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Q9UMR2

- DD19B_HUMAN

UniProt

Q9UMR2 - DD19B_HUMAN

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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

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
Complete GO annotation...

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 pore Source: ProtInc
Complete GO annotation...

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

BgeeiQ9UMR2.
CleanExiHS_DDX19B.
ExpressionAtlasiQ9UMR2. baseline and differential.
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. 85 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 – 6611Combined sources
Helixi67 – 704Combined sources
Helixi76 – 805Combined sources
Beta strandi82 – 865Combined sources
Helixi95 – 973Combined sources
Helixi101 – 1099Combined sources
Helixi117 – 12711Combined sources
Beta strandi128 – 1303Combined sources
Beta strandi134 – 1374Combined sources
Helixi144 – 15512Combined sources
Beta strandi165 – 1684Combined sources
Helixi172 – 18514Combined sources
Turni186 – 1883Combined sources
Beta strandi194 – 1974Combined sources
Beta strandi212 – 2165Combined sources
Helixi218 – 2258Combined sources
Turni226 – 2283Combined sources
Helixi233 – 2353Combined sources
Beta strandi238 – 2425Combined sources
Helixi244 – 2485Combined sources
Turni250 – 2534Combined sources
Helixi254 – 2629Combined sources
Beta strandi269 – 2757Combined sources
Helixi279 – 28810Combined sources
Beta strandi289 – 2913Combined sources
Beta strandi293 – 2953Combined sources
Helixi299 – 3013Combined sources
Helixi304 – 3063Combined sources
Beta strandi307 – 3137Combined sources
Helixi317 – 33115Combined sources
Beta strandi332 – 3398Combined sources
Helixi343 – 35513Combined sources
Beta strandi361 – 3633Combined sources
Helixi369 – 38012Combined sources
Beta strandi385 – 3895Combined sources
Helixi391 – 3933Combined sources
Beta strandi394 – 3963Combined sources
Beta strandi402 – 4098Combined sources
Beta strandi414 – 4185Combined sources
Helixi420 – 4278Combined sources
Beta strandi437 – 4437Combined sources
Helixi446 – 45914Combined sources

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.
GeneTreeiENSGT00530000063236.
HOGENOMiHOG000268797.
HOVERGENiHBG107989.
InParanoidiQ9UMR2.
PhylomeDBiQ9UMR2.
TreeFamiTF314957.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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

        10         20         30         40         50
MATDSWALAV DEQEAAAESL SNLHLKEEKI KPDTNGAVVK TNANAEKTDE
60 70 80 90 100
EEKEDRAAQS LLNKLIRSNL VDNTNQVEVL QRDPNSPLYS VKSFEELRLK
110 120 130 140 150
PQLLQGVYAM GFNRPSKIQE NALPLMLAEP PQNLIAQSQS GTGKTAAFVL
160 170 180 190 200
AMLSQVEPAN KYPQCLCLSP TYELALQTGK VIEQMGKFYP ELKLAYAVRG
210 220 230 240 250
NKLERGQKIS EQIVIGTPGT VLDWCSKLKF IDPKKIKVFV LDEADVMIAT
260 270 280 290 300
QGHQDQSIRI QRMLPRNCQM LLFSATFEDS VWKFAQKVVP DPNVIKLKRE
310 320 330 340 350
EETLDTIKQY YVLCSSRDEK FQALCNLYGA ITIAQAMIFC HTRKTASWLA
360 370 380 390 400
AELSKEGHQV ALLSGEMMVE QRAAVIERFR EGKEKVLVTT NVCARGIDVE
410 420 430 440 450
QVSVVINFDL PVDKDGNPDN ETYLHRIGRT GRFGKRGLAV NMVDSKHSMN
460 470
ILNRIQEHFN KKIERLDTDD LDEIEKIAN
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. 85 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.
GeneTreei ENSGT00530000063236.
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

Bgeei Q9UMR2.
CleanExi HS_DDX19B.
ExpressionAtlasi Q9UMR2. baseline and differential.
Genevestigatori Q9UMR2.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011545. DEAD/DEAH_box_helicase_dom.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 138 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