SNIP1

SNIP1
Identifiers
Aliases	SNIP1 , PMRED, Smad nuclear interacting protein 1, PML1, NEDHCS
External IDs	OMIM: 608241 MGI: 2156003 HomoloGene: 110886 GeneCards: SNIP1
Gene location (Human)
Chr.	Chromosome 1 (human)
End	37,554,293 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	124,967,835 bp
RNA expression pattern
	Top expressed in
	sural nerve; ; bone marrow; ; testicle; ; Achilles tendon; ; organ system; ; blood; ; liver; ; islet of Langerhans; ; adrenal gland;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	GO:0001948 protein binding ; mRNA binding ; RNA binding ;
Cellular component	nucleoplasm ; nucleus ; cytosol ; U2-type precatalytic spliceosome ;
Biological process	positive regulation of protein targeting to mitochondrion ; I-kappaB kinase/NF-kappaB signaling ; gene silencing ; regulation of transcription, DNA-templated ; production of miRNAs involved in gene silencing by miRNA ; mRNA splicing, via spliceosome ;
	Sources:Amigo / QuickGO
Orthologs
	79753
	76793
	ENSG00000163877
	ENSMUSG00000050213
	Q8TAD8
	Q8BIZ6
	NM_024700
	NM_175246 ; NM_001356560
	NP_078976
	NP_780455 ; NP_001343489
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated April 09, 2022

Smad nuclear-interacting protein 1 is a protein that in humans is encoded by the SNIP1 gene.^[5]^[6]^[7]

Interactions

SNIP1 has been shown to interact with EP300.^[5]

Related Research Articles

Histone acetyltransferase p300 also known as p300 HAT or E1A-associated protein p300 also known as EP300 or p300 is an enzyme that, in humans, is encoded by the EP300 gene. It functions as histone acetyltransferase that regulates transcription of genes via chromatin remodeling by allowing histone proteins to wrap DNA less tightly. This enzyme plays an essential role in regulating cell growth and division, prompting cells to mature and assume specialized functions (differentiate), and preventing the growth of cancerous tumors. The p300 protein appears to be critical for normal development before and after birth.

Mothers against decapentaplegic homolog 2 also known as SMAD family member 2 or SMAD2 is a protein that in humans is encoded by the SMAD2 gene. MAD homolog 2 belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways.

Mothers against decapentaplegic homolog 3 also known as SMAD family member 3 or SMAD3 is a protein that in humans is encoded by the SMAD3 gene.

SMAD4, also called SMAD family member 4, Mothers against decapentaplegic homolog 4, or DPC4 is a highly conserved protein present in all metazoans. It belongs to the SMAD family of transcription factor proteins, which act as mediators of TGF-β signal transduction. The TGFβ family of cytokines regulates critical processes during the lifecycle of metazoans, with important roles during embryo development, tissue homeostasis, regeneration, and immune regulation.

Mothers against decapentaplegic homolog 7 or SMAD7 is a protein that in humans is encoded by the SMAD7 gene.

Smads comprise a family of structurally similar proteins that are the main signal transducers for receptors of the transforming growth factor beta (TGF-B) superfamily, which are critically important for regulating cell development and growth. The abbreviation refers to the homologies to the Caenorhabditis elegans SMA and MAD family of genes in Drosophila.

Activin receptor type-1B is a protein that in humans is encoded by the ACVR1B gene.

Activin receptor type-2B is a protein that in humans is encoded by the ACVR2B gene. ACVR2B is an activin type 2 receptor.

Transforming growth factor, beta receptor II (70/80kDa) is a TGF beta receptor. TGFBR2 is its human gene.

The SKI protein is a nuclear proto-oncogene that is associated with tumors at high cellular concentrations. SKI has been shown to interfere with normal cellular functioning by both directly impeding expression of certain genes inside the nucleus of the cell as well as disrupting signaling proteins that activate genes.

Serine/threonine-protein kinase receptor R3 is an enzyme that in humans is encoded by the ACVRL1 gene.

Protein Mdm4 is a protein that in humans is encoded by the MDM4 gene.

Transcription factor E3 is a protein that in humans is encoded by the TFE3 gene.

E3 ubiquitin-protein ligase SMURF1 is an enzyme that in humans is encoded by the SMURF1 gene.

