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Q9Y6Y0

- NS1BP_HUMAN

UniProt

Q9Y6Y0 - NS1BP_HUMAN

Protein

Influenza virus NS1A-binding protein

Gene

IVNS1ABP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 3 (01 May 2007)
      Previous versions | rss
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    Functioni

    Plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats. Protects cells from cell death induced by actin destabilization; Protects neurons from dendritic spines and actin filaments damage induced by the actin-destabilizing cytochalasin B when overexpressed. Activates Erk signaling pathway when overexpressed in cultured cell lines By similarity. May be a component of the cellular splicing machinery with a role in pre-mRNA splicing; may mediate the inhibition of splicing by NS/influenza virus NS1A protein. Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription.By similarity1 Publication

    GO - Biological processi

    1. negative regulation of intrinsic apoptotic signaling pathway Source: Ensembl
    2. response to virus Source: ProtInc
    3. RNA splicing Source: ProtInc
    4. transcription from RNA polymerase III promoter Source: ProtInc
    5. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Influenza virus NS1A-binding protein
    Short name:
    NS1-BP
    Short name:
    NS1-binding protein
    Alternative name(s):
    Aryl hydrocarbon receptor-associated protein 3
    Gene namesi
    Name:IVNS1ABP
    Synonyms:ARA3, FLARA3, KIAA0850, NS1, NS1BP
    ORF Names:HSPC068
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:16951. IVNS1ABP.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytoskeleton 1 Publication. Nucleusnucleoplasm 1 Publication
    Note: Associated with actin filaments By similarity. Localization related to speckle domains which correspond to interchromatin granules and are enriched in factors involved in pre-mRNA splicing. Following influenza A virus infection, redistribution from speckles to a more diffuse distribution in the nucleoplasm.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoskeleton Source: UniProtKB-SubCell
    3. nucleoplasm Source: UniProtKB-SubCell
    4. spliceosomal complex Source: ProtInc
    5. transcription factor complex Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi198 – 1981V → M: Significant inhibition of interaction with AHR; partial decrease of AHR signaling induced by IVNS1ABP. 1 Publication
    Mutagenesisi288 – 2881E → K: Significant inhibition of interaction with AHR; partial decrease of AHR signaling induced by IVNS1ABP. 1 Publication

    Organism-specific databases

    PharmGKBiPA134875300.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 642642Influenza virus NS1A-binding proteinPRO_0000285077Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei246 – 2461Phosphoserine1 Publication
    Modified residuei277 – 2771Phosphoserine1 Publication
    Modified residuei322 – 3221Phosphoserine1 Publication
    Modified residuei336 – 3361Phosphoserine1 Publication
    Modified residuei338 – 3381Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y6Y0.
    PaxDbiQ9Y6Y0.
    PRIDEiQ9Y6Y0.

    PTM databases

    PhosphoSiteiQ9Y6Y0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y6Y0.
    BgeeiQ9Y6Y0.
    CleanExiHS_IVNS1ABP.
    GenevestigatoriQ9Y6Y0.

    Organism-specific databases

    HPAiHPA003405.

    Interactioni

    Subunit structurei

    Homodimer; through the BTB domain By similarity. Interacts with NS/Influenza virus NS1A protein and with AHR/Aryl hydrocarbon receptor.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi115869. 19 interactions.
    IntActiQ9Y6Y0. 9 interactions.
    MINTiMINT-1371090.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y6Y0.
    SMRiQ9Y6Y0. Positions 19-202, 273-634.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 9968BTBPROSITE-ProRule annotationAdd
    BLAST
    Domaini134 – 233100BACKAdd
    BLAST
    Repeati369 – 41547Kelch 1Add
    BLAST
    Repeati416 – 46348Kelch 2Add
    BLAST
    Repeati465 – 51248Kelch 3Add
    BLAST
    Repeati513 – 55947Kelch 4Add
    BLAST
    Repeati560 – 60647Kelch 5Add
    BLAST
    Repeati608 – 64235Kelch 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni164 – 368205Sufficient for AHR interaction and signalingAdd
    BLAST

    Domaini

    When the BTB domain is lacking, AHR signaling induction promoted by IVNS1ABP is massively increased; Thus, the BTB domain inhibits AHR signaling induced by IVNS1ABP.1 Publication

    Sequence similaritiesi

    Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
    Contains 6 Kelch repeats.Curated

    Keywords - Domaini

    Kelch repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG236155.
    HOVERGENiHBG082407.
    InParanoidiQ9Y6Y0.
    KOiK15046.
    OMAiKLWTSCA.
    OrthoDBiEOG7327N7.
    PhylomeDBiQ9Y6Y0.
    TreeFamiTF329218.

