Details for: SNW1

Gene ID: 22938

Symbol: SNW1

Ensembl ID: ENSG00000100603

Description: SNW domain containing 1

Associated with

Other Information

Genular Protein ID: 733847209

Symbol: SNW1_HUMAN

Name: SNW domain-containing protein 1

UniProtKB Accession Codes:

Q13573 A8K8A9 Q13483 Q32N03 Q5D0D6

Database IDs:

AGR 1 AlphaFoldDB 1 Antibodypedia 1 Bgee 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 1 CORUM 1 CTD 1 ChiTaRS 1 ComplexPortal 1 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 DisProt 1 EMBL 11 EMDB 21 EPD 1 Ensembl 1 ExpressionAtlas 1 GO 33 GeneCards 1 GeneTree 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyCosmos 1 GlyGen 1 HGNC 1 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 2 KEGG 1 MANE-Select 1 MIM 1 MINT 1 MassIVE 1 MaxQB 1 MetOSite 1 NCBI Taxonomy 1 OMA 1 OpenTargets 1 OrthoDB 1 PANTHER 2 PDB 33 PDBsum 23 PRO 1 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 1 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 1 Pumba 1 RNAct 1 Reactome 12 RefSeq 1 SABIO-RK 1 SAM 1 SIGNOR 1 SMR 1 STRING 1 SignaLink 1 SwissPalm 1 TopDownProteomics 1 TreeFam 1 UCSC 1 UniProtKB 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 9632709

Title: Isolation and characterization of a novel coactivator protein, NCoA-62, involved in vitamin D-mediated transcription.

PubMed ID: 9632709

DOI: 10.1074/jbc.273.26.16434

PubMed ID: 9569025

Title: The Ski oncoprotein interacts with Skip, the human homolog of Drosophila Bx42.

PubMed ID: 9569025

DOI: 10.1038/sj.onc.1201687

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 12508121

Title: The DNA sequence and analysis of human chromosome 14.

PubMed ID: 12508121

DOI: 10.1038/nature01348

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8973337

Title: The homolog of chromatin binding protein Bx42 identified in Dictyostelium.

PubMed ID: 8973337

DOI: 10.1016/s0378-1119(96)00483-0

PubMed ID: 10644367

Title: A role for SKIP in EBNA2 activation of CBF1-repressed promoters.

PubMed ID: 10644367

DOI: 10.1128/jvi.74.4.1939-1947.2000

PubMed ID: 10713164

Title: SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain of NotchIC To facilitate NotchIC function.

PubMed ID: 10713164

DOI: 10.1128/mcb.20.7.2400-2410.2000

PubMed ID: 11371506

Title: The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression.

PubMed ID: 11371506

DOI: 10.1093/hmg/10.11.1129

PubMed ID: 11278756

Title: Ski-interacting protein interacts with Smad proteins to augment transforming growth factor-beta-dependent transcription.

PubMed ID: 11278756

DOI: 10.1074/jbc.m010815200

PubMed ID: 11514567

Title: Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription.

PubMed ID: 11514567

DOI: 10.1074/jbc.m106263200

PubMed ID: 11753645

Title: The HPV-16 E7 oncoprotein binds Skip and suppresses its transcriptional activity.

PubMed ID: 11753645

DOI: 10.1038/sj.onc.1204960

PubMed ID: 12466551

Title: Skip interacts with the retinoblastoma tumor suppressor and inhibits its transcriptional repression activity.

PubMed ID: 12466551

DOI: 10.1093/nar/gkf658

PubMed ID: 11991638

Title: Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.

PubMed ID: 11991638

DOI: 10.1017/s1355838202021088

PubMed ID: 12529369

Title: Interactions of SKIP/NCoA-62, TFIIB, and retinoid X receptor with vitamin D receptor helix H10 residues.

PubMed ID: 12529369

DOI: 10.1074/jbc.c200712200

PubMed ID: 12840015

Title: Nuclear coactivator-62 kDa/Ski-interacting protein is a nuclear matrix-associated coactivator that may couple vitamin D receptor-mediated transcription and RNA splicing.

PubMed ID: 12840015

DOI: 10.1074/jbc.m305191200

PubMed ID: 14985122

Title: Ski-interacting protein, a bifunctional nuclear receptor coregulator that interacts with N-CoR/SMRT and p300.

PubMed ID: 14985122

DOI: 10.1016/j.bbrc.2004.02.004

PubMed ID: 15316101

Title: MAGE-A1 interacts with adaptor SKIP and the deacetylase HDAC1 to repress transcription.

PubMed ID: 15316101

DOI: 10.1093/nar/gkh735

PubMed ID: 15194481

Title: The human Ski-interacting protein functionally substitutes for the yeast PRP45 gene.

PubMed ID: 15194481

DOI: 10.1016/j.bbrc.2004.05.096

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16595688

Title: Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP.

PubMed ID: 16595688

DOI: 10.1074/jbc.m511155200

PubMed ID: 16102918

Title: CHES1/FOXN3 interacts with Ski-interacting protein and acts as a transcriptional repressor.

PubMed ID: 16102918

DOI: 10.1016/j.gene.2005.06.014

PubMed ID: 15905409

Title: A human splicing factor, SKIP, associates with P-TEFb and enhances transcription elongation by HIV-1 Tat.

PubMed ID: 15905409

DOI: 10.1101/gad.1291705

PubMed ID: 18794151

Title: Regulation of cyclin D1 RNA stability by SNIP1.

PubMed ID: 18794151

DOI: 10.1158/0008-5472.can-08-1217

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19818711

Title: SKIP interacts with c-Myc and Menin to promote HIV-1 Tat transactivation.

PubMed ID: 19818711

DOI: 10.1016/j.molcel.2009.08.015

PubMed ID: 20007319

Title: A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR.

PubMed ID: 20007319

DOI: 10.1074/jbc.m109.087528

PubMed ID: 20368803

Title: The crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode for a linear epitope of the SKIP protein.

PubMed ID: 20368803

DOI: 10.1371/journal.pone.0010013

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21460037

Title: SKIP counteracts p53-mediated apoptosis via selective regulation of p21Cip1 mRNA splicing.

PubMed ID: 21460037

DOI: 10.1101/gad.2002611

PubMed ID: 21245387

Title: Assembly of a Notch transcriptional activation complex requires multimerization.

PubMed ID: 21245387

DOI: 10.1128/mcb.00360-10

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 33220177

Title: Mutations in Spliceosomal Genes PPIL1 and PRP17 Cause Neurodegenerative Pontocerebellar Hypoplasia with Microcephaly.

PubMed ID: 33220177

DOI: 10.1016/j.neuron.2020.10.035

PubMed ID: 28502770

Title: An Atomic Structure of the Human Spliceosome.

PubMed ID: 28502770

DOI: 10.1016/j.cell.2017.04.033

PubMed ID: 28076346

Title: Cryo-EM structure of a human spliceosome activated for step 2 of splicing.

PubMed ID: 28076346

DOI: 10.1038/nature21079

PubMed ID: 33509932

Title: Structure of the activated human minor spliceosome.

PubMed ID: 33509932

DOI: 10.1126/science.abg0879

Sequence Information:

  • Length: 536
  • Mass: 61494
  • Checksum: 0CC75E0D0B2CF842
  • Sequence:
    • MALTSFLPAP TQLSQDQLEA EEKARSQRSR QTSLVSSRRE PPPYGYRKGW IPRLLEDFGD 
GGAFPEIHVA QYPLDMGRKK KMSNALAIQV DSEGKIKYDA IARQGQSKDK VIYSKYTDLV 
PKEVMNADDP DLQRPDEEAI KEITEKTRVA LEKSVSQKVA AAMPVRAADK LAPAQYIRYT 
PSQQGVAFNS GAKQRVIRMV EMQKDPMEPP RFKINKKIPR GPPSPPAPVM HSPSRKMTVK 
EQQEWKIPPC ISNWKNAKGY TIPLDKRLAA DGRGLQTVHI NENFAKLAEA LYIADRKARE 
AVEMRAQVER KMAQKEKEKH EEKLREMAQK ARERRAGIKT HVEKEDGEAR ERDEIRHDRR 
KERQHDRNLS RAAPDKRSKL QRNENRDISE VIALGVPNPR TSNEVQYDQR LFNQSKGMDS 
GFAGGEDEIY NVYDQAWRGG KDMAQSIYRP SKNLDKDMYG DDLEARIKTN RFVPDKEFSG 
SDRRQRGREG PVQFEEDPFG LDKFLEEAKQ HGGSKRPSDS SRPKEHEHEG KKRRKE

Genular Protein ID: 1517795387

Symbol: G3V3A4_HUMAN

Name: N/A

UniProtKB Accession Codes:

G3V3A4

Database IDs:

ARBA 1 AlphaFoldDB 1 Antibodypedia 1 Bgee 1 BioGRID-ORCS 1 CTD 1 ChiTaRS 1 DNASU 1 EMBL 1 EPD 2 Ensembl 2 ExpressionAtlas 1 GO 3 GeneTree 1 GenomeRNAi 1 HGNC 1 InterPro 2 MassIVE 1 MaxQB 2 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PeptideAtlas 1 Pfam 2 PhylomeDB 1 Proteomes 2 ProteomicsDB 1 RefSeq 1 RuleBase 1 SAM 1 SMR 1 UCSC 1 VEuPathDB 1

Citations:

PubMed ID: 12508121

Title: The DNA sequence and analysis of human chromosome 14.

PubMed ID: 12508121

DOI: 10.1038/nature01348

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.M111.015131

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

Sequence Information:

  • Length: 571
  • Mass: 65391
  • Checksum: 74CC3F650EFB8768
  • Sequence:
    • MALTSFLPAP TQLSQDQLEA EEKARSQRSR QTSLVSSRRE PPPYGYRKGW IPRLLEDFGD 
GGAFPEIHVA QYPLDMGRKK KMSNALAIQV DSEGKIKYDA IARQGQSKDK VIYSKYTDLV 
PKEVMNADDP DLQRPDEEAI KEITEKTRVA LEKSVSQKVA AAMPVRAADK LAPAQYIRYT 
PSQQGVAFNS GAKQRVIRMV EMQKDPMEPP RFKINKKIPR GPPSPPAPVM HSPSRKMTVK 
EQQEWKIPPC ISNWKNAKGY TIPLDKRLAA DGRGLQTVHI NENFAKLAEA LYIADRKARE 
AVEMRAQVER KMAQKEKEKH EEKLREMAQK ARERRAGIKT HVEKEDGEAR ERDEIRHDRR 
KERQHDRNLS RAAPDKRSKL QRNENRDISE VIALGVPNPR TSNEVQYDQR LFNQSKGMDS 
GFAGGEDEIY NVYDQAWRGG KDMAQSIYRP SKNLDKDMYG DDLEARIKTN RCQAIQLNFS 
VYTGESKVVH SFFSFSLDLF PTRSFLVQTV DREAEKDQCS LRKILLVWTS FWKKPNSMVA 
LKDPQIAAAP RNTSMKARRG GRNRHRSLQS E

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.