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Q9CSN1 (SNW1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SNW domain-containing protein 1
Alternative name(s):
Nuclear protein SkiP
Ski-interacting protein
Gene names
Name:Snw1
Synonyms:Skiip
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length536 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.2 Ref.3

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the SNW family.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentNucleus
Spliceosome
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to retinoic acid

Inferred from direct assay PubMed 19934264. Source: UniProtKB

intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA splicing, via spliceosome

Inferred from electronic annotation. Source: InterPro

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence orthology Ref.2. Source: MGI

positive regulation of histone H3-K4 methylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mRNA splicing, via spliceosome

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neurogenesis

Inferred from direct assay PubMed 19934264. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of retinoic acid receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of vitamin D receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

retinoic acid receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

skeletal muscle cell differentiation

Inferred from mutant phenotype PubMed 22147266. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnuclear matrix

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence orthology Ref.2. Source: MGI

spliceosomal complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionSMAD binding

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear hormone receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.3. Source: UniProtKB

retinoic acid receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription corepressor activity

Inferred from sequence or structural similarity. Source: UniProtKB

vitamin D receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 536535SNW domain-containing protein 1
PRO_0000084828

Regions

Region59 – 7921Interaction with PPIL1 By similarity
Region174 – 339166SNW
Compositional bias219 – 23315Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue2241Phosphoserine Ref.2 Ref.4 Ref.5
Modified residue2321Phosphoserine Ref.4 Ref.5
Modified residue2341Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CSN1 [UniParc].

Last modified February 15, 2005. Version 3.
Checksum: 1B5D050105BC6AAC

FASTA53661,475
        10         20         30         40         50         60 
MALTSFLPAP TQLSQDQLEA EERARSQRSL QTSLVSSRRE PPPYGYRKGW IPRLLEDFGD 

        70         80         90        100        110        120 
GGAFPEIHVA QYPLDMGRKK KMSNALAIQV DPEGKIKYDA IARQGQSKDK VIYSKYTDLV 

       130        140        150        160        170        180 
PKEVMNADDP DLQRPDEEAI KEITEKTRVA LEKSVSQKVA AAMPVRAADK LAPAQYIRYT 

       190        200        210        220        230        240 
PSQQGVAFNS GAKQRVIRMV EMQKEPMEPP RFKINKKIPR GPPSPPAPVM HSPSRKMTVK 

       250        260        270        280        290        300 
EQQEWKIPPC ISNWKNAKGY TIPIDKRLAA DGRGLQTVHI NENFAKLAEA LYIADRKARE 

       310        320        330        340        350        360 
AVEMRAQVER KMAQKEKEKH EEKLREMAQK ARERRAGIKT HVEKEDGEAR ERDEIRHDRR 

       370        380        390        400        410        420 
KERQHDRNLS RAAPDKRSKL QRNENRDISE VIALGVPNPR TSNEVQYDQR LFNQSKGMDS 

       430        440        450        460        470        480 
GFAGGEDEIY NVYDQAWRGG KDMAQSIYRP SKNLDKDMYG DDLEARIKTN RFVPDKEFSG 

       490        500        510        520        530 
SDRKQRGREG PVQFEEDPFG LDKFLEEAKQ HGGSKRPSDS SRPKEHEHEG KKRRKE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK012384 mRNA. Translation: BAB28203.2.
BY734581 mRNA. No translation available.
CCDSCCDS49121.1.
RefSeqNP_079783.2. NM_025507.2.
UniGeneMm.271174.

3D structure databases

ProteinModelPortalQ9CSN1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211406. 29 interactions.
IntActQ9CSN1. 34 interactions.
MINTMINT-1346847.
STRING10090.ENSMUSP00000021428.

PTM databases

PhosphoSiteQ9CSN1.

Proteomic databases

MaxQBQ9CSN1.
PaxDbQ9CSN1.
PRIDEQ9CSN1.

Protocols and materials databases

DNASU66354.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID66354.
KEGGmmu:66354.
UCSCuc007ojf.1. mouse.

Organism-specific databases

CTD22938.
MGIMGI:1913604. Snw1.

Phylogenomic databases

eggNOGNOG295848.
HOGENOMHOG000160386.
HOVERGENHBG047516.
InParanoidQ9CSN1.
KOK06063.
OrthoDBEOG72JWFX.
PhylomeDBQ9CSN1.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_189085. Disease.

Gene expression databases

CleanExMM_SNW1.
GenevestigatorQ9CSN1.

Family and domain databases

InterProIPR017862. SKI-int_prot_SKIP.
IPR004015. SKI-int_prot_SKIP_SNW-dom.
[Graphical view]
PANTHERPTHR12096. PTHR12096. 1 hit.
PfamPF02731. SKIP_SNW. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNW1. mouse.
NextBio321413.
PROQ9CSN1.
SOURCESearch...

Entry information

Entry nameSNW1_MOUSE
AccessionPrimary (citable) accession number: Q9CSN1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: July 9, 2014
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot