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Histone deacetylase complex subunit SAP18 (18 kDa Sin3-associated polypeptide) (2HOR0202) (Cell growth-inhibiting gene 38 protein) (Sin3-associated polypeptide p18)

 SAP18_HUMAN             Reviewed;         153 AA.
O00422; B2R494; Q2TTR4; Q6IAW9; Q8N606; Q9UF14;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
25-OCT-2017, entry version 161.
RecName: Full=Histone deacetylase complex subunit SAP18;
AltName: Full=18 kDa Sin3-associated polypeptide;
AltName: Full=2HOR0202;
AltName: Full=Cell growth-inhibiting gene 38 protein;
AltName: Full=Sin3-associated polypeptide p18;
Name=SAP18; ORFNames=GIG38;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH SIN3A AND
HDAC1.
PubMed=9150135; DOI=10.1016/S0092-8674(00)80216-0;
Zhang Y., Iratni R., Erdjument-Bromage H., Tempst P., Reinberg D.;
"Histone deacetylases and SAP18, a novel polypeptide, are components
of a human Sin3 complex.";
Cell 89:357-364(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Kawasaki H., Housman D.E., Graybiel A.M.;
"Characterization of proteins interacting with CAMPGEF.";
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hair follicle dermal papilla;
Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Chung H.J., Sohn M.Y.,
Hwang S.Y., Im S.U., Jung E.J., Lee H.D., Kim J.C.;
"A catalogue of genes in the human dermal papilla cells as identified
by expressed sequence tags.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim J.W.;
"Identification of a human cell growth inhibiting gene.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain cortex;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hypothalamus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
IDENTIFICATION IN THE ASAP COMPLEX, AND FUNCTION OF THE ASAP COMPLEX.
PubMed=12665594; DOI=10.1128/MCB.23.8.2981-2990.2003;
Schwerk C., Prasad J., Degenhardt K., Erdjument-Bromage H., White E.,
Tempst P., Kidd V.J., Manley J.L., Lahti J.M., Reinberg D.;
"ASAP, a novel protein complex involved in RNA processing and
apoptosis.";
Mol. Cell. Biol. 23:2981-2990(2003).
[11]
IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX,
IDENTIFICATION IN THE ASAP COMPLEX, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16314458; DOI=10.1261/rna.2155905;
Tange T.O., Shibuya T., Jurica M.S., Moore M.J.;
"Biochemical analysis of the EJC reveals two new factors and a stable
tetrameric protein core.";
RNA 11:1869-1883(2005).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RNPS1 AND ACIN1, AND
MUTAGENESIS OF ASP-118; THR-121 AND LYS-126.
PubMed=20966198; DOI=10.1261/rna.2304410;
Singh K.K., Erkelenz S., Rattay S., Dehof A.K., Hildebrandt A.,
Schulze-Osthoff K., Schaal H., Schwerk C.;
"Human SAP18 mediates assembly of a splicing regulatory multiprotein
complex via its ubiquitin-like fold.";
RNA 16:2442-2454(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
FUNCTION.
PubMed=22203037; DOI=10.1128/MCB.06130-11;
Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P.,
Durand M., Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H.,
Klinck R., Elela S.A., Prinos P., Chabot B.;
"Proteins associated with the exon junction complex also control the
alternative splicing of apoptotic regulators.";
Mol. Cell. Biol. 32:954-967(2012).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[20]
STRUCTURE BY NMR OF 6-149, AND INTERACTION WITH SUFU.
PubMed=17002296; DOI=10.1021/bi060687l;
McCallum S.A., Bazan J.F., Merchant M., Yin J., Pan B.,
de Sauvage F.J., Fairbrother W.J.;
"Structure of SAP18: a ubiquitin fold in histone deacetylase complex
assembly.";
Biochemistry 45:11974-11982(2006).
-!- FUNCTION: Component of the SIN3-repressing complex. Enhances the
ability of SIN3-HDAC1-mediated transcriptional repression. When
tethered to the promoter, it can direct the formation of a
repressive complex to core histone proteins. Auxiliary component
of the splicing-dependent multiprotein exon junction complex (EJC)
deposited at splice junction on mRNAs. The EJC is a dynamic
structure consisting of core proteins and several peripheral
nuclear and cytoplasmic associated factors that join the complex
only transiently either during EJC assembly or during subsequent
mRNA metabolism. Component of the ASAP and PSAP complexes which
bind RNA in a sequence-independent manner and are proposed to be
recruited to the EJC prior to or during the splicing process and
to regulate specific excision of introns in specific transcription
subsets. The ASAP complex can inhibit mRNA processing during in
vitro splicing reactions. The ASAP complex promotes apoptosis and
is disassembled after induction of apoptosis. Involved in the
splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic
genes); specifically inhibits the formation of proapoptotic
isoforms such as Bcl-X(S); the activity is different from the
established EJC assembly and function.
{ECO:0000269|PubMed:12665594, ECO:0000269|PubMed:20966198,
ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:9150135}.
-!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex
(EJC). Component of the heterotrimeric ASAP (apoptosis- and
splicing-associated protein) and PSAP complexes consisting of
RNPS1, SAP18 and either ACIN1 or PNN, respectively; the ASAP and
PSAP complexes probably are formed mutually exclusive. For the
ASAP complex, the association of SAP18 seems to require a
preformed RNPS1:ACIN1 complex. Forms a complex with SIN3A and
HDAC1. Interacts with SUFU. {ECO:0000269|PubMed:12665594,
ECO:0000269|PubMed:16314458, ECO:0000269|PubMed:17002296,
ECO:0000269|PubMed:20966198, ECO:0000269|PubMed:9150135}.
-!- INTERACTION:
Q13547:HDAC1; NbExp=2; IntAct=EBI-1044156, EBI-301834;
Q0VD86:INCA1; NbExp=3; IntAct=EBI-1044156, EBI-6509505;
Q9H307:PNN; NbExp=2; IntAct=EBI-1044156, EBI-681904;
Q14498:RBM39; NbExp=6; IntAct=EBI-1044156, EBI-395290;
Q14498-3:RBM39; NbExp=3; IntAct=EBI-1044156, EBI-6654703;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16314458}.
Cytoplasm {ECO:0000269|PubMed:16314458}. Nucleus speckle
{ECO:0000269|PubMed:20966198}. Note=Shuttles between the nucleus
and the cytoplasm (PubMed:16314458). Colocalizes with ACIN1 and
SRSF2 in nuclear speckles (PubMed:20966198).
{ECO:0000269|PubMed:16314458, ECO:0000269|PubMed:20966198}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- SIMILARITY: Belongs to the SAP18 family. {ECO:0000305}.
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EMBL; U96915; AAC51322.1; -; mRNA.
EMBL; U78303; AAF21220.1; -; mRNA.
EMBL; AF153608; AAD41090.1; -; mRNA.
EMBL; AY550970; AAT52216.1; -; mRNA.
EMBL; CR457035; CAG33316.1; -; mRNA.
EMBL; AK311748; BAG34691.1; -; mRNA.
EMBL; AL158032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471075; EAX08291.1; -; Genomic_DNA.
EMBL; BC030836; AAH30836.1; -; mRNA.
RefSeq; NP_005861.2; NM_005870.4.
UniGene; Hs.524899; -.
PDB; 2HDE; NMR; -; A=6-149.
PDBsum; 2HDE; -.
ProteinModelPortal; O00422; -.
SMR; O00422; -.
BioGrid; 115573; 144.
CORUM; O00422; -.
DIP; DIP-33590N; -.
IntAct; O00422; 25.
MINT; MINT-5002140; -.
STRING; 9606.ENSP00000371973; -.
TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
iPTMnet; O00422; -.
PhosphoSitePlus; O00422; -.
EPD; O00422; -.
MaxQB; O00422; -.
PaxDb; O00422; -.
PeptideAtlas; O00422; -.
PRIDE; O00422; -.
TopDownProteomics; O00422; -.
DNASU; 10284; -.
Ensembl; ENST00000607003; ENSP00000475925; ENSG00000150459.
GeneID; 10284; -.
KEGG; hsa:10284; -.
UCSC; uc058vux.1; human.
CTD; 10284; -.
EuPathDB; HostDB:ENSG00000150459.12; -.
GeneCards; SAP18; -.
H-InvDB; HIX0011163; -.
HGNC; HGNC:10530; SAP18.
HPA; CAB012273; -.
HPA; HPA011352; -.
MIM; 602949; gene.
neXtProt; NX_O00422; -.
OpenTargets; ENSG00000150459; -.
PharmGKB; PA34940; -.
eggNOG; KOG3391; Eukaryota.
eggNOG; ENOG4111FBB; LUCA.
GeneTree; ENSGT00390000003152; -.
HOGENOM; HOG000238745; -.
HOVERGEN; HBG003465; -.
InParanoid; O00422; -.
KO; K14324; -.
PhylomeDB; O00422; -.
TreeFam; TF313032; -.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
SignaLink; O00422; -.
SIGNOR; O00422; -.
ChiTaRS; SAP18; human.
EvolutionaryTrace; O00422; -.
GeneWiki; SAP18; -.
GenomeRNAi; 10284; -.
PRO; PR:O00422; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000150459; -.
CleanEx; HS_SAP18; -.
ExpressionAtlas; O00422; baseline and differential.
Genevisible; O00422; HS.
GO; GO:0061574; C:ASAP complex; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000118; C:histone deacetylase complex; TAS:ProtInc.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0004407; F:histone deacetylase activity; TAS:Reactome.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR017250; Hist_deAcase_cplx_SAP18.
InterPro; IPR010516; SAP18.
PANTHER; PTHR13082; PTHR13082; 1.
Pfam; PF06487; SAP18; 1.
PIRSF; PIRSF037637; HDAC_SAP18; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 153 Histone deacetylase complex subunit
SAP18.
/FTId=PRO_0000220975.
REGION 93 153 Involved in splicing regulation activity.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
CROSSLNK 13 13 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
MUTAGEN 118 118 D->A: Abolishes splicing regulation
activity and interaction with RNPS1 and
ACIN1; when associated with A-121.
{ECO:0000269|PubMed:20966198}.
MUTAGEN 121 121 T->A: Abolishes splicing regulation
activity and interaction with RNPS1 and
ACIN1; when associated with A-118.
{ECO:0000269|PubMed:20966198}.
MUTAGEN 126 126 K->A: No effect on splicing regulation
activity. {ECO:0000269|PubMed:20966198}.
CONFLICT 114 114 K -> E (in Ref. 2; AAF21220).
{ECO:0000305}.
CONFLICT 146 146 P -> T (in Ref. 9; AAH30836).
{ECO:0000305}.
TURN 22 24 {ECO:0000244|PDB:2HDE}.
STRAND 28 37 {ECO:0000244|PDB:2HDE}.
HELIX 43 45 {ECO:0000244|PDB:2HDE}.
TURN 52 54 {ECO:0000244|PDB:2HDE}.
STRAND 55 60 {ECO:0000244|PDB:2HDE}.
HELIX 66 76 {ECO:0000244|PDB:2HDE}.
HELIX 78 81 {ECO:0000244|PDB:2HDE}.
STRAND 86 91 {ECO:0000244|PDB:2HDE}.
STRAND 95 98 {ECO:0000244|PDB:2HDE}.
STRAND 104 112 {ECO:0000244|PDB:2HDE}.
HELIX 122 125 {ECO:0000244|PDB:2HDE}.
STRAND 132 138 {ECO:0000244|PDB:2HDE}.
STRAND 144 147 {ECO:0000244|PDB:2HDE}.
SEQUENCE 153 AA; 17561 MW; C7E479FFE9CA5774 CRC64;
MAVESRVTQE EIKKEPEKPI DREKTCPLLL RVFTTNNGRH HRMDEFSRGN VPSSELQIYT
WMDATLKELT SLVKEVYPEA RKKGTHFNFA IVFTDVKRPG YRVKEIGSTM SGRKGTDDSM
TLQSQKFQIG DYLDIAITPP NRAPPPSGRM RPY


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EIAAB37269 18 kDa Sin3-associated polypeptide,Bos taurus,Bovine,Histone deacetylase complex subunit SAP18,SAP18,Sin3-associated polypeptide p18
EIAAB37271 18 kDa Sin3-associated polypeptide,Histone deacetylase complex subunit SAP18,Mouse,Mus musculus,Sap18,Sin3-associated polypeptide p18
18-783-78579 GOAT ANTI RBP1-LIKE PROTEIN - ARID domain-containing protein 4B; Histone deacetylase complex subunit SAP180; 180 kDa Sin3-associated polypeptide; Sin3-associated polypeptide p180; Retinoblastoma-bindi 0.1 mg
EIAAB37277 30 kDa Sin3-associated polypeptide,Histone deacetylase complex subunit SAP30,Homo sapiens,Human,SAP30,Sin3 corepressor complex subunit SAP30,Sin3-associated polypeptide p30
EIAAB37276 30 kDa Sin3-associated polypeptide,Histone deacetylase complex subunit SAP30,Mouse,Mus musculus,Sap30,Sin3 corepressor complex subunit SAP30,Sin3-associated polypeptide p30
EIAAB39316 130 kDa Sin3-associated polypeptide,Histone deacetylase complex subunit SAP130,Homo sapiens,Human,SAP130,Sin3-associated polypeptide p130
EIAAB39317 130 kDa Sin3-associated polypeptide,Histone deacetylase complex subunit SAP130,Mouse,Mus musculus,Sap130,Sin3-associated polypeptide p130
EIAAB37273 25 kDa Sin3-associated polypeptide,Histone deacetylase complex subunit SAP25,Mouse,mSin3A-binding protein,Mus musculus,Sap25,Sin3 corepressor complex subunit SAP25
EIAAB39315 130 kDa Sin3-associated polypeptide,Chicken,Gallus gallus,Histone deacetylase complex subunit SAP130,RCJMB04_7d5,SAP130,Sin3-associated polypeptide p130
18-003-43340 Histone deacetylase complex subunit SAP30 - Sin3-associated polypeptide. 30 kDa; Sin3 corepressor complex subunit SAP30 Polyclonal 0.1 mg Protein A
EIAAB37272 25 kDa Sin3-associated polypeptide,Histone deacetylase complex subunit SAP25,Homo sapiens,Human,SAP25,Sin3 corepressor complex subunit SAP25
EIAAB37751 45 kDa Sin3-associated polypeptide,Homo sapiens,Human,SAP45,SDS3,Sin3 histone deacetylase corepressor complex component SDS3,SUDS3,Suppressor of defective silencing 3 protein homolog
EIAAB39327 Histone deacetylase complex subunit SAP30L,Mouse,Mus musculus,Sap30l,Sin3 corepressor complex subunit SAP30L,Sin3-associated protein p30-like
EIAAB39326 HCV non-structural protein 4A-transactivated protein 2,Histone deacetylase complex subunit SAP30L,Homo sapiens,Human,NS4ATP2,SAP30L,Sin3 corepressor complex subunit SAP30L,Sin3-associated protein p30-
18-272-196233 SAP30 - Rabbit polyclonal to SAP30; Sin3-associated polypeptide. 30 kDa; Sin3 corepressor complex subunit SAP30 Polyclonal 0.05 mg
18-272-196234 SAP30 - Rabbit polyclonal to SAP30; Sin3-associated polypeptide. 30 kDa; Sin3 corepressor complex subunit SAP30 Polyclonal 0.1 mg
SDS3_MOUSE ELISA Kit FOR Sin3 histone deacetylase corepressor complex component SDS3; organism: Mouse; gene name: Suds3 96T
SAP18_MOUSE ELISA Kit FOR Histone deacetylase complex subunit SAP18; organism: Mouse; gene name: Sap18 96T
CSB-EL022922MO Mouse Sin3 histone deacetylase corepressor complex component SDS3(SUDS3) ELISA kit 96T
H0981 Sin3 histone deacetylase corepressor complex component SDS3 (SUDS3), Human, ELISA Kit 96T
H0982 Sin3 histone deacetylase corepressor complex component SDS3 (SUDS3), Mouse, ELISA Kit 96T
CSB-EL022922BO Bovine Sin3 histone deacetylase corepressor complex component SDS3(SUDS3) ELISA kit 96T
CSB-EL022922HU Human Sin3 histone deacetylase corepressor complex component SDS3(SUDS3) ELISA kit 96T


 

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