STAU2_HUMAN
ID STAU2_HUMAN Reviewed; 570 AA.
AC Q9NUL3; A0A0A0MTC5; B7Z1I6; B7Z292; B7Z8B4; E7ER74; E9PEI3; E9PF26; E9PF50;
AC Q6AHY7; Q96HM0; Q96HM1; Q9NVI5; Q9UGG6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Double-stranded RNA-binding protein Staufen homolog 2;
GN Name=STAU2;
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 VARIANT MET-198.
RX PubMed=10585778; DOI=10.1006/geno.1999.6015;
RA Buchner G., Bassi M.T., Andolfi G., Ballabio A., Franco B.;
RT "Identification of a novel homolog of the Drosophila staufen protein in the
RT chromosome 8q13-q21.1 region.";
RL Genomics 62:113-118(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT MET-198.
RX PubMed=12140260; DOI=10.1242/jcs.115.16.3285;
RA Duchaine T.F., Hemraj I., Furic L., Deitinghoff A., Kiebler M.A.,
RA DesGroseillers L.;
RT "Staufen2 isoforms localize to the somatodendritic domain of neurons and
RT interact with different organelles.";
RL J. Cell Sci. 115:3285-3295(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 6; 7 AND 8), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 256-570 (ISOFORMS 3/4), AND VARIANT MET-198.
RC TISSUE=Amygdala, Cerebellum, Ovary, Placenta, Teratocarcinoma, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT MET-198.
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-198.
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5), AND VARIANT
RP MET-198.
RC TISSUE=Urinary bladder carcinoma;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-416, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-440; SER-455 AND
RP SER-492, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
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 [12]
RP IDENTIFICATION IN A MRNP COMPLEX, AND IDENTIFICATION 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440 AND SER-492, AND
RP IDENTIFICATION BY 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; THR-405; SER-416;
RP SER-426; SER-440 AND SER-455, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-440 AND SER-455, 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 [18]
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).
CC -!- FUNCTION: RNA-binding protein required for the microtubule-dependent
CC transport of neuronal RNA from the cell body to the dendrite. As
CC protein synthesis occurs within the dendrite, the localization of
CC specific mRNAs to dendrites may be a prerequisite for neurite outgrowth
CC and plasticity at sites distant from the cell body (By similarity).
CC {ECO:0000250|UniProtKB:Q68SB1}.
CC -!- SUBUNIT: Interacts with the exportin XPO5. This requires RNA and RAN
CC bound to GTP. Interacts with microtubules. Isoform 2 and isoform 3 may
CC also interact with ribosomes, and this association is independent of
CC translation (By similarity). Identified in a mRNP complex, at least
CC composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2,
CC PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Interacts with TRIM71 (via NHL
CC repeats) in an RNA-dependent manner (PubMed:23125361).
CC {ECO:0000250|UniProtKB:Q68SB1, ECO:0000269|PubMed:19029303,
CC ECO:0000269|PubMed:23125361}.
CC -!- INTERACTION:
CC Q9NUL3; Q96C10: DHX58; NbExp=2; IntAct=EBI-722938, EBI-744193;
CC Q9NUL3; P19525: EIF2AK2; NbExp=3; IntAct=EBI-722938, EBI-640775;
CC Q9NUL3; PRO_0000449620 [P0DTD1]: rep; Xeno; NbExp=2; IntAct=EBI-722938, EBI-25475859;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus.
CC Endoplasmic reticulum. Note=Shuttles between the nucleolus, nucleus and
CC the cytoplasm. Nuclear export of isoform 1 is independent of XPO1/CRM1
CC and requires the exportin XPO5. Nuclear export of isoform 2 and isoform
CC 3 can occur by both XPO1/CRM1-dependent and XPO1/CRM1-independent
CC pathways. Found in large cytoplasmic ribonucleoprotein (RNP) granules
CC which are present in the actin rich regions of myelinating processes
CC and associated with microtubules, polysomes and the endoplasmic
CC reticulum. Also recruited to stress granules (SGs) upon inhibition of
CC translation or oxidative stress. These structures are thought to harbor
CC housekeeping mRNAs when translation is aborted (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=Long;
CC IsoId=Q9NUL3-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q9NUL3-2; Sequence=VSP_015374;
CC Name=3;
CC IsoId=Q9NUL3-3; Sequence=VSP_015374, VSP_015376, VSP_015377;
CC Name=4;
CC IsoId=Q9NUL3-4; Sequence=VSP_015373, VSP_015376, VSP_015377;
CC Name=5;
CC IsoId=Q9NUL3-5; Sequence=VSP_015374, VSP_015375;
CC Name=6;
CC IsoId=Q9NUL3-6; Sequence=VSP_046138;
CC Name=7;
CC IsoId=Q9NUL3-7; Sequence=VSP_046139, VSP_046141;
CC Name=8;
CC IsoId=Q9NUL3-8; Sequence=VSP_046140, VSP_046142;
CC -!- DOMAIN: The DRBM 3 domain appears to be the major RNA-binding
CC determinant. This domain also mediates interaction with XPO5 and is
CC required for XPO1/CRM1-independent nuclear export (By similarity).
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91766.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14522.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH10527.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y19062; CAB64341.1; -; mRNA.
DR EMBL; AF459097; AAN37926.1; -; mRNA.
DR EMBL; AF459098; AAN37927.1; -; mRNA.
DR EMBL; AK001576; BAA91766.1; ALT_INIT; mRNA.
DR EMBL; AK002152; BAA92111.1; -; mRNA.
DR EMBL; AK023314; BAB14522.1; ALT_INIT; mRNA.
DR EMBL; AK293496; BAH11522.1; -; mRNA.
DR EMBL; AK294466; BAH11778.1; -; mRNA.
DR EMBL; AK303104; BAH13900.1; -; mRNA.
DR EMBL; CR627442; CAH10527.1; ALT_INIT; mRNA.
DR EMBL; AC018620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC100784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF458781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008369; AAH08369.1; -; mRNA.
DR EMBL; BC008370; AAH08370.1; -; mRNA.
DR CCDS; CCDS55244.1; -. [Q9NUL3-6]
DR CCDS; CCDS55245.1; -. [Q9NUL3-7]
DR CCDS; CCDS55246.1; -. [Q9NUL3-8]
DR CCDS; CCDS55247.1; -. [Q9NUL3-1]
DR CCDS; CCDS55248.1; -. [Q9NUL3-2]
DR CCDS; CCDS6214.1; -. [Q9NUL3-3]
DR RefSeq; NP_001157852.1; NM_001164380.1. [Q9NUL3-1]
DR RefSeq; NP_001157853.1; NM_001164381.1. [Q9NUL3-2]
DR RefSeq; NP_001157854.1; NM_001164382.1. [Q9NUL3-7]
DR RefSeq; NP_001157855.1; NM_001164383.1. [Q9NUL3-6]
DR RefSeq; NP_001157856.1; NM_001164384.1. [Q9NUL3-3]
DR RefSeq; NP_001157857.1; NM_001164385.1. [Q9NUL3-8]
DR RefSeq; NP_055208.2; NM_014393.2. [Q9NUL3-3]
DR AlphaFoldDB; Q9NUL3; -.
DR SMR; Q9NUL3; -.
DR BioGRID; 117978; 228.
DR IntAct; Q9NUL3; 56.
DR MINT; Q9NUL3; -.
DR STRING; 9606.ENSP00000428756; -.
DR GlyGen; Q9NUL3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NUL3; -.
DR MetOSite; Q9NUL3; -.
DR PhosphoSitePlus; Q9NUL3; -.
DR BioMuta; STAU2; -.
DR DMDM; 73919458; -.
DR EPD; Q9NUL3; -.
DR jPOST; Q9NUL3; -.
DR MassIVE; Q9NUL3; -.
DR MaxQB; Q9NUL3; -.
DR PaxDb; Q9NUL3; -.
DR PeptideAtlas; Q9NUL3; -.
DR PRIDE; Q9NUL3; -.
DR ProteomicsDB; 17731; -.
DR ProteomicsDB; 19897; -.
DR ProteomicsDB; 20012; -.
DR ProteomicsDB; 20028; -.
DR ProteomicsDB; 82683; -. [Q9NUL3-1]
DR ProteomicsDB; 82684; -. [Q9NUL3-2]
DR ProteomicsDB; 82685; -. [Q9NUL3-3]
DR ProteomicsDB; 82686; -. [Q9NUL3-4]
DR ProteomicsDB; 82687; -. [Q9NUL3-5]
DR Antibodypedia; 1305; 241 antibodies from 25 providers.
DR DNASU; 27067; -.
DR Ensembl; ENST00000355780.9; ENSP00000348026.5; ENSG00000040341.18. [Q9NUL3-3]
DR Ensembl; ENST00000517542.5; ENSP00000431111.1; ENSG00000040341.18. [Q9NUL3-8]
DR Ensembl; ENST00000521210.5; ENSP00000429173.1; ENSG00000040341.18. [Q9NUL3-7]
DR Ensembl; ENST00000521451.5; ENSP00000428476.1; ENSG00000040341.18. [Q9NUL3-4]
DR Ensembl; ENST00000522509.5; ENSP00000427977.1; ENSG00000040341.18. [Q9NUL3-3]
DR Ensembl; ENST00000522695.5; ENSP00000428456.1; ENSG00000040341.18. [Q9NUL3-2]
DR Ensembl; ENST00000523558.5; ENSP00000428741.1; ENSG00000040341.18. [Q9NUL3-6]
DR Ensembl; ENST00000524104.5; ENSP00000430611.1; ENSG00000040341.18. [Q9NUL3-5]
DR Ensembl; ENST00000524300.6; ENSP00000428756.1; ENSG00000040341.18. [Q9NUL3-1]
DR GeneID; 27067; -.
DR KEGG; hsa:27067; -.
DR MANE-Select; ENST00000524300.6; ENSP00000428756.1; NM_001164380.2; NP_001157852.1.
DR UCSC; uc003xzs.5; human. [Q9NUL3-1]
DR CTD; 27067; -.
DR DisGeNET; 27067; -.
DR GeneCards; STAU2; -.
DR HGNC; HGNC:11371; STAU2.
DR HPA; ENSG00000040341; Low tissue specificity.
DR MIM; 605920; gene.
DR neXtProt; NX_Q9NUL3; -.
DR OpenTargets; ENSG00000040341; -.
DR PharmGKB; PA36189; -.
DR VEuPathDB; HostDB:ENSG00000040341; -.
DR eggNOG; KOG3732; Eukaryota.
DR GeneTree; ENSGT00940000154977; -.
DR HOGENOM; CLU_162783_0_0_1; -.
DR InParanoid; Q9NUL3; -.
DR OMA; GSPQENM; -.
DR OrthoDB; 823092at2759; -.
DR PhylomeDB; Q9NUL3; -.
DR TreeFam; TF350296; -.
DR PathwayCommons; Q9NUL3; -.
DR SignaLink; Q9NUL3; -.
DR BioGRID-ORCS; 27067; 14 hits in 1086 CRISPR screens.
DR ChiTaRS; STAU2; human.
DR GeneWiki; STAU2; -.
DR GenomeRNAi; 27067; -.
DR Pharos; Q9NUL3; Tbio.
DR PRO; PR:Q9NUL3; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9NUL3; protein.
DR Bgee; ENSG00000040341; Expressed in cortical plate and 192 other tissues.
DR ExpressionAtlas; Q9NUL3; baseline and differential.
DR Genevisible; Q9NUL3; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
DR GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome 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:0048592; P:eye morphogenesis; 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:0061003; P:positive regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; IEA:Ensembl.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR GO; GO:0035418; P:protein localization to synapse; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0051489; P:regulation of filopodium assembly; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR CDD; cd19880; DSRM_STAU2_rpt1; 1.
DR CDD; cd19882; DSRM_STAU2_rpt2; 1.
DR CDD; cd19884; DSRM_STAU2_rpt3; 1.
DR CDD; cd19886; DSRM_STAU2_rpt4; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR044476; STAU2_DSRM_1.
DR InterPro; IPR044464; STAU2_DSRM_2.
DR InterPro; IPR044473; STAU2_DSRM_3.
DR InterPro; IPR044474; STAU2_DSRM_4.
DR InterPro; IPR032478; Staufen_C.
DR Pfam; PF00035; dsrm; 4.
DR Pfam; PF16482; Staufen_C; 1.
DR SMART; SM00358; DSRM; 4.
DR PROSITE; PS50137; DS_RBD; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endoplasmic reticulum; Microtubule;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Transport.
FT CHAIN 1..570
FT /note="Double-stranded RNA-binding protein Staufen homolog
FT 2"
FT /id="PRO_0000072246"
FT DOMAIN 8..75
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 95..181
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 207..274
FT /note="DRBM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 307..375
FT /note="DRBM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 71..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..570
FT /note="Required for dendritic transport"
FT /evidence="ECO:0000250"
FT REGION 387..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 273..291
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 373..412
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 554..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 405
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..220
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_015373"
FT VAR_SEQ 1..172
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046138"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046139"
FT VAR_SEQ 1..38
FT /note="MANPKEKTAMCLVNELARFNRVQPQYKLLNERGPAHSK -> MLQINQ (in
FT isoform 2, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10585778,
FT ECO:0000303|PubMed:12140260, ECO:0000303|PubMed:15489334"
FT /id="VSP_015374"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046140"
FT VAR_SEQ 138..570
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015375"
FT VAR_SEQ 509
FT /note="F -> FQVHYCDRQSGKECVTCLTLAPVQMTFHAIGSSIEASHD (in
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046141"
FT VAR_SEQ 511..570
FT /note="AALSALKQFSEQGLDPIDGAMNIEKGSLEKQAKHLREKADNNQAPPGSIAQD
FT CKKSNSAV -> V (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046142"
FT VAR_SEQ 511
FT /note="A -> V (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10585778,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_015376"
FT VAR_SEQ 512..570
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10585778,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_015377"
FT VARIANT 198
FT /note="V -> M (in dbSNP:rs949493)"
FT /evidence="ECO:0000269|PubMed:10585778,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16421571, ECO:0000269|PubMed:17974005"
FT /id="VAR_023394"
FT CONFLICT 345
FT /note="K -> T (in Ref. 3; BAH11778)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="G -> D (in Ref. 4; CAH10527)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 62608 MW; 0F07B59D9456D9FA CRC64;
MANPKEKTAM CLVNELARFN RVQPQYKLLN ERGPAHSKMF SVQLSLGEQT WESEGSSIKK
AQQAVANKAL TESTLPKPVQ KPPKSNVNNN PGSITPTVEL NGLAMKRGEP AIYRPLDPKP
FPNYRANYNF RGMYNQRYHC PVPKIFYVQL TVGNNEFFGE GKTRQAARHN AAMKALQALQ
NEPIPERSPQ NGESGKDVDD DKDANKSEIS LVFEIALKRN MPVSFEVIKE SGPPHMKSFV
TRVSVGEFSA EGEGNSKKLS KKRAATTVLQ ELKKLPPLPV VEKPKLFFKK RPKTIVKAGP
EYGQGMNPIS RLAQIQQAKK EKEPDYVLLS ERGMPRRREF VMQVKVGNEV ATGTGPNKKI
AKKNAAEAML LQLGYKASTN LQDQLEKTGE NKGWSGPKPG FPEPTNNTPK GILHLSPDVY
QEMEASRHKV ISGTTLGYLS PKDMNQPSSS FFSISPTSNS SATIARELLM NGTSSTAEAI
GLKGSSPTPP CSPVQPSKQL EYLARIQGFQ AALSALKQFS EQGLDPIDGA MNIEKGSLEK
QAKHLREKAD NNQAPPGSIA QDCKKSNSAV
