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O95793

- STAU1_HUMAN

UniProt

O95793 - STAU1_HUMAN

Protein

Double-stranded RNA-binding protein Staufen homolog 1

Gene

STAU1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. double-stranded RNA binding Source: ProtInc
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct

    GO - Biological processi

    1. intracellular mRNA localization Source: Ensembl

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Double-stranded RNA-binding protein Staufen homolog 1
    Gene namesi
    Name:STAU1
    Synonyms:STAU
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:11370. STAU1.

    Subcellular locationi

    Cytoplasm 1 Publication. Rough endoplasmic reticulum 1 Publication
    Note: Localizes exclusively with the rough reticulum endoplasmic (RER).

    GO - Cellular componenti

    1. cell body Source: ParkinsonsUK-UCL
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    4. cytoplasmic stress granule Source: BHF-UCL
    5. dendrite Source: ParkinsonsUK-UCL
    6. extracellular vesicular exosome Source: UniProt
    7. membrane Source: UniProtKB
    8. microtubule associated complex Source: ProtInc
    9. neuronal cell body Source: Ensembl
    10. rough endoplasmic reticulum Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36188.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 577576Double-stranded RNA-binding protein Staufen homolog 1PRO_0000072243Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei390 – 3901Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95793.
    PaxDbiO95793.
    PRIDEiO95793.

    PTM databases

    PhosphoSiteiO95793.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiO95793.
    BgeeiO95793.
    CleanExiHS_STAU1.
    GenevestigatoriO95793.

    Organism-specific databases

    HPAiCAB020839.

    Interactioni

    Subunit structurei

    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.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NSP034963EBI-358174,EBI-2547442From a different organism.
    RPL7AP624242EBI-358174,EBI-354172
    RPLP0P053884EBI-358174,EBI-354101
    UPF1Q929005EBI-358174,EBI-373471

    Protein-protein interaction databases

    BioGridi112657. 55 interactions.
    IntActiO95793. 59 interactions.
    MINTiMINT-1160018.
    STRINGi9606.ENSP00000360922.

    Structurei

    Secondary structure

    1
    577
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi448 – 46215
    Helixi466 – 4727
    Helixi489 – 50012
    Beta strandi504 – 5096
    Beta strandi517 – 5237
    Beta strandi525 – 5273
    Beta strandi529 – 5379
    Helixi538 – 55316

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4DKKX-ray1.70A448-557[»]
    ProteinModelPortaliO95793.
    SMRiO95793. Positions 186-252, 287-355.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini72 – 16291DRBM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini184 – 25168DRBM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini286 – 35469DRBM 3PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    One of the DRDB could be involved in RER binding.
    The C-terminal contains the tubulin binding domain (TBD).By similarity

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG299502.
    HOGENOMiHOG000231025.
    HOVERGENiHBG005013.
    InParanoidiO95793.
    KOiK17597.
    OMAiQGIQVEY.
    OrthoDBiEOG7NGQCG.
    PhylomeDBiO95793.
    TreeFamiTF350296.

    Family and domain databases

    Gene3Di3.30.160.20. 3 hits.
    InterProiIPR014720. dsRNA-bd_dom.
    [Graphical view]
    PfamiPF00035. dsrm. 3 hits.
    [Graphical view]
    SMARTiSM00358. DSRM. 3 hits.
    [Graphical view]
    PROSITEiPS50137. DS_RBD. 3 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: O95793-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSQVQVQVQN PSAALSGSQI LNKNQSLLSQ PLMSIPSTTS SLPSENAGRP    50
    IQNSALPSAS ITSTSAAAES ITPTVELNAL CMKLGKKPMY KPVDPYSRMQ 100
    STYNYNMRGG AYPPRYFYPF PVPPLLYQVE LSVGGQQFNG KGKTRQAAKH 150
    DAAAKALRIL QNEPLPERLE VNGRESEEEN LNKSEISQVF EIALKRNLPV 200
    NFEVARESGP PHMKNFVTKV SVGEFVGEGE GKSKKISKKN AAIAVLEELK 250
    KLPPLPAVER VKPRIKKKTK PIVKPQTSPE YGQGINPISR LAQIQQAKKE 300
    KEPEYTLLTE RGLPRRREFV MQVKVGNHTA EGTGTNKKVA KRNAAENMLE 350
    ILGFKVPQAQ PTKPALKSEE KTPIKKPGDG RKVTFFEPGS GDENGTSNKE 400
    DEFRMPYLSH QQLPAGILPM VPEVAQAVGV SQGHHTKDFT RAAPNPAKAT 450
    VTAMIARELL YGGTSPTAET ILKNNISSGH VPHGPLTRPS EQLDYLSRVQ 500
    GFQVEYKDFP KNNKNEFVSL INCSSQPPLI SHGIGKDVES CHDMAALNIL 550
    KLLSELDQQS TEMPRTGNGP MSVCGRC 577
    Length:577
    Mass (Da):63,182
    Last modified:March 7, 2006 - v2
    Checksum:i0977CEF40FD99517
    GO
    Isoform Short (identifier: O95793-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:496
    Mass (Da):54,934
    Checksum:i509B6CF2B928C02C
    GO
    Isoform 3 (identifier: O95793-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:502
    Mass (Da):55,635
    Checksum:i3AA2A672D9D87081
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti359 – 3591A → R(PubMed:10022909)Curated
    Sequence conflicti359 – 3591A → R(PubMed:10325410)Curated
    Sequence conflicti360 – 39233QPTKP…PGSGD → SHQTRTQVRGEDTHKETRGW KKSNLFLNLALGM(PubMed:10325410)CuratedAdd
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8181Missing in isoform Short and isoform 3. 5 PublicationsVSP_004434Add
    BLAST
    Alternative sequencei203 – 2031E → ESFPLKQ in isoform 3. 1 PublicationVSP_043701

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS13414.1. [O95793-1]
    CCDS13415.1. [O95793-2]
    CCDS33481.1. [O95793-3]
    RefSeqiNP_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]
    UniGeneiHs.596704.

    Genome annotation databases

    EnsembliENST00000340954; 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]
    GeneIDi6780.
    KEGGihsa:6780.
    UCSCiuc002xua.3. human. [O95793-1]
    uc002xub.3. human. [O95793-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS13414.1. [O95793-1 ]
    CCDS13415.1. [O95793-2 ]
    CCDS33481.1. [O95793-3 ]
    RefSeqi NP_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 ]
    UniGenei Hs.596704.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4DKK X-ray 1.70 A 448-557 [» ]
    ProteinModelPortali O95793.
    SMRi O95793. Positions 186-252, 287-355.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112657. 55 interactions.
    IntActi O95793. 59 interactions.
    MINTi MINT-1160018.
    STRINGi 9606.ENSP00000360922.

    PTM databases

    PhosphoSitei O95793.

    Proteomic databases

    MaxQBi O95793.
    PaxDbi O95793.
    PRIDEi O95793.

    Protocols and materials databases

    DNASUi 6780.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340954 ; 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 ]
    GeneIDi 6780.
    KEGGi hsa:6780.
    UCSCi uc002xua.3. human. [O95793-1 ]
    uc002xub.3. human. [O95793-3 ]

    Organism-specific databases

    CTDi 6780.
    GeneCardsi GC20M047729.
    HGNCi HGNC:11370. STAU1.
    HPAi CAB020839.
    MIMi 601716. gene.
    neXtProti NX_O95793.
    PharmGKBi PA36188.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG299502.
    HOGENOMi HOG000231025.
    HOVERGENi HBG005013.
    InParanoidi O95793.
    KOi K17597.
    OMAi QGIQVEY.
    OrthoDBi EOG7NGQCG.
    PhylomeDBi O95793.
    TreeFami TF350296.

    Miscellaneous databases

    ChiTaRSi STAU1. human.
    GeneWikii STAU1.
    GenomeRNAii 6780.
    NextBioi 26468.
    PROi O95793.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95793.
    Bgeei O95793.
    CleanExi HS_STAU1.
    Genevestigatori O95793.

    Family and domain databases

    Gene3Di 3.30.160.20. 3 hits.
    InterProi IPR014720. dsRNA-bd_dom.
    [Graphical view ]
    Pfami PF00035. dsrm. 3 hits.
    [Graphical view ]
    SMARTi SM00358. DSRM. 3 hits.
    [Graphical view ]
    PROSITEi PS50137. DS_RBD. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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.
      , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSTAU1_HUMAN
    AccessioniPrimary (citable) accession number: O95793
    Secondary accession number(s): A8K9Z4
    , E1P5Y1, E1P608, Q5JW29, Q6GTM4, Q9H5B4, Q9H5B5, Q9Y3Q2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3