ID STAU1_HUMAN Reviewed; 577 AA. AC O95793; A8K9Z4; E1P5Y1; E1P608; Q5JW29; Q6GTM4; Q9H5B4; Q9H5B5; Q9Y3Q2; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 2. DT 27-MAR-2024, entry version 218. DE RecName: Full=Double-stranded RNA-binding protein Staufen homolog 1; GN Name=STAU1; Synonyms=STAU; 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 LONG). RC TISSUE=CNS; RX PubMed=10022909; DOI=10.1128/mcb.19.3.2220; RA Wickham L., Duchaine T., Luo M., Nabi I.R., DesGroseillers L.; RT "Mammalian Staufen is a double-stranded-RNA- and tubulin-binding protein RT which localizes to the rough endoplasmic reticulum."; RL Mol. Cell. Biol. 19:2220-2230(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), FUNCTION (MICROBIAL INFECTION), RP AND INTERACTION WITH INFLUENZA VIRUS NS1 (MICROBIAL INFECTION). RC TISSUE=Kidney; RX PubMed=10325410; DOI=10.1093/nar/27.11.2241; RA Falcon A.M., Fortes P., Marion R.M., Beloso A., Ortin J.; RT "Interaction of influenza virus NS1 protein and the human homologue of RT Staufen in vivo and in vitro."; RL Nucleic Acids Res. 27:2241-2247(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Mao Y., Xie Y., Jin F.; RT "Cloning and characterization of a splicing variant of human staufen RT protein."; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). 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] (ISOFORMS LONG AND SHORT). RC TISSUE=Placenta, and Skin; 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 FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 GAG POLYPROTEIN RP (MICROBIAL INFECTION). RX PubMed=18498651; DOI=10.1186/1742-4690-5-41; RA Chatel-Chaix L., Boulay K., Mouland A.J., Desgroseillers L.; RT "The host protein Staufen1 interacts with the Pr55Gag zinc fingers and RT regulates HIV-1 assembly via its N-terminus."; RL Retrovirology 5:41-41(2008). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RX PubMed=19029303; DOI=10.1261/rna.1175909; RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., RA Buchmeier S., Wahle E., Huettelmaiery S.; RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."; RL RNA 15:104-115(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-278 AND SER-390, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HERV-K REC AND GAG RP PROTEINS (MICROBIAL INFECTION). RX PubMed=23926355; DOI=10.1128/jvi.03031-12; RA Hanke K., Hohn O., Liedgens L., Fiddeke K., Wamara J., Kurth R., RA Bannert N.; RT "Staufen-1 interacts with the human endogenous retrovirus family HERV- RT K(HML-2) rec and gag proteins and increases virion production."; RL J. Virol. 87:11019-11030(2013). RN [17] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-108 AND ARG-115, 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 [18] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH EBOLA VIRUS NP (MICROBIAL RP INFECTION), INTERACTION WITH EBOLAVIRUS VP30 (MICROBIAL INFECTION), AND RP INTERACTION WITH EBOLA VIRUS VP35 (MICROBIAL INFECTION). RX PubMed=30301857; DOI=10.1128/mbio.01771-18; RA Fang J., Pietzsch C., Ramanathan P., Santos R.I., Ilinykh P.A., RA Garcia-Blanco M.A., Bukreyev A., Bradrick S.S.; RT "Staufen1 Interacts with Multiple Components of the Ebola Virus RT Ribonucleoprotein and Enhances Viral RNA Synthesis."; RL MBio 9:0-0(2018). CC -!- FUNCTION: Binds double-stranded RNA (regardless of the sequence) and CC tubulin. May play a role in specific positioning of mRNAs at given CC sites in the cell by cross-linking cytoskeletal and RNA components, and CC in stimulating their translation at the site. CC -!- FUNCTION: (Microbial infection) Plays a role in virus particles CC production of many viruses including of HIV-1, HERV-K, ebola virus and CC influenza virus. Acts by interacting with various viral proteins CC involved in particle budding process. {ECO:0000269|PubMed:10325410, CC ECO:0000269|PubMed:18498651, ECO:0000269|PubMed:23926355, CC ECO:0000269|PubMed:30301857}. CC -!- SUBUNIT: Binds tubulin. Binds with low affinity single-stranded RNA or CC DNA homopolymers. Interacts with CASC3 in an RNA-dependent manner (By CC similarity). Identified in a mRNP complex, at least composed of DHX9, CC DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, CC STAU2, SYNCRIP and YBX1. {ECO:0000250, ECO:0000269|PubMed:19029303}. CC -!- SUBUNIT: (Microbial infection) Interacts with HERV-K rec and gag CC proteins. {ECO:0000269|PubMed:23926355}. CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 GAG polyprotein. CC {ECO:0000269|PubMed:18498651}. CC -!- SUBUNIT: (Microbial infection) Interacts with influenza virus NS1 CC protein. {ECO:0000269|PubMed:10325410}. CC -!- SUBUNIT: (Microbial infection) Interacts with Ebola virus NP, VP30 and CC VP35. {ECO:0000269|PubMed:30301857}. CC -!- INTERACTION: CC O95793; P78563-4: ADARB1; NbExp=3; IntAct=EBI-358174, EBI-12002366; CC O95793; P05067-4: APP; NbExp=2; IntAct=EBI-358174, EBI-302641; CC O95793; P13569: CFTR; NbExp=13; IntAct=EBI-358174, EBI-349854; CC O95793; O76003: GLRX3; NbExp=3; IntAct=EBI-358174, EBI-374781; CC O95793; Q9NZI8: IGF2BP1; NbExp=6; IntAct=EBI-358174, EBI-1053892; CC O95793; Q17RB8: LONRF1; NbExp=6; IntAct=EBI-358174, EBI-2341787; CC O95793; O15226: NKRF; NbExp=3; IntAct=EBI-358174, EBI-766011; CC O95793; Q9UKK6: NXT1; NbExp=6; IntAct=EBI-358174, EBI-301889; CC O95793; O75569: PRKRA; NbExp=3; IntAct=EBI-358174, EBI-713955; CC O95793; P62424: RPL7A; NbExp=2; IntAct=EBI-358174, EBI-354172; CC O95793; P05388: RPLP0; NbExp=4; IntAct=EBI-358174, EBI-354101; CC O95793; Q96SI9: STRBP; NbExp=3; IntAct=EBI-358174, EBI-740355; CC O95793; Q92900: UPF1; NbExp=5; IntAct=EBI-358174, EBI-373471; CC O95793; Q9HA38: ZMAT3; NbExp=3; IntAct=EBI-358174, EBI-2548480; CC O95793; Q60793: Klf4; Xeno; NbExp=7; IntAct=EBI-358174, EBI-3043905; CC O95793; P03496: NS; Xeno; NbExp=6; IntAct=EBI-358174, EBI-2547442; CC O95793-2; Q96H20: SNF8; NbExp=3; IntAct=EBI-358189, EBI-747719; CC O95793-2; P04591: gag; Xeno; NbExp=4; IntAct=EBI-358189, EBI-6163428; CC O95793-2; PRO_0000038594 [P04591]: gag; Xeno; NbExp=2; IntAct=EBI-358189, EBI-9871255; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19029303}. Rough CC endoplasmic reticulum {ECO:0000269|PubMed:19029303}. Note=Localizes CC exclusively with the rough reticulum endoplasmic (RER). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Long; CC IsoId=O95793-1; Sequence=Displayed; CC Name=Short; CC IsoId=O95793-2; Sequence=VSP_004434; CC Name=3; CC IsoId=O95793-3; Sequence=VSP_004434, VSP_043701; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, pancreas, CC heart, skeletal muscles, liver, lung, kidney and placenta. CC -!