Nuclear pore complex protein Nup153 Recombinant Protein | NUP153 recombinant protein

Recombinant Human Nuclear pore complex protein Nup153

Cat. Num. AAA949865

• Gene Names: NUP153; N153; HNUP153
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Nuclear pore complex protein Nup153; Recombinant Human Nuclear pore complex protein Nup153; 153 kDa nucleoporin; Nucleoporin Nup153; NUP153 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 657-880aa; Partial
• Sequence: KAGSSWQCDTCLLQNKVTDNKCIACQAAKLSPRDTAKQTGIETPNKSGKTTLSASGTGFGDKFKPVIGTWDCDTCLVQNKPEAIKCVACETPKPGTCVKRALTLTVVSESAETMTASSSSCTVTTGTLGFGDKFKRPIGSWECSVCCVSNNAEDNKCVSCMSEKPGSSVPASSSSTVPVSLPSGGSLGLEKFKKPEGSWDCELCLVQNKADSTKCLACESAKPG
• Sequence Length: 1,506

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for NUP153 recombinant protein

Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC).

Product Categories/Family for NUP153 recombinant protein

Immunology

References

Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153.McMorrow I., Bastos R., Horton H., Burke B.Biochim. Biophys. 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The DNA sequence and analysis of human chromosome 6.Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.Nature 425:805-811(2003) Bienvenut W.V., Dozynkiewicz M., Norman J.C.Submitted (MAR-2009) to UniProtKB Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins.Brownawell A.M., Macara I.G.J. Cell Biol. 156:53-64(2002) Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export.Frosst P., Guan T., Subauste C., Hahn K., Gerace L.J. Cell Biol. 156:617-630(2002) Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex.Hase M.E., Cordes V.C.Mol. Biol. Cell 14:1923-1940(2003) Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket.Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.Mol. Biol. Cell 15:4261-4277(2004) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) A probability-based approach for high-throughput protein phosphorylation analysis and site localization.Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.Nat. Biotechnol. 24:1285-1292(2006) Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. IIIJ. Proteome Res. 7:1346-1351(2008) Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.Mol. Cell 31:438-448(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Integrase interacts with nucleoporin NUP153 to mediate the nuclear import of human immunodeficiency virus type 1.Woodward C.L., Prakobwanakit S., Mosessian S., Chow S.A.J. Virol. 83:6522-6533(2009) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion.Krull S., Dorries J., Boysen B., Reidenbach S., Magnius L., Norder H., Thyberg J., Cordes V.C.EMBO J. 29:1659-1673(2010) Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis.Nakano H., Funasaka T., Hashizume C., Wong R.W.J. Biol. Chem. 285:10841-10849(2010) Nucleoporin 153 arrests the nuclear import of hepatitis B virus capsids in the nuclear basket.Schmitz A., Schwarz A., Foss M., Zhou L., Rabe B., Hoellenriegel J., Stoeber M., Pante N., Kann M.PLoS Pathog. 6:E1000741-E1000741(2010) Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis.Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K., Cheung W.D., Shabanowitz J., Hunt D.F., Hart G.W.Sci. Signal. 3:RA2-RA2(2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.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.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) Hikeshi, a nuclear import carrier for hsp70s, protects cells from heat shock-induced nuclear damage.Kose S., Furuta M., Imamoto N.Cell 149:578-589(2012) Localization of nucleoporin Tpr to the nuclear pore complex is essential for Tpr mediated regulation of the export of unspliced RNA.Rajanala K., Nandicoori V.K.PLoS ONE 7:E29921-E29921(2012) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Solution structure of the second and third ZF-RANBP domains from human nuclear pore complex protein NUP153.RIKEN structural genomics initiative (RSGI) Submitted (AUG-2007) to the PDB data bankSolution structure of the second ZF-ranbp domain from human nuclear pore complex protein nup153.RIKEN structural genomics initiative (RSGI) Submitted (FEB-2009) to the PDB data bank+Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 503774352
• NCBI GeneID: 9972
• NCBI Accession #: NP_001265138.1
• NCBI GenBank Nucleotide #: NM_001278209.1
• UniProt Accession #: P49790; Q4LE47; Q5T9I7; Q7Z743; B4DIK2; E7EPX5; F6QR24
• Molecular Weight: 27.3 kDa
• NCBI Official Full Name: nuclear pore complex protein Nup153 isoform 1
• NCBI Official Synonym Full Names: nucleoporin 153kDa
• NCBI Official Symbol: NUP153
• NCBI Official Synonym Symbols: N153; HNUP153
• NCBI Protein Information: nuclear pore complex protein Nup153
• UniProt Protein Name: Nuclear pore complex protein Nup153
• Protein Family: Nuclear pore complex protein
• UniProt Gene Name: NUP153
• UniProt Entry Name: NU153_HUMAN

NCBI Description

Nuclear pore complexes regulate the transport of macromolecules between the nucleus and cytoplasm. They are composed of at least 100 different polypeptide subunits, many of which belong to the nucleoporin family. Nucleoporins are glycoproteins found in nuclear pores and contain characteristic pentapeptide XFXFG repeats as well as O-linked N-acetylglucosamine residues oriented towards the cytoplasm. The protein encoded by this gene has three distinct domains: a N-terminal region containing a pore targeting and an RNA-binding domain domain, a central region containing multiple zinc finger motifs, and a C-terminal region containing multiple XFXFG repeats. Alternative splicing results in multiple transcript variants of this gene. [provided by RefSeq, May 2013]

Uniprot Description

NUP153: Possible DNA-binding subunit of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane.

Protein type: Nuclear export; Nucleoporin

Chromosomal Location of Human Ortholog: 6p22.3

Cellular Component: annulate lamellae; cytoplasm; nuclear inclusion body; nuclear membrane; nuclear pore; nucleolus; nucleoplasm

Molecular Function: chromatin binding; double-stranded DNA binding; identical protein binding; nuclear localization sequence binding; nucleocytoplasmic transporter activity; protein anchor; protein binding; Ran GTPase binding; structural constituent of nuclear pore; zinc ion binding

Biological Process: carbohydrate metabolic process; cellular protein metabolic process; cytokine and chemokine mediated signaling pathway; entry of virus into host cell; gene expression; glucose transport; hexose transport; mitosis; mitotic cell cycle; mitotic nuclear envelope disassembly; modification by virus of host cellular process; mRNA transport; negative regulation of RNA export from nucleus; nuclear pore complex assembly; post-translational protein modification; protein sumoylation; protein transport; RNA-mediated gene silencing; transmembrane transport; tRNA processing; viral infectious cycle; viral reproduction; viral transcription; virus-host interaction