Details for: NUP153

Gene ID: 9972

Symbol: NUP153

Ensembl ID: ENSG00000124789

Description: nucleoporin 153

Associated with

Other Information

Genular Protein ID: 2823900187

Symbol: NU153_HUMAN

Name: Nuclear pore complex protein Nup153

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 8110839

Title: Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153.

PubMed ID: 8110839

DOI: 10.1016/0167-4781(94)90040-x

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 14574404

Title: The DNA sequence and analysis of human chromosome 6.

PubMed ID: 14574404

DOI: 10.1038/nature02055

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 11777942

Title: Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins.

PubMed ID: 11777942

DOI: 10.1083/jcb.200110082

PubMed ID: 11839768

Title: Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export.

PubMed ID: 11839768

DOI: 10.1083/jcb.200106046

PubMed ID: 12802065

Title: Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex.

PubMed ID: 12802065

DOI: 10.1091/mbc.e02-09-0620

PubMed ID: 15229283

Title: Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket.

PubMed ID: 15229283

DOI: 10.1091/mbc.e04-03-0165

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19369352

Title: Integrase interacts with nucleoporin NUP153 to mediate the nuclear import of human immunodeficiency virus type 1.

PubMed ID: 19369352

DOI: 10.1128/jvi.02061-08

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20005110

Title: mRNA export from mammalian cell nuclei is dependent on GANP.

PubMed ID: 20005110

DOI: 10.1016/j.cub.2009.10.078

PubMed ID: 20407419

Title: Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion.

PubMed ID: 20407419

DOI: 10.1038/emboj.2010.54

PubMed ID: 20133940

Title: Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis.

PubMed ID: 20133940

DOI: 10.1074/jbc.m110.105890

PubMed ID: 20126445

Title: Nucleoporin 153 arrests the nuclear import of hepatitis B virus capsids in the nuclear basket.

PubMed ID: 20126445

DOI: 10.1371/journal.ppat.1000741

PubMed ID: 20068230

Title: Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis.

PubMed ID: 20068230

DOI: 10.1126/scisignal.2000526

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22541429

Title: Hikeshi, a nuclear import carrier for hsp70s, protects cells from heat shock-induced nuclear damage.

PubMed ID: 22541429

DOI: 10.1016/j.cell.2012.02.058

PubMed ID: 22623767

Title: Epstein-Barr virus protein kinase BGLF4 targets the nucleus through interaction with nucleoporins.

PubMed ID: 22623767

DOI: 10.1128/jvi.01058-12

PubMed ID: 22253824

Title: Localization of nucleoporin Tpr to the nuclear pore complex is essential for Tpr mediated regulation of the export of unspliced RNA.

PubMed ID: 22253824

DOI: 10.1371/journal.pone.0029921

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23652018

Title: GANP regulates recruitment of AID to immunoglobulin variable regions by modulating transcription and nucleosome occupancy.

PubMed ID: 23652018

DOI: 10.1038/ncomms2823

PubMed ID: 24130490

Title: Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity.

PubMed ID: 24130490

DOI: 10.1371/journal.ppat.1003693

PubMed ID: 23523133

Title: Nup153 and Nup98 bind the HIV-1 core and contribute to the early steps of HIV-1 replication.

PubMed ID: 23523133

DOI: 10.1016/j.virol.2013.02.008

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 31913756

Title: Viral protein X unlocks the nuclear pore complex through a human Nup153-dependent pathway to promote nuclear translocation of the lentiviral genome.

PubMed ID: 31913756

DOI: 10.1091/mbc.e19-08-0438

PubMed ID: 29997211

Title: Nup153 Unlocks the Nuclear Pore Complex for HIV-1 Nuclear Translocation in Nondividing Cells.

PubMed ID: 29997211

DOI: 10.1128/jvi.00648-18

Sequence Information:

  • Length: 1475
  • Mass: 153938
  • Checksum: D07455A691F7CD1F
  • Sequence:
  • MASGAGGVGG GGGGKIRTRR CHQGPIKPYQ QGRQQHQGIL SRVTESVKNI VPGWLQRYFN 
    KNEDVCSCST DTSEVPRWPE NKEDHLVYAD EESSNITDGR ITPEPAVSNT EEPSTTSTAS 
    NYPDVLTRPS LHRSHLNFSM LESPALHCQP STSSAFPIGS SGFSLVKEIK DSTSQHDDDN 
    ISTTSGFSSR ASDKDITVSK NTSLPPLWSP EAERSHSLSQ HTATSSKKPA FNLSAFGTLS 
    PSLGNSSILK TSQLGDSPFY PGKTTYGGAA AAVRQSKLRN TPYQAPVRRQ MKAKQLSAQS 
    YGVTSSTARR ILQSLEKMSS PLADAKRIPS IVSSPLNSPL DRSGIDITDF QAKREKVDSQ 
    YPPVQRLMTP KPVSIATNRS VYFKPSLTPS GEFRKTNQRI DNKCSTGYEK NMTPGQNREQ 
    RESGFSYPNF SLPAANGLSS GVGGGGGKMR RERTRFVASK PLEEEEMEVP VLPKISLPIT 
    SSSLPTFNFS SPEITTSSPS PINSSQALTN KVQMTSPSST GSPMFKFSSP IVKSTEANVL 
    PPSSIGFTFS VPVAKTAELS GSSSTLEPII SSSAHHVTTV NSTNCKKTPP EDCEGPFRPA 
    EILKEGSVLD ILKSPGFASP KIDSVAAQPT ATSPVVYTRP AISSFSSSGI GFGESLKAGS 
    SWQCDTCLLQ NKVTDNKCIA CQAAKLSPRD TAKQTGIETP NKSGKTTLSA SGTGFGDKFK 
    PVIGTWDCDT CLVQNKPEAI KCVACETPKP GTCVKRALTL TVVSESAETM TASSSSCTVT 
    TGTLGFGDKF KRPIGSWECS VCCVSNNAED NKCVSCMSEK PGSSVPASSS STVPVSLPSG 
    GSLGLEKFKK PEGSWDCELC LVQNKADSTK CLACESAKPG TKSGFKGFDT SSSSSNSAAS 
    SSFKFGVSSS SSGPSQTLTS TGNFKFGDQG GFKIGVSSDS GSINPMSEGF KFSKPIGDFK 
    FGVSSESKPE EVKKDSKNDN FKFGLSSGLS NPVSLTPFQF GVSNLGQEEK KEELPKSSSA 
    GFSFGTGVIN STPAPANTIV TSENKSSFNL GTIETKSASV APFTCKTSEA KKEEMPATKG 
    GFSFGNVEPA SLPSASVFVL GRTEEKQQEP VTSTSLVFGK KADNEEPKCQ PVFSFGNSEQ 
    TKDENSSKST FSFSMTKPSE KESEQPAKAT FAFGAQTSTT ADQGAAKPVF SFLNNSSSSS 
    STPATSAGGG IFGSSTSSSN PPVATFVFGQ SSNPVSSSAF GNTAESSTSQ SLLFSQDSKL 
    ATTSSTGTAV TPFVFGPGAS SNNTTTSGFG FGATTTSSSA GSSFVFGTGP SAPSASPAFG 
    ANQTPTFGQS QGASQPNPPG FGSISSSTAL FPTGSQPAPP TFGTVSSSSQ PPVFGQQPSQ 
    SAFGSGTTPN SSSAFQFGSS TTNFNFTNNS PSGVFTFGAN SSTPAASAQP SGSGGFPFNQ 
    SPAAFTVGSN GKNVFSSSGT SFSGRKIKTA VRRRK

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.