- DOMAIN: One of the DRDB could be involved in RER binding. CC -!- DOMAIN: The C-terminal contains the tubulin binding domain (TBD). CC {ECO:0000250}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF061939; AAD17531.1; -; mRNA. DR EMBL; AF061941; AAD17533.1; -; mRNA. DR EMBL; AF061938; AAD17530.1; -; mRNA. DR EMBL; AF061940; AAD17532.1; -; mRNA. DR EMBL; AJ132258; CAB40082.1; -; mRNA. DR EMBL; AY529074; AAS76636.1; -; mRNA. DR EMBL; AY546099; AAS76637.1; -; mRNA. DR EMBL; AL136601; CAB66536.1; -; mRNA. DR EMBL; AK292859; BAF85548.1; -; mRNA. DR EMBL; AL133174; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW75669.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75671.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75672.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75673.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75674.1; -; Genomic_DNA. DR EMBL; BC050432; AAH50432.1; -; mRNA. DR EMBL; BC095397; AAH95397.1; -; mRNA. DR CCDS; CCDS13414.1; -. [O95793-1] DR CCDS; CCDS13415.1; -. [O95793-2] DR CCDS; CCDS33481.1; -. [O95793-3] DR RefSeq; NP_001032405.1; NM_001037328.2. [O95793-3] DR RefSeq; NP_001306063.1; NM_001319134.1. [O95793-3] DR RefSeq; NP_001306064.1; NM_001319135.1. [O95793-1] DR RefSeq; NP_001309856.1; NM_001322927.1. [O95793-3] DR RefSeq; NP_001309858.1; NM_001322929.1. [O95793-1] DR RefSeq; NP_001309859.1; NM_001322930.1. [O95793-1] DR RefSeq; NP_004593.2; NM_004602.3. [O95793-2] DR RefSeq; NP_059346.2; NM_017452.3. [O95793-2] DR RefSeq; NP_059347.2; NM_017453.3. [O95793-1] DR RefSeq; NP_059348.2; NM_017454.3. [O95793-2] DR RefSeq; XP_005260584.1; XM_005260527.1. [O95793-3] DR PDB; 4DKK; X-ray; 1.70 A; A=448-557. DR PDB; 6HTU; X-ray; 2.89 A; A/B/C=182-360. DR PDB; 6SDW; NMR; -; A=183-355. DR PDB; 6SDY; NMR; -; A=286-355. DR PDBsum; 4DKK; -. DR PDBsum; 6HTU; -. DR PDBsum; 6SDW; -. DR PDBsum; 6SDY; -. DR AlphaFoldDB; O95793; -. DR SASBDB; O95793; -. DR SMR; O95793; -. DR BioGRID; 112657; 1539. DR CORUM; O95793; -. DR IntAct; O95793; 182. DR MINT; O95793; -. DR STRING; 9606.ENSP00000360922; -. DR GlyGen; O95793; 6 sites, 2 O-linked glycans (5 sites). DR iPTMnet; O95793; -. DR MetOSite; O95793; -. DR PhosphoSitePlus; O95793; -. DR SwissPalm; O95793; -. DR BioMuta; STAU1; -. DR EPD; O95793; -. DR jPOST; O95793; -. DR MassIVE; O95793; -. DR MaxQB; O95793; -. DR PaxDb; 9606-ENSP00000360922; -. DR PeptideAtlas; O95793; -. DR ProteomicsDB; 51054; -. [O95793-1] DR ProteomicsDB; 51055; -. [O95793-2] DR ProteomicsDB; 51056; -. [O95793-3] DR Pumba; O95793; -. DR Antibodypedia; 13554; 486 antibodies from 37 providers. DR DNASU; 6780; -. DR Ensembl; ENST00000340954.11; ENSP00000345425.6; ENSG00000124214.21. [O95793-2] DR Ensembl; ENST00000347458.9; ENSP00000323443.7; ENSG00000124214.21. [O95793-2] DR Ensembl; ENST00000360426.8; ENSP00000353604.4; ENSG00000124214.21. [O95793-2] DR Ensembl; ENST00000371802.5; ENSP00000360867.1; ENSG00000124214.21. [O95793-3] DR Ensembl; ENST00000371828.7; ENSP00000360893.3; ENSG00000124214.21. [O95793-3] DR Ensembl; ENST00000371856.7; ENSP00000360922.2; ENSG00000124214.21. [O95793-1] DR GeneID; 6780; -. DR KEGG; hsa:6780; -. DR MANE-Select; ENST00000371856.7; ENSP00000360922.2; NM_017453.4; NP_059347.2. DR UCSC; uc002xua.4; human. [O95793-1] DR AGR; HGNC:11370; -. DR CTD; 6780; -. DR DisGeNET; 6780; -. DR GeneCards; STAU1; -. DR HGNC; HGNC:11370; STAU1. DR HPA; ENSG00000124214; Low tissue specificity. DR MIM; 601716; gene. DR neXtProt; NX_O95793; -. DR OpenTargets; ENSG00000124214; -. DR PharmGKB; PA36188; -. DR VEuPathDB; HostDB:ENSG00000124214; -. DR eggNOG; KOG3732; Eukaryota. DR GeneTree; ENSGT00940000157304; -. DR InParanoid; O95793; -. DR OMA; DIESCHD; -. DR OrthoDB; 2882160at2759; -. DR PhylomeDB; O95793; -. DR TreeFam; TF350296; -. DR PathwayCommons; O95793; -. DR SignaLink; O95793; -. DR BioGRID-ORCS; 6780; 20 hits in 1168 CRISPR screens. DR ChiTaRS; STAU1; human. DR GeneWiki; STAU1; -. DR GenomeRNAi; 6780; -. DR Pharos; O95793; Tbio. DR PRO; PR:O95793; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; O95793; Protein. DR Bgee; ENSG00000124214; Expressed in nephron tubule and 212 other cell types or tissues. DR ExpressionAtlas; O95793; baseline and differential. DR GO; GO:0044297; C:cell body; IDA:ParkinsonsUK-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL. DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:BHF-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0030425; C:dendrite; IDA:ParkinsonsUK-UCL. DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central. DR GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005791; C:rough endoplasmic reticulum; TAS:ProtInc. DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0008157; F:protein phosphatase 1 binding; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0098964; P:anterograde dendritic transport of messenger ribonucleoprotein complex; IBA:GO_Central. DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl. DR GO; GO:0007281; P:germ cell development; IBA:GO_Central. DR GO; GO:0008298; P:intracellular mRNA localization; IBA:GO_Central. DR GO; GO:0000512; P:lncRNA-mediated post-transcriptional gene silencing; TAS:ARUK-UCL. DR GO; GO:0099010; P:modification of postsynaptic structure; IEA:Ensembl. DR GO; GO:0046726; P:positive regulation by virus of viral protein levels in host cell; IMP:AgBase. DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl. DR GO; GO:0045070; P:positive regulation of viral genome replication; IMP:AgBase. DR GO; GO:0035418; P:protein localization to synapse; IBA:GO_Central. DR CDD; cd19881; DSRM_STAU1_rpt2; 1. DR CDD; cd19883; DSRM_STAU1_rpt3; 1. DR CDD; cd19885; DSRM_STAU1_rpt4; 1. DR CDD; cd19887; DSRM_STAU1_rpt5; 1. DR Gene3D; 3.30.160.20; -; 4. DR Gene3D; 6.10.250.1360; -; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR044475; STAU1_DSRM_3. DR InterPro; IPR032478; Staufen_C. DR PANTHER; PTHR46054:SF2; DOUBLE-STRANDED RNA-BINDING PROTEIN STAUFEN HOMOLOG 1; 1. DR PANTHER; PTHR46054; MATERNAL EFFECT PROTEIN STAUFEN; 1. DR Pfam; PF00035; dsrm; 3. DR Pfam; PF16482; Staufen_C; 1. DR SMART; SM00358; DSRM; 3. DR SUPFAM; SSF54768; dsRNA-binding domain-like; 3. DR PROSITE; PS50137; DS_RBD; 3. DR Genevisible; O95793; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Endoplasmic reticulum; Host-virus interaction; Methylation; Phosphoprotein; KW Reference proteome; Repeat; RNA-binding. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..577 FT /note="Double-stranded RNA-binding protein Staufen homolog FT 1" FT /id="PRO_0000072243" FT DOMAIN 72..162 FT /note="DRBM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266" FT DOMAIN 184..251 FT /note="DRBM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266" FT DOMAIN 286..354 FT /note="DRBM 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266" FT REGION 34..55 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 360..397 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 368..382 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 108 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 115 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 115 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 176 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 278 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 390 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..81 FT /note="Missing (in isoform Short and isoform 3)" FT /evidence="ECO:0000303|PubMed:10325410, FT ECO:0000303|PubMed:11230166, ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_004434" FT VAR_SEQ 203 FT /note="E -> ESFPLKQ (in isoform 3)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_043701" FT CONFLICT 359 FT /note="A -> R (in Ref. 1 and 2)" FT /evidence="ECO:0000305" FT CONFLICT 360..392 FT /note="QPTKPALKSEEKTPIKKPGDGRKVTFFEPGSGD -> SHQTRTQVRGEDTHK FT ETRGWKKSNLFLNLALGM (in Ref. 2)" FT /evidence="ECO:0000305" FT HELIX 185..195 FT /evidence="ECO:0007829|PDB:6HTU" FT STRAND 200..209 FT /evidence="ECO:0007829|PDB:6HTU" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:6HTU" FT STRAND 215..222 FT /evidence="ECO:0007829|PDB:6HTU" FT STRAND 225..233 FT /evidence="ECO:0007829|PDB:6HTU" FT HELIX 234..249 FT /evidence="ECO:0007829|PDB:6HTU" FT STRAND 256..258 FT /evidence="ECO:0007829|PDB:6SDW" FT HELIX 287..292 FT /evidence="ECO:0007829|PDB:6HTU" FT TURN 293..296 FT /evidence="ECO:0007829|PDB:6HTU" FT STRAND 304..308 FT /evidence="ECO:0007829|PDB:6HTU" FT STRAND 319..324 FT /evidence="ECO:0007829|PDB:6HTU" FT STRAND 329..332 FT /evidence="ECO:0007829|PDB:6SDW" FT STRAND 333..336 FT /evidence="ECO:0007829|PDB:6HTU" FT HELIX 337..346 FT /evidence="ECO:0007829|PDB:6HTU" FT TURN 350..353 FT /evidence="ECO:0007829|PDB:6HTU" FT HELIX 448..462 FT /evidence="ECO:0007829|PDB:4DKK" FT HELIX 466..472 FT /evidence="ECO:0007829|PDB:4DKK" FT HELIX 489..500 FT /evidence="ECO:0007829|PDB:4DKK" FT STRAND 504..509 FT /evidence="ECO:0007829|PDB:4DKK" FT STRAND 517..523 FT /evidence="ECO:0007829|PDB:4DKK" FT STRAND 525..527 FT /evidence="ECO:0007829|PDB:4DKK" FT STRAND 529..537 FT /evidence="ECO:0007829|PDB:4DKK" FT HELIX 538..553 FT /evidence="ECO:0007829|PDB:4DKK" SQ SEQUENCE 577 AA; 63182 MW; 0977CEF40FD99517 CRC64; MSQVQVQVQN PSAALSGSQI LNKNQSLLSQ PLMSIPSTTS SLPSENAGRP IQNSALPSAS ITSTSAAAES ITPTVELNAL CMKLGKKPMY KPVDPYSRMQ STYNYNMRGG AYPPRYFYPF PVPPLLYQVE LSVGGQQFNG KGKTRQAAKH DAAAKALRIL QNEPLPERLE VNGRESEEEN LNKSEISQVF EIALKRNLPV NFEVARESGP PHMKNFVTKV SVGEFVGEGE GKSKKISKKN AAIAVLEELK KLPPLPAVER VKPRIKKKTK PIVKPQTSPE YGQGINPISR LAQIQQAKKE KEPEYTLLTE RGLPRRREFV MQVKVGNHTA EGTGTNKKVA KRNAAENMLE ILGFKVPQAQ PTKPALKSEE KTPIKKPGDG RKVTFFEPGS GDENGTSNKE DEFRMPYLSH QQLPAGILPM VPEVAQAVGV SQGHHTKDFT RAAPNPAKAT VTAMIARELL YGGTSPTAET ILKNNISSGH VPHGPLTRPS EQLDYLSRVQ GFQVEYKDFP KNNKNEFVSL INCSSQPPLI SHGIGKDVES CHDMAALNIL KLLSELDQQS TEMPRTGNGP MSVCGRC //