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Q9CSN1

- SNW1_MOUSE

UniProt

Q9CSN1 - SNW1_MOUSE

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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

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. retinoic acid receptor binding Source: UniProtKB
  3. SMAD binding Source: UniProtKB
  4. transcription coactivator activity Source: UniProtKB
  5. transcription corepressor activity Source: UniProtKB
  6. 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
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_268602. 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
Complete GO annotation...

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

        10         20         30         40         50
MALTSFLPAP TQLSQDQLEA EERARSQRSL QTSLVSSRRE PPPYGYRKGW
60 70 80 90 100
IPRLLEDFGD GGAFPEIHVA QYPLDMGRKK KMSNALAIQV DPEGKIKYDA
110 120 130 140 150
IARQGQSKDK VIYSKYTDLV PKEVMNADDP DLQRPDEEAI KEITEKTRVA
160 170 180 190 200
LEKSVSQKVA AAMPVRAADK LAPAQYIRYT PSQQGVAFNS GAKQRVIRMV
210 220 230 240 250
EMQKEPMEPP RFKINKKIPR GPPSPPAPVM HSPSRKMTVK EQQEWKIPPC
260 270 280 290 300
ISNWKNAKGY TIPIDKRLAA DGRGLQTVHI NENFAKLAEA LYIADRKARE
310 320 330 340 350
AVEMRAQVER KMAQKEKEKH EEKLREMAQK ARERRAGIKT HVEKEDGEAR
360 370 380 390 400
ERDEIRHDRR KERQHDRNLS RAAPDKRSKL QRNENRDISE VIALGVPNPR
410 420 430 440 450
TSNEVQYDQR LFNQSKGMDS GFAGGEDEIY NVYDQAWRGG KDMAQSIYRP
460 470 480 490 500
SKNLDKDMYG DDLEARIKTN RFVPDKEFSG SDRKQRGREG PVQFEEDPFG
510 520 530
LDKFLEEAKQ HGGSKRPSDS SRPKEHEHEG KKRRKE
Length:536
Mass (Da):61,475
Last modified:February 15, 2005 - v3
Checksum:i1B5D050105BC6AAC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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_268602. Pre-NOTCH Transcription and Translation.

Miscellaneous databases

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 98 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