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Remodeling and spacing factor 1 (Rsf-1) (HBV pX-associated protein 8) (Hepatitis B virus X-associated protein) (p325 subunit of RSF chromatin-remodeling complex)

 RSF1_HUMAN              Reviewed;        1441 AA.
Q96T23; Q86X86; Q9H3L8; Q9NVZ8; Q9NYU0;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
07-JUL-2009, sequence version 2.
18-JUL-2018, entry version 154.
RecName: Full=Remodeling and spacing factor 1;
Short=Rsf-1;
AltName: Full=HBV pX-associated protein 8;
AltName: Full=Hepatitis B virus X-associated protein;
AltName: Full=p325 subunit of RSF chromatin-remodeling complex;
Name=RSF1; Synonyms=HBXAP, XAP8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF
4-1441 (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH PX OF HBV, AND
SUBCELLULAR LOCATION.
PubMed=11944984; DOI=10.1006/geno.2002.6717;
Shamay M., Barak O., Shaul Y.;
"HBXAP, a novel PHD-finger protein, possesses transcription repression
activity.";
Genomics 79:523-529(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH PX OF HBV,
SUBCELLULAR LOCATION, AND FUNCTION.
TISSUE=Spleen;
PubMed=11788598; DOI=10.1074/jbc.M111354200;
Shamay M., Barak O., Doitsh G., Ben-Dor I., Shaul Y.;
"Hepatitis B virus pX interacts with HBXAP, a PHD finger protein to
coactivate transcription.";
J. Biol. Chem. 277:9982-9988(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 111-703.
TISSUE=Brain;
Mao Y.M., Xie Y., Zheng Z.H.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 200-1002.
TISSUE=Lymph;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 494-1068.
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]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=12972596; DOI=10.1128/MCB.23.19.6759-6768.2003;
Loyola A., Huang J.-Y., LeRoy G., Hu S., Wang Y.-H., Donnelly R.J.,
Lane W.S., Lee S.-C., Reinberg D.;
"Functional analysis of the subunits of the chromatin assembly factor
RSF.";
Mol. Cell. Biol. 23:6759-6768(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-604; SER-622;
SER-1096; SER-1098; SER-1105; SER-1345; SER-1359 AND SER-1375, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1345, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524 AND SER-1325, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-622; SER-629; SER-1221;
SER-1223; SER-1226; SER-1277; THR-1278; THR-1305 AND SER-1359, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1305; SER-1345; SER-1359
AND SER-1375, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1050 AND LYS-1339, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-397; SER-473;
SER-604; SER-748; SER-882; SER-1345; SER-1359 AND SER-1375, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-397; SER-604;
SER-748; SER-1221; SER-1226; SER-1258; THR-1305; SER-1345 AND
SER-1375, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; SER-397; SER-429;
SER-473; SER-570; SER-604; SER-622; SER-748; THR-1305; SER-1336;
SER-1345; SER-1359 AND SER-1375, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604; THR-628; SER-629;
THR-1305 AND SER-1345, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-254; LYS-277; LYS-294;
LYS-309; LYS-323; LYS-337; LYS-390; LYS-419; LYS-456; LYS-468;
LYS-663; LYS-670; LYS-677; LYS-758 AND LYS-768, 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).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-277 AND LYS-456, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-254; LYS-277; LYS-284;
LYS-294; LYS-309; LYS-323; LYS-419; LYS-456; LYS-670 AND LYS-768, 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).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-243; LYS-254; LYS-277;
LYS-284; LYS-294; LYS-309; LYS-323; LYS-390; LYS-415; LYS-419;
LYS-456; LYS-670 AND LYS-758, 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).
[23]
SUBUNIT.
PubMed=27499292; DOI=10.1016/j.molcel.2016.06.023;
Roulland Y., Ouararhni K., Naidenov M., Ramos L., Shuaib M.,
Syed S.H., Lone I.N., Boopathi R., Fontaine E., Papai G.,
Tachiwana H., Gautier T., Skoufias D., Padmanabhan K., Bednar J.,
Kurumizaka H., Schultz P., Angelov D., Hamiche A., Dimitrov S.;
"The flexible ends of CENP-A nucleosome are required for mitotic
fidelity.";
Mol. Cell 63:674-685(2016).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-136; LYS-215; LYS-236;
LYS-243; LYS-248; LYS-252; LYS-254; LYS-277; LYS-284; LYS-288;
LYS-294; LYS-305; LYS-306; LYS-309; LYS-323; LYS-327; LYS-337;
LYS-342; LYS-358; LYS-373; LYS-381; LYS-390; LYS-400; LYS-405;
LYS-415; LYS-419; LYS-439; LYS-456; LYS-463; LYS-468; LYS-498;
LYS-565; LYS-662; LYS-663; LYS-670; LYS-677; LYS-698; LYS-709;
LYS-758; LYS-768; LYS-795; LYS-799 AND LYS-1039, 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).
-!- FUNCTION: Required for assembly of regular nucleosome arrays by
the RSF chromatin-remodeling complex (PubMed:12972596).
Facilitates transcription of hepatitis B virus (HBV) genes by the
pX transcription activator. In case of infection by HBV, together
with pX, it represses TNF-alpha induced NF-kappa-B transcription
activation. Represses transcription when artificially recruited to
chromatin by fusion to a heterogeneous DNA binding domain
(PubMed:11944984, PubMed:11788598). {ECO:0000269|PubMed:11788598,
ECO:0000269|PubMed:11944984, ECO:0000269|PubMed:12972596}.
-!- SUBUNIT: Interacts with SMARCA5/SNF2H to form the RSF complex
(PubMed:12972596). Identified in a centromere complex containing
histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT,
CENPN, HJURP, SUPT16H, SSRP1 and RSF1 (PubMed:27499292). Also
binds the HBV pX/HBx protein, which is required to activate
transcription of the viral genome (PubMed:11944984,
PubMed:11788598). {ECO:0000269|PubMed:11788598,
ECO:0000269|PubMed:11944984, ECO:0000269|PubMed:27499292}.
-!- INTERACTION:
O60264:SMARCA5; NbExp=5; IntAct=EBI-926768, EBI-352588;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11788598,
ECO:0000269|PubMed:11944984, ECO:0000269|PubMed:12972596}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=1; Synonyms=Alpha, XAP8alpha;
IsoId=Q96T23-1; Sequence=Displayed;
Name=2; Synonyms=Beta;
IsoId=Q96T23-2; Sequence=VSP_012500;
Name=3; Synonyms=Gamma;
IsoId=Q96T23-3; Sequence=VSP_012499;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
-!- SEQUENCE CAUTION:
Sequence=AAG43114.1; Type=Frameshift; Positions=549; Evidence={ECO:0000305};
Sequence=AAH46124.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAK57515.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA91591.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RSF1ID44107ch11q13.html";
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EMBL; AF380176; AAK57515.1; ALT_INIT; mRNA.
EMBL; AF227948; AAF61709.2; -; mRNA.
EMBL; AP000580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF059317; AAG43114.1; ALT_SEQ; mRNA.
EMBL; BC046124; AAH46124.2; ALT_SEQ; mRNA.
EMBL; AK001268; BAA91591.1; ALT_INIT; mRNA.
CCDS; CCDS8253.1; -. [Q96T23-1]
RefSeq; NP_057662.3; NM_016578.3. [Q96T23-1]
UniGene; Hs.420229; -.
UniGene; Hs.593415; -.
ProteinModelPortal; Q96T23; -.
BioGrid; 119724; 22.
ComplexPortal; CPX-455; RSF complex.
CORUM; Q96T23; -.
IntAct; Q96T23; 30.
MINT; Q96T23; -.
STRING; 9606.ENSP00000311513; -.
iPTMnet; Q96T23; -.
PhosphoSitePlus; Q96T23; -.
BioMuta; RSF1; -.
DMDM; 251757329; -.
EPD; Q96T23; -.
MaxQB; Q96T23; -.
PaxDb; Q96T23; -.
PeptideAtlas; Q96T23; -.
PRIDE; Q96T23; -.
ProteomicsDB; 78175; -.
ProteomicsDB; 78176; -. [Q96T23-2]
ProteomicsDB; 78177; -. [Q96T23-3]
DNASU; 51773; -.
Ensembl; ENST00000308488; ENSP00000311513; ENSG00000048649. [Q96T23-1]
Ensembl; ENST00000480887; ENSP00000434509; ENSG00000048649. [Q96T23-3]
GeneID; 51773; -.
KEGG; hsa:51773; -.
UCSC; uc001oym.4; human. [Q96T23-1]
CTD; 51773; -.
DisGeNET; 51773; -.
EuPathDB; HostDB:ENSG00000048649.13; -.
GeneCards; RSF1; -.
H-InvDB; HIX0022742; -.
HGNC; HGNC:18118; RSF1.
HPA; CAB022626; -.
HPA; HPA046129; -.
HPA; HPA057547; -.
HPA; HPA064567; -.
MIM; 608522; gene.
neXtProt; NX_Q96T23; -.
OpenTargets; ENSG00000048649; -.
PharmGKB; PA29210; -.
eggNOG; ENOG410IFYI; Eukaryota.
eggNOG; ENOG410YTDT; LUCA.
GeneTree; ENSGT00530000064411; -.
HOGENOM; HOG000154205; -.
HOVERGEN; HBG105728; -.
InParanoid; Q96T23; -.
KO; K11657; -.
OMA; QINYKED; -.
OrthoDB; EOG091G02DZ; -.
PhylomeDB; Q96T23; -.
TreeFam; TF106405; -.
Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
ChiTaRS; RSF1; human.
GeneWiki; RSF1; -.
GenomeRNAi; 51773; -.
PRO; PR:Q96T23; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000048649; -.
CleanEx; HS_RSF1; -.
ExpressionAtlas; Q96T23; baseline and differential.
Genevisible; Q96T23; HS.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0031213; C:RSF complex; IPI:UniProtKB.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0034080; P:CENP-A containing nucleosome assembly; TAS:Reactome.
GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB.
GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
GO; GO:0016584; P:nucleosome positioning; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0050434; P:positive regulation of viral transcription; IDA:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR028938; Rsf-1.
InterPro; IPR028942; WHIM1_dom.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR10615:SF156; PTHR10615:SF156; 1.
Pfam; PF00628; PHD; 1.
Pfam; PF15612; WHIM1; 1.
SMART; SM00249; PHD; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Chromatin regulator; Coiled coil;
Complete proteome; Isopeptide bond; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1441 Remodeling and spacing factor 1.
/FTId=PRO_0000059326.
DOMAIN 17 84 DDT.
ZN_FING 891 941 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
COILED 942 1012 {ECO:0000255}.
COMPBIAS 226 372 Glu-rich.
COMPBIAS 875 884 Poly-Glu.
COMPBIAS 1080 1083 Poly-Ala.
COMPBIAS 1146 1243 Arg-rich.
COMPBIAS 1286 1292 Poly-Glu.
COMPBIAS 1419 1424 Poly-Glu.
MOD_RES 227 227 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 392 392 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 429 429 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 473 473 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 604 604 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 622 622 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 628 628 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 629 629 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 748 748 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 882 882 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1050 1050 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1096 1096 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 1098 1098 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 1105 1105 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 1221 1221 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 1223 1223 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1226 1226 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 1258 1258 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1277 1277 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1278 1278 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1305 1305 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1325 1325 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 1336 1336 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1339 1339 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1345 1345 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1359 1359 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1375 1375 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 136 136 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 215 215 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 236 236 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 243 243 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 248 248 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 252 252 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 254 254 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}.
CROSSLNK 277 277 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 277 277 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 284 284 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 288 288 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 294 294 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}.
CROSSLNK 305 305 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 306 306 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 309 309 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}.
CROSSLNK 323 323 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}.
CROSSLNK 327 327 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 337 337 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 342 342 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 358 358 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 373 373 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 381 381 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 390 390 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 400 400 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 405 405 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 415 415 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 419 419 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}.
CROSSLNK 439 439 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 456 456 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 456 456 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 463 463 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 468 468 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 498 498 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 565 565 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 662 662 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 663 663 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 670 670 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}.
CROSSLNK 677 677 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 698 698 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 709 709 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 758 758 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 768 768 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 795 795 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 799 799 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1039 1039 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 252 Missing (in isoform 3).
{ECO:0000303|PubMed:11788598,
ECO:0000303|PubMed:11944984}.
/FTId=VSP_012499.
VAR_SEQ 93 123 Missing (in isoform 2).
{ECO:0000303|PubMed:11944984}.
/FTId=VSP_012500.
VARIANT 304 304 E -> D (in dbSNP:rs58758035).
/FTId=VAR_061741.
VARIANT 475 475 S -> P (in dbSNP:rs7950873).
/FTId=VAR_020885.
CONFLICT 132 132 D -> G (in Ref. 4; AAG43114).
{ECO:0000305}.
CONFLICT 270 270 V -> G (in Ref. 4; AAG43114).
{ECO:0000305}.
CONFLICT 276 276 V -> G (in Ref. 4; AAG43114).
{ECO:0000305}.
CONFLICT 287 287 V -> A (in Ref. 4; AAG43114).
{ECO:0000305}.
CONFLICT 291 291 V -> G (in Ref. 4; AAG43114).
{ECO:0000305}.
CONFLICT 305 305 K -> N (in Ref. 4; AAG43114).
{ECO:0000305}.
CONFLICT 314 315 SF -> PS (in Ref. 4; AAG43114).
{ECO:0000305}.
CONFLICT 353 353 F -> L (in Ref. 4; AAG43114).
{ECO:0000305}.
CONFLICT 381 381 K -> E (in Ref. 4; AAG43114).
{ECO:0000305}.
CONFLICT 1063 1063 I -> V (in Ref. 6; BAA91591).
{ECO:0000305}.
CONFLICT 1137 1137 D -> E (in Ref. 1; AAK57515 and 2;
AAF61709). {ECO:0000305}.
SEQUENCE 1441 AA; 163821 MW; 0FCB9499B5097A2F CRC64;
MATAAAAAAV MAPPGCPGSC PNFAVVCSFL ERYGPLLDLP ELPFPELERV LQAPPPDVGN
GEVPKELVEL HLKLMRKIGK SVTADRWEKY LIKICQEFNS TWAWEMEKKG YLEMSVECKL
ALLKYLCECQ FDDNLKFKNI INEEDADTMR LQPIGRDKDG LMYWYQLDQD HNVRMYIEEQ
DDQDGSSWKC IVRNRNELAE TLALLKAQID PVLLKNSSQQ DNSSRESPSL EDEETKKEEE
TPKQEEQKES EKMKSEEQPM DLENRSTANV LEETTVKKEK EDEKELVKLP VIVKLEKPLP
ENEEKKIIKE ESDSFKENVK PIKVEVKECR ADPKDTKSSM EKPVAQEPER IEFGGNIKSS
HEITEKSTEE TEKLKNDQQA KIPLKKREIK LSDDFDSPVK GPLCKSVTPT KEFLKDEIKQ
EEETCKRIST ITALGHEGKQ LVNGEVSDER VAPNFKTEPI ETKFYETKEE SYSPSKDRNI
ITEGNGTESL NSVITSMKTG ELEKETAPLR KDADSSISVL EIHSQKAQIE EPDPPEMETS
LDSSEMAKDL SSKTALSSTE SCTMKGEEKS PKTKKDKRPP ILECLEKLEK SKKTFLDKDA
QRLSPIPEEV PKSTLESEKP GSPEAAETSP PSNIIDHCEK LASEKEVVEC QSTSTVGGQS
VKKVDLETLK EDSEFTKVEM DNLDNAQTSG IEEPSETKGS MQKSKFKYKL VPEEETTASE
NTEITSERQK EGIKLTIRIS SRKKKPDSPP KVLEPENKQE KTEKEEEKTN VGRTLRRSPR
ISRPTAKVAE IRDQKADKKR GEGEDEVEEE STALQKTDKK EILKKSEKDT NSKVSKVKPK
GKVRWTGSRT RGRWKYSSND ESEGSGSEKS SAASEEEEEK ESEEAILADD DEPCKKCGLP
NHPELILLCD SCDSGYHTAC LRPPLMIIPD GEWFCPPCQH KLLCEKLEEQ LQDLDVALKK
KERAERRKER LVYVGISIEN IIPPQEPDFS EDQEEKKKDS KKSKANLLER RSTRTRKCIS
YRFDEFDEAI DEAIEDDIKE ADGGGVGRGK DISTITGHRG KDISTILDEE RKENKRPQRA
AAARRKKRRR LNDLDSDSNL DEEESEDEFK ISDGSQDEFV VSDENPDESE EDPPSNDDSD
TDFCSRRLRR HPSRPMRQSR RLRRKTPKKK YSDDDEEEES EENSRDSESD FSDDFSDDFV
ETRRRRSRRN QKRQINYKED SESDGSQKSL RRGKEIRRVH KRRLSSSESE ESYLSKNSED
DELAKESKRS VRKRGRSTDE YSEADEEEEE EEGKPSRKRL HRIETDEEES CDNAHGDANQ
PARDSQPRVL PSEQESTKKP YRIESDEEED FENVGKVGSP LDYSLVDLPS TNGQSPGKAI
ENLIGKPTEK SQTPKDNSTA SASLASNGTS GGQEAGAPEE EEDELLRVTD LVDYVCNSEQ
L


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