Q9UMR2 (DD19B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	DDX19B
Synonyms:	DBP5, DDX19, TDBP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	479 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	ATP + H2O = ADP + phosphate.
Subunit structure	Interacts with NUP214 or RNA in a mutually exclusive manner.
Subcellular location	Cytoplasm. Nucleus › nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note: Nuclear pore complex cytoplasmic fibrils.
Domain	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. Ref.9
Sequence similarities	Belongs to the DEAD box helicase family. DDX19/DBP5 subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport mRNA transport
Cellular component	Cytoplasm Membrane Nuclear pore complex Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA export from nucleus Traceable author statement Ref.1. Source: ProtInc protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Traceable author statement Ref.1. Source: ProtInc nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear pore Traceable author statement Ref.1. Source: ProtInc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro RNA binding Traceable author statement Ref.1. Source: ProtInc helicase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UMR2-1)

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.

Isoform 2 (identifier: Q9UMR2-2)

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

Isoform 3 (identifier: Q9UMR2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-109: Missing.

Isoform 4 (identifier: Q9UMR2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MATDSWALAVDEQEAAAES → MAGAAGRVQDRALRRFPITLPVGD
     100-130: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 479

479

ATP-dependent RNA helicase DDX19B

PRO_0000055022

Regions

Domain

125 – 295

171

Helicase ATP-binding

Domain

306 – 474

169

Helicase C-terminal

Nucleotide binding

138 – 145

8

ATP

Region

1 – 300

300

N-terminal lobe

Region

55 – 68

14

N-terminal helix

Region

301 – 479

179

C-terminal lobe

Motif

92 – 120

29

Q motif

Motif

242 – 245

4

DEAD box

Sites

Binding site

119

1

ATP

Binding site

429

1

ATP

Binding site

432

1

ATP

Natural variations

Alternative sequence

1 – 109

109

Missing in isoform 3.

VSP_041347

Alternative sequence

1 – 19

19

MATDS…AAAES → MAGAAGRVQDRALRRFPITL PVGD in isoform 4.

VSP_044727

Alternative sequence

100 – 130

31

Missing in isoform 2 and isoform 4.

VSP_015239

Natural variant

149

1

V → L.
Corresponds to variant rs34607244 [ dbSNP | Ensembl ].

VAR_052160

Experimental info

Mutagenesis

223

1

D → R: Impairs interaction with NUP214 and RNA. Ref.10

Mutagenesis

243

1

E → Q: Loss of activity. Ref.1

Mutagenesis

258

1

I → A: Impairs interaction with NUP214. Ref.10

Mutagenesis

259

1

R → D: Impairs interaction with NUP214. Ref.10

Mutagenesis

262

1

R → A: Impairs interaction with NUP214. Ref.10

Sequence conflict

128

1

A → V in CAG33496. Ref.4

Sequence conflict

201

1

N → Y in BAG63488. Ref.5

Sequence conflict

331

1

I → T in CAG33496. Ref.4

Sequence conflict

367

1

M → V in CAG38540. Ref.4

Secondary structure

1

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479

Helix Strand Turn

Details...

