Q13573 (SNW1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SNW domain-containing protein 1

Alternative name(s):
Nuclear protein SkiP
Nuclear receptor coactivator NCoA-62
Ski-interacting protein

Gene names

Name:	SNW1
Synonyms:	SKIIP, SKIP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	536 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. 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 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. Ref.1 Ref.10 Ref.12 Ref.13 Ref.14 Ref.19 Ref.20 Ref.22 Ref.26 Ref.27 Ref.29 Ref.34 Ref.35
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 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. Ref.1 Ref.2 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31 Ref.34 Ref.35
Subcellular location	Nucleus Ref.19.
Sequence similarities	Belongs to the SNW family.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling pathway Traceable author statement. Source: Reactome cellular 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 mutant phenotype Ref.34. Source: UniProtKB mRNA splicing, via spliceosome Inferred from direct assay Ref.22. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.20. Source: UniProtKB positive regulation by host of viral transcription Inferred from direct assay Ref.26. Source: UniProtKB positive regulation of histone H3-K4 methylation Inferred from mutant phenotype Ref.29. Source: UniProtKB positive regulation of mRNA splicing, via spliceosome Inferred from mutant phenotype Ref.19. Source: UniProtKB positive regulation of neurogenesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.20PubMed 19934264. Source: UniProtKB positive regulation of transforming growth factor beta receptor signaling pathway Inferred from direct assay Ref.13. Source: UniProtKB positive regulation of vitamin D receptor signaling pathway Inferred from direct assay Ref.14Ref.1. Source: UniProtKB regulation of retinoic acid receptor signaling pathway Inferred from direct assay Ref.20. Source: UniProtKB retinoic acid receptor signaling pathway Inferred from direct assay PubMed 19934264. Source: UniProtKB transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	catalytic step 2 spliceosome Inferred from direct assay Ref.17. Source: UniProtKB chromatin Inferred from electronic annotation. Source: Compara nuclear matrix Inferred from direct assay Ref.19. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	SMAD binding Inferred from direct assay Ref.13. Source: UniProtKB retinoic acid receptor binding Inferred from direct assay Ref.14. Source: UniProtKB transcription coactivator activity Inferred from direct assay Ref.14Ref.20. Source: UniProtKB transcription corepressor activity Inferred from direct assay Ref.20. Source: UniProtKB vitamin D receptor binding Inferred from direct assay Ref.18. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FOXN3	O00409	3	EBI-632715,EBI-372721
MAGEA1	P43355	3	EBI-632715,EBI-740978
Ncor1	Q60974	3	EBI-632715,EBI-349004	From a different organism.
NCOR2	Q9Y618	3	EBI-632715,EBI-80830
NOTCH1	P46531	3	EBI-632715,EBI-636374
PABPN1	Q86U42	4	EBI-632715,EBI-1226435
PPIL1	Q9Y3C6	4	EBI-632715,EBI-2557649
RBPJ	Q06330	2	EBI-632715,EBI-632552
SIRT1	Q96EB6	7	EBI-632715,EBI-1802965
SKI	P49140	4	EBI-632715,EBI-6392357	From a different organism.
SMAD2	Q15796	3	EBI-632715,EBI-1040141
SMAD3	P84022	5	EBI-632715,EBI-347161
THRAP3	Q9Y2W1	3	EBI-632715,EBI-352039
U2AF2	P26368	4	EBI-632715,EBI-742339
V-SKI	P17863	4	EBI-632715,EBI-6392320	From a different organism.
VDR	P11473	5	EBI-632715,EBI-286357
Vdr	P48281	2	EBI-632715,EBI-346797	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.8
	Chain	2 – 536	535	SNW domain-containing protein 1		PRO_0000084827
Regions
	Region	59 – 79	21	Interaction with PPIL1
	Region	174 – 339	166	SNW
	Compositional bias	219 – 233	15	Pro-rich
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.8
	Modified residue	224	1	Phosphoserine Ref.28 Ref.32 Ref.36
	Modified residue	232	1	Phosphoserine Ref.28 Ref.32
	Modified residue	234	1	Phosphoserine Ref.32 Ref.36
Experimental info
	Mutagenesis	66	1	E → A or R: Abolishes interaction with PPIL1. Ref.30
	Mutagenesis	76	1	M → A: Abolishes interaction with PPIL1. Ref.30

Sequences

	Sequence		Length	Mass (Da)
	Q13573 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 0CC75E0D0B2CF842	FASTA	536	61,494
	10 20 30 40 50 60 MALTSFLPAP TQLSQDQLEA EEKARSQRSR QTSLVSSRRE PPPYGYRKGW IPRLLEDFGD 70 80 90 100 110 120 GGAFPEIHVA QYPLDMGRKK KMSNALAIQV DSEGKIKYDA IARQGQSKDK VIYSKYTDLV 130 140 150 160 170 180 PKEVMNADDP DLQRPDEEAI KEITEKTRVA LEKSVSQKVA AAMPVRAADK LAPAQYIRYT 190 200 210 220 230 240 PSQQGVAFNS GAKQRVIRMV EMQKDPMEPP RFKINKKIPR GPPSPPAPVM HSPSRKMTVK 250 260 270 280 290 300 EQQEWKIPPC ISNWKNAKGY TIPLDKRLAA 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 SDRRQRGREG PVQFEEDPFG LDKFLEEAKQ HGGSKRPSDS SRPKEHEHEG KKRRKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of a novel coactivator protein, NCoA-62, involved in vitamin D-mediated transcription." Baudino T.A., Kraichely D.M., Jefcoat S.C. Jr., Winchester S.K., Partridge N.C., Macdonald P.N. J. Biol. Chem. 273:16434-16441(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH VDR.
[2]	"The Ski oncoprotein interacts with Skip, the human homolog of Drosophila Bx42." Dahl R., Wani B., Hayman M.J. Oncogene 16:1579-1586(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[5]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix.
[8]	Bienvenut W.V., Dozynkiewicz M., Norman J.C. Submitted (JUN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-23; 82-95; 179-193 AND 401-410, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[9]	"The homolog of chromatin binding protein Bx42 identified in Dictyostelium." Folk P., Puta F., Krpejsova L., Blahuskova A., Markos A., Rabino M., Dottin R.P. Gene 181:229-231(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 282-536.
[10]	"A role for SKIP in EBNA2 activation of CBF1-repressed promoters." Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D. J. Virol. 74:1939-1947(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RBPJ; CIR1; HDAC2 AND EPSTEIN-BARR VIRUS EBNA2 PROTEIN.
[11]	"SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain of NotchIC To facilitate NotchIC function." Zhou S., Fujimuro M., Hsieh J.J., Chen L., Miyamoto A., Weinmaster G., Hayward S.D. Mol. Cell. Biol. 20:2400-2410(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NOTCH1.
[12]	"The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression." Kim Y.-J., Noguchi S., Hayashi Y.K., Tsukahara T., Shimizu T., Arahata K. Hum. Mol. Genet. 10:1129-1139(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PABPN1.
[13]	"Ski-interacting protein interacts with Smad proteins to augment transforming growth factor-beta-dependent transcription." Leong G.M., Subramaniam N., Figueroa J., Flanagan J.L., Hayman M.J., Eisman J.A., Kouzmenko A.P. J. Biol. Chem. 276:18243-18248(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SMAD2 AND SMAD3.
[14]	"Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription." Zhang C., Baudino T.A., Dowd D.R., Tokumaru H., Wang W., MacDonald P.N. J. Biol. Chem. 276:40614-40620(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[15]	"The HPV-16 E7 oncoprotein binds Skip and suppresses its transcriptional activity." Prathapam T., Kuhne C., Banks L. Oncogene 20:7677-7685(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HPV16 PROTEIN E7.
[16]	"Skip interacts with the retinoblastoma tumor suppressor and inhibits its transcriptional repression activity." Prathapam T., Kuhne C., Banks L. Nucleic Acids Res. 30:5261-5268(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RB1.
[17]	"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis." Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J. RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[18]	"Interactions of SKIP/NCoA-62, TFIIB, and retinoid X receptor with vitamin D receptor helix H10 residues." Barry J.B., Leong G.M., Church W.B., Issa L.L., Eisman J.A., Gardiner E.M. J. Biol. Chem. 278:8224-8228(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH VDR.
[19]	"Nuclear coactivator-62 kDa/Ski-interacting protein is a nuclear matrix-associated coactivator that may couple vitamin D receptor-mediated transcription and RNA splicing." Zhang C., Dowd D.R., Staal A., Gu C., Lian J.B., van Wijnen A.J., Stein G.S., MacDonald P.N. J. Biol. Chem. 278:35325-35336(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[20]	"Ski-interacting protein, a bifunctional nuclear receptor coregulator that interacts with N-CoR/SMRT and p300." Leong G.M., Subramaniam N., Issa L.L., Barry J.B., Kino T., Driggers P.H., Hayman M.J., Eisman J.A., Gardiner E.M. Biochem. Biophys. Res. Commun. 315:1070-1076(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[21]	"MAGE-A1 interacts with adaptor SKIP and the deacetylase HDAC1 to repress transcription." Laduron S., Deplus R., Zhou S., Kholmanskikh O., Godelaine D., De Smet C., Hayward S.D., Fuks F., Boon T., De Plaen E. Nucleic Acids Res. 32:4340-4350(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAGEA1.
[22]	"The human Ski-interacting protein functionally substitutes for the yeast PRP45 gene." Figueroa J.D., Hayman M.J. Biochem. Biophys. Res. Commun. 319:1105-1109(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[23]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[24]	"Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP." Xu C., Zhang J., Huang X., Sun J., Xu Y., Tang Y., Wu J., Shi Y., Huang Q., Zhang Q. J. Biol. Chem. 281:15900-15908(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPIL1.
[25]	"CHES1/FOXN3 interacts with Ski-interacting protein and acts as a transcriptional repressor." Scott K.L., Plon S.E. Gene 359:119-126(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FOXN3.
[26]	"A human splicing factor, SKIP, associates with P-TEFb and enhances transcription elongation by HIV-1 Tat." Bres V., Gomes N., Pickle L., Jones K.A. Genes Dev. 19:1211-1226(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[27]	"Regulation of cyclin D1 RNA stability by SNIP1." Bracken C.P., Wall S.J., Barre B., Panov K.I., Ajuh P.M., Perkins N.D. Cancer Res. 68:7621-7628(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE SNARP COMPLEX.
[28]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-232, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"SKIP interacts with c-Myc and Menin to promote HIV-1 Tat transactivation." Bres V., Yoshida T., Pickle L., Jones K.A. Mol. Cell 36:75-87(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[30]	"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR." Wang X., Zhang S., Zhang J., Huang X., Xu C., Wang W., Liu Z., Wu J., Shi Y. J. Biol. Chem. 285:4951-4963(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPIL, MUTAGENESIS OF GLU-66 AND MET-76.
[31]	"The crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode for a linear epitope of the SKIP protein." Stegmann C.M., Luhrmann R., Wahl M.C. PLoS ONE 5:E10013-E10013(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPIL.
[32]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-232 AND SER-234, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[33]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]	"SKIP counteracts p53-mediated apoptosis via selective regulation of p21Cip1 mRNA splicing." Chen Y., Zhang L., Jones K.A. Genes Dev. 25:701-716(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH U2AF2.
[35]	"Assembly of a Notch transcriptional activation complex requires multimerization." Vasquez-Del Carpio R., Kaplan F.M., Weaver K.L., VanWye J.D., Alves-Guerra M.C., Robbins D.J., Capobianco A.J. Mol. Cell. Biol. 31:1396-1408(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH NOTCH1 AND MAML1.
[36]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-234, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00013830.
RefSeq	NP_036377.1. NM_012245.2.
UniGene	Hs.445498.
3D structure databases
ProteinModelPortal	Q13573.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13573. 48 interactions.
MINT	MINT-193944.
STRING	9606.ENSP00000261531.
PTM databases
PhosphoSite	Q13573.
Polymorphism databases
DMDM	2500813.
Proteomic databases
PaxDb	Q13573.
PeptideAtlas	Q13573.
PRIDE	Q13573.
Protocols and materials databases
DNASU	22938.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261531; ENSP00000261531; ENSG00000100603.
GeneID	22938.
KEGG	hsa:22938.
UCSC	uc001xuf.3. human.
Organism-specific databases
CTD	22938.
GeneCards	GC14M078183.
HGNC	HGNC:16696. SNW1.
HPA	CAB009931. HPA002457. HPA017370.
MIM	603055. gene.
neXtProt	NX_Q13573.
PharmGKB	PA134883977.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG295848.
HOGENOM	HOG000160386.
HOVERGEN	HBG047516.
InParanoid	Q13573.
KO	K06063.
OrthoDB	EOG4RBQJG.
PhylomeDB	Q13573.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_2155. NICD traffics to nucleus. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q13573.
Bgee	Q13573.
CleanEx	HS_SNW1.
Genevestigator	Q13573.
GermOnline	ENSG00000100603. Homo sapiens.
Family and domain databases
InterPro	IPR017862. SKI-int_prot_SKIP. IPR004015. SKI-int_prot_SKIP_SNW-dom. [Graphical view]
PANTHER	PTHR12096. PTHR12096. 1 hit.
Pfam	PF02731. SKIP_SNW. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	22938.
NextBio	43687.
SOURCE	Search...

Entry information

Entry name

SNW1_HUMAN

Accession

Primary (citable) accession number: Q13573
Secondary accession number(s): A8K8A9 , Q13483, Q32N03, Q5D0D6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.