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Splicing factor U2AF 35 kDa subunit (U2 auxiliary factor 35 kDa subunit) (U2 small nuclear RNA auxiliary factor 1) (U2 snRNP auxiliary factor small subunit)

 U2AF1_HUMAN             Reviewed;         240 AA.
Q01081; Q701P4; Q71RF1;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 199.
RecName: Full=Splicing factor U2AF 35 kDa subunit;
AltName: Full=U2 auxiliary factor 35 kDa subunit;
AltName: Full=U2 small nuclear RNA auxiliary factor 1;
AltName: Full=U2 snRNP auxiliary factor small subunit;
Name=U2AF1; Synonyms=U2AF35, U2AFBP; ORFNames=FP793;
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 PROTEIN SEQUENCE OF 68-89
AND 126-151.
TISSUE=Fetal brain;
PubMed=1388271; DOI=10.1073/pnas.89.18.8769;
Zhang M., Zamore P.D., Carmo-Fonseca M., Lamond A.I., Green M.R.;
"Cloning and intracellular localization of the U2 small nuclear
ribonucleoprotein auxiliary factor small subunit.";
Proc. Natl. Acad. Sci. U.S.A. 89:8769-8773(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORMS
1; 2 AND 3), AND SUBCELLULAR LOCATION.
TISSUE=Spleen;
PubMed=15096518; DOI=10.1074/jbc.M402136200;
Pacheco T.R.D., Gomes N.L., Benes V., Ansorge W., Wollerton M.,
Smith C.W., Valcarcel J., Carmo-Fonseca M.;
"Diversity of vertebrate splicing factor U2AF35: identification of
alternatively spliced U2AF1 mRNAs.";
J. Biol. Chem. 279:27039-27049(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
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).
[7]
PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUL-2005) to UniProtKB.
[8]
FUNCTION.
PubMed=8647433; DOI=10.1101/gad.10.11.1356;
Zuo P., Maniatis T.;
"The splicing factor U2AF35 mediates critical protein-protein
interactions in constitutive and enhancer-dependent splicing.";
Genes Dev. 10:1356-1368(1996).
[9]
INTERACTION WITH ZRANB2.
PubMed=11448987; DOI=10.1083/jcb.200010059;
Adams D.J., van der Weyden L., Mayeda A., Stamm S., Morris B.J.,
Rasko J.E.J.;
"ZNF265 -- a novel spliceosomal protein able to induce alternative
splicing.";
J. Cell Biol. 154:25-32(2001).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[11]
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).
[12]
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]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[16]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-39 AND ARG-165, METHYLATION
[LARGE SCALE ANALYSIS] AT LYS-39 (ISOFORMS 2 AND 3), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 43-146 IN COMPLEX WITH U2AF2,
AND MUTAGENESIS OF TRP-134.
PubMed=11551507; DOI=10.1016/S0092-8674(01)00480-9;
Kielkopf C.L., Rodionova N.A., Green M.R., Burley S.K.;
"A novel peptide recognition mode revealed by the X-ray structure of a
core U2AF35/U2AF65 heterodimer.";
Cell 106:595-605(2001).
-!- FUNCTION: Plays a critical role in both constitutive and enhancer-
dependent splicing by mediating protein-protein interactions and
protein-RNA interactions required for accurate 3'-splice site
selection. Recruits U2 snRNP to the branch point. Directly
mediates interactions between U2AF2 and proteins bound to the
enhancers and thus may function as a bridge between U2AF2 and the
enhancer complex to recruit it to the adjacent intron.
{ECO:0000269|PubMed:8647433}.
-!- SUBUNIT: Interacts (via RS domain) with PHF5A (via N-terminus) (By
similarity). Identified in the spliceosome C complex. Heterodimer
with U2AF2. Interacts with ZRANB2. {ECO:0000269|PubMed:11448987,
ECO:0000269|PubMed:11551507, ECO:0000269|PubMed:11991638,
ECO:0007001}.
-!- INTERACTION:
P63010:AP2B1; NbExp=3; IntAct=EBI-632461, EBI-432924;
Q86X95:CIR1; NbExp=4; IntAct=EBI-632461, EBI-627102;
P49760:CLK2; NbExp=3; IntAct=EBI-10176676, EBI-750020;
P61978:HNRNPK; NbExp=3; IntAct=EBI-632461, EBI-304185;
Q6NYC1:JMJD6; NbExp=2; IntAct=EBI-632461, EBI-8464037;
Q8N5F7:NKAP; NbExp=2; IntAct=EBI-632461, EBI-721539;
D3DU92:RNPS1; NbExp=3; IntAct=EBI-10176676, EBI-10176640;
Q13435:SF3B2; NbExp=2; IntAct=EBI-632461, EBI-749111;
P78362:SRPK2; NbExp=7; IntAct=EBI-632461, EBI-593303;
O43463:SUV39H1; NbExp=2; IntAct=EBI-632461, EBI-349968;
P26368:U2AF2; NbExp=11; IntAct=EBI-632461, EBI-742339;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15096518}.
Nucleus speckle {ECO:0000269|PubMed:15096518}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=U2AF35a;
IsoId=Q01081-1; Sequence=Displayed;
Name=2; Synonyms=U2AF35b;
IsoId=Q01081-2; Sequence=VSP_042665;
Note=Interacts with U2AF2 and stimulates U2AF splicing activity
in vitro. Less efficient than isoform 1. Contains a
N6-methyllysine at position 39. {ECO:0000307|PubMed:24129315};
Name=3; Synonyms=U2AF35c;
IsoId=Q01081-3; Sequence=VSP_042665, VSP_042666, VSP_042667;
Note=Produced at very low levels due to a premature stop codon
in the mRNA, leading to nonsense-mediated mRNA decay. Contains a
N6-methyllysine at position 39. {ECO:0000307|PubMed:24129315};
Name=4;
IsoId=Q01081-4; Sequence=VSP_042664;
-!- DOMAIN: The C-terminal SR-rich domain is required for interactions
with SR proteins and the splicing regulators TRA and TRA2, and the
N-terminal domain is required for formation of the U2AF1/U2AF2
heterodimer.
-!- SIMILARITY: Belongs to the splicing factor SR family.
{ECO:0000320}.
-!- CAUTION: There is a duplication of the U2AF1 gene on chromosome
21. U2AF1 (AC Q01081) and U2AF1L5 (AC P0DN76) encode identical
proteins. {ECO:0000320}.
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EMBL; M96982; AAA36619.1; -; mRNA.
EMBL; AJ627978; CAF29556.1; -; mRNA.
EMBL; AF370386; AAQ15222.1; -; mRNA.
EMBL; AP001631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001748; BAA95534.1; -; Genomic_DNA.
EMBL; CH471079; EAX09501.1; -; Genomic_DNA.
EMBL; CH471079; EAX09502.1; -; Genomic_DNA.
EMBL; CH471079; EAX09504.1; -; Genomic_DNA.
EMBL; CH471079; EAX09505.1; -; Genomic_DNA.
EMBL; BC001177; AAH01177.1; -; mRNA.
EMBL; BC001923; AAH01923.1; -; mRNA.
CCDS; CCDS13694.1; -. [Q01081-1]
CCDS; CCDS33574.1; -. [Q01081-2]
CCDS; CCDS42948.1; -. [Q01081-4]
PIR; A46179; A46179.
RefSeq; NP_001020374.1; NM_001025203.1. [Q01081-2]
RefSeq; NP_001020375.1; NM_001025204.1. [Q01081-4]
RefSeq; NP_001307575.1; NM_001320646.1. [Q01081-1]
RefSeq; NP_001307577.1; NM_001320648.1. [Q01081-2]
RefSeq; NP_001307580.1; NM_001320651.1. [Q01081-4]
RefSeq; NP_006749.1; NM_006758.2. [Q01081-1]
UniGene; Hs.365116; -.
PDB; 1JMT; X-ray; 2.20 A; A=43-146.
PDBsum; 1JMT; -.
ProteinModelPortal; Q01081; -.
SMR; Q01081; -.
BioGrid; 113157; 128.
BioGrid; 3195698; 2.
CORUM; Q01081; -.
DIP; DIP-1108N; -.
IntAct; Q01081; 44.
MINT; MINT-1468226; -.
STRING; 9606.ENSP00000291552; -.
iPTMnet; Q01081; -.
PhosphoSitePlus; Q01081; -.
SwissPalm; Q01081; -.
BioMuta; U2AF1; -.
DMDM; 267187; -.
EPD; Q01081; -.
MaxQB; Q01081; -.
PaxDb; Q01081; -.
PeptideAtlas; Q01081; -.
PRIDE; Q01081; -.
DNASU; 7307; -.
Ensembl; ENST00000291552; ENSP00000291552; ENSG00000160201. [Q01081-1]
Ensembl; ENST00000380276; ENSP00000369629; ENSG00000160201. [Q01081-2]
Ensembl; ENST00000398137; ENSP00000381205; ENSG00000160201. [Q01081-4]
Ensembl; ENST00000459639; ENSP00000418705; ENSG00000160201. [Q01081-4]
Ensembl; ENST00000464750; ENSP00000420672; ENSG00000160201. [Q01081-3]
GeneID; 102724594; -.
GeneID; 7307; -.
KEGG; hsa:102724594; -.
KEGG; hsa:7307; -.
UCSC; uc002zcy.1; human. [Q01081-1]
CTD; 102724594; -.
CTD; 7307; -.
DisGeNET; 102724594; -.
DisGeNET; 7307; -.
EuPathDB; HostDB:ENSG00000160201.11; -.
GeneCards; U2AF1; -.
HGNC; HGNC:12453; U2AF1.
HPA; HPA044833; -.
HPA; HPA052083; -.
MIM; 191317; gene.
neXtProt; NX_Q01081; -.
OpenTargets; ENSG00000160201; -.
PharmGKB; PA37103; -.
eggNOG; KOG2202; Eukaryota.
eggNOG; ENOG410Z5PX; LUCA.
GeneTree; ENSGT00530000063193; -.
HOGENOM; HOG000178619; -.
HOVERGEN; HBG054605; -.
InParanoid; Q01081; -.
KO; K12836; -.
OMA; MHLRLAS; -.
OrthoDB; EOG091G0CUI; -.
PhylomeDB; Q01081; -.
TreeFam; TF300143; -.
Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72187; mRNA 3'-end processing.
SIGNOR; Q01081; -.
ChiTaRS; U2AF1; human.
EvolutionaryTrace; Q01081; -.
GeneWiki; U2_small_nuclear_RNA_auxiliary_factor_1; -.
PRO; PR:Q01081; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000160201; -.
CleanEx; HS_U2AF1; -.
ExpressionAtlas; Q01081; baseline and differential.
Genevisible; Q01081; HS.
GO; GO:0015030; C:Cajal body; IBA:ProtInc.
GO; GO:0071013; C:catalytic step 2 spliceosome; HTP:UniProtKB.
GO; GO:0016607; C:nuclear speck; HMP:UniProtKB.
GO; GO:0005654; C:nucleoplasm; HTP:HPA.
GO; GO:0005681; C:spliceosomal complex; HTP:HGNC.
GO; GO:0089701; C:U2AF; HTP:GO_Central.
GO; GO:0046872; F:metal ion binding; RCA:UniProtKB-KW.
GO; GO:0030628; F:pre-mRNA 3'-splice site binding; ISS:GO_Central.
GO; GO:0003723; F:RNA binding; HTP:UniProtKB.
GO; GO:0031124; P:mRNA 3'-end processing; IBA:Reactome.
GO; GO:0006406; P:mRNA export from nucleus; IBA:Reactome.
GO; GO:0006397; P:mRNA processing; IBA:ProtInc.
GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:GO_Central.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HDA:ParkinsonsUK-UCL.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; HDA:ParkinsonsUK-UCL.
GO; GO:0006405; P:RNA export from nucleus; IBA:Reactome.
GO; GO:0008380; P:RNA splicing; IBA:ProtInc.
GO; GO:0006369; P:termination of RNA polymerase II transcription; IBA:Reactome.
Gene3D; 4.10.1000.10; -; 1.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR003954; RRM_dom_euk.
InterPro; IPR009145; U2AF_small.
InterPro; IPR000571; Znf_CCCH.
InterPro; IPR036855; Znf_CCCH_sf.
PANTHER; PTHR12620; PTHR12620; 1.
Pfam; PF00076; RRM_1; 1.
Pfam; PF00642; zf-CCCH; 2.
PRINTS; PR01848; U2AUXFACTOR.
SMART; SM00360; RRM; 1.
SMART; SM00361; RRM_1; 1.
SMART; SM00356; ZnF_C3H1; 2.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
PROSITE; PS50103; ZF_C3H1; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Metal-binding; Methylation;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; Spliceosome; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.7}.
CHAIN 2 240 Splicing factor U2AF 35 kDa subunit.
/FTId=PRO_0000081994.
DOMAIN 65 147 RRM. {ECO:0000270|PROSITE-
ProRule:PRU00176}.
ZN_FING 12 40 C3H1-type 1. {ECO:0000270|PROSITE-
ProRule:PRU00723}.
ZN_FING 149 176 C3H1-type 2. {ECO:0000270|PROSITE-
ProRule:PRU00723}.
COMPBIAS 178 240 Arg/Gly/Ser-rich (RS domain).
COMPBIAS 210 223 Poly-Gly.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.7}.
MOD_RES 39 39 N6-methyllysine.
{ECO:0000307|PubMed:24129315}.
MOD_RES 61 61 Phosphoserine.
{ECO:0000307|PubMed:21406692}.
MOD_RES 145 145 Phosphoserine.
{ECO:0000307|PubMed:23186163}.
MOD_RES 165 165 Omega-N-methylarginine.
{ECO:0000307|PubMed:24129315}.
VAR_SEQ 1 73 Missing (in isoform 4).
{ECO:0000319|PubMed:15498874}.
/FTId=VSP_042664.
VAR_SEQ 47 66 ALLNIYRNPQNSSQSADGLR -> LIQNIYRNPQNSAQTAD
GSH (in isoform 2 and isoform 3).
{ECO:0000319|PubMed:15096518}.
/FTId=VSP_042665.
VAR_SEQ 67 75 CAVSDVEMQ -> YHCPLEHLP (in isoform 3).
{ECO:0000320}.
/FTId=VSP_042666.
VAR_SEQ 76 240 Missing (in isoform 3). {ECO:0000320}.
/FTId=VSP_042667.
MUTAGEN 134 134 W->A: Decreases affinity for UAF2 by 3
orders of magnitude.
{ECO:0000269|PubMed:11551507}.
STRAND 45 53 {ECO:0000307|PDB:1JMT}.
HELIX 64 92 {ECO:0000307|PDB:1JMT}.
STRAND 96 101 {ECO:0000307|PDB:1JMT}.
STRAND 104 118 {ECO:0000307|PDB:1JMT}.
HELIX 120 130 {ECO:0000307|PDB:1JMT}.
STRAND 142 144 {ECO:0000307|PDB:1JMT}.
SEQUENCE 240 AA; 27872 MW; 3DA130DCE0B953F6 CRC64;
MAEYLASIFG TEKDKVNCSF YFKIGACRHG DRCSRLHNKP TFSQTIALLN IYRNPQNSSQ
SADGLRCAVS DVEMQEHYDE FFEEVFTEME EKYGEVEEMN VCDNLGDHLV GNVYVKFRRE
EDAEKAVIDL NNRWFNGQPI HAELSPVTDF REACCRQYEM GECTRGGFCN FMHLKPISRE
LRRELYGRRR KKHRSRSRSR ERRSRSRDRG RGGGGGGGGG GGGRERDRRR SRDRERSGRF


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EIAAB44746 Mouse,Mus musculus,Splicing factor U2AF 26 kDa subunit,U2 auxiliary factor 26,U2 small nuclear RNA auxiliary factor 1-like protein 4,U2af1l4,U2af26
EIAAB44742 Homo sapiens,hU2AF(65),hU2AF65,Human,Splicing factor U2AF 65 kDa subunit,U2 auxiliary factor 65 kDa subunit,U2 snRNP auxiliary factor large subunit,U2AF2,U2AF65
EIAAB44743 Mouse,Mus musculus,Splicing factor U2AF 65 kDa subunit,U2 auxiliary factor 65 kDa subunit,U2 snRNP auxiliary factor large subunit,U2af2,U2af65
18-003-44165 Splicing factor U2AF 65 kDa subunit - U2 auxiliary factor 65 kDa subunit; U2 snRNP auxiliary factor large subunit; hU2AF(65) Polyclonal 0.1 mg Protein A
EIAAB44747 Cb2-806,Cb2-807,Liver regeneration-related protein LRRG157_LRRG158,Rat,Rattus norvegicus,Splicing factor U2AF 26 kDa subunit,U2 auxiliary factor 26,U2 small nuclear RNA auxiliary factor 1-like protein
EIAAB44745 Bos taurus,Bovine,Splicing factor U2AF 26 kDa subunit,U2 small nuclear RNA auxiliary factor 1-like protein 4,U2AF1L4
18-003-43607 U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2 - U2(RNU2) small nuclear RNA auxiliary factor 1-like 2; CCCH type zinc finger. RNA-binding motif and serine_arginin 0.1 mg Protein A
29-247 U2 auxiliary factor (U2AF), comprised of a large and a small subunit, is a non-snRNP protein required for the binding of U2 snRNP to the pre-mRNA branch site. U2AF2 is the U2AF large subunit which con 0.1 mg
H9874 U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2 (ZRSR2), Mouse, ELISA Kit 96T
CSB-EL027129HU Human U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2(ZRSR2) ELISA kit 96T
CSB-EL027129MO Mouse U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2(ZRSR2) ELISA kit 96T
H9872 U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1 (U2AF1L1), Human, ELISA Kit 96T
CSB-EL025406HU Human U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1(U2AF1L1) ELISA kit 96T
H9873 U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2 (ZRSR2), Human, ELISA Kit 96T
CSB-EL027129HU Human U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2(ZRSR2) ELISA kit SpeciesHuman 96T
CSB-EL027129MO Mouse U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2(ZRSR2) ELISA kit SpeciesMouse 96T
CSB-EL025406HU Human U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1(U2AF1L1) ELISA kit SpeciesHuman 96T
EIAAB44750 CCCH type zinc finger, RNA-binding motif and serine_arginine rich protein 2,Mouse,Mus musculus,U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2,U2(RNU2) small nucle
EIAAB44749 CCCH type zinc finger, RNA-binding motif and serine_arginine rich protein 1,Homo sapiens,Human,U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1,U2(RNU2) small nucle
29-408 SF3B1 is subunit 1 of the splicing factor 3b protein complex. Splicing factor 3b, together with splicing factor 3a and a 12S RNA unit, forms the U2 small nuclear ribonucleoproteins complex (U2 snRNP). 0.1 mg


 

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