MDS1 and EVI1 complex locus protein EVI1 (MECOM) also known as ecotropic virus integration site 1 protein homolog (EVI-1) or positive regulatory domain zinc finger protein 3 (PRDM3) is a protein that in humans is encoded by the MECOM gene. EVI1 was first identified as a common retroviral integration site in AKXD murine myeloid tumors. It has since been identified in a plethora of other organisms, and seems to play a relatively conserved developmental role in embryogenesis. EVI1 is a nuclear transcription factor involved in many signaling pathways for both coexpression and coactivation of cell cycle genes.

Axin-2 also known as axin-like protein (Axil) or axis inhibition protein 2 (AXIN2) or conductin is a protein that in humans is encoded by the AXIN2 gene.

E3 ubiquitin-protein ligase SMURF2 is an enzyme that in humans is encoded by the SMURF2 gene.

NEDD4-like E3 ubiquitin-protein ligase WWP2 also known as atrophin-1-interacting protein 2 (AIP2) or WW domain-containing protein 2 (WWP2) is an enzyme that in humans is encoded by the WWP2 gene.

Forkhead box protein H1 is a protein that in humans is encoded by the FOXH1 gene.

Tripartite motif-containing 33 (TRIM33) also known as transcriptional intermediary factor 1 gamma (TIF1-γ), is a human gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000163877 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000050213 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 Kim RH, Wang D, Tsang M, Martin J, Huff C, de Caestecker MP, Parks WT, Meng X, Lechleider RJ, Wang T, Roberts AB (2000). "A novel smad nuclear interacting protein, SNIP1, suppresses p300-dependent TGF-beta signal transduction". Genes Dev. 14 (13): 1605–16. doi:10.1101/gad.14.13.1605. PMC 316742 . PMID 10887155.
↑ Roche KC, Wiechens N, Owen-Hughes T, Perkins ND (2004). "The FHA domain protein SNIP1 is a regulator of the cell cycle and cyclin D1 expression". Oncogene. 23 (50): 8185–8195. doi: 10.1038/sj.onc.1208025 . PMID 15378006.
↑ "Entrez Gene: SNIP1 Smad nuclear interacting protein 1".

Kim RH, Flanders KC, Birkey Reffey S, Anderson LA, Duckett CS, Perkins ND, Roberts AB (2001). "SNIP1 inhibits NF-kappa B signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators". J. Biol. Chem. 276 (49): 46297–46304. doi: 10.1074/jbc.M103819200 . PMID 11567019.
Lin Y, Martin J, Gruendler C, Farley J, Meng X, Li BY, Lechleider R, Huff C, Kim RH, Grasser WA, Paralkar V, Wang T (2002). "A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs)". BMC Cell Biol. 3: 15. doi:10.1186/1471-2121-3-15. PMC 117437 . PMID 12097147.
Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–1332. doi:10.1101/gr.2334104. PMC 442148 . PMID 15231748.
Cui Q, Lim SK, Zhao B, Hoffmann FM (2005). "Selective inhibition of TGF-beta responsive genes by Smad-interacting peptide aptamers from FoxH1, Lef1 and CBP". Oncogene. 24 (24): 3864–3874. doi: 10.1038/sj.onc.1208556 . PMID 15750622.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–1178. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–648. doi: 10.1016/j.cell.2006.09.026 . PMID 17081983. S2CID 7827573.
Fujii M, Lyakh LA, Bracken CP, Fukuoka J, Hayakawa M, Tsukiyama T, Soll SJ, Harris M, Rocha S, Roche KC, Tominaga S, Jen J, Perkins ND, Lechleider RJ, Roberts AB (2006). "SNIP1 is a candidate modifier of the transcriptional activity of c-Myc on E box-dependent target genes". Mol. Cell. 24 (5): 771–783. doi: 10.1016/j.molcel.2006.11.006 . PMID 17157259.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000163877 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000050213 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10887155-5] 1 2 Kim RH, Wang D, Tsang M, Martin J, Huff C, de Caestecker MP, Parks WT, Meng X, Lechleider RJ, Wang T, Roberts AB (2000). "A novel smad nuclear interacting protein, SNIP1, suppresses p300-dependent TGF-beta signal transduction". Genes Dev. 14 (13): 1605–16. doi:10.1101/gad.14.13.1605. PMC 316742 . PMID 10887155.

[pmid15378006-6] Roche KC, Wiechens N, Owen-Hughes T, Perkins ND (2004). "The FHA domain protein SNIP1 is a regulator of the cell cycle and cyclin D1 expression". Oncogene. 23 (50): 8185–8195. doi: 10.1038/sj.onc.1208025 . PMID 15378006.

[entrez-7] "Entrez Gene: SNIP1 Smad nuclear interacting protein 1".

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SNIP1

Contents

Interactions

Related Research Articles

References

Further reading