    Family and domain databases

    Gene3Di2.130.10.80. 2 hits.
    3.30.710.10. 1 hit.
    InterProiIPR011705. BACK.
    IPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR015916. Gal_Oxidase_b-propeller.
    IPR017096. Kelch-like_gigaxonin-typ.
    IPR006652. Kelch_1.
    [Graphical view]
    PfamiPF07707. BACK. 1 hit.
    PF00651. BTB. 1 hit.
    PF01344. Kelch_1. 6 hits.
    [Graphical view]
    PIRSFiPIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
    SMARTiSM00875. BACK. 1 hit.
    SM00225. BTB. 1 hit.
    SM00612. Kelch. 6 hits.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.
    PROSITEiPS50097. BTB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y6Y0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIPNGYLMFE DENFIESSVA KLNALRKSGQ FCDVRLQVCG HEMLAHRAVL    50
    ACCSPYLFEI FNSDSDPHGI SHVKFDDLNP EAVEVLLNYA YTAQLKADKE 100
    LVKDVYSAAK KLKMDRVKQV CGDYLLSRMD VTSCISYRNF ASCMGDSRLL 150
    NKVDAYIQEH LLQISEEEEF LKLPRLKLEV MLEDNVCLPS NGKLYTKVIN 200
    WVQRSIWENG DSLEELMEEV QTLYYSADHK LLDGNLLDGQ AEVFGSDDDH 250
    IQFVQKKPPR ENGHKQISSS STGCLSSPNA TVQSPKHEWK IVASEKTSNN 300
    TYLCLAVLDG IFCVIFLHGR NSPQSSPTST PKLSKSLSFE MQQDELIEKP 350
    MSPMQYARSG LGTAEMNGKL IAAGGYNREE CLRTVECYNP HTDHWSFLAP 400
    MRTPRARFQM AVLMGQLYVV GGSNGHSDDL SCGEMYDSNI DDWIPVPELR 450
    TNRCNAGVCA LNGKLYIVGG SDPYGQKGLK NCDVFDPVTK LWTSCAPLNI 500
    RRHQSAVCEL GGYLYIIGGA ESWNCLNTVE RYNPENNTWT LIAPMNVARR 550
    GAGVAVLNGK LFVCGGFDGS HAISCVEMYD PTRNEWKMMG NMTSPRSNAG 600
    IATVGNTIYA VGGFDGNEFL NTVEVYNLES NEWSPYTKIF QF 642
    Length:642
    Mass (Da):71,729
    Last modified:May 1, 2007 - v3
    Checksum:i456E30DC4E351CCD
    GO

    Sequence cautioni

    The sequence AAF29040.1 differs from that shown. Reason: Frameshift at positions 100 and 102.
    The sequence CAA10029.1 differs from that shown. Reason: Frameshift at position 612.
    The sequence BAA74873.2 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI17867.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti111 – 1111K → E in CAA10029. (PubMed:9696811)Curated
    Sequence conflicti148 – 1481R → H in CAA10029. (PubMed:9696811)Curated
    Sequence conflicti218 – 2181E → G in AAH67739. (PubMed:15489334)Curated
    Sequence conflicti579 – 5791Y → H in ABE03889. (PubMed:16582008)Curated
    Sequence conflicti579 – 5791Y → H in ABE03890. (PubMed:16582008)Curated
    Sequence conflicti591 – 5911N → H in CAA10029. (PubMed:9696811)Curated
    Sequence conflicti623 – 6231V → A in CAA10029. (PubMed:9696811)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ012449 mRNA. Translation: CAA10029.1. Frameshift.
    DQ443528 mRNA. Translation: ABE03889.1.
    DQ443529 mRNA. Translation: ABE03890.1.
    AF205218 mRNA. Translation: AAG43485.1.
    AB020657 mRNA. Translation: BAA74873.2. Different initiation.
    AF161553 mRNA. Translation: AAF29040.1. Frameshift.
    AL078644, AL356273 Genomic DNA. Translation: CAB72329.1.
    AK292431 mRNA. Translation: BAF85120.1.
    AL078644 Genomic DNA. Translation: CAI17867.1. Sequence problems.
    AL356273, AL078644 Genomic DNA. Translation: CAI22094.1.
    CH471067 Genomic DNA. Translation: EAW91194.1.
    BC067739 mRNA. Translation: AAH67739.1.
    CCDSiCCDS1368.1.
    RefSeqiNP_006460.2. NM_006469.4.
    UniGeneiHs.497183.

    Genome annotation databases

    EnsembliENST00000367498; ENSP00000356468; ENSG00000116679.
    GeneIDi10625.
    KEGGihsa:10625.
    UCSCiuc001grl.3. human.

    Polymorphism databases

    DMDMi146325015.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ012449 mRNA. Translation: CAA10029.1 . Frameshift.
    DQ443528 mRNA. Translation: ABE03889.1 .
    DQ443529 mRNA. Translation: ABE03890.1 .
    AF205218 mRNA. Translation: AAG43485.1 .
    AB020657 mRNA. Translation: BAA74873.2 . Different initiation.
    AF161553 mRNA. Translation: AAF29040.1 . Frameshift.
    AL078644 , AL356273 Genomic DNA. Translation: CAB72329.1 .
    AK292431 mRNA. Translation: BAF85120.1 .
    AL078644 Genomic DNA. Translation: CAI17867.1 . Sequence problems.
    AL356273 , AL078644 Genomic DNA. Translation: CAI22094.1 .
    CH471067 Genomic DNA. Translation: EAW91194.1 .
    BC067739 mRNA. Translation: AAH67739.1 .
    CCDSi CCDS1368.1.
    RefSeqi NP_006460.2. NM_006469.4.
    UniGenei Hs.497183.

    3D structure databases

    ProteinModelPortali Q9Y6Y0.
    SMRi Q9Y6Y0. Positions 19-202, 273-634.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115869. 19 interactions.
    IntActi Q9Y6Y0. 9 interactions.
    MINTi MINT-1371090.

    PTM databases

    PhosphoSitei Q9Y6Y0.

    Polymorphism databases

    DMDMi 146325015.

    Proteomic databases

    MaxQBi Q9Y6Y0.
    PaxDbi Q9Y6Y0.
    PRIDEi Q9Y6Y0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367498 ; ENSP00000356468 ; ENSG00000116679 .
    GeneIDi 10625.
    KEGGi hsa:10625.
    UCSCi uc001grl.3. human.

    Organism-specific databases

    CTDi 10625.
    GeneCardsi GC01M185265.
    HGNCi HGNC:16951. IVNS1ABP.
    HPAi HPA003405.
    MIMi 609209. gene.
    neXtProti NX_Q9Y6Y0.
    PharmGKBi PA134875300.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG236155.
    HOVERGENi HBG082407.
    InParanoidi Q9Y6Y0.
    KOi K15046.
    OMAi KLWTSCA.
    OrthoDBi EOG7327N7.
    PhylomeDBi Q9Y6Y0.
    TreeFami TF329218.

    Miscellaneous databases

    ChiTaRSi IVNS1ABP. human.
    GeneWikii IVNS1ABP.
    GenomeRNAii 10625.
    NextBioi 40368.
    PROi Q9Y6Y0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y6Y0.
    Bgeei Q9Y6Y0.
    CleanExi HS_IVNS1ABP.
    Genevestigatori Q9Y6Y0.

    Family and domain databases

    Gene3Di 2.130.10.80. 2 hits.
    3.30.710.10. 1 hit.
    InterProi IPR011705. BACK.
    IPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR015916. Gal_Oxidase_b-propeller.
    IPR017096. Kelch-like_gigaxonin-typ.
    IPR006652. Kelch_1.
    [Graphical view ]
    Pfami PF07707. BACK. 1 hit.
    PF00651. BTB. 1 hit.
    PF01344. Kelch_1. 6 hits.
    [Graphical view ]
    PIRSFi PIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
    SMARTi SM00875. BACK. 1 hit.
    SM00225. BTB. 1 hit.
    SM00612. Kelch. 6 hits.
    [Graphical view ]
    SUPFAMi SSF54695. SSF54695. 1 hit.
    PROSITEi PS50097. BTB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "NS1-Binding protein (NS1-BP): a novel human protein that interacts with the influenza A virus nonstructural NS1 protein is relocalized in the nuclei of infected cells."
      Wolff T., O'Neill R.E., Palese P.
      J. Virol. 72:7170-7180(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH NS, SUBCELLULAR LOCATION.
    2. "The aryl hydrocarbon receptor signaling pathway is modified through interactions with a Kelch protein."
      Dunham E.E., Stevens E.A., Glover E., Bradfield C.A.
      Mol. Pharmacol. 70:8-15(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, REGION, MUTAGENESIS OF VAL-198 AND GLU-288, INTERACTION WITH AHR.
    3. "A novel gene from endothelium cells stimulated by human plasma LDL --similar to NS1-binding protein."
      Chen B.S., Zhang K.M.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    6. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Blood.
    7. "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].
      Tissue: Testis.
    8. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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].
      Tissue: Testis.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277 AND SER-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336 AND SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNS1BP_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6Y0
    Secondary accession number(s): A8K8R6
    , Q1G4T6, Q1G4T7, Q5TF75, Q6NW38, Q7LCG2, Q9NZX0, Q9Y480
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 106 of the entry and version 3 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3