Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9CSN1

- SNW1_MOUSE

UniProt

Q9CSN1 - SNW1_MOUSE

Protein

SNW domain-containing protein 1

Gene

Snw1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 3 (15 Feb 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in transcriptional regulation. Modulates TGF-beta-mediated transcription via association with SMAD proteins, MYOD1-mediated transcription via association with PABPN1, RB1-mediated transcriptional repression, and retinoid-X receptor (RXR)- and vitamin D receptor (VDR)-dependent gene transcription in a cell line-specific manner probably involving coactivators NCOA1 and GRIP1. Is involved in NOTCH1-mediated transcriptional activation. Binds to multimerized forms of Notch intracellular domain (NICD) and is proposed to recruit transcriptional coactivators such as MAML1 to form an intermediate preactivation complex which associates with DNA-bound CBF-1/RBPJ to form a transcriptional activation complex by releasing SNW1 and redundant NOTCH1 NICD. Functions as a splicing factor in pre-mRNA splicing. Is required in the specific splicing of CDKN1A pre-mRNA; the function probbaly involves the recruitment of U2AF2 to the mRNA. Is proposed to recruit PPIL1 to the spliceosome. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA By similarity.By similarity

    GO - Molecular functioni

    1. nuclear hormone receptor binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. retinoic acid receptor binding Source: UniProtKB
    4. SMAD binding Source: UniProtKB
    5. transcription coactivator activity Source: UniProtKB
    6. transcription corepressor activity Source: UniProtKB
    7. vitamin D receptor binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to retinoic acid Source: UniProtKB
    2. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
    3. mRNA splicing, via spliceosome Source: InterPro
    4. negative regulation of transcription, DNA-templated Source: MGI
    5. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    6. positive regulation of histone H3-K4 methylation Source: UniProtKB
    7. positive regulation of mRNA splicing, via spliceosome Source: UniProtKB
    8. positive regulation of neurogenesis Source: UniProtKB
    9. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    10. positive regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
    11. regulation of retinoic acid receptor signaling pathway Source: UniProtKB
    12. regulation of vitamin D receptor signaling pathway Source: UniProtKB
    13. retinoic acid receptor signaling pathway Source: UniProtKB
    14. skeletal muscle cell differentiation Source: MGI
    15. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    mRNA processing, mRNA splicing, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_196520. Pre-NOTCH Transcription and Translation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SNW domain-containing protein 1
    Alternative name(s):
    Nuclear protein SkiP
    Ski-interacting protein
    Gene namesi
    Name:Snw1
    Synonyms:Skiip
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1913604. Snw1.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nuclear matrix Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: MGI
    4. spliceosomal complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 536535SNW domain-containing protein 1PRO_0000084828Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei224 – 2241Phosphoserine3 Publications
    Modified residuei232 – 2321Phosphoserine2 Publications
    Modified residuei234 – 2341PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9CSN1.
    PaxDbiQ9CSN1.
    PRIDEiQ9CSN1.

    PTM databases

    PhosphoSiteiQ9CSN1.

    Expressioni

    Gene expression databases

    CleanExiMM_SNW1.
    GenevestigatoriQ9CSN1.

    Interactioni

    Subunit structurei

    Interacts SKI, SMAD2,SMAD3, RBPJ, RB1, PABPN1, MAGEA1, SIRT1, FOXN3, U2AF2, PPIL1, DAXX and ATP1B4. Interacts with VDR and RXRA; preferentially associates with VDR:RXRA heterodimers. Interacts with NCOR2. Interacts with MAML1. Interacts with NOTCH1 NICD; the interaction involves multimerized NOTCH1 NICD. Forms a complex with NOTCH1 NICD and MAML1; the association is dissociated by RBPJ. Identified in the spliceosome C complex. Associates with U4/U6-U5 tri-small nuclear ribonucleoproteins (U4/U6-U5 tri-snRNPs). Associates with positive transcription elongation factor b (P-TEFb). Component of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN.2 Publications

    Protein-protein interaction databases

    BioGridi211406. 29 interactions.
    DIPiDIP-42051N.
    IntActiQ9CSN1. 34 interactions.
    MINTiMINT-1346847.
    STRINGi10090.ENSMUSP00000021428.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CSN1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni59 – 7921Interaction with PPIL1By similarityAdd
    BLAST
    Regioni174 – 339166SNWAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi219 – 23315Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SNW family.Curated

    Phylogenomic databases

    eggNOGiNOG295848.
    HOGENOMiHOG000160386.
    HOVERGENiHBG047516.
    InParanoidiQ9CSN1.
    KOiK06063.
    OrthoDBiEOG72JWFX.
    PhylomeDBiQ9CSN1.

    Family and domain databases

    InterProiIPR017862. SKI-int_prot_SKIP.
    IPR004015. SKI-int_prot_SKIP_SNW-dom.
    [Graphical view]
    PANTHERiPTHR12096. PTHR12096. 1 hit.
    PfamiPF02731. SKIP_SNW. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9CSN1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALTSFLPAP TQLSQDQLEA EERARSQRSL QTSLVSSRRE PPPYGYRKGW    50
    IPRLLEDFGD GGAFPEIHVA QYPLDMGRKK KMSNALAIQV DPEGKIKYDA 100
    IARQGQSKDK VIYSKYTDLV PKEVMNADDP DLQRPDEEAI KEITEKTRVA 150
    LEKSVSQKVA AAMPVRAADK LAPAQYIRYT PSQQGVAFNS GAKQRVIRMV 200
    EMQKEPMEPP RFKINKKIPR GPPSPPAPVM HSPSRKMTVK EQQEWKIPPC 250
    ISNWKNAKGY TIPIDKRLAA DGRGLQTVHI NENFAKLAEA LYIADRKARE 300
    AVEMRAQVER KMAQKEKEKH EEKLREMAQK ARERRAGIKT HVEKEDGEAR 350
    ERDEIRHDRR KERQHDRNLS RAAPDKRSKL QRNENRDISE VIALGVPNPR 400
    TSNEVQYDQR LFNQSKGMDS GFAGGEDEIY NVYDQAWRGG KDMAQSIYRP 450
    SKNLDKDMYG DDLEARIKTN RFVPDKEFSG SDRKQRGREG PVQFEEDPFG 500
    LDKFLEEAKQ HGGSKRPSDS SRPKEHEHEG KKRRKE 536
    Length:536
    Mass (Da):61,475
    Last modified:February 15, 2005 - v3
    Checksum:i1B5D050105BC6AAC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK012384 mRNA. Translation: BAB28203.2.
    BY734581 mRNA. No translation available.
    CCDSiCCDS49121.1.
    RefSeqiNP_079783.2. NM_025507.2.
    UniGeneiMm.271174.

    Genome annotation databases

    GeneIDi66354.
    KEGGimmu:66354.
    UCSCiuc007ojf.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK012384 mRNA. Translation: BAB28203.2 .
    BY734581 mRNA. No translation available.
    CCDSi CCDS49121.1.
    RefSeqi NP_079783.2. NM_025507.2.
    UniGenei Mm.271174.

    3D structure databases

    ProteinModelPortali Q9CSN1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211406. 29 interactions.
    DIPi DIP-42051N.
    IntActi Q9CSN1. 34 interactions.
    MINTi MINT-1346847.
    STRINGi 10090.ENSMUSP00000021428.

    PTM databases

    PhosphoSitei Q9CSN1.

    Proteomic databases

    MaxQBi Q9CSN1.
    PaxDbi Q9CSN1.
    PRIDEi Q9CSN1.

    Protocols and materials databases

    DNASUi 66354.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 66354.
    KEGGi mmu:66354.
    UCSCi uc007ojf.1. mouse.

    Organism-specific databases

    CTDi 22938.
    MGIi MGI:1913604. Snw1.

    Phylogenomic databases

    eggNOGi NOG295848.
    HOGENOMi HOG000160386.
    HOVERGENi HBG047516.
    InParanoidi Q9CSN1.
    KOi K06063.
    OrthoDBi EOG72JWFX.
    PhylomeDBi Q9CSN1.

    Enzyme and pathway databases

    Reactomei REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_196520. Pre-NOTCH Transcription and Translation.

    Miscellaneous databases

    ChiTaRSi SNW1. mouse.
    NextBioi 321413.
    PROi Q9CSN1.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_SNW1.
    Genevestigatori Q9CSN1.

    Family and domain databases

    InterProi IPR017862. SKI-int_prot_SKIP.
    IPR004015. SKI-int_prot_SKIP_SNW-dom.
    [Graphical view ]
    PANTHERi PTHR12096. PTHR12096. 1 hit.
    Pfami PF02731. SKIP_SNW. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo.
    2. "The death domain-associated protein modulates activity of the transcription co-factor Skip/NcoA62."
      Tang J., Chang H.Y., Yang X.
      FEBS Lett. 579:2883-2890(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAXX, PHOSPHORYLATION AT SER-224.
    3. "Evolution of Na,K-ATPase betam-subunit into a coregulator of transcription in placental mammals."
      Pestov N.B., Ahmad N., Korneenko T.V., Zhao H., Radkov R., Schaer D., Roy S., Bibert S., Geering K., Modyanov N.N.
      Proc. Natl. Acad. Sci. U.S.A. 104:11215-11220(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATP1B4.
    4. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiSNW1_MOUSE
    AccessioniPrimary (citable) accession number: Q9CSN1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 96 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3