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Q13573

- SNW1_HUMAN

UniProt

Q13573 - SNW1_HUMAN

Protein

SNW domain-containing protein 1

Gene

SNW1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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. Proposed to be involved in transcriptional activation by EBV EBNA2 of CBF-1/RBPJ-repressed promoters. Is recruited by HIV-1 Tat to Tat:P-TEFb:TAR RNA complexes and is involved in Tat transcription by recruitment of MYC, MEN1 and TRRAP to the HIV promoter. 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.13 Publications

    GO - Molecular functioni

    1. Notch binding Source: UniProtKB
    2. nuclear hormone receptor binding Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. retinoic acid receptor binding Source: UniProtKB
    6. SMAD binding Source: UniProtKB
    7. transcription coactivator activity Source: UniProtKB
    8. transcription corepressor activity Source: UniProtKB
    9. vitamin D receptor binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to retinoic acid Source: UniProtKB
    2. gene expression Source: Reactome
    3. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
    4. mRNA splicing, via spliceosome Source: UniProtKB
    5. negative regulation of transcription, DNA-templated Source: UniProtKB
    6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. Notch signaling pathway Source: Reactome
    8. positive regulation by host of viral transcription Source: UniProtKB
    9. positive regulation of histone H3-K4 methylation Source: UniProtKB
    10. positive regulation of mRNA splicing, via spliceosome Source: UniProtKB
    11. positive regulation of neurogenesis Source: UniProtKB
    12. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    13. positive regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
    14. positive regulation of vitamin D receptor signaling pathway Source: UniProtKB
    15. regulation of retinoic acid receptor signaling pathway Source: UniProtKB
    16. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    17. regulation of vitamin D receptor signaling pathway Source: UniProtKB
    18. retinoic acid receptor signaling pathway Source: UniProtKB
    19. transcription initiation from RNA polymerase II promoter Source: Reactome
    20. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, mRNA processing, mRNA splicing, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_14835. Notch-HLH transcription pathway.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    SignaLinkiQ13573.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SNW domain-containing protein 1
    Alternative name(s):
    Nuclear protein SkiP
    Nuclear receptor coactivator NCoA-62
    Ski-interacting protein
    Gene namesi
    Name:SNW1
    Synonyms:SKIIP, SKIP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:16696. SNW1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. chromatin Source: Ensembl
    3. nuclear matrix Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB
    6. spliceosomal complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi66 – 661E → A or R: Abolishes interaction with PPIL1. 1 Publication
    Mutagenesisi76 – 761M → A: Abolishes interaction with PPIL1. 1 Publication

    Organism-specific databases

    PharmGKBiPA134883977.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 536535SNW domain-containing protein 1PRO_0000084827Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei224 – 2241Phosphoserine3 Publications
    Modified residuei232 – 2321Phosphoserine2 Publications
    Modified residuei234 – 2341Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13573.
    PaxDbiQ13573.
    PeptideAtlasiQ13573.
    PRIDEiQ13573.

    PTM databases

    PhosphoSiteiQ13573.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13573.
    BgeeiQ13573.
    CleanExiHS_SNW1.
    GenevestigatoriQ13573.

    Organism-specific databases

    HPAiCAB009931.
    HPA002457.
    HPA017370.

    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 and EBV EBNA2; NCOR2 and EBV EBNA2 compete for interaction with SNW1. 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. Interacts with human papillomavirus type-16 (HPV16) E7 protein.23 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTNNBL1Q8WYA62EBI-632715,EBI-748128
    FOXN3O004093EBI-632715,EBI-372721
    MAGEA1P433553EBI-632715,EBI-740978
    Ncor1Q609743EBI-632715,EBI-349004From a different organism.
    NCOR2Q9Y6184EBI-632715,EBI-80830
    NOTCH1P465313EBI-632715,EBI-636374
    PABPN1Q86U425EBI-632715,EBI-1226435
    PPIL1Q9Y3C64EBI-632715,EBI-2557649
    RBPJQ063302EBI-632715,EBI-632552
    SART1O432903EBI-632715,EBI-607761
    SIRT1Q96EB67EBI-632715,EBI-1802965
    SKIP491404EBI-632715,EBI-6392357From a different organism.
    SMAD2Q157963EBI-632715,EBI-1040141
    SMAD3P840225EBI-632715,EBI-347161
    SNIP1Q8TAD87EBI-632715,EBI-749336
    THRAP3Q9Y2W14EBI-632715,EBI-352039
    U2AF2P263685EBI-632715,EBI-742339
    V-SKIP178634EBI-632715,EBI-6392320From a different organism.
    VDRP114735EBI-632715,EBI-286357
    VdrP482812EBI-632715,EBI-346797From a different organism.
    XAB2Q9HCS72EBI-632715,EBI-295232
    ZNF830Q96NB32EBI-632715,EBI-3920997

