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Q13573

- SNW1_HUMAN

UniProt

Q13573 - SNW1_HUMAN

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Protein

SNW domain-containing protein 1

Gene

SNW1

Organism
Homo sapiens (Human)
Status
Reviewed - 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 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.13 Publications

GO - Molecular functioni

  1. Notch binding Source: UniProtKB
  2. nuclear hormone receptor binding Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB
  4. retinoic acid receptor binding Source: UniProtKB
  5. SMAD binding Source: UniProtKB
  6. transcription coactivator activity Source: UniProtKB
  7. transcription corepressor activity Source: UniProtKB
  8. vitamin D receptor binding Source: UniProtKB

GO - Biological processi

  1. cellular response to retinoic acid Source: UniProtKB
  2. gene expression Source: Reactome
  3. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  4. mRNA splicing, via spliceosome Source: UniProtKB
  5. negative regulation of transcription, DNA-templated Source: UniProtKB
  6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  7. Notch signaling pathway Source: Reactome
  8. positive regulation by host of viral transcription Source: UniProtKB
  9. positive regulation of histone H3-K4 methylation Source: UniProtKB
  10. positive regulation of mRNA splicing, via spliceosome Source: UniProtKB
  11. positive regulation of neurogenesis Source: UniProtKB
  12. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  13. positive regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  14. positive regulation of vitamin D receptor signaling pathway Source: UniProtKB
  15. regulation of retinoic acid receptor signaling pathway Source: UniProtKB
  16. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  17. regulation of vitamin D receptor signaling pathway Source: UniProtKB
  18. retinoic acid receptor signaling pathway Source: UniProtKB
  19. transcription initiation from RNA polymerase II promoter Source: Reactome
  20. 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

ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_14835. Notch-HLH transcription pathway.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
SignaLinkiQ13573.

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
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:16696. SNW1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. chromatin Source: Ensembl
  3. nuclear matrix Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
  6. spliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi66 – 661E → A or R: Abolishes interaction with PPIL1. 1 Publication
Mutagenesisi76 – 761M → A: Abolishes interaction with PPIL1. 1 Publication

Organism-specific databases

PharmGKBiPA134883977.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 536535SNW domain-containing protein 1PRO_0000084827Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei224 – 2241Phosphoserine3 Publications
Modified residuei232 – 2321Phosphoserine2 Publications
Modified residuei234 – 2341Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13573.
PaxDbiQ13573.
PeptideAtlasiQ13573.
PRIDEiQ13573.

PTM databases

PhosphoSiteiQ13573.

Expressioni

Gene expression databases

BgeeiQ13573.
CleanExiHS_SNW1.
ExpressionAtlasiQ13573. baseline and differential.
GenevestigatoriQ13573.

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
CTNNBL1Q8WYA62EBI-632715,EBI-748128
FOXN3O004093EBI-632715,EBI-372721
HSPB1P047923EBI-632715,EBI-352682
MAGEA1P433553EBI-632715,EBI-740978
Ncor1Q609743EBI-632715,EBI-349004From a different organism.
NCOR2Q9Y6184EBI-632715,EBI-80830
NOTCH1P465313EBI-632715,EBI-636374
PABPN1Q86U425EBI-632715,EBI-1226435
PPIL1Q9Y3C64EBI-632715,EBI-2557649
RBPJQ063302EBI-632715,EBI-632552
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
THRAP3Q9Y2W14EBI-632715,EBI-352039
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

Protein-protein interaction databases

BioGridi116597. 115 interactions.
IntActiQ13573. 588 interactions.
MINTiMINT-193944.
STRINGi9606.ENSP00000261531.

Structurei

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni59 – 7921Interaction with PPIL1Add
BLAST
Regioni174 – 339166SNWAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi219 – 23315Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the SNW family.Curated

Phylogenomic databases

eggNOGiNOG295848.
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.3. human.

Polymorphism databases

DMDMi2500813.

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 .
CCDSi CCDS9867.1.
RefSeqi NP_036377.1. NM_012245.2.
UniGenei Hs.445498.

3D structure databases

DisProti DP00608.
ProteinModelPortali Q13573.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116597. 115 interactions.
IntActi Q13573. 588 interactions.
MINTi MINT-193944.
STRINGi 9606.ENSP00000261531.

PTM databases

PhosphoSitei Q13573.

Polymorphism databases

DMDMi 2500813.

Proteomic databases

MaxQBi Q13573.
PaxDbi Q13573.
PeptideAtlasi Q13573.
PRIDEi Q13573.

Protocols and materials databases

DNASUi 22938.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261531 ; ENSP00000261531 ; ENSG00000100603 .
GeneIDi 22938.
KEGGi hsa:22938.
UCSCi uc001xuf.3. human.

Organism-specific databases

CTDi 22938.
GeneCardsi GC14M078183.
HGNCi HGNC:16696. SNW1.
HPAi CAB009931.
HPA002457.
HPA017370.
MIMi 603055. gene.
neXtProti NX_Q13573.
PharmGKBi PA134883977.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG295848.
GeneTreei ENSGT00390000010423.
HOGENOMi HOG000160386.
HOVERGENi HBG047516.
InParanoidi Q13573.
KOi K06063.
PhylomeDBi Q13573.
TreeFami TF300782.

Enzyme and pathway databases

Reactomei REACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_14835. Notch-HLH transcription pathway.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
SignaLinki Q13573.

Miscellaneous databases

ChiTaRSi SNW1. human.
GeneWikii SNW1.
GenomeRNAii 22938.
NextBioi 43687.
PROi Q13573.
SOURCEi Search...

Gene expression databases

Bgeei Q13573.
CleanExi HS_SNW1.
ExpressionAtlasi Q13573. baseline and differential.
Genevestigatori Q13573.

Family and domain databases

InterProi IPR017862. SKI-int_prot_SKIP.
IPR004015. SKI-int_prot_SKIP_SNW-dom.
[Graphical view ]
PANTHERi PTHR12096. PTHR12096. 1 hit.
Pfami PF02731. SKIP_SNW. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: FUNCTION, IDENTIFICATION IN THE SNARP COMPLEX.
  28. 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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 26, 2014
This is version 142 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

External Data

Dasty 3