LOCUS       NP_079783                536 aa            linear   ROD 02-JUN-2024
DEFINITION  SNW domain-containing protein 1 [Mus musculus].
ACCESSION   NP_079783
VERSION     NP_079783.2
DBSOURCE    REFSEQ: accession NM_025507.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Liao,Z.M., Li,A.N., Cai,Y., Chen,J.J., Xu,Y., Sui,L.H., Wang,J.L.,
            Jin,P., Wang,K.S. and Yang,Z.C.
  TITLE     Skip participates in formation and lipid metabolism of beige
            adipose and might mediate the effects of SIRT1 activator BTM-0512
            on beige remodeling
  JOURNAL   Biochem Biophys Res Commun 537, 109-117 (2021)
   PUBMED   33388413
  REMARK    GeneRIF: Skip participates in formation and lipid metabolism of
            beige adipose and might mediate the effects of SIRT1 activator
            BTM-0512 on beige remodeling.
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Zhang,D., Qiao,X., Wang,L., Zhang,L., Yao,J., Wu,X., Yu,T.,
            Bostrom,K.I. and Yao,Y.
  TITLE     Skip is essential for Notch signaling to induce Sox2 in cerebral
            arteriovenous malformations
  JOURNAL   Cell Signal 68, 109537 (2020)
   PUBMED   31927035
  REMARK    GeneRIF: Skip is essential for Notch signaling to induce Sox2 in
            cerebral arteriovenous malformations.
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Rajan,S., Chu Pham Dang,H., Djambazian,H., Zuzan,H., Fedyshyn,Y.,
            Ketela,T., Moffat,J., Hudson,T.J. and Sladek,R.
  TITLE     Analysis of early C2C12 myogenesis identifies stably and
            differentially expressed transcriptional regulators whose
            knock-down inhibits myoblast differentiation
  JOURNAL   Physiol Genomics 44 (2), 183-197 (2012)
   PUBMED   22147266
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Kang,M.R., Lee,S.W., Um,E., Kang,H.T., Hwang,E.S., Kim,E.J. and
            Um,S.J.
  TITLE     Reciprocal roles of SIRT1 and SKIP in the regulation of RAR
            activity: implication in the retinoic acid-induced neuronal
            differentiation of P19 cells
  JOURNAL   Nucleic Acids Res 38 (3), 822-831 (2010)
   PUBMED   19934264
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Pestov,N.B., Ahmad,N., Korneenko,T.V., Zhao,H., Radkov,R.,
            Schaer,D., Roy,S., Bibert,S., Geering,K. and Modyanov,N.N.
  TITLE     Evolution of Na,K-ATPase beta m-subunit into a coregulator of
            transcription in placental mammals
  JOURNAL   Proc Natl Acad Sci U S A 104 (27), 11215-11220 (2007)
   PUBMED   17592128
REFERENCE   7  (residues 1 to 536)
  AUTHORS   Tang,J., Chang,H.Y. and Yang,X.
  TITLE     The death domain-associated protein modulates activity of the
            transcription co-factor Skip/NcoA62
  JOURNAL   FEBS Lett 579 (13), 2883-2890 (2005)
   PUBMED   15878163
REFERENCE   8  (residues 1 to 536)
  AUTHORS   Shu,H., Chen,S., Bi,Q., Mumby,M. and Brekken,D.L.
  TITLE     Identification of phosphoproteins and their phosphorylation sites
            in the WEHI-231 B lymphoma cell line
  JOURNAL   Mol Cell Proteomics 3 (3), 279-286 (2004)
   PUBMED   14729942
REFERENCE   9  (residues 1 to 536)
  AUTHORS   Barry,J.B., Leong,G.M., Church,W.B., Issa,L.L., Eisman,J.A. and
            Gardiner,E.M.
  TITLE     Interactions of SKIP/NCoA-62, TFIIB, and retinoid X receptor with
            vitamin D receptor helix H10 residues
  JOURNAL   J Biol Chem 278 (10), 8224-8228 (2003)
   PUBMED   12529369
  REMARK    GeneRIF: interaction with vitamin D receptor helix H10 residues
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK166163.1, AK009218.1 and AK012384.1.
            
            On May 1, 2007 this sequence version replaced NP_079783.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164138,
                              SAMN01164140 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 41.67 cM"
     Protein         1..536
                     /product="SNW domain-containing protein 1"
                     /note="SKI interacting protein; nuclear protein SkiP;
                     ski-interacting protein"
                     /calculated_mol_wt=61331
     Region          1..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CSN1.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q13573; propagated from
                     UniProtKB/Swiss-Prot (Q9CSN1.3)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13573; propagated from
                     UniProtKB/Swiss-Prot (Q9CSN1.3)"
     Region          59..79
                     /region_name="Interaction with PPIL1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CSN1.3)"
     Region          174..339
                     /region_name="SNW"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CSN1.3)"
     Region          178..334
                     /region_name="SKIP_SNW"
                     /note="SKIP/SNW domain; pfam02731"
                     /db_xref="CDD:460666"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13573; propagated from
                     UniProtKB/Swiss-Prot (Q9CSN1.3)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13573; propagated from
                     UniProtKB/Swiss-Prot (Q9CSN1.3)"
     Region          212..233
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CSN1.3)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15878163,
                     ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CSN1.3)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19131326,
                     ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (Q9CSN1.3)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13573; propagated from
                     UniProtKB/Swiss-Prot (Q9CSN1.3)"
     Region          311..386
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CSN1.3)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13573; propagated from
                     UniProtKB/Swiss-Prot (Q9CSN1.3)"
     Region          467..536
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CSN1.3)"
     Site            479
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13573; propagated from
                     UniProtKB/Swiss-Prot (Q9CSN1.3)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13573; propagated from
                     UniProtKB/Swiss-Prot (Q9CSN1.3)"
     CDS             1..536
                     /gene="Snw1"
                     /gene_synonym="2310008B08Rik; NCoA-62; Skiip; SKIP"
                     /coded_by="NM_025507.2:39..1649"
                     /db_xref="CCDS:CCDS49121.1"
                     /db_xref="GeneID:66354"
                     /db_xref="MGI:MGI:1913604"
ORIGIN      
        1 maltsflpap tqlsqdqlea eerarsqrsl qtslvssrre pppygyrkgw iprlledfgd
       61 ggafpeihva qypldmgrkk kmsnalaiqv dpegkikyda iarqgqskdk viyskytdlv
      121 pkevmnaddp dlqrpdeeai keitektrva leksvsqkva aampvraadk lapaqyiryt
      181 psqqgvafns gakqrvirmv emqkdpmepp rfkinkkipr gppsppapvm hspsrkmtvk
      241 eqqewkippc isnwknakgy tipldkrlaa dgrglqtvhi nenfaklaea lyiadrkare
      301 avemraqver kmaqkekekh eeklremaqk arerragikt hvekedgear erdeirhdrr
      361 kerqhdrnls raapdkrskl qrnenrdise vialgvpnpr tsnevqydqr lfnqskgmds
      421 gfaggedeiy nvydqawrgg kdmaqsiyrp sknldkdmyg ddleariktn rfvpdkefsg
      481 sdrkqrgreg pvqfeedpfg ldkfleeakq hggskrpsds srpkeheheg kkrrke
//