Helix

56 – 66

11

Helix

67 – 70

4

Helix

76 – 80

5

Beta strand

82 – 86

5

Helix

95 – 97

3

Helix

101 – 109

9

Helix

117 – 127

11

Beta strand

128 – 130

3

Beta strand

134 – 137

4

Helix

144 – 155

12

Beta strand

165 – 168

4

Helix

172 – 185

14

Turn

186 – 188

3

Beta strand

194 – 197

4

Beta strand

212 – 216

5

Helix

218 – 225

8

Turn

226 – 228

3

Helix

233 – 235

3

Beta strand

238 – 242

5

Helix

244 – 248

5

Turn

250 – 253

4

Helix

254 – 262

9

Beta strand

269 – 275

7

Helix

279 – 288

10

Beta strand

289 – 291

3

Beta strand

293 – 295

3

Helix

299 – 301

3

Helix

304 – 306

3

Beta strand

307 – 313

7

Helix

317 – 331

15

Beta strand

332 – 339

8

Helix

343 – 355

13

Beta strand

361 – 363

3

Helix

369 – 380

12

Beta strand

385 – 389

5

Helix

391 – 393

3

Beta strand

394 – 396

3

Beta strand

402 – 409

8

Beta strand

414 – 418

5

Helix

420 – 427

8

Beta strand

437 – 443

7

Helix

446 – 459

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 8F6F93B12B7E9871	FASTA	479	53,927
	10 20 30 40 50 60 MATDSWALAV DEQEAAAESL SNLHLKEEKI KPDTNGAVVK TNANAEKTDE EEKEDRAAQS 70 80 90 100 110 120 LLNKLIRSNL VDNTNQVEVL QRDPNSPLYS VKSFEELRLK PQLLQGVYAM GFNRPSKIQE 130 140 150 160 170 180 NALPLMLAEP PQNLIAQSQS GTGKTAAFVL AMLSQVEPAN KYPQCLCLSP TYELALQTGK 190 200 210 220 230 240 VIEQMGKFYP ELKLAYAVRG NKLERGQKIS EQIVIGTPGT VLDWCSKLKF IDPKKIKVFV 250 260 270 280 290 300 LDEADVMIAT QGHQDQSIRI QRMLPRNCQM LLFSATFEDS VWKFAQKVVP DPNVIKLKRE 310 320 330 340 350 360 EETLDTIKQY YVLCSSRDEK FQALCNLYGA ITIAQAMIFC HTRKTASWLA AELSKEGHQV 370 380 390 400 410 420 ALLSGEMMVE QRAAVIERFR EGKEKVLVTT NVCARGIDVE QVSVVINFDL PVDKDGNPDN 430 440 450 460 470 ETYLHRIGRT GRFGKRGLAV NMVDSKHSMN ILNRIQEHFN KKIERLDTDD LDEIEKIAN
	Isoform 2 [UniParc]. Checksum: 178321CBF4CA276A	FASTA	448	50,490
	10 20 30 40 50 60 MATDSWALAV DEQEAAAESL SNLHLKEEKI KPDTNGAVVK TNANAEKTDE EEKEDRAAQS 70 80 90 100 110 120 LLNKLIRSNL VDNTNQVEVL QRDPNSPLYS VKSFEELRLP QNLIAQSQSG TGKTAAFVLA 130 140 150 160 170 180 MLSQVEPANK YPQCLCLSPT YELALQTGKV IEQMGKFYPE LKLAYAVRGN KLERGQKISE 190 200 210 220 230 240 QIVIGTPGTV LDWCSKLKFI DPKKIKVFVL DEADVMIATQ GHQDQSIRIQ RMLPRNCQML 250 260 270 280 290 300 LFSATFEDSV WKFAQKVVPD PNVIKLKREE ETLDTIKQYY VLCSSRDEKF QALCNLYGAI 310 320 330 340 350 360 TIAQAMIFCH TRKTASWLAA ELSKEGHQVA LLSGEMMVEQ RAAVIERFRE GKEKVLVTTN 370 380 390 400 410 420 VCARGIDVEQ VSVVINFDLP VDKDGNPDNE TYLHRIGRTG RFGKRGLAVN MVDSKHSMNI 430 440 LNRIQEHFNK KIERLDTDDL DEIEKIAN
	Isoform 3 [UniParc]. Checksum: A268A0E259FCF3E2	FASTA	370	41,779
	10 20 30 40 50 60 MGFNRPSKIQ ENALPLMLAE PPQNLIAQSQ SGTGKTAAFV LAMLSQVEPA NKYPQCLCLS 70 80 90 100 110 120 PTYELALQTG KVIEQMGKFY PELKLAYAVR GNKLERGQKI SEQIVIGTPG TVLDWCSKLK 130 140 150 160 170 180 FIDPKKIKVF VLDEADVMIA TQGHQDQSIR IQRMLPRNCQ MLLFSATFED SVWKFAQKVV 190 200 210 220 230 240 PDPNVIKLKR EEETLDTIKQ YYVLCSSRDE KFQALCNLYG AITIAQAMIF CHTRKTASWL 250 260 270 280 290 300 AAELSKEGHQ VALLSGEMMV EQRAAVIERF REGKEKVLVT TNVCARGIDV EQVSVVINFD 310 320 330 340 350 360 LPVDKDGNPD NETYLHRIGR TGRFGKRGLA VNMVDSKHSM NILNRIQEHF NKKIERLDTD 370 DLDEