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Splicing factor, suppressor of white-apricot homolog (Splicing factor, arginine/serine-rich 8) (Suppressor of white apricot protein homolog)

 SFSWA_HUMAN             Reviewed;         951 AA.
Q12872; B2RN45; B7ZM97; F5H6B8; Q6PJF7;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
23-MAR-2010, sequence version 3.
18-JUL-2018, entry version 158.
RecName: Full=Splicing factor, suppressor of white-apricot homolog;
AltName: Full=Splicing factor, arginine/serine-rich 8;
AltName: Full=Suppressor of white apricot protein homolog;
Name=SFSWAP; Synonyms=SFRS8, SWAP;
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 1), AND VARIANTS GLN-52; PHE-136
AND PRO-421.
TISSUE=Placenta;
PubMed=8206918;
Denhez F., Lafyatis R.;
"Conservation of regulated alternative splicing and identification of
functional domains in vertebrate homologs to the Drosophila splicing
regulator, suppressor-of-white-apricot.";
J. Biol. Chem. 269:16170-16179(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-421.
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
PRO-421.
TISSUE=Brain, and Skin;
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).
[5]
FUNCTION.
PubMed=8940107; DOI=10.1074/jbc.271.49.31106;
Sarkissian M., Winne A., Lafyatis R.;
"The mammalian homolog of suppressor-of-white-apricot regulates
alternative mRNA splicing of CD45 exon 4 and fibronectin IIICS.";
J. Biol. Chem. 271:31106-31114(1996).
[6]
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-642, 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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-604 AND
SER-909, 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).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-909, 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).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-315, 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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-832; SER-834
AND SER-909, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, 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).
[16]
STRUCTURE BY NMR OF 189-282 AND 434-522.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SURP1 and SURP2 domain in splicing factor,
arginine/serine-rich 8.";
Submitted (JUN-2007) to the PDB data bank.
-!- FUNCTION: Plays a role as an alternative splicing regulator.
Regulate its own expression at the level of RNA processing. Also
regulates the splicing of fibronectin and CD45 genes. May act, at
least in part, by interaction with other R/S-containing splicing
factors. Represses the splicing of MAPT/Tau exon 10.
{ECO:0000269|PubMed:8940107}.
-!- INTERACTION:
Q15637:SF1; NbExp=2; IntAct=EBI-1055938, EBI-744603;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q12872-1; Sequence=Displayed;
Name=2;
IsoId=Q12872-2; Sequence=VSP_044786;
Note=No experimental confirmation available.;
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EMBL; U08377; AAA19604.1; -; mRNA.
EMBL; AC117500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC131009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW98526.1; -; Genomic_DNA.
EMBL; BC008707; AAH08707.1; -; mRNA.
EMBL; BC015953; AAH15953.1; -; mRNA.
EMBL; BC136678; AAI36679.1; -; mRNA.
EMBL; BC144364; AAI44365.1; -; mRNA.
CCDS; CCDS58290.1; -. [Q12872-2]
CCDS; CCDS9273.1; -. [Q12872-1]
PIR; A54037; A54037.
PIR; B54037; B54037.
PIR; C54037; C54037.
RefSeq; NP_001248340.1; NM_001261411.1. [Q12872-2]
RefSeq; NP_004583.2; NM_004592.3. [Q12872-1]
UniGene; Hs.308171; -.
PDB; 2E5Z; NMR; -; A=440-522.
PDB; 2E60; NMR; -; A=189-282.
PDBsum; 2E5Z; -.
PDBsum; 2E60; -.
ProteinModelPortal; Q12872; -.
SMR; Q12872; -.
BioGrid; 112331; 24.
IntAct; Q12872; 9.
MINT; Q12872; -.
STRING; 9606.ENSP00000261674; -.
iPTMnet; Q12872; -.
PhosphoSitePlus; Q12872; -.
BioMuta; SFSWAP; -.
DMDM; 292495067; -.
EPD; Q12872; -.
MaxQB; Q12872; -.
PaxDb; Q12872; -.
PeptideAtlas; Q12872; -.
PRIDE; Q12872; -.
ProteomicsDB; 58994; -.
Ensembl; ENST00000261674; ENSP00000261674; ENSG00000061936. [Q12872-1]
Ensembl; ENST00000541286; ENSP00000437738; ENSG00000061936. [Q12872-2]
GeneID; 6433; -.
KEGG; hsa:6433; -.
UCSC; uc001uja.3; human. [Q12872-1]
CTD; 6433; -.
DisGeNET; 6433; -.
EuPathDB; HostDB:ENSG00000061936.9; -.
GeneCards; SFSWAP; -.
H-InvDB; HIX0036782; -.
HGNC; HGNC:10790; SFSWAP.
HPA; HPA039362; -.
HPA; HPA040063; -.
MIM; 601945; gene.
neXtProt; NX_Q12872; -.
OpenTargets; ENSG00000061936; -.
PharmGKB; PA35706; -.
eggNOG; KOG1847; Eukaryota.
eggNOG; ENOG410ZQGI; LUCA.
GeneTree; ENSGT00730000111096; -.
HOVERGEN; HBG079184; -.
InParanoid; Q12872; -.
OMA; MYYSYYM; -.
OrthoDB; EOG091G09RJ; -.
PhylomeDB; Q12872; -.
TreeFam; TF106264; -.
ChiTaRS; SFSWAP; human.
EvolutionaryTrace; Q12872; -.
GenomeRNAi; 6433; -.
PRO; PR:Q12872; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000061936; -.
CleanEx; HS_SFRS8; -.
ExpressionAtlas; Q12872; baseline and differential.
Genevisible; Q12872; HS.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IEA:Ensembl.
GO; GO:0000395; P:mRNA 5'-splice site recognition; IBA:GO_Central.
GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.10.790; -; 2.
InterPro; IPR000061; Surp.
InterPro; IPR035967; SWAP/Surp_sf.
InterPro; IPR019147; SWAP_N_domain.
Pfam; PF09750; DRY_EERY; 1.
Pfam; PF01805; Surp; 2.
SMART; SM01141; DRY_EERY; 1.
SMART; SM00648; SWAP; 2.
SUPFAM; SSF109905; SSF109905; 2.
PROSITE; PS50128; SURP; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Repressor; RNA-binding; Transcription;
Transcription regulation.
CHAIN 1 951 Splicing factor, suppressor of white-
apricot homolog.
/FTId=PRO_0000081934.
REPEAT 211 253 SURP motif 1.
REPEAT 459 499 SURP motif 2.
COMPBIAS 165 168 Poly-Glu.
COMPBIAS 287 290 Poly-Asp.
COMPBIAS 382 385 Poly-Pro.
COMPBIAS 413 416 Poly-Pro.
COMPBIAS 420 424 Poly-Pro.
COMPBIAS 434 440 Poly-Thr.
COMPBIAS 451 454 Poly-Pro.
COMPBIAS 616 619 Poly-Ser.
COMPBIAS 660 663 Poly-Ala.
COMPBIAS 754 763 Poly-Lys.
COMPBIAS 789 951 Arg/Ser-rich (RS domain).
COMPBIAS 850 853 Poly-Lys.
MOD_RES 283 283 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 315 315 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 604 604 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 642 642 Phosphothreonine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 832 832 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 834 834 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 905 905 Phosphoserine.
{ECO:0000250|UniProtKB:Q3USH5}.
MOD_RES 909 909 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 801 801 R -> RSRVTASPGTLRAEPCQSSASVTAAAEPGSYQAAST
TTRFDSASSFEGKPGKT (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044786.
VARIANT 52 52 L -> Q (in dbSNP:rs1051207).
{ECO:0000269|PubMed:8206918}.
/FTId=VAR_046442.
VARIANT 122 122 L -> F (in dbSNP:rs1051314).
/FTId=VAR_046443.
VARIANT 136 136 L -> F (in dbSNP:rs1131564).
{ECO:0000269|PubMed:8206918}.
/FTId=VAR_046444.
VARIANT 421 421 L -> P (in dbSNP:rs1982528).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8206918,
ECO:0000269|Ref.3}.
/FTId=VAR_021789.
VARIANT 512 512 G -> S (in dbSNP:rs34541796).
/FTId=VAR_057248.
VARIANT 538 538 E -> G (in dbSNP:rs34744641).
/FTId=VAR_057249.
VARIANT 887 887 A -> E (in dbSNP:rs34729193).
/FTId=VAR_057250.
CONFLICT 236 236 R -> P (in Ref. 1; AAA19604).
{ECO:0000305}.
CONFLICT 493 493 H -> Y (in Ref. 1; AAA19604).
{ECO:0000305}.
STRAND 192 194 {ECO:0000244|PDB:2E60}.
STRAND 198 200 {ECO:0000244|PDB:2E60}.
HELIX 206 221 {ECO:0000244|PDB:2E60}.
HELIX 224 233 {ECO:0000244|PDB:2E60}.
HELIX 241 243 {ECO:0000244|PDB:2E60}.
HELIX 249 262 {ECO:0000244|PDB:2E60}.
TURN 454 456 {ECO:0000244|PDB:2E5Z}.
HELIX 457 469 {ECO:0000244|PDB:2E5Z}.
HELIX 472 481 {ECO:0000244|PDB:2E5Z}.
HELIX 484 486 {ECO:0000244|PDB:2E5Z}.
STRAND 490 492 {ECO:0000244|PDB:2E5Z}.
HELIX 496 509 {ECO:0000244|PDB:2E5Z}.
SEQUENCE 951 AA; 104822 MW; A942D589F4B6BF47 CRC64;
MYGASGGRAK PERKSGAKEE AGPGGAGGGG SRVELLVFGY ACKLFRDDER ALAQEQGQHL
IPWMGDHKIL IDRYDGRGHL HDLSEYDAEY STWNRDYQLS EEEARIEALC DEERYLALHT
DLLEEEARQE EEYKRLSEAL AEDGSYNAVG FTYGSDYYDP SEPTEEEEPS KQREKNEAEN
LEENEEPFVA PLGLSVPSDV ELPPTAKMHA IIERTASFVC RQGAQFEIML KAKQARNSQF
DFLRFDHYLN PYYKFIQKAM KEGRYTVLAE NKSDEKKKSG VSSDNEDDDD EEDGNYLHPS
LFASKKCNRL EELMKPLKVV DPDHPLAALV RKAQADSSTP TPHNADGAPV QPSQVEYTAD
STVAAMYYSY YMLPDGTYCL APPPPGIDVT TYYSTLPAGV TVSNSPGVTT TAPPPPGTTP
LPPPTTAETS SGATSTTTTT SALAPVAAII PPPPDVQPVI DKLAEYVARN GLKFETSVRA
KNDQRFEFLQ PWHQYNAYYE FKKQFFLQKE GGDSMQAVSA PEEAPTDSAP EKPSDAGEDG
APEDAAEVGA RAGSGGKKEA SSSKTVPDGK LVKASFAPIS FAIKAKENDL LPLEKNRVKL
DDDSDDDEES KEGQESSSSA ANTNPAVAPP CVVVEEKKPQ LTQEELEAKQ AKQKLEDRLA
AAAREKLAQA SKESKEKQLQ AERKRKAALF LQTLKNPLPE AEAGKIEESP FSVEESSTTP
CPLLTGGRPL PTLEVKPPDR PSSKSKDPPR EEEKEKKKKK HKKRSRTRSR SPKYHSSSKS
RSRSHSKAKH SLPSAYRTVR RSRSRSRSPR RRAHSPERRR EERSVPTAYR VSRSPGASRK
RTRSRSPHEK KKKRRSRSRT KSKARSQSVS PSKQAAPRPA APAAHSAHSA SVSPVESRGS
SQERSRGVSQ EKEAQISSAI VSSVQSKITQ DLMAKVRAML AASKNLQTSA S


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SFSWA_MOUSE ELISA Kit FOR Splicing factor, suppressor of white-apricot homolog; organism: Mouse; gene name: Sfswap 96T
CSB-EL021160HU Human splicing factor, arginine_serine-rich 8 (suppressor-of-white-apricot homolog, Drosophila) (SFRS8) ELISA kit, Species Human, Sample Type serum, plasma 96T
EIAAB39954 40 kDa SR-repressor protein,FUS-interacting serine-arginine-rich protein 1,FUSIP1,FUSIP2,Homo sapiens,Human,Serine_arginine-rich splicing factor 10,SFRS13A,Splicing factor SRp38,Splicing factor, argin
EIAAB38025 Homo sapiens,Human,SCAF,SCAF1,Serine arginine-rich pre-mRNA splicing factor SR-A1,SFRS19,Splicing factor, arginine_serine-rich 19,SRA1,SR-A1,SR-related and CTD-associated factor 1,SR-related-CTD-assoc
GWB-D07755 Anti- SFRS10 (splicing factor. arginine serine-rich 10 (transformer 2 homolog. Drosophila)) Antibody
GWB-7F7D04 Anti- SFRS10 (splicing factor. arginine serine-rich 10 (transformer 2 homolog. Drosophila)) Antibody
PR-774 ASF per SF2 (SFRS1 or SRp30a)His Splicing Factor, Arginine per Serine-rich 1, Pre-mRNA Splicing Factor human, recombinant, E. coli 10
PR-775 ASF per SF2 (SFRS1 or SRp30a)His Splicing Factor, Arginine per Serine-rich 1, Pre-mRNA Splicing Factor human, recombinant, Sf9 insect cells 5
EIAAB39967 Homo sapiens,Human,Protein PR264,SC-35,Serine_arginine-rich splicing factor 2,SFRS2,Splicing component, 35 kDa,Splicing factor SC35,Splicing factor, arginine_serine-rich 2,SRSF2
EIAAB39955 Arginine-rich 54 kDa nuclear protein,Homo sapiens,Human,p54,Serine_arginine-rich splicing factor 11,SFRS11,Splicing factor, arginine_serine-rich 11,SRSF11
EIAAB39966 Chicken,Gallus gallus,Protein PR264,SC-35,Serine_arginine-rich splicing factor 2,SFRS2,Splicing component, 35 kDa,Splicing factor SC35,Splicing factor, arginine_serine-rich 2,SRSF2
EIAAB39968 Bos taurus,Bovine,SC-35,Serine_arginine-rich splicing factor 2,SFRS2,Splicing component, 35 kDa,Splicing factor SC35,Splicing factor, arginine_serine-rich 2,SRSF2
EIAAB39965 Rat,Rattus norvegicus,SC-35,Serine_arginine-rich splicing factor 2,Sfrs2,Splicing component, 35 kDa,Splicing factor SC35,Splicing factor, arginine_serine-rich 2,Srsf2
EIAAB39962 Alternative-splicing factor 1,ASF,ASF-1,Homo sapiens,Human,OK_SW-cl.3,pre-mRNA-splicing factor SF2, P33 subunit,Serine_arginine-rich splicing factor 1,SF2,SF2P33,SFRS1,Splicing factor, arginine_serine
EIAAB39976 Delayed-early protein HRS,Hrs,Mouse,Mus musculus,Pre-mRNA-splicing factor SRP40,Serine_arginine-rich splicing factor 5,Sfrs5,Splicing factor, arginine_serine-rich 5,Srsf5
EIAAB39963 Pig,SC-35,Serine_arginine-rich splicing factor 2,SFRS2,Splicing component, 35 kDa,Splicing factor SC35,Splicing factor, arginine_serine-rich 2,SRSF2,Sus scrofa


 

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