Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Far upstream element-binding protein 2 (FUSE-binding protein 2) (KH type-splicing regulatory protein) (KSRP) (MAP2 RNA trans-acting protein 1) (MARTA1)

 FUBP2_RAT               Reviewed;         721 AA.
Q99PF5;
26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
23-MAY-2018, entry version 111.
RecName: Full=Far upstream element-binding protein 2;
Short=FUSE-binding protein 2;
AltName: Full=KH type-splicing regulatory protein;
Short=KSRP;
AltName: Full=MAP2 RNA trans-acting protein 1;
Short=MARTA1;
Name=Khsrp; Synonyms=Fubp2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 73-87; 89-108 AND
475-486, SUBCELLULAR LOCATION, AND FUNCTION.
TISSUE=Brain;
PubMed=12358751; DOI=10.1046/j.1471-4159.2002.01058.x;
Rehbein M., Wege K., Buck F., Schweizer M., Richter D., Kindler S.;
"Molecular characterization of MARTA1, a protein interacting with the
dendritic targeting element of MAP2 mRNAs.";
J. Neurochem. 82:1039-1046(2002).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-185, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Part of a ternary complex that binds to the downstream
control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in
transcripts that are subject to tissue-specific alternative
splicing. May interact with single-stranded DNA from the far-
upstream element (FUSE). May activate gene expression. Also
involved in degradation of inherently unstable mRNAs that contain
AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting
degradation machinery to ARE-containing mRNAs (By similarity).
Binds to the dendritic targeting element and may play a role in
mRNA trafficking. {ECO:0000250, ECO:0000269|PubMed:12358751}.
-!- SUBUNIT: Part of a ternary complex containing FUBP2, PTBP1, PTBP2
and HNRPH1. Interacts with PARN. Interacts with PQBP1.
{ECO:0000250|UniProtKB:Q92945}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12358751}.
Cytoplasm {ECO:0000269|PubMed:12358751}. Note=A small proportion
is also found in the cytoplasm of neuronal cell bodies and
dendrites.
-!- SIMILARITY: Belongs to the KHSRP family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF308818; AAG59811.1; -; mRNA.
RefSeq; NP_598286.1; NM_133602.1.
UniGene; Rn.92643; -.
ProteinModelPortal; Q99PF5; -.
SMR; Q99PF5; -.
CORUM; Q99PF5; -.
STRING; 10116.ENSRNOP00000066023; -.
iPTMnet; Q99PF5; -.
PhosphoSitePlus; Q99PF5; -.
SwissPalm; Q99PF5; -.
REPRODUCTION-2DPAGE; Q99PF5; -.
PaxDb; Q99PF5; -.
PRIDE; Q99PF5; -.
GeneID; 171137; -.
KEGG; rno:171137; -.
CTD; 8570; -.
RGD; 621828; Khsrp.
eggNOG; KOG1676; Eukaryota.
eggNOG; ENOG410XZYE; LUCA.
HOVERGEN; HBG000625; -.
InParanoid; Q99PF5; -.
KO; K13210; -.
PhylomeDB; Q99PF5; -.
PRO; PR:Q99PF5; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:RGD.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; ISS:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.1370.10; -; 4.
InterPro; IPR015096; FUBP_C.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
Pfam; PF09005; DUF1897; 2.
Pfam; PF00013; KH_1; 4.
SMART; SM00322; KH; 4.
SUPFAM; SSF54791; SSF54791; 4.
PROSITE; PS50084; KH_TYPE_1; 4.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
DNA-binding; Isopeptide bond; Methylation; mRNA processing;
mRNA splicing; mRNA transport; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; Transcription;
Transcription regulation; Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q92945}.
CHAIN 2 721 Far upstream element-binding protein 2.
/FTId=PRO_0000050138.
DOMAIN 145 209 KH 1. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 234 300 KH 2. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 323 387 KH 3. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 425 492 KH 4. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
REPEAT 572 583 1.
REPEAT 618 629 2.
REPEAT 644 655 3.
REPEAT 674 685 4.
REGION 572 685 4 X 12 AA imperfect repeats.
COMPBIAS 7 68 Gly/Pro-rich.
COMPBIAS 69 498 Gly-rich.
COMPBIAS 499 613 Ala/Gly/Pro-rich.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 40 40 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q3U0V1}.
MOD_RES 88 88 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q3U0V1}.
MOD_RES 101 101 Phosphothreonine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 126 126 Phosphoserine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 130 130 Phosphoserine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 412 412 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 414 414 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 416 416 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 443 443 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q92945}.
MOD_RES 481 481 Phosphoserine.
{ECO:0000250|UniProtKB:Q92945}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q92945}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q92945}.
SEQUENCE 721 AA; 74226 MW; 482C7A765C60EE4A CRC64;
MSDYSTGGPP PGPPPPAGGG GGAAGAGGGP PPGPPGAGDR GGGGPGGGGP GGGGASGGPS
QPPGGGGPGI RKDAFADAVQ RARQIAAKIG GDAATTVNNN TPDFGFGGQK RQLEDGDQPD
SKKLASQGDS IGSQLGPIHP PPRTSMTEEY RVPDGMVGLI IGRGGEQINK IQQDSGCKVQ
ISPDSGGLPE RSVSLTGAPE SVQKAKMMLD DIVSRGRGGP PGQFHDNANG GQNGTVQEIM
IPAGKAGLVI GKGGETIKQL QERAGVKMIL IQDGSQNTNV DKPLRIIGDP YKVQQACEMV
MDILRERDQG GFGDRNEYGS RVGGGIDVPV PRHSVGVVIG RSGEMIKKIQ NDAGVRIQFK
QDDGTGPEKI AHIMGPPDRC EHAARIINDL LQSLRSGPPG PPGAPGMPPG GRGRGRGQGN
WGPPGGEMTF SIPTHKCGLV IGRGGENVKA INQQTGAFVE ISRQLPPNGD PNFKLFVIRG
SPQQIDHAKQ LIEEKIEGPL CPVGPGPGGP GPAGPMGPFH PGPFNQGPPG APPHAGGPPP
HQYPPQGWGN TYPEWQPPAP HDPNKAAAAA TDPNAAWAAY YSHYYQQPPG PVPGPAPAPA
APPAQGEPPQ PPPTGQSDYT KAWEEYYKKI GQQPQQPGAP PQQDYTKAWE EYYKKQAQVA
TGGGPGAPPG SQPDYSAAWA EYYRQQAAYY GQTPGPGGPQ PPSTQQGQQQ ATEANGYELH
L


Related products :

Catalog number Product name Quantity
20-372-60058 KH-type splicing regulatory protein (FUSE binding protein 2) - Mouse monoclonal anti-human KHSRP antibody; FUSE-binding protein 2; KH type-splicing regulatory protein; KSRP; p75 Monoclonal 0.1 mg
28-733 Far upstream element-binding protein activates the far upstream element (FUSE) of c-myc and stimulates expression of c-myc in undifferentiated cells. Regulation of FUSE by FUBP occurs through single-s 0.1 mg
28-332 Far upstream element-binding protein activates the far upstream element (FUSE) of c-myc and stimulates expression of c-myc in undifferentiated cells. Regulation of FUSE by FUBP occurs through single-s 0.1 mg
GWB-251C97 KH-type splicing regulatory protein (FUSE binding protein 2), Antibody
25-281 FUBP1 is a ssDNA binding protein that activates the far upstream element (FUSE) of c-myc and stimulates expression of c-myc in undifferentiated cells. Regulation of FUSE by FUBP occurs through single- 0.05 mg
CSB-EL009060RA Rat far upstream element (FUSE) binding protein 1 (FUBP1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
ARP51747_P050 FUBP3(far upstream element (FUSE) binding protein 3) 50 µg
ARP35704_P050 FUBP1(far upstream element (FUSE) binding protein 1) 50 µg
60058 IgG,KH_type splicing regulatory protein (FUSE binding protein 2) 0.1 mg
FUCA1 FUBP1 Gene far upstream element (FUSE) binding protein 1
FUCA2 FUBP3 Gene far upstream element (FUSE) binding protein 3
GWB-72E4AE Anti- FUBP1 (far upstream element (FUSE) binding protein 1) Antibody
GWB-E7AE5F Anti- FUBP1 (far upstream element (FUSE) binding protein 1) Antibody
CSB-EL009060MO Mouse far upstream element (FUSE) binding protein 1 (FUBP1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL009061HU Human far upstream element (FUSE) binding protein 3 (FUBP3) ELISA kit, Species Human, Sample Type serum, plasma 96T
201-20-2119 FUBP3{Homo sapiens far upstream element (FUSE) binding protein 3, mRNA (cDNA clone MGC 14157 IMAGE 3957939), complete cds}rabbit.pAb 0.2ml
EIAAB39218 BASS1,Bax antagonist selected in saccharomyces 1,C21orf50,DBP5,Homo sapiens,HSPC310,HSPC312,Human,KIAA1019,Negative regulatory element-binding protein,NRE-binding protein,NREBP,Protein DBP-5,Protein S
EIAAB13331 Epithelial splicing regulatory protein 1,ESRP1,Homo sapiens,Human,RBM35A,RNA-binding motif protein 35A,RNA-binding protein 35A
EIAAB13335 Epithelial splicing regulatory protein 2,ESRP2,Homo sapiens,Human,PP7059,RBM35B,RNA-binding motif protein 35B,RNA-binding protein 35B
EIAAB13336 Epithelial splicing regulatory protein 2,Esrp2,Rat,Rattus norvegicus,Rbm35b,RNA-binding motif protein 35B,RNA-binding protein 35B
EIAAB13330 Epithelial splicing regulatory protein 1,Esrp1,Rat,Rattus norvegicus,Rbm35a,RNA-binding motif protein 35A,RNA-binding protein 35A
EIAAB13333 Epithelial splicing regulatory protein 2,Esrp2,Mouse,Mus musculus,Rbm35b,RNA-binding motif protein 35B,RNA-binding protein 35B
EIAAB13332 Epithelial splicing regulatory protein 1,Esrp1,Mouse,Mus musculus,Rbm35a,RNA-binding motif protein 35A,RNA-binding protein 35A
EIAAB39217 Mouse,Mus musculus,Negative regulatory element-binding protein,NRE-binding protein,Nrebp,Protein SON,Son
EIAAB10489 Albumin D box-binding protein,Albumin D-element-binding protein,D site-binding protein,DBP,Homo sapiens,Human,TaxREB302,Tax-responsive enhancer element-binding protein 302


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur