Details for: DDX46

Gene ID: 9879

Symbol: DDX46

Ensembl ID: ENSG00000145833

Description: DEAD-box helicase 46

Associated with

Other Information

Genular Protein ID: 2962943571

Symbol: DDX46_HUMAN

Name: Probable ATP-dependent RNA helicase DDX46

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 9872452

Title: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.

PubMed ID: 9872452

DOI: 10.1093/dnares/5.5.277

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: 12234937

Title: Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein.

PubMed ID: 12234937

DOI: 10.1093/emboj/cdf480

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: 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: 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: 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: 23186163

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

PubMed ID: 23186163

DOI: 10.1021/pr300630k

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: 25255805

Title: Global profiling of co- and post-translationally N-myristoylated proteomes in human cells.

PubMed ID: 25255805

DOI: 10.1038/ncomms5919

PubMed ID: 25218447

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

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

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: 36797247

Title: Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP assembly.

PubMed ID: 36797247

DOI: 10.1038/s41467-023-36489-x

PubMed ID: 32494006

Title: Molecular architecture of the human 17S U2 snRNP.

PubMed ID: 32494006

DOI: 10.1038/s41586-020-2344-3

PubMed ID: 34822310

Title: Structural basis of branch site recognition by the human spliceosome.

PubMed ID: 34822310

DOI: 10.1126/science.abm4245

Sequence Information:

  • Length: 1031
  • Mass: 117362
  • Checksum: 52535164FEB48A72
  • Sequence:
  • MGRESRHYRK RSASRGRSGS RSRSRSPSDK RSKRGDDRRS RSRDRDRRRE RSRSRDKRRS 
    RSRDRKRLRR SRSRERDRSR ERRRSRSRDR RRSRSRSRGR RSRSSSPGNK SKKTENRSRS 
    KEKTDGGESS KEKKKDKDDK EDEKEKDAGN FDQNKLEEEM RKRKERVEKW REEQRKKAME 
    NIGELKKEIE EMKQGKKWSL EDDDDDEDDP AEAEKEGNEM EGEELDPLDA YMEEVKEEVK 
    KFNMRSVKGG GGNEKKSGPT VTKVVTVVTT KKAVVDSDKK KGELMENDQD AMEYSSEEEE 
    VDLQTALTGY QTKQRKLLEP VDHGKIEYEP FRKNFYVEVP ELAKMSQEEV NVFRLEMEGI 
    TVKGKGCPKP IKSWVQCGIS MKILNSLKKH GYEKPTPIQT QAIPAIMSGR DLIGIAKTGS 
    GKTIAFLLPM FRHIMDQRSL EEGEGPIAVI MTPTRELALQ ITKECKKFSK TLGLRVVCVY 
    GGTGISEQIA ELKRGAEIIV CTPGRMIDML AANSGRVTNL RRVTYVVLDE ADRMFDMGFE 
    PQVMRIVDNV RPDRQTVMFS ATFPRAMEAL ARRILSKPIE VQVGGRSVVC SDVEQQVIVI 
    EEEKKFLKLL ELLGHYQESG SVIIFVDKQE HADGLLKDLM RASYPCMSLH GGIDQYDRDS 
    IINDFKNGTC KLLVATSVAA RGLDVKHLIL VVNYSCPNHY EDYVHRAGRT GRAGNKGYAY 
    TFITEDQARY AGDIIKALEL SGTAVPPDLE KLWSDFKDQQ KAEGKIIKKS SGFSGKGFKF 
    DETEQALANE RKKLQKAALG LQDSDDEDAA VDIDEQIESM FNSKKRVKDM AAPGTSSVPA 
    PTAGNAEKLE IAKRLALRIN AQKNLGIESQ DVMQQATNAI LRGGTILAPT VSAKTIAEQL 
    AEKINAKLNY VPLEKQEEER QDGGQNESFK RYEEELEIND FPQTARWKVT SKEALQRISE 
    YSEAAITIRG TYFPPGKEPK EGERKIYLAI ESANELAVQK AKAEITRLIK EELIRLQNSY 
    QPTNKGRYKV L

Genular Protein ID: 1737019070

Symbol: A0A0C4DG89_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 15372022

Title: The DNA sequence and comparative analysis of human chromosome 5.

PubMed ID: 15372022

DOI: 10.1038/nature02919

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: 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: 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: 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: 23186163

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

PubMed ID: 23186163

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

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.O114.044792

PubMed ID: 28112733

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

PubMed ID: 28112733

Sequence Information:

  • Length: 1032
  • Mass: 117461
  • Checksum: 4BA0BEDA8EF45683
  • Sequence:
  • MGRESRHYRK RSASRGRSGS RSRSRSPSDK RSKRGDDRRS RSRDRDRRRE RSRSRDKRRS 
    RSRDRKRLRR SRSRERDRSR ERRRSRSRDR RRSRSRSRGR RSRSSSPGNK SKKTENRSRS 
    KEKTDGGESS KEKKKDKDDK EDEKEKDAGN FDQNKLEEEM RKRKERVEKW REEQRKKAME 
    NIGELKKEIE EMKQGKKWSL EDDDDDEDDP AEAEKEGNEM EGEELDPLDA YMEEVKEEVK 
    KFNMRSVKGG GGNEKKSGPT VTKVVTVVTT KKAVVDSDKK KGELMENDQD AMEYSSEEEE 
    VDLQTALTGY QTKQRKLLEP VDHGKIEYEP FRKNFYVEVP ELAKMSQEEV NVFRLEMEGI 
    TVKGKGCPKP IKSWVQCGIS MKILNSLKKH GYEKPTPIQT QAIPAIMSGR DLIGIAKTGS 
    GKTIAFLLPM FRHIMDQRSL EEGEGPIAVI MTPTRELALQ ITKECKKFSK TLGLRVVCVY 
    GGTGISEQIA ELKRGAEIIV CTPGRMIDML AANSGRVTNL RRVTYVVLDE ADRMFDMGFE 
    PQVMRIVDNV RPDRQTVMFS ATFPRAMEAL ARRILSKPIE VQVGGRSVVC SDVEQQVIVI 
    EEEKKFLKLL ELLGHYQESG SVIIFVDKQE HADGLLKDLM RASYPCMSLH GGIDQYDRDS 
    IINDFKNGTC KLLVATSVAA RGLDVKHLIL VVNYSCPNHY EDYVHRAGRT GRAGNKGYAY 
    TFITEDQARY AGDIIKALEL SGTAVPPDLE KLWSDFKDQQ KAEGKIIKKS SGFSGKGFKF 
    DETEQALANE RKKLQKAALG LQDSDDEDAA VDIDEQIESM FNSKKRVKDM AAPGTSSVPA 
    PTAGNAEKLE IAKRLALRIN AQKNLGIESQ VDVMQQATNA ILRGGTILAP TVSAKTIAEQ 
    LAEKINAKLN YVPLEKQEEE RQDGGQNESF KRYEEELEIN DFPQTARWKV TSKEALQRIS 
    EYSEAAITIR GTYFPPGKEP KEGERKIYLA IESANELAVQ KAKAEITRLI KEELIRLQNS 
    YQPTNKGRYK VL

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.