of cognate RNA recognition by human PUMILIO
proteins.";
Structure 19:361-367(2011).
-!- FUNCTION: Sequence-specific RNA-binding protein that acts as a
post-transcriptional repressor by binding the 3'-UTR of mRNA
targets. Binds to an RNA consensus sequence, the Pumilio Response
Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos
Response Element (NRE) (PubMed:21572425, PubMed:18328718,
PubMed:21653694, PubMed:21397187). Mediates post-transcriptional
repression of transcripts via different mechanisms: acts via
direct recruitment of the CCR4-POP2-NOT deadenylase leading to
translational inhibition and mRNA degradation (PubMed:22955276).
Also mediates deadenylation-independent repression by promoting
accessibility of miRNAs (PubMed:18776931, PubMed:20818387,
PubMed:20860814, PubMed:22345517). Following growth factor
stimulation, phosphorylated and binds to the 3'-UTR of CDKN1B/p27
mRNA, inducing a local conformational change that exposes miRNA-
binding sites, promoting association of miR-221 and miR-222,
efficient suppression of CDKN1B/p27 expression, and rapid entry to
the cell cycle (PubMed:20818387). Acts as a post-transcriptional
repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating
miRNA regulation (PubMed:22345517). Represses a program of genes
necessary to maintain genomic stability such as key mitotic, DNA
repair and DNA replication factors. Its ability to repress those
target mRNAs is regulated by the lncRNA NORAD (non-coding RNA
activated by DNA damage) which, due to its high abundance and
multitude of PUMILIO binding sites, is able to sequester a
significant fraction of PUM1 and PUM2 in the cytoplasm
(PubMed:26724866). Involved in neuronal functions by regulating
ATXN1 mRNA levels: acts by binding to the 3'-UTR of ATXN1
transcripts, leading to their down-regulation independently of the
miRNA machinery (PubMed:25768905). Plays a role in cytoplasmic
sensing of viral infection (PubMed:25340845). In testis, acts as a
post-transcriptional regulator of spermatogenesis by binding to
the 3'-UTR of mRNAs coding for regulators of p53/TP53. Involved in
embryonic stem cell renewal by facilitating the exit from the
ground state: acts by targeting mRNAs coding for naive
pluripotency transcription factors and accelerates their down-
regulation at the onset of differentiation (By similarity). Binds
specifically to miRNA MIR199A precursor, with PUM2, regulates
miRNA MIR199A expression at a postranscriptional level
(PubMed:28431233). {ECO:0000250|UniProtKB:Q80U78,
ECO:0000269|PubMed:18328718, ECO:0000269|PubMed:18776931,
ECO:0000269|PubMed:20818387, ECO:0000269|PubMed:20860814,
ECO:0000269|PubMed:21397187, ECO:0000269|PubMed:21572425,
ECO:0000269|PubMed:21653694, ECO:0000269|PubMed:22345517,
ECO:0000269|PubMed:22955276, ECO:0000269|PubMed:25340845,
ECO:0000269|PubMed:25768905, ECO:0000269|PubMed:26724866,
ECO:0000269|PubMed:28431233}.
-!- SUBUNIT: Recruits the CCR4-POP2-NOT deadenylase leading to
translational inhibition and mRNA degradation (PubMed:22955276).
In case of viral infection, interacts with DHX58
(PubMed:25340845). Interacts with TRIM71 (via NHL repeats) in an
RNA-dependent manner (PubMed:23125361).
{ECO:0000269|PubMed:22955276, ECO:0000269|PubMed:23125361,
ECO:0000269|PubMed:25340845}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:26724866}.
Cytoplasm, P-body {ECO:0000305|PubMed:20818387}. Cytoplasmic
granule {ECO:0000269|PubMed:25340845}. Note=Recruited to
cytoplasmic stress granules upon viral infection.
{ECO:0000269|PubMed:25340845}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q14671-1; Sequence=Displayed;
Name=2;
IsoId=Q14671-2; Sequence=VSP_017059, VSP_017060, VSP_017061;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q14671-3; Sequence=VSP_017061;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q14671-4; Sequence=VSP_053703, VSP_053704, VSP_017059;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, muscle,
intestine and stomach. Not expressed in cerebellum, corpus
callosum, caudate nucleus, hippocampus, medulla oblongata and
putamen. Expressed in all fetal tissues tested.
{ECO:0000269|PubMed:12459267}.
-!- INDUCTION: Strongly down-regulated in keratinocytes upon UVB
irradiation. {ECO:0000269|PubMed:12771951}.
-!- DOMAIN: The pumilio repeats mediate the association with RNA by
packing together to form a right-handed superhelix that
approximates a half donut. RNA-binding occurs on the concave side
of the surface (PubMed:21397187). PUM1 is composed of 8 pumilio
repeats of 36 residues; each repeat binds a single nucleotide in
its RNA target. Residues at positions 12 and 16 of the pumilio
repeat bind each RNA base via hydrogen bonding or van der Waals
contacts with the Watson-Crick edge, while the amino acid at
position 13 makes a stacking interaction. The recognition of RNA
by pumilio repeats is base specific: cysteine and glutamine at
position 12 and 16, respectively, bind adenine; asparagine and
glutamine bind uracil; and serine and glutamate bind guanine
(PubMed:21572425. PubMed:18328718, PubMed:21653694).
{ECO:0000269|PubMed:18328718, ECO:0000269|PubMed:21397187,
ECO:0000269|PubMed:21572425, ECO:0000269|PubMed:21653694}.
-!- PTM: Phosphorylation at Ser-714 promotes RNA-binding activity.
Following growth factor stimulation phosphorylated at Ser-714,
promoting binding to the 3'-UTR of CDKN1B/p27 mRNA.
{ECO:0000269|PubMed:20818387}.
-!- SEQUENCE CAUTION:
Sequence=BAA07895.3; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF315592; AAG31807.1; -; mRNA.
EMBL; D43951; BAA07895.3; ALT_INIT; mRNA.
EMBL; AL356320; CAH71203.1; -; Genomic_DNA.
EMBL; AL445235; CAH71203.1; JOINED; Genomic_DNA.
EMBL; AK291779; BAF84468.1; -; mRNA.
EMBL; AK294477; BAG57703.1; -; mRNA.
EMBL; AK222605; BAD96325.1; -; mRNA.
EMBL; AL445235; CAI22246.1; -; Genomic_DNA.
EMBL; AL356320; CAI22246.1; JOINED; Genomic_DNA.
EMBL; CH471059; EAX07633.1; -; Genomic_DNA.
EMBL; CH471059; EAX07634.1; -; Genomic_DNA.
EMBL; BC013398; AAH13398.1; -; mRNA.
CCDS; CCDS338.1; -. [Q14671-1]
CCDS; CCDS44099.1; -. [Q14671-3]
RefSeq; NP_001018494.1; NM_001020658.1. [Q14671-3]
RefSeq; NP_055491.1; NM_014676.2. [Q14671-1]
UniGene; Hs.281707; -.
PDB; 1IB2; X-ray; 1.90 A; A=828-1176.
PDB; 1M8W; X-ray; 2.20 A; A/B=828-1176.
PDB; 1M8X; X-ray; 2.20 A; A/B=828-1176.
PDB; 1M8Y; X-ray; 2.60 A; A/B=828-1176.
PDB; 1M8Z; X-ray; 1.90 A; A=828-1176.
PDB; 2YJY; X-ray; 2.60 A; A/B=828-1176.
PDB; 3BSB; X-ray; 2.80 A; A/B=828-1170.
PDB; 3BSX; X-ray; 2.32 A; A/B=828-1170.
PDB; 3Q0L; X-ray; 2.50 A; A/B=828-1176.
PDB; 3Q0M; X-ray; 2.70 A; A/B=828-1176.
PDB; 3Q0N; X-ray; 2.40 A; A/B=828-1176.
PDB; 3Q0O; X-ray; 2.80 A; A/B=828-1176.
PDB; 3Q0P; X-ray; 2.60 A; A/B=828-1176.
PDBsum; 1IB2; -.
PDBsum; 1M8W; -.
PDBsum; 1M8X; -.
PDBsum; 1M8Y; -.
PDBsum; 1M8Z; -.
PDBsum; 2YJY; -.
PDBsum; 3BSB; -.
PDBsum; 3BSX; -.
PDBsum; 3Q0L; -.
PDBsum; 3Q0M; -.
PDBsum; 3Q0N; -.
PDBsum; 3Q0O; -.
PDBsum; 3Q0P; -.
ProteinModelPortal; Q14671; -.
SMR; Q14671; -.
BioGrid; 115050; 44.
DIP; DIP-29082N; -.
IntAct; Q14671; 22.
MINT; MINT-1199500; -.
STRING; 9606.ENSP00000391723; -.
iPTMnet; Q14671; -.
PhosphoSitePlus; Q14671; -.
BioMuta; PUM1; -.
DMDM; 41688619; -.
UCD-2DPAGE; Q14671; -.
EPD; Q14671; -.
MaxQB; Q14671; -.
PaxDb; Q14671; -.
PeptideAtlas; Q14671; -.
PRIDE; Q14671; -.
DNASU; 9698; -.
Ensembl; ENST00000257075; ENSP00000257075; ENSG00000134644. [Q14671-1]
Ensembl; ENST00000373742; ENSP00000362847; ENSG00000134644. [Q14671-4]
Ensembl; ENST00000426105; ENSP00000391723; ENSG00000134644. [Q14671-3]
Ensembl; ENST00000440538; ENSP00000401777; ENSG00000134644. [Q14671-2]
GeneID; 9698; -.
KEGG; hsa:9698; -.
UCSC; uc001bsh.2; human. [Q14671-1]
CTD; 9698; -.
DisGeNET; 9698; -.
EuPathDB; HostDB:ENSG00000134644.15; -.
GeneCards; PUM1; -.
HGNC; HGNC:14957; PUM1.
HPA; HPA027424; -.
HPA; HPA027449; -.
MIM; 607204; gene.
neXtProt; NX_Q14671; -.
OpenTargets; ENSG00000134644; -.
PharmGKB; PA34042; -.
eggNOG; KOG1488; Eukaryota.
eggNOG; COG5099; LUCA.
GeneTree; ENSGT00390000017241; -.
HOGENOM; HOG000238461; -.
HOVERGEN; HBG049462; -.
InParanoid; Q14671; -.
KO; K17943; -.
PhylomeDB; Q14671; -.
TreeFam; TF318160; -.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
ChiTaRS; PUM1; human.
EvolutionaryTrace; Q14671; -.
GeneWiki; PUM1; -.
GenomeRNAi; 9698; -.
PRO; PR:Q14671; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134644; -.
CleanEx; HS_PUM1; -.
ExpressionAtlas; Q14671; baseline and differential.
Genevisible; Q14671; HS.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0000932; C:P-body; IDA:UniProtKB.
GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0008344; P:adult locomotory behavior; ISS:UniProtKB.
GO; GO:0061157; P:mRNA destabilization; ISS:UniProtKB.
GO; GO:2000637; P:positive regulation of gene silencing by miRNA; IDA:UniProtKB.
GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; IDA:UniProtKB.
GO; GO:0016441; P:posttranscriptional gene silencing; ISS:UniProtKB.
GO; GO:0010608; P:posttranscriptional regulation of gene expression; IDA:MGI.
GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IMP:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
GO; GO:0051983; P:regulation of chromosome segregation; IDA:UniProtKB.
GO; GO:0060964; P:regulation of gene silencing by miRNA; TAS:UniProtKB.
GO; GO:0043488; P:regulation of mRNA stability; IDA:UniProtKB.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
CDD; cd07920; Pumilio; 1.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR033133; PUM-HD.
InterPro; IPR033712; Pumilio_RNA-bd.
InterPro; IPR001313; Pumilio_RNA-bd_rpt.
Pfam; PF00806; PUF; 8.
SMART; SM00025; Pumilio; 8.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS50302; PUM; 8.
PROSITE; PS50303; PUM_HD; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Differentiation; Methylation; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; Spermatogenesis;
Translation regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 1186 Pumilio homolog 1.
/FTId=PRO_0000075917.
DOMAIN 828 1168 PUM-HD. {ECO:0000255|PROSITE-
ProRule:PRU00318}.
REPEAT 848 883 Pumilio 1. {ECO:0000255|PROSITE-
ProRule:PRU00317,
ECO:0000269|PubMed:21397187}.
REPEAT 884 919 Pumilio 2. {ECO:0000255|PROSITE-
ProRule:PRU00317,
ECO:0000269|PubMed:21397187}.
REPEAT 920 955 Pumilio 3. {ECO:0000255|PROSITE-
ProRule:PRU00317,
ECO:0000269|PubMed:21397187}.
REPEAT 956 991 Pumilio 4. {ECO:0000255|PROSITE-
ProRule:PRU00317,
ECO:0000269|PubMed:21397187}.
REPEAT 992 1027 Pumilio 5. {ECO:0000255|PROSITE-
ProRule:PRU00317,
ECO:0000269|PubMed:21397187}.
REPEAT 1028 1063 Pumilio 6. {ECO:0000255|PROSITE-
ProRule:PRU00317,
ECO:0000269|PubMed:21397187}.
REPEAT 1064 1099 Pumilio 7. {ECO:0000255|PROSITE-
ProRule:PRU00317,
ECO:0000269|PubMed:21397187}.
REPEAT 1103 1142 Pumilio 8. {ECO:0000255|PROSITE-
ProRule:PRU00317,
ECO:0000269|PubMed:21397187}.
REGION 863 867 Adenine-nucleotide binding in RNA target.
{ECO:0000269|PubMed:18328718}.
REGION 899 903 Uracil-nucleotide binding in RNA target.
{ECO:0000269|PubMed:18328718}.
REGION 935 939 Adenine-nucleotide binding in RNA target.
{ECO:0000269|PubMed:18328718}.
REGION 971 975 Non-specific-nucleotide binding in RNA
target. {ECO:0000269|PubMed:18328718}.
REGION 1007 1011 Adenine-nucleotide binding in RNA target.
{ECO:0000269|PubMed:18328718}.
REGION 1043 1047 Uracil-nucleotide binding in RNA target.
{ECO:0000244|PDB:3BSB,
ECO:0000269|PubMed:18328718,
ECO:0000269|PubMed:21397187}.
REGION 1079 1083 Guanine-nucleotide binding in RNA target.
{ECO:0000244|PDB:3BSB,
ECO:0000269|PubMed:18328718,
ECO:0000269|PubMed:21397187}.
REGION 1122 1126 Uracil-nucleotide binding in RNA target.
{ECO:0000244|PDB:1M8W,
ECO:0000244|PDB:1M8X,
ECO:0000244|PDB:3BSB,
ECO:0000244|PDB:3BSX,
ECO:0000244|PDB:3Q0L,
ECO:0000244|PDB:3Q0M,
ECO:0000244|PDB:3Q0N,
ECO:0000244|PDB:3Q0O,
ECO:0000244|PDB:3Q0P,
ECO:0000269|PubMed:18328718,
ECO:0000269|PubMed:21397187}.
COMPBIAS 393 613 Ala-rich.
COMPBIAS 475 523 Gln-rich.
COMPBIAS 642 815 Ser-rich.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 75 75 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 112 112 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 159 159 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 197 197 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 209 209 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:20818387}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 305 305 Phosphoserine.
{ECO:0000250|UniProtKB:Q8TB72}.
MOD_RES 514 514 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8TB72}.
MOD_RES 709 709 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 714 714 Phosphoserine.
{ECO:0000269|PubMed:20818387}.
MOD_RES 796 796 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 806 806 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 822 822 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 1 M -> MPLPPPGPGPEPIPGCTAPTQSPVGRHVVGVKGVGG
M (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053703.
VAR_SEQ 145 240 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053704.
VAR_SEQ 417 417 I -> IA (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:7788527}.
/FTId=VSP_017059.
VAR_SEQ 597 623 Missing (in isoform 2).
{ECO:0000303|PubMed:7788527}.
/FTId=VSP_017060.
VAR_SEQ 950 950 Q -> QVI (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:7788527,
ECO:0000303|Ref.4}.
/FTId=VSP_017061.
MUTAGEN 209 209 S->A: Does not affect RNA-binding
activity. {ECO:0000269|PubMed:20818387}.
MUTAGEN 714 714 S->A: Decreased RNA-binding activity.
{ECO:0000269|PubMed:20818387}.
MUTAGEN 714 714 S->E: Phospho-mimic mutant; persistent
RNA-binding activity in quiescent cells.
{ECO:0000269|PubMed:20818387}.
MUTAGEN 863 867 SRFIQ->GRFIR: B and inds cytosine-
nucleotide in RNA target.
{ECO:0000269|PubMed:21572425}.
MUTAGEN 899 903 NYVIQ->GYVIR: Specifically binds
cytosine-nucleotide in RNA target.
{ECO:0000269|PubMed:21572425}.
MUTAGEN 935 939 CRVIQ->GRVIR: Specifically binds
cytosine-nucleotide in RNA target.
{ECO:0000269|PubMed:21572425}.
MUTAGEN 971 975 NHVVQ->GHVVR: Specifically binds
cytosine-nucleotide in RNA target.
{ECO:0000269|PubMed:21572425}.
MUTAGEN 1007 1011 CRVIQ->GRVIR,ARVIR,SRVIR,TRVIR,CRVIR:
Specifically binds cytosine-nucleotide in
RNA target.
{ECO:0000269|PubMed:21572425}.
MUTAGEN 1007 1011 CRVIQ->SRVIE: Specifically binds guanine-
nucleotide in RNA target.
{ECO:0000269|PubMed:21572425}.
MUTAGEN 1007 1007 C->N: Specifically binds uracil-
nucleotide in RNA target.
{ECO:0000269|PubMed:21572425}.
MUTAGEN 1043 1047 NYVIQ->GYVIR: Specifically binds
cytosine-nucleotide in RNA target.
{ECO:0000269|PubMed:21572425}.
MUTAGEN 1043 1044 NY->SN: Changes the specificity for RNA;
when associated with E-1047.
{ECO:0000269|PubMed:12202039}.
MUTAGEN 1047 1047 Q->E: Changes the specificity for RNA;
when associated with 1043-SN-1044.
{ECO:0000269|PubMed:12202039}.
MUTAGEN 1079 1083 SNVVE->GNVVR: Specifically binds
cytosine-nucleotide in RNA target.
{ECO:0000269|PubMed:21572425}.
MUTAGEN 1122 1126 NYVVQ->GYVVR: Specifically binds
cytosine-nucleotide in RNA target.
{ECO:0000269|PubMed:21572425}.
CONFLICT 216 216 G -> E (in Ref. 4; BAD96325).
{ECO:0000305}.
CONFLICT 469 469 Y -> N (in Ref. 4; BAD96325).
{ECO:0000305}.
CONFLICT 893 893 M -> N (in Ref. 2; BAA07895).
{ECO:0000305}.
HELIX 831 837 {ECO:0000244|PDB:1IB2}.
HELIX 846 849 {ECO:0000244|PDB:1IB2}.
TURN 850 852 {ECO:0000244|PDB:2YJY}.
HELIX 853 857 {ECO:0000244|PDB:1IB2}.
HELIX 860 872 {ECO:0000244|PDB:1IB2}.
HELIX 875 885 {ECO:0000244|PDB:1IB2}.
HELIX 886 888 {ECO:0000244|PDB:1IB2}.
HELIX 889 893 {ECO:0000244|PDB:1IB2}.
HELIX 898 908 {ECO:0000244|PDB:1IB2}.
HELIX 911 921 {ECO:0000244|PDB:1IB2}.
HELIX 925 929 {ECO:0000244|PDB:1IB2}.
HELIX 934 944 {ECO:0000244|PDB:1IB2}.
HELIX 947 954 {ECO:0000244|PDB:1IB2}.
HELIX 955 957 {ECO:0000244|PDB:1IB2}.
HELIX 961 966 {ECO:0000244|PDB:1IB2}.
HELIX 970 980 {ECO:0000244|PDB:1IB2}.
HELIX 983 986 {ECO:0000244|PDB:1IB2}.
HELIX 987 992 {ECO:0000244|PDB:1IB2}.
TURN 993 996 {ECO:0000244|PDB:1IB2}.
HELIX 997 1001 {ECO:0000244|PDB:1IB2}.
HELIX 1006 1016 {ECO:0000244|PDB:1IB2}.
HELIX 1019 1031 {ECO:0000244|PDB:1IB2}.
HELIX 1033 1036 {ECO:0000244|PDB:1IB2}.
HELIX 1042 1052 {ECO:0000244|PDB:1IB2}.
HELIX 1055 1065 {ECO:0000244|PDB:1IB2}.
TURN 1066 1068 {ECO:0000244|PDB:3Q0M}.
HELIX 1069 1073 {ECO:0000244|PDB:1IB2}.
HELIX 1078 1088 {ECO:0000244|PDB:1IB2}.
HELIX 1091 1103 {ECO:0000244|PDB:1IB2}.
STRAND 1104 1106 {ECO:0000244|PDB:3Q0N}.
STRAND 1107 1109 {ECO:0000244|PDB:3Q0M}.
HELIX 1111 1116 {ECO:0000244|PDB:1IB2}.
HELIX 1121 1131 {ECO:0000244|PDB:1IB2}.
HELIX 1134 1142 {ECO:0000244|PDB:1IB2}.
HELIX 1145 1147 {ECO:0000244|PDB:1M8Z}.
HELIX 1148 1151 {ECO:0000244|PDB:1M8Z}.
STRAND 1153 1155 {ECO:0000244|PDB:3BSB}.
HELIX 1157 1164 {ECO:0000244|PDB:1M8Z}.
HELIX 1165 1167 {ECO:0000244|PDB:2YJY}.
SEQUENCE 1186 AA; 126473 MW; E1E0D8B3B0181308 CRC64;
MSVACVLKRK AVLWQDSFSP HLKHHPQEPA NPNMPVVLTS GTGSQAQPQP AANQALAAGT
HSSPVPGSIG VAGRSQDDAM VDYFFQRQHG EQLGGGGSGG GGYNNSKHRW PTGDNIHAEH
QVRSMDELNH DFQALALEGR AMGEQLLPGK KFWETDESSK DGPKGIFLGD QWRDSAWGTS
DHSVSQPIMV QRRPGQSFHV NSEVNSVLSP RSESGGLGVS MVEYVLSSSP GDSCLRKGGF
GPRDADSDEN DKGEKKNKGT FDGDKLGDLK EEGDVMDKTN GLPVQNGIDA DVKDFSRTPG
NCQNSANEVD LLGPNQNGSE GLAQLTSTNG AKPVEDFSNM ESQSVPLDPM EHVGMEPLQF
DYSGTQVPVD SAAATVGLFD YNSQQQLFQR PNALAVQQLT AAQQQQYALA AAHQPHIGLA
PAAFVPNPYI ISAAPPGTDP YTAGLAAAAT LGPAVVPHQY YGVTPWGVYP ASLFQQQAAA
AAAATNSANQ QTTPQAQQGQ QQVLRGGASQ RPLTPNQNQQ GQQTDPLVAA AAVNSALAFG
QGLAAGMPGY PVLAPAAYYD QTGALVVNAG ARNGLGAPVR LVAPAPVIIS SSAAQAAVAA
AAASANGAAG GLAGTTNGPF RPLGTQQPQP QPQQQPNNNL ASSSFYGNNS LNSNSQSSSL
FSQGSAQPAN TSLGFGSSSS LGATLGSALG GFGTAVANSN TGSGSRRDSL TGSSDLYKRT
SSSLTPIGHS FYNGLSFSSS PGPVGMPLPS QGPGHSQTPP PSLSSHGSSS SLNLGGLTNG
SGRYISAAPG AEAKYRSASS ASSLFSPSST LFSSSRLRYG MSDVMPSGRS RLLEDFRNNR
YPNLQLREIA GHIMEFSQDQ HGSRFIQLKL ERATPAERQL VFNEILQAAY QLMVDVFGNY
