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O95793 (STAU1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Double-stranded RNA-binding protein Staufen homolog 1
Gene names
Name:STAU1
Synonyms:STAU
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.

Subunit structure

Binds tubulin. Binds with low affinity single-stranded RNA or DNA homopolymers. Interacts with CASC3 in an RNA-dependent manner By similarity. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Interacts with the influenza virus nonstructural protein NS1. Ref.10

Subcellular location

Cytoplasm. Rough endoplasmic reticulum. Note: Localizes exclusively with the rough reticulum endoplasmic (RER). Ref.10

Tissue specificity

Widely expressed. Expressed in brain, pancreas, heart, skeletal muscles, liver, lung, kidney and placenta.

Domain

One of the DRDB could be involved in RER binding.

The C-terminal contains the tubulin binding domain (TBD) By similarity.

Sequence similarities

Contains 3 DRBM (double-stranded RNA-binding) domains.

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: O95793-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: O95793-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
Isoform 3 (identifier: O95793-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
     203-203: E → ESFPLKQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 577576Double-stranded RNA-binding protein Staufen homolog 1
PRO_0000072243

Regions

Domain72 – 16291DRBM 1
Domain184 – 25168DRBM 2
Domain286 – 35469DRBM 3

Amino acid modifications

Modified residue21N-acetylserine Ref.9
Modified residue3901Phosphoserine Ref.13

Natural variations

Alternative sequence1 – 8181Missing in isoform Short and isoform 3.
VSP_004434
Alternative sequence2031E → ESFPLKQ in isoform 3.
VSP_043701

Experimental info

Sequence conflict3591A → R Ref.1
Sequence conflict3591A → R Ref.2
Sequence conflict360 – 39233QPTKP…PGSGD → SHQTRTQVRGEDTHKETRGW KKSNLFLNLALGM Ref.2

Secondary structure

................ 577
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 0977CEF40FD99517

FASTA57763,182
        10         20         30         40         50         60 
MSQVQVQVQN PSAALSGSQI LNKNQSLLSQ PLMSIPSTTS SLPSENAGRP IQNSALPSAS 

        70         80         90        100        110        120 
ITSTSAAAES ITPTVELNAL CMKLGKKPMY KPVDPYSRMQ STYNYNMRGG AYPPRYFYPF 

       130        140        150        160        170        180 
PVPPLLYQVE LSVGGQQFNG KGKTRQAAKH DAAAKALRIL QNEPLPERLE VNGRESEEEN 

       190        200        210        220        230        240 
LNKSEISQVF EIALKRNLPV NFEVARESGP PHMKNFVTKV SVGEFVGEGE GKSKKISKKN 

       250        260        270        280        290        300 
AAIAVLEELK KLPPLPAVER VKPRIKKKTK PIVKPQTSPE YGQGINPISR LAQIQQAKKE 

       310        320        330        340        350        360 
KEPEYTLLTE RGLPRRREFV MQVKVGNHTA EGTGTNKKVA KRNAAENMLE ILGFKVPQAQ 

       370        380        390        400        410        420 
PTKPALKSEE KTPIKKPGDG RKVTFFEPGS GDENGTSNKE DEFRMPYLSH QQLPAGILPM 

       430        440        450        460        470        480 
VPEVAQAVGV SQGHHTKDFT RAAPNPAKAT VTAMIARELL YGGTSPTAET ILKNNISSGH 

       490        500        510        520        530        540 
VPHGPLTRPS EQLDYLSRVQ GFQVEYKDFP KNNKNEFVSL INCSSQPPLI SHGIGKDVES 

       550        560        570 
CHDMAALNIL KLLSELDQQS TEMPRTGNGP MSVCGRC 

« Hide

Isoform Short [UniParc].

Checksum: 509B6CF2B928C02C
Show »

FASTA49654,934
Isoform 3 [UniParc].

Checksum: 3AA2A672D9D87081
Show »