    Protein-protein interaction databases

    BioGridi116597. 103 interactions.
    IntActiQ13573. 588 interactions.
    MINTiMINT-193944.
    STRINGi9606.ENSP00000261531.

    Structurei

    3D structure databases

    DisProtiDP00608.
    ProteinModelPortaliQ13573.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni59 – 7921Interaction with PPIL1Add
    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.
    InParanoidiQ13573.
    KOiK06063.
    PhylomeDBiQ13573.
    TreeFamiTF300782.

    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.

    Q13573-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALTSFLPAP TQLSQDQLEA EEKARSQRSR QTSLVSSRRE PPPYGYRKGW    50
    IPRLLEDFGD GGAFPEIHVA QYPLDMGRKK KMSNALAIQV DSEGKIKYDA 100
    IARQGQSKDK VIYSKYTDLV PKEVMNADDP DLQRPDEEAI KEITEKTRVA 150
    LEKSVSQKVA AAMPVRAADK LAPAQYIRYT PSQQGVAFNS GAKQRVIRMV 200
    EMQKDPMEPP RFKINKKIPR GPPSPPAPVM HSPSRKMTVK EQQEWKIPPC 250
    ISNWKNAKGY TIPLDKRLAA 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 SDRRQRGREG PVQFEEDPFG 500
    LDKFLEEAKQ HGGSKRPSDS SRPKEHEHEG KKRRKE 536
    Length:536
    Mass (Da):61,494
    Last modified:November 1, 1996 - v1
    Checksum:i0CC75E0D0B2CF842
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF045184 mRNA. Translation: AAC31697.1.
    U51432 mRNA. Translation: AAC15912.1.
    BT020060 mRNA. Translation: AAV38863.1.
    BT020061 mRNA. Translation: AAV38864.1.
    AK292274 mRNA. Translation: BAF84963.1.
    AC008372 Genomic DNA. Translation: AAF23325.1.
    CH471061 Genomic DNA. Translation: EAW81308.1.
    BC040112 mRNA. Translation: AAH40112.1.
    BC046105 mRNA. Translation: AAH46105.2.
    BC108903 mRNA. Translation: AAI08904.1.
    U43960 Genomic DNA. Translation: AAB48857.1.
    CCDSiCCDS9867.1.
    RefSeqiNP_036377.1. NM_012245.2.
    UniGeneiHs.445498.

    Genome annotation databases

    EnsembliENST00000261531; ENSP00000261531; ENSG00000100603.
    GeneIDi22938.
    KEGGihsa:22938.
    UCSCiuc001xuf.3. human.

    Polymorphism databases

    DMDMi2500813.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF045184 mRNA. Translation: AAC31697.1 .
    U51432 mRNA. Translation: AAC15912.1 .
    BT020060 mRNA. Translation: AAV38863.1 .
    BT020061 mRNA. Translation: AAV38864.1 .
    AK292274 mRNA. Translation: BAF84963.1 .
    AC008372 Genomic DNA. Translation: AAF23325.1 .
    CH471061 Genomic DNA. Translation: EAW81308.1 .
    BC040112 mRNA. Translation: AAH40112.1 .
    BC046105 mRNA. Translation: AAH46105.2 .
    BC108903 mRNA. Translation: AAI08904.1 .
    U43960 Genomic DNA. Translation: AAB48857.1 .
    CCDSi CCDS9867.1.
    RefSeqi NP_036377.1. NM_012245.2.
    UniGenei Hs.445498.

    3D structure databases

    DisProti DP00608.
    ProteinModelPortali Q13573.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116597. 103 interactions.
    IntActi Q13573. 588 interactions.
    MINTi MINT-193944.
    STRINGi 9606.ENSP00000261531.

    PTM databases

    PhosphoSitei Q13573.

    Polymorphism databases

    DMDMi 2500813.

    Proteomic databases

    MaxQBi Q13573.
    PaxDbi Q13573.
    PeptideAtlasi Q13573.
    PRIDEi Q13573.

    Protocols and materials databases

    DNASUi 22938.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261531 ; ENSP00000261531 ; ENSG00000100603 .
    GeneIDi 22938.
    KEGGi hsa:22938.
    UCSCi uc001xuf.3. human.

    Organism-specific databases

    CTDi 22938.
    GeneCardsi GC14M078183.
    HGNCi HGNC:16696. SNW1.
    HPAi CAB009931.
    HPA002457.
    HPA017370.
    MIMi 603055. gene.
    neXtProti NX_Q13573.
    PharmGKBi PA134883977.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295848.
    HOGENOMi HOG000160386.
    HOVERGENi HBG047516.
    InParanoidi Q13573.
    KOi K06063.
    PhylomeDBi Q13573.
    TreeFami TF300782.

    Enzyme and pathway databases

    Reactomei REACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_14835. Notch-HLH transcription pathway.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    SignaLinki Q13573.

    Miscellaneous databases

    GeneWikii SNW1.
    GenomeRNAii 22938.
    NextBioi 43687.
    PROi Q13573.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13573.
    Bgeei Q13573.
    CleanExi HS_SNW1.
    Genevestigatori Q13573.

    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. "Isolation and characterization of a novel coactivator protein, NCoA-62, involved in vitamin D-mediated transcription."
      Baudino T.A., Kraichely D.M., Jefcoat S.C. Jr., Winchester S.K., Partridge N.C., Macdonald P.N.
      J. Biol. Chem. 273:16434-16441(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH VDR.
    2. "The Ski oncoprotein interacts with Skip, the human homolog of Drosophila Bx42."
      Dahl R., Wani B., Hayman M.J.
      Oncogene 16:1579-1586(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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.
    5. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Cervix.
    8. Bienvenut W.V., Dozynkiewicz M., Norman J.C.
      Submitted (JUN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-23; 82-95; 179-193 AND 401-410, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    9. "The homolog of chromatin binding protein Bx42 identified in Dictyostelium."
      Folk P., Puta F., Krpejsova L., Blahuskova A., Markos A., Rabino M., Dottin R.P.
      Gene 181:229-231(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 282-536.
    10. "A role for SKIP in EBNA2 activation of CBF1-repressed promoters."
      Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D.
      J. Virol. 74:1939-1947(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RBPJ; CIR1; HDAC2 AND EPSTEIN-BARR VIRUS EBNA2 PROTEIN.
    11. "SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain of NotchIC To facilitate NotchIC function."
      Zhou S., Fujimuro M., Hsieh J.J., Chen L., Miyamoto A., Weinmaster G., Hayward S.D.
      Mol. Cell. Biol. 20:2400-2410(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NOTCH1.
    12. "The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression."
      Kim Y.-J., Noguchi S., Hayashi Y.K., Tsukahara T., Shimizu T., Arahata K.
      Hum. Mol. Genet. 10:1129-1139(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PABPN1.
    13. "Ski-interacting protein interacts with Smad proteins to augment transforming growth factor-beta-dependent transcription."
      Leong G.M., Subramaniam N., Figueroa J., Flanagan J.L., Hayman M.J., Eisman J.A., Kouzmenko A.P.
      J. Biol. Chem. 276:18243-18248(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SMAD2 AND SMAD3.
    14. "Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription."
      Zhang C., Baudino T.A., Dowd D.R., Tokumaru H., Wang W., MacDonald P.N.
      J. Biol. Chem. 276:40614-40620(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    15. "The HPV-16 E7 oncoprotein binds Skip and suppresses its transcriptional activity."
      Prathapam T., Kuhne C., Banks L.
      Oncogene 20:7677-7685(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HPV16 PROTEIN E7.
    16. "Skip interacts with the retinoblastoma tumor suppressor and inhibits its transcriptional repression activity."
      Prathapam T., Kuhne C., Banks L.
      Nucleic Acids Res. 30:5261-5268(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RB1.
    17. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
      Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
      RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
    18. "Interactions of SKIP/NCoA-62, TFIIB, and retinoid X receptor with vitamin D receptor helix H10 residues."
      Barry J.B., Leong G.M., Church W.B., Issa L.L., Eisman J.A., Gardiner E.M.
      J. Biol. Chem. 278:8224-8228(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VDR.
    19. "Nuclear coactivator-62 kDa/Ski-interacting protein is a nuclear matrix-associated coactivator that may couple vitamin D receptor-mediated transcription and RNA splicing."
      Zhang C., Dowd D.R., Staal A., Gu C., Lian J.B., van Wijnen A.J., Stein G.S., MacDonald P.N.
      J. Biol. Chem. 278:35325-35336(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    20. "Ski-interacting protein, a bifunctional nuclear receptor coregulator that interacts with N-CoR/SMRT and p300."
      Leong G.M., Subramaniam N., Issa L.L., Barry J.B., Kino T., Driggers P.H., Hayman M.J., Eisman J.A., Gardiner E.M.
      Biochem. Biophys. Res. Commun. 315:1070-1076(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "MAGE-A1 interacts with adaptor SKIP and the deacetylase HDAC1 to repress transcription."
      Laduron S., Deplus R., Zhou S., Kholmanskikh O., Godelaine D., De Smet C., Hayward S.D., Fuks F., Boon T., De Plaen E.
      Nucleic Acids Res. 32:4340-4350(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAGEA1.
    22. "The human Ski-interacting protein functionally substitutes for the yeast PRP45 gene."
      Figueroa J.D., Hayman M.J.
      Biochem. Biophys. Res. Commun. 319:1105-1109(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    23. "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.
    24. "Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP."
      Xu C., Zhang J., Huang X., Sun J., Xu Y., Tang Y., Wu J., Shi Y., Huang Q., Zhang Q.
      J. Biol. Chem. 281:15900-15908(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPIL1.
    25. "CHES1/FOXN3 interacts with Ski-interacting protein and acts as a transcriptional repressor."
      Scott K.L., Plon S.E.
      Gene 359:119-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FOXN3.
    26. "A human splicing factor, SKIP, associates with P-TEFb and enhances transcription elongation by HIV-1 Tat."
      Bres V., Gomes N., Pickle L., Jones K.A.
      Genes Dev. 19:1211-1226(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    27. Cited for: FUNCTION, IDENTIFICATION IN THE SNARP COMPLEX.
    28. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "SKIP interacts with c-Myc and Menin to promote HIV-1 Tat transactivation."
      Bres V., Yoshida T., Pickle L., Jones K.A.
      Mol. Cell 36:75-87(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    31. "A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR."
      Wang X., Zhang S., Zhang J., Huang X., Xu C., Wang W., Liu Z., Wu J., Shi Y.
      J. Biol. Chem. 285:4951-4963(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPIL, MUTAGENESIS OF GLU-66 AND MET-76.
    32. "The crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode for a linear epitope of the SKIP protein."
      Stegmann C.M., Luhrmann R., Wahl M.C.
      PLoS ONE 5:E10013-E10013(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPIL.
    33. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-232 AND SER-234, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    34. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. "SKIP counteracts p53-mediated apoptosis via selective regulation of p21Cip1 mRNA splicing."
      Chen Y., Zhang L., Jones K.A.
      Genes Dev. 25:701-716(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH U2AF2.
    36. Cited for: FUNCTION, INTERACTION WITH NOTCH1 AND MAML1.
    37. "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-224 AND SER-234, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    38. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    39. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSNW1_HUMAN
    AccessioniPrimary (citable) accession number: Q13573
    Secondary accession number(s): A8K8A9
    , Q13483, Q32N03, Q5D0D6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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