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Protein

SNW domain-containing protein 1

Gene

SNW1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. 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 probably 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

  • Notch binding Source: UniProtKB
  • nuclear hormone receptor binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • retinoic acid receptor binding Source: UniProtKB
  • SMAD binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • transcription corepressor activity Source: UniProtKB
  • vitamin D receptor binding Source: UniProtKB

GO - Biological processi

  • cellular response to retinoic acid Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  • mRNA splicing, via spliceosome Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • Notch signaling pathway Source: Reactome
  • positive regulation by host of viral transcription Source: UniProtKB
  • positive regulation of histone H3-K4 methylation Source: UniProtKB
  • positive regulation of mRNA splicing, via spliceosome Source: UniProtKB
  • positive regulation of neurogenesis Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  • positive regulation of vitamin D receptor signaling pathway Source: UniProtKB
  • regulation of retinoic acid receptor signaling pathway Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
  • regulation of vitamin D receptor signaling pathway Source: UniProtKB
  • retinoic acid receptor signaling pathway Source: UniProtKB
  • Schwann cell proliferation Source: Ensembl
  • transcription initiation from RNA polymerase II promoter Source: Reactome
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiR-HSA-1912408. Pre-NOTCH Transcription and Translation.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-350054. Notch-HLH transcription pathway.
R-HSA-72163. mRNA Splicing - Major Pathway.
SignaLinkiQ13573.
SIGNORiQ13573.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:16696. SNW1.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • chromatin Source: Ensembl
  • cytoplasm Source: Ensembl
  • nuclear matrix Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • SMAD protein complex Source: Ensembl
  • spliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi66E → A or R: Abolishes interaction with PPIL1. 1 Publication1
Mutagenesisi76M → A: Abolishes interaction with PPIL1. 1 Publication1

Organism-specific databases

DisGeNETi22938.
OpenTargetsiENSG00000100603.
PharmGKBiPA134883977.

Polymorphism and mutation databases

BioMutaiSNW1.
DMDMi2500813.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000848272 – 536SNW domain-containing protein 1Add BLAST535

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei14PhosphoserineCombined sources1
Cross-linki81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki97Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki170Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei182PhosphoserineCombined sources1
Modified residuei190PhosphoserineCombined sources1
Cross-linki193Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei224PhosphoserineCombined sources1
Modified residuei232PhosphoserineCombined sources1
Modified residuei234PhosphoserineCombined sources1
Cross-linki240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei446PhosphoserineCombined sources1
Modified residuei479PhosphoserineCombined sources1
Modified residuei481PhosphoserineCombined sources1
Cross-linki509Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13573.
MaxQBiQ13573.
PaxDbiQ13573.
PeptideAtlasiQ13573.
PRIDEiQ13573.
TopDownProteomicsiQ13573.

PTM databases

iPTMnetiQ13573.
PhosphoSitePlusiQ13573.

Expressioni

Gene expression databases

BgeeiENSG00000100603.
CleanExiHS_SNW1.
ExpressionAtlasiQ13573. baseline and differential.
GenevisibleiQ13573. HS.

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
CEP55D3DR373EBI-632715,EBI-10173536
CTNNBL1Q8WYA62EBI-632715,EBI-748128
FOXN3O004093EBI-632715,EBI-372721
GOLGA2Q083793EBI-632715,EBI-618309
HSPB1P047923EBI-632715,EBI-352682
IKZF1Q134223EBI-632715,EBI-745305
KRT40Q6A1623EBI-632715,EBI-10171697
LZTS2Q9BRK43EBI-632715,EBI-741037
MAGEA1P433553EBI-632715,EBI-740978
MTUS2Q5JR593EBI-632715,EBI-742948
Ncor1Q609743EBI-632715,EBI-349004From a different organism.
NCOR2Q9Y6184EBI-632715,EBI-80830
NOTCH1P465313EBI-632715,EBI-636374
PABPN1Q86U425EBI-632715,EBI-1226435
PPIL1Q9Y3C611EBI-632715,EBI-2557649
RBPJQ063302EBI-632715,EBI-632552
RINT1Q6NUQ15EBI-632715,EBI-726876
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
TEX11Q8IYF33EBI-632715,EBI-742397
TFIP11Q9UBB95EBI-632715,EBI-1105213
THRAP3Q9Y2W14EBI-632715,EBI-352039
TRAF1Q130773EBI-632715,EBI-359224
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

GO - Molecular functioni

  • Notch binding Source: UniProtKB
  • nuclear hormone receptor binding Source: UniProtKB
  • retinoic acid receptor binding Source: UniProtKB
  • SMAD binding Source: UniProtKB
  • vitamin D receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116597. 540 interactors.
DIPiDIP-34800N.
IntActiQ13573. 613 interactors.
MINTiMINT-193944.
STRINGi9606.ENSP00000261531.

Structurei

3D structure databases

DisProtiDP00608.
ProteinModelPortaliQ13573.
SMRiQ13573.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni59 – 79Interaction with PPIL11 PublicationAdd BLAST21
Regioni174 – 339SNWAdd BLAST166

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi219 – 233Pro-richAdd BLAST15

Sequence similaritiesi

Belongs to the SNW family.Curated

Phylogenomic databases

eggNOGiKOG2441. Eukaryota.
ENOG410XQGT. LUCA.
GeneTreeiENSGT00390000010423.
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

        10         20         30         40         50
MALTSFLPAP TQLSQDQLEA EEKARSQRSR QTSLVSSRRE PPPYGYRKGW
60 70 80 90 100
IPRLLEDFGD GGAFPEIHVA QYPLDMGRKK KMSNALAIQV DSEGKIKYDA
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
EMQKDPMEPP RFKINKKIPR GPPSPPAPVM HSPSRKMTVK EQQEWKIPPC
260 270 280 290 300
ISNWKNAKGY TIPLDKRLAA 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 SDRRQRGREG PVQFEEDPFG
510 520 530
LDKFLEEAKQ HGGSKRPSDS SRPKEHEHEG KKRRKE
Length:536
Mass (Da):61,494
Last modified:November 1, 1996 - v1
Checksum:i0CC75E0D0B2CF842
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

DisProtiDP00608.
ProteinModelPortaliQ13573.
SMRiQ13573.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116597. 540 interactors.
DIPiDIP-34800N.
IntActiQ13573. 613 interactors.
MINTiMINT-193944.
STRINGi9606.ENSP00000261531.

PTM databases

iPTMnetiQ13573.
PhosphoSitePlusiQ13573.

Polymorphism and mutation databases

BioMutaiSNW1.
DMDMi2500813.

Proteomic databases

EPDiQ13573.
MaxQBiQ13573.
PaxDbiQ13573.
PeptideAtlasiQ13573.
PRIDEiQ13573.
TopDownProteomicsiQ13573.

Protocols and materials databases

DNASUi22938.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261531; ENSP00000261531; ENSG00000100603.
GeneIDi22938.
KEGGihsa:22938.
UCSCiuc001xuf.4. human.

Organism-specific databases

CTDi22938.
DisGeNETi22938.
GeneCardsiSNW1.
HGNCiHGNC:16696. SNW1.
HPAiCAB009931.
HPA002457.
HPA017370.
MIMi603055. gene.
neXtProtiNX_Q13573.
OpenTargetsiENSG00000100603.
PharmGKBiPA134883977.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2441. Eukaryota.
ENOG410XQGT. LUCA.
GeneTreeiENSGT00390000010423.
HOGENOMiHOG000160386.
HOVERGENiHBG047516.
InParanoidiQ13573.
KOiK06063.
PhylomeDBiQ13573.
TreeFamiTF300782.

Enzyme and pathway databases

ReactomeiR-HSA-1912408. Pre-NOTCH Transcription and Translation.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-350054. Notch-HLH transcription pathway.
R-HSA-72163. mRNA Splicing - Major Pathway.
SignaLinkiQ13573.
SIGNORiQ13573.

Miscellaneous databases

ChiTaRSiSNW1. human.
GeneWikiiSNW1.
GenomeRNAii22938.
PROiQ13573.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100603.
CleanExiHS_SNW1.
ExpressionAtlasiQ13573. baseline and differential.
GenevisibleiQ13573. HS.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 165 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.