Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13573 (SNW1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length536 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.30 Ref.35 Ref.36

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.30 Ref.31 Ref.32 Ref.35 Ref.36

Subcellular location

Nucleus Ref.19.

Sequence similarities

Belongs to the SNW family.

Ontologies

Keywords
   Biological processHost-virus interaction
mRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentNucleus
Spliceosome
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Traceable author statement. Source: Reactome

cellular response to retinoic acid

Inferred from direct assay PubMed 19934264. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from mutant phenotype Ref.35. 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

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.11. 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.30. 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

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

regulation of vitamin D 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

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.17. Source: UniProtKB

chromatin

Inferred from electronic annotation. Source: Ensembl

nuclear matrix

Inferred from direct assay Ref.19. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.2. Source: UniProtKB

spliceosomal complex

Inferred from direct assay Ref.22. Source: UniProtKB

   Molecular_functionNotch binding

Inferred from physical interaction Ref.11. Source: UniProtKB

SMAD binding

Inferred from direct assay Ref.13. Source: UniProtKB

nuclear hormone receptor binding

Inferred from direct assay PubMed 19934264. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. 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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 536535SNW domain-containing protein 1
PRO_0000084827

Regions

Region59 – 7921Interaction with PPIL1
Region174 – 339166SNW
Compositional bias219 – 23315Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.29 Ref.38 Ref.39
Modified residue2241Phosphoserine Ref.28 Ref.33 Ref.37
Modified residue2321Phosphoserine Ref.28 Ref.33
Modified residue2341Phosphoserine Ref.33 Ref.37

Experimental info

Mutagenesis661E → A or R: Abolishes interaction with PPIL1. Ref.31
Mutagenesis761M → A: Abolishes interaction with PPIL1. Ref.31

Sequences

Sequence LengthMass (Da)Tools
Q13573 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0CC75E0D0B2CF842

FASTA53661,494
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"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.
[31]"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.
[32]"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.
[33]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[34]"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].
[35]"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.
[36]"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.
[37]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
RefSeqNP_036377.1. NM_012245.2.
UniGeneHs.445498.

3D structure databases

DisProtDP00608.
ProteinModelPortalQ13573.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116597. 100 interactions.
IntActQ13573. 587 interactions.
MINTMINT-193944.
STRING9606.ENSP00000261531.

PTM databases

PhosphoSiteQ13573.

Polymorphism databases

DMDM2500813.

Proteomic databases

PaxDbQ13573.
PeptideAtlasQ13573.
PRIDEQ13573.

Protocols and materials databases

DNASU22938.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261531; ENSP00000261531; ENSG00000100603.
GeneID22938.
KEGGhsa:22938.
UCSCuc001xuf.3. human.

Organism-specific databases

CTD22938.
GeneCardsGC14M078183.
HGNCHGNC:16696. SNW1.
HPACAB009931.
HPA002457.
HPA017370.
MIM603055. gene.
neXtProtNX_Q13573.
PharmGKBPA134883977.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295848.
HOGENOMHOG000160386.
HOVERGENHBG047516.
InParanoidQ13573.
KOK06063.
PhylomeDBQ13573.
TreeFamTF300782.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_2155. NICD traffics to nucleus.
REACT_71. Gene Expression.
SignaLinkQ13573.

Gene expression databases

ArrayExpressQ13573.
BgeeQ13573.
CleanExHS_SNW1.
GenevestigatorQ13573.

Family and domain databases

InterProIPR017862. SKI-int_prot_SKIP.
IPR004015. SKI-int_prot_SKIP_SNW-dom.
[Graphical view]
PANTHERPTHR12096. PTHR12096. 1 hit.
PfamPF02731. SKIP_SNW. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSNW1.
GenomeRNAi22938.
NextBio43687.
PROQ13573.
SOURCESearch...

Entry information

Entry nameSNW1_HUMAN
AccessionPrimary (citable) accession number: Q13573
Secondary accession number(s): A8K8A9 expand/collapse secondary AC list , Q13483, Q32N03, Q5D0D6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM