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Q9UMR2

- DD19B_HUMAN

UniProt

Q9UMR2 - DD19B_HUMAN

Protein

ATP-dependent RNA helicase DDX19B

Gene

DDX19B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19B functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins.

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei119 – 1191ATP
    Binding sitei429 – 4291ATP
    Binding sitei432 – 4321ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi138 – 1458ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. helicase activity Source: ProtInc
    3. RNA binding Source: ProtInc

    GO - Biological processi

    1. mRNA export from nucleus Source: ProtInc
    2. protein transport Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    mRNA transport, Protein transport, Translocation, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent RNA helicase DDX19B (EC:3.6.4.13)
    Alternative name(s):
    DEAD box RNA helicase DEAD5
    DEAD box protein 19B
    Gene namesi
    Name:DDX19B
    Synonyms:DBP5, DDX19, TDBP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:2742. DDX19B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB
    4. nuclear envelope Source: UniProtKB
    5. nuclear membrane Source: UniProtKB-SubCell
    6. nuclear pore Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nuclear pore complex, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi223 – 2231D → R: Impairs interaction with NUP214 and RNA. 1 Publication
    Mutagenesisi243 – 2431E → Q: Loss of activity. 1 Publication
    Mutagenesisi258 – 2581I → A: Impairs interaction with NUP214. 1 Publication
    Mutagenesisi259 – 2591R → D: Impairs interaction with NUP214. 1 Publication
    Mutagenesisi262 – 2621R → A: Impairs interaction with NUP214. 1 Publication

    Organism-specific databases

    PharmGKBiPA27208.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 479478ATP-dependent RNA helicase DDX19BPRO_0000055022Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9UMR2.
    PaxDbiQ9UMR2.
    PRIDEiQ9UMR2.

    PTM databases

    PhosphoSiteiQ9UMR2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UMR2.
    BgeeiQ9UMR2.
    CleanExiHS_DDX19B.
    GenevestigatoriQ9UMR2.

    Organism-specific databases

    HPAiCAB037229.
    CAB037284.
    HPA046380.

    Interactioni

    Subunit structurei

    Interacts with NUP214 or RNA in a mutually exclusive manner.3 Publications

    Protein-protein interaction databases

    BioGridi116426. 14 interactions.
    DIPiDIP-48486N.
    IntActiQ9UMR2. 13 interactions.
    MINTiMINT-4831823.
    STRINGi9606.ENSP00000288071.

    Structurei

    Secondary structure

    1
    479
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi56 – 6611
    Helixi67 – 704
    Helixi76 – 805
    Beta strandi82 – 865
    Helixi95 – 973
    Helixi101 – 1099
    Helixi117 – 12711
    Beta strandi128 – 1303
    Beta strandi134 – 1374
    Helixi144 – 15512
    Beta strandi165 – 1684
    Helixi172 – 18514
    Turni186 – 1883
    Beta strandi194 – 1974
    Beta strandi212 – 2165
    Helixi218 – 2258
    Turni226 – 2283
    Helixi233 – 2353
    Beta strandi238 – 2425
    Helixi244 – 2485
    Turni250 – 2534
    Helixi254 – 2629
    Beta strandi269 – 2757
    Helixi279 – 28810
    Beta strandi289 – 2913
    Beta strandi293 – 2953
    Helixi299 – 3013
    Helixi304 – 3063
    Beta strandi307 – 3137
    Helixi317 – 33115
    Beta strandi332 – 3398
    Helixi343 – 35513
    Beta strandi361 – 3633
    Helixi369 – 38012
    Beta strandi385 – 3895
    Helixi391 – 3933
    Beta strandi394 – 3963
    Beta strandi402 – 4098
    Beta strandi414 – 4185
    Helixi420 – 4278
    Beta strandi437 – 4437
    Helixi446 – 45914

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EWSX-ray2.70A/B54-475[»]
    3FHCX-ray2.80B68-302[»]
    3FHTX-ray2.20A/B68-479[»]
    3FMOX-ray2.51B1-300[»]
    3FMPX-ray3.19B/D1-479[»]
    3G0HX-ray2.70A54-475[»]
    ProteinModelPortaliQ9UMR2.
    SMRiQ9UMR2. Positions 60-467.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UMR2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini125 – 295171Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini306 – 474169Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 300299N-terminal lobeAdd
    BLAST
    Regioni55 – 6814N-terminal helixAdd
    BLAST
    Regioni301 – 479179C-terminal lobeAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi92 – 12029Q motifAdd
    BLAST
    Motifi242 – 2454DEAD box

    Domaini

    The N-terminal extension helix acts as an autoinhibitory domain, preventing ATP hydrolysis, unless the N-terminus of the protein is displaced by RNA binding, allowing cleft closure to bring key side chains into position for catalysis.

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0513.
    HOGENOMiHOG000268797.
    HOVERGENiHBG107989.
    InParanoidiQ9UMR2.
    PhylomeDBiQ9UMR2.
    TreeFamiTF314957.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UMR2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MATDSWALAV DEQEAAAESL SNLHLKEEKI KPDTNGAVVK TNANAEKTDE    50
    EEKEDRAAQS LLNKLIRSNL VDNTNQVEVL QRDPNSPLYS VKSFEELRLK 100
    PQLLQGVYAM GFNRPSKIQE NALPLMLAEP PQNLIAQSQS GTGKTAAFVL 150
    AMLSQVEPAN KYPQCLCLSP TYELALQTGK VIEQMGKFYP ELKLAYAVRG 200
    NKLERGQKIS EQIVIGTPGT VLDWCSKLKF IDPKKIKVFV LDEADVMIAT 250
    QGHQDQSIRI QRMLPRNCQM LLFSATFEDS VWKFAQKVVP DPNVIKLKRE 300
    EETLDTIKQY YVLCSSRDEK FQALCNLYGA ITIAQAMIFC HTRKTASWLA 350
    AELSKEGHQV ALLSGEMMVE QRAAVIERFR EGKEKVLVTT NVCARGIDVE 400
    QVSVVINFDL PVDKDGNPDN ETYLHRIGRT GRFGKRGLAV NMVDSKHSMN 450
    ILNRIQEHFN KKIERLDTDD LDEIEKIAN 479
    Length:479
    Mass (Da):53,927
    Last modified:May 1, 2000 - v1
    Checksum:i8F6F93B12B7E9871
    GO
    Isoform 2 (identifier: Q9UMR2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         100-130: Missing.

    Show »
    Length:448
    Mass (Da):50,490
    Checksum:i178321CBF4CA276A
    GO
    Isoform 3 (identifier: Q9UMR2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-109: Missing.

    Show »
    Length:371
    Mass (Da):41,911
    Checksum:i0BA1AD0FFF915AED
    GO
    Isoform 4 (identifier: Q9UMR2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-19: ATDSWALAVDEQEAAAES → MAGAAGRVQDRALRRFPITLPVGD
         100-130: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:454
    Mass (Da):51,194
    Checksum:iA1A34DAB7C730309
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti128 – 1281A → V in CAG33496. 1 PublicationCurated
    Sequence conflicti201 – 2011N → Y in BAG63488. (PubMed:14702039)Curated
    Sequence conflicti331 – 3311I → T in CAG33496. 1 PublicationCurated
    Sequence conflicti367 – 3671M → V in CAG38540. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti149 – 1491V → L.
    Corresponds to variant rs34607244 [ dbSNP | Ensembl ].
    VAR_052160

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 109108Missing in isoform 3. 3 PublicationsVSP_041347Add
    BLAST
    Alternative sequencei2 – 1918ATDSW…AAAES → MAGAAGRVQDRALRRFPITL PVGD in isoform 4. 1 PublicationVSP_044727Add
    BLAST
    Alternative sequencei100 – 13031Missing in isoform 2 and isoform 4. 3 PublicationsVSP_015239Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ237946 mRNA. Translation: CAB52189.1.
    AF353720 mRNA. Translation: AAK40102.1.
    AL136639 mRNA. Translation: CAB66574.1.
    CR457215 mRNA. Translation: CAG33496.1.
    CR533509 mRNA. Translation: CAG38540.1.
    AK027378 mRNA. Translation: BAG51311.1.
    AK301938 mRNA. Translation: BAG63358.1.
    AK302107 mRNA. Translation: BAG63488.1.
    AK316346 mRNA. Translation: BAH14717.1.
    AC012184 Genomic DNA. No translation available.
    CH471241 Genomic DNA. Translation: EAW51827.1.
    CH471241 Genomic DNA. Translation: EAW51831.1.
    CH471241 Genomic DNA. Translation: EAW51832.1.
    CH471241 Genomic DNA. Translation: EAW51834.1.
    BC003626 mRNA. Translation: AAH03626.1.
    BC010008 mRNA. Translation: AAH10008.1.
    CCDSiCCDS10888.1. [Q9UMR2-1]
    CCDS32475.1. [Q9UMR2-2]
    RefSeqiNP_001014449.1. NM_001014449.2.
    NP_001014451.1. NM_001014451.2. [Q9UMR2-2]
    NP_001244101.1. NM_001257172.1.
    NP_001244102.1. NM_001257173.1.
    NP_001244103.1. NM_001257174.1.
    NP_009173.1. NM_007242.5. [Q9UMR2-1]
    XP_006721190.1. XM_006721127.1.
    UniGeneiHs.221761.

    Genome annotation databases

    EnsembliENST00000288071; ENSP00000288071; ENSG00000157349. [Q9UMR2-1]
    ENST00000355992; ENSP00000348271; ENSG00000157349. [Q9UMR2-2]
    GeneIDi11269.
    KEGGihsa:11269.
    UCSCiuc002eyo.4. human. [Q9UMR2-1]
    uc002eyp.4. human. [Q9UMR2-2]

    Polymorphism databases

    DMDMi10719979.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ237946 mRNA. Translation: CAB52189.1 .
    AF353720 mRNA. Translation: AAK40102.1 .
    AL136639 mRNA. Translation: CAB66574.1 .
    CR457215 mRNA. Translation: CAG33496.1 .
    CR533509 mRNA. Translation: CAG38540.1 .
    AK027378 mRNA. Translation: BAG51311.1 .
    AK301938 mRNA. Translation: BAG63358.1 .
    AK302107 mRNA. Translation: BAG63488.1 .
    AK316346 mRNA. Translation: BAH14717.1 .
    AC012184 Genomic DNA. No translation available.
    CH471241 Genomic DNA. Translation: EAW51827.1 .
    CH471241 Genomic DNA. Translation: EAW51831.1 .
    CH471241 Genomic DNA. Translation: EAW51832.1 .
    CH471241 Genomic DNA. Translation: EAW51834.1 .
    BC003626 mRNA. Translation: AAH03626.1 .
    BC010008 mRNA. Translation: AAH10008.1 .
    CCDSi CCDS10888.1. [Q9UMR2-1 ]
    CCDS32475.1. [Q9UMR2-2 ]
    RefSeqi NP_001014449.1. NM_001014449.2.
    NP_001014451.1. NM_001014451.2. [Q9UMR2-2 ]
    NP_001244101.1. NM_001257172.1.
    NP_001244102.1. NM_001257173.1.
    NP_001244103.1. NM_001257174.1.
    NP_009173.1. NM_007242.5. [Q9UMR2-1 ]
    XP_006721190.1. XM_006721127.1.
    UniGenei Hs.221761.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EWS X-ray 2.70 A/B 54-475 [» ]
    3FHC X-ray 2.80 B 68-302 [» ]
    3FHT X-ray 2.20 A/B 68-479 [» ]
    3FMO X-ray 2.51 B 1-300 [» ]
    3FMP X-ray 3.19 B/D 1-479 [» ]
    3G0H X-ray 2.70 A 54-475 [» ]
    ProteinModelPortali Q9UMR2.
    SMRi Q9UMR2. Positions 60-467.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116426. 14 interactions.
    DIPi DIP-48486N.
    IntActi Q9UMR2. 13 interactions.
    MINTi MINT-4831823.
    STRINGi 9606.ENSP00000288071.

    PTM databases

    PhosphoSitei Q9UMR2.

    Polymorphism databases

    DMDMi 10719979.

    Proteomic databases

    MaxQBi Q9UMR2.
    PaxDbi Q9UMR2.
    PRIDEi Q9UMR2.

    Protocols and materials databases

    DNASUi 11269.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000288071 ; ENSP00000288071 ; ENSG00000157349 . [Q9UMR2-1 ]
    ENST00000355992 ; ENSP00000348271 ; ENSG00000157349 . [Q9UMR2-2 ]
    GeneIDi 11269.
    KEGGi hsa:11269.
    UCSCi uc002eyo.4. human. [Q9UMR2-1 ]
    uc002eyp.4. human. [Q9UMR2-2 ]

    Organism-specific databases

    CTDi 11269.
    GeneCardsi GC16P070328.
    HGNCi HGNC:2742. DDX19B.
    HPAi CAB037229.
    CAB037284.
    HPA046380.
    MIMi 605812. gene.
    neXtProti NX_Q9UMR2.
    PharmGKBi PA27208.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0513.
    HOGENOMi HOG000268797.
    HOVERGENi HBG107989.
    InParanoidi Q9UMR2.
    PhylomeDBi Q9UMR2.
    TreeFami TF314957.

    Miscellaneous databases

    ChiTaRSi DDX19B. human.
    EvolutionaryTracei Q9UMR2.
    GeneWikii DDX19B.
    GenomeRNAii 11269.
    NextBioi 42879.
    PROi Q9UMR2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UMR2.
    Bgeei Q9UMR2.
    CleanExi HS_DDX19B.
    Genevestigatori Q9UMR2.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p."
      Schmitt C., von Kobbe C., Bachi A., Pante N., Rodrigues J.P., Boscheron C., Rigaut G., Wilm M., Seraphin B., Carmo-Fonseca M., Izaurralde E.
      EMBO J. 18:4332-4347(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, MUTAGENESIS OF GLU-243.
    2. "Identification and characterization of a gene coding a novel isoform of DEAD-box protein."
      Yin L., Li J., Zhu H., Lin M., Cheng L., Wang Y., Zhou Z., Sha J.
      Reprod. Fertil. Dev. 14:185-189(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
      Tissue: Mammary gland, Stomach and Testis.
    6. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Ovary and Skin.
    9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 54-475 ALONE AND IN COMPLEX WITH RNA, REGULATION BY N-TERMINAL HELIX DOMAIN.
    11. "The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner."
      von Moeller H., Basquin C., Conti E.
      Nat. Struct. Mol. Biol. 16:247-254(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 68-479 IN COMPLEX WITH NUP214 AND ATP ANALOG, ATP-BINDING SITES, MUTAGENESIS OF ASP-223; ILE-258; ARG-259 AND ARG-262.
    12. "Structural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19."
      Napetschnig J., Kassube S.A., Debler E.W., Wong R.W., Blobel G., Hoelz A.
      Proc. Natl. Acad. Sci. U.S.A. 106:3089-3094(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 1-300 IN COMPLEX WITH NUP214 AND ADP.

    Entry informationi

    Entry nameiDD19B_HUMAN
    AccessioniPrimary (citable) accession number: Q9UMR2
    Secondary accession number(s): B3KNE9
    , B4DXS6, E7EMK4, Q6FIB7, Q6IAE0, Q96KE7, Q9H0U0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 137 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3