VIQKFFEFGS LEQKLALAER IRGHVLSLAL QMYGCRVIQK ALEFIPSDQQ NEMVRELDGH
VLKCVKDQNG NHVVQKCIEC VQPQSLQFII DAFKGQVFAL STHPYGCRVI QRILEHCLPD
QTLPILEELH QHTEQLVQDQ YGNYVIQHVL EHGRPEDKSK IVAEIRGNVL VLSQHKFASN
VVEKCVTHAS RTERAVLIDE VCTMNDGPHS ALYTMMKDQY ANYVVQKMID VAEPGQRKIV
MHKIRPHIAT LRKYTYGKHI LAKLEKYYMK NGVDLGPICG PPNGII


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EIAAB33152 Homo sapiens,HsPUM,Human,KIAA0099,PUM1,PUMH1,Pumilio homolog 1,Pumilio-1
OBT1768 PUM2 (Pumilio homolog 2 encoded within exon 4), Pumilio like_2, PUMH2, Pumilio homolog2, KIAA0235, Rabbit anti_Human, Mouse; IP_WB 0.1 mg.
EIAAB33155 Homo sapiens,Human,KIAA0235,PUM2,PUMH2,Pumilio homolog 2,Pumilio-2
18-272-195051 Pumilio 2 - Rabbit polyclonal to Pumilio 2; Pumilio-2 Polyclonal 0.05 mg
E3195h Human Pumilio Homolog 1 ELISA Kit 96T
G5172 Pumilio homolog 1 (PUM1), Mouse, ELISA Kit 96T
G5173 Pumilio homolog 2 (PUM2), Human, ELISA Kit 96T
G5174 Pumilio homolog 2 (PUM2), Mouse, ELISA Kit 96T
G5170 Pumilio homolog 1 (PUM1), Chicken, ELISA Kit 96T
CSB-EL019082HU Human Pumilio homolog 2(PUM2) ELISA kit 96T
CSB-EL019081MO Mouse Pumilio homolog 1(PUM1) ELISA kit 96T
G5171 Pumilio homolog 1 (PUM1), Human, ELISA Kit 96T
CSB-EL019081HU Human Pumilio homolog 1(PUM1) ELISA kit 96T
201-20-4638 PUM2{pumilio homolog 2 (Drosophila)}rabbit.pAb 0.2ml
CSB-EL019082MO Mouse Pumilio homolog 2(PUM2) ELISA kit 96T
CSB-EL019081CH Chicken Pumilio homolog 1(PUM1) ELISA kit 96T
GWB-E4059A Anti- PUM2 (pumilio homolog 2 (Drosophila)) Antibody
CSB-EL019081CH Chicken Pumilio homolog 1(PUM1) ELISA kit SpeciesChicken 96T
CSB-EL019081MO Mouse Pumilio homolog 1(PUM1) ELISA kit SpeciesMouse 96T
EIAAB33153 Kiaa0099,Mouse,Mus musculus,Pum1,Pumilio homolog 1
CSB-EL019082HU Human Pumilio homolog 2(PUM2) ELISA kit SpeciesHuman 96T
CSB-EL019082MO Mouse Pumilio homolog 2(PUM2) ELISA kit SpeciesMouse 96T
EIAAB33156 Kiaa0235,Mouse,Mus musculus,Pum2,Pumilio homolog 2
CSB-EL019081HU Human Pumilio homolog 1(PUM1) ELISA kit SpeciesHuman 96T
PUM1_MOUSE ELISA Kit FOR Pumilio homolog 1; organism: Mouse; gene name: Pum1 96T


 

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