STAU1_HUMAN
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 03-AUG-2022, entry version 209.
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; 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}.
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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; 957.
DR CORUM; O95793; -.
DR IntAct; O95793; 167.
DR MINT; O95793; -.
DR STRING; 9606.ENSP00000360922; -.
DR GlyGen; O95793; 2 sites, 1 O-linked glycan (1 site).
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; O95793; -.
DR PeptideAtlas; O95793; -.
DR PRIDE; O95793; -.
DR ProteomicsDB; 51054; -. [O95793-1]
DR ProteomicsDB; 51055; -. [O95793-2]
DR ProteomicsDB; 51056; -. [O95793-3]
DR Antibodypedia; 13554; 416 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 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; FPPVGPI; -.
DR OrthoDB; 823092at2759; -.
DR PhylomeDB; O95793; -.
DR TreeFam; TF350296; -.
DR PathwayCommons; O95793; -.
DR SignaLink; O95793; -.
DR BioGRID-ORCS; 6780; 19 hits in 1090 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 210 other tissues.
DR ExpressionAtlas; O95793; baseline and differential.
DR Genevisible; O95793; HS.
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: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: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; cd19883; DSRM_STAU1_rpt3; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR044475; STAU1_DSRM_3.
DR InterPro; IPR032478; Staufen_C.
DR Pfam; PF00035; dsrm; 3.
DR Pfam; PF16482; Staufen_C; 1.
DR SMART; SM00358; DSRM; 3.
DR PROSITE; PS50137; DS_RBD; 3.
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
