Details for: XRN2
Associated with
Other Information
Genular Protein ID: 2731805112
Symbol: XRN2_HUMAN
Name: 5'-3' exoribonuclease 2
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 10409438
Title: Cloning and mapping of the XRN2 gene to human chromosome 20p11.1-p11.2.
PubMed ID: 10409438
PubMed ID: 16147866
Title: A novel splice variant of human XRN2 gene is mainly expressed in blood leukocyte.
PubMed ID: 16147866
PubMed ID: 11230166
Title: Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.
PubMed ID: 11230166
DOI: 10.1101/gr.gr1547r
PubMed ID: 11780052
Title: The DNA sequence and comparative analysis of human chromosome 20.
PubMed ID: 11780052
DOI: 10.1038/414865a
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
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: 12429849
Title: Functional proteomic analysis of human nucleolus.
PubMed ID: 12429849
PubMed ID: 15565158
Title: Human 5' -> 3' exonuclease Xrn2 promotes transcription termination at co-transcriptional cleavage sites.
PubMed ID: 15565158
DOI: 10.1038/nature03035
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 16648491
Title: Pause sites promote transcriptional termination of mammalian RNA polymerase II.
PubMed ID: 16648491
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: 17924679
Title: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.
PubMed ID: 17924679
DOI: 10.1021/pr070152u
PubMed ID: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 18318008
Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.
PubMed ID: 18318008
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: 19369195
Title: Large-scale proteomics analysis of the human kinome.
PubMed ID: 19369195
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21700224
Title: Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause sites to promote Xrn2-dependent termination.
PubMed ID: 21700224
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 23125361
Title: The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA function.
PubMed ID: 23125361
DOI: 10.1093/nar/gks1032
PubMed ID: 25220460
Title: The RNA helicase DHX34 activates NMD by promoting a transition from the surveillance to the decay-inducing complex.
PubMed ID: 25220460
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 24462208
Title: PAXT-1 promotes XRN2 activity by stabilizing it through a conserved domain.
PubMed ID: 24462208
PubMed ID: 24129315
Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.
PubMed ID: 24129315
PubMed ID: 26700805
Title: SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control termination.
PubMed ID: 26700805
DOI: 10.1038/nature16469
PubMed ID: 26779609
Title: Structural basis and function of XRN2 binding by XTB domains.
PubMed ID: 26779609
DOI: 10.1038/nsmb.3155
Sequence Information:
- Length: 950
- Mass: 108582
- Checksum: 763B5E0E628F97A8
- Sequence:
MGVPAFFRWL SRKYPSIIVN CVEEKPKECN GVKIPVDASK PNPNDVEFDN LYLDMNGIIH PCTHPEDKPA PKNEDEMMVA IFEYIDRLFS IVRPRRLLYM AIDGVAPRAK MNQQRSRRFR ASKEGMEAAV EKQRVREEIL AKGGFLPPEE IKERFDSNCI TPGTEFMDNL AKCLRYYIAD RLNNDPGWKN LTVILSDASA PGEGEHKIMD YIRRQRAQPN HDPNTHHCLC GADADLIMLG LATHEPNFTI IREEFKPNKP KPCGLCNQFG HEVKDCEGLP REKKGKHDEL ADSLPCAEGE FIFLRLNVLR EYLERELTMA SLPFTFDVER SIDDWVFMCF FVGNDFLPHL PSLEIRENAI DRLVNIYKNV VHKTGGYLTE SGYVNLQRVQ MIMLAVGEVE DSIFKKRKDD EDSFRRRQKE KRKRMKRDQP AFTPSGILTP HALGSRNSPG SQVASNPRQA AYEMRMQNNS SPSISPNTSF TSDGSPSPLG GIKRKAEDSD SEPEPEDNVR LWEAGWKQRY YKNKFDVDAA DEKFRRKVVQ SYVEGLCWVL RYYYQGCASW KWYYPFHYAP FASDFEGIAD MPSDFEKGTK PFKPLEQLMG VFPAASGNFL PPSWRKLMSD PDSSIIDFYP EDFAIDLNGK KYAWQGVALL PFVDERRLRA ALEEVYPDLT PEETRRNSLG GDVLFVGKHH PLHDFILELY QTGSTEPVEV PPELCHGIQG KFSLDEEAIL PDQIVCSPVP MLRDLTQNTV VSINFKDPQF AEDYIFKAVM LPGARKPAAV LKPSDWEKSS NGRQWKPQLG FNRDRRPVHL DQAAFRTLGH VMPRGSGTGI YSNAAPPPVT YQGNLYRPLL RGQAQIPKLM SNMRPQDSWR GPPPLFQQQR FDRGVGAEPL LPWNRMLQTQ NAAFQPNQYQ MLAGPGGYPP RRDDRGGRQG YPREGRKYPL PPPSGRYNWN
Genular Protein ID: 2342243408
Symbol: B4DZC3_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Sequence Information:
- Length: 896
- Mass: 102416
- Checksum: 84C2A716C0D9294B
- Sequence:
MNGIIHPCTH PEDKPAPKNE DEMMVAIFEY IDRLFSIVRP RRLLYMAIDG VAPRAKMNQQ RSRRFRASKE GMEAAVEKQR VREEILAKGG FLPPEEIKER FDSNCITPGT EFMDNLAKCL RYYIADRLNN DPGWKNLTVI LSDASAPGEG EHKIMDYIRR QRAQPNHDPN THHCLCGADA DLIMLGLATH EPNFTIIREE FKPNKPKPCG LCNQFGHEVK DCEGLPREKK GKHDELADSL PCAEGEFIFL RLNVLREYLE RELTMASLPF TFDVERSIDD WVFMCFFVGN DFLPHLPSLE IRENAIDRLV NIYKNVVHKT GGYLTESGYV NLQRVQMIML AVGEVEDSIF KKRKDDEDSF RRRQKEKRKR MKRDQPAFTP SGILTPHALG SRNSPGSQVA SNPRQAAYEM RMQNNSSPSI SPNTSFTSDG SPSPLGGIKR KAEDSDSEPE PEDNVRLWEA GWKQRYYKNK FDVDAADEKF RRKVVQSYVE GLCWVLRYYY QGCASWKWYY PFHYAPFASD FEGIADMPSD FEKGTKPFKP LEQLMGVFPA ASGNFLPPSW RKLMSDPDSS IIDFYPEDFA IDLNGKKYAW QGVALLPFVD ERRLRAALEE VYPDLTPEET RRNSLGGDVL FVGKHHPLHD FILELYQTGS TEPVEVPPEL CHGIQGKFSL DEEAILPDQI VCSPVPMLRD LTQNTVVSIN FKDPQFAEDY IFKAVMLPGA RKPAAVLKPS DWEKSSNGRQ WKPQLGFNRD RRPVHLDQAA FRTLGHVMPR GSGTGIYSNA APPPVTYQGN LYRPLLRGQA QIPKLMSNMR PQDSWRGPPP LFQQQRFDRG VGAEPLLPWN RMLQTQNAAF QPNQYQMLAG PGGYPPRRDD RGGRQGYPRE GRKYPLPPPS GRYNWN
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.