FASTA50255,635

References

« Hide 'large scale' references
[1]"Mammalian Staufen is a double-stranded-RNA- and tubulin-binding protein which localizes to the rough endoplasmic reticulum."
Wickham L., Duchaine T., Luo M., Nabi I.R., DesGroseillers L.
Mol. Cell. Biol. 19:2220-2230(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: CNS.
[2]"Interaction of influenza virus NS1 protein and the human homologue of Staufen in vivo and in vitro."
Falcon A.M., Fortes P., Marion R.M., Beloso A., Ortin J.
Nucleic Acids Res. 27:2241-2247(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Tissue: Kidney.
[3]"Cloning and characterization of a splicing variant of human staufen protein."
Mao Y., Xie Y., Jin F.
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
Tissue: Brain.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
Tissue: Trachea.
[6]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT).
Tissue: Placenta and Skin.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF061939 mRNA. Translation: AAD17531.1.
AF061941 mRNA. Translation: AAD17533.1.
AF061938 mRNA. Translation: AAD17530.1.
AF061940 mRNA. Translation: AAD17532.1.
AJ132258 mRNA. Translation: CAB40082.1.
AY529074 mRNA. Translation: AAS76636.1.
AY546099 mRNA. Translation: AAS76637.1.
AL136601 mRNA. Translation: CAB66536.1.
AK292859 mRNA. Translation: BAF85548.1.
AL133174 Genomic DNA. Translation: CAC14084.1.
AL133174 Genomic DNA. Translation: CAC14085.1.
AL133174 Genomic DNA. Translation: CAI42820.1.
CH471077 Genomic DNA. Translation: EAW75669.1.
CH471077 Genomic DNA. Translation: EAW75671.1.
CH471077 Genomic DNA. Translation: EAW75672.1.
CH471077 Genomic DNA. Translation: EAW75673.1.
CH471077 Genomic DNA. Translation: EAW75674.1.
BC050432 mRNA. Translation: AAH50432.1.
BC095397 mRNA. Translation: AAH95397.1.
CCDSCCDS13414.1. [O95793-1]
CCDS13415.1. [O95793-2]
CCDS33481.1. [O95793-3]
RefSeqNP_001032405.1. NM_001037328.1. [O95793-3]
NP_004593.2. NM_004602.2. [O95793-2]
NP_059346.2. NM_017452.2. [O95793-2]
NP_059347.2. NM_017453.2. [O95793-1]
NP_059348.2. NM_017454.2. [O95793-2]
XP_005260583.1. XM_005260526.1. [O95793-3]
XP_005260584.1. XM_005260527.1. [O95793-3]
XP_005260585.1. XM_005260528.1. [O95793-3]
XP_005260586.1. XM_005260529.1. [O95793-2]
XP_006723930.1. XM_006723867.1. [O95793-1]
UniGeneHs.596704.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DKKX-ray1.70A448-557[»]
ProteinModelPortalO95793.
SMRO95793. Positions 186-252, 287-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112657. 52 interactions.
IntActO95793. 59 interactions.
MINTMINT-1160018.
STRING9606.ENSP00000360922.

PTM databases

PhosphoSiteO95793.

Proteomic databases

MaxQBO95793.
PaxDbO95793.
PRIDEO95793.

Protocols and materials databases

DNASU6780.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340954; ENSP00000345425; ENSG00000124214. [O95793-2]
ENST00000347458; ENSP00000323443; ENSG00000124214. [O95793-2]
ENST00000360426; ENSP00000353604; ENSG00000124214. [O95793-2]
ENST00000371802; ENSP00000360867; ENSG00000124214. [O95793-3]
ENST00000371828; ENSP00000360893; ENSG00000124214. [O95793-3]
ENST00000371856; ENSP00000360922; ENSG00000124214. [O95793-1]
GeneID6780.
KEGGhsa:6780.
UCSCuc002xua.3. human. [O95793-1]
uc002xub.3. human. [O95793-3]

Organism-specific databases

CTD6780.
GeneCardsGC20M047729.
HGNCHGNC:11370. STAU1.
HPACAB020839.
MIM601716. gene.
neXtProtNX_O95793.
PharmGKBPA36188.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG299502.
HOGENOMHOG000231025.
HOVERGENHBG005013.
InParanoidO95793.
KOK17597.
OMAQGIQVEY.
OrthoDBEOG7NGQCG.
PhylomeDBO95793.
TreeFamTF350296.

Gene expression databases

ArrayExpressO95793.
BgeeO95793.
CleanExHS_STAU1.
GenevestigatorO95793.

Family and domain databases

Gene3D3.30.160.20. 3 hits.
InterProIPR014720. dsRNA-bd_dom.
[Graphical view]
PfamPF00035. dsrm. 3 hits.
[Graphical view]
SMARTSM00358. DSRM. 3 hits.
[Graphical view]
PROSITEPS50137. DS_RBD. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTAU1. human.
GeneWikiSTAU1.
GenomeRNAi6780.
NextBio26468.
PROO95793.
SOURCESearch...

Entry information

Entry nameSTAU1_HUMAN
AccessionPrimary (citable) accession number: O95793
Secondary accession number(s): A8K9Z4 expand/collapse secondary AC list , E1P5Y1, E1P608, Q5JW29, Q6GTM4, Q9H5B4, Q9H5B5, Q9Y3Q2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: March 7, 2006
Last modified: July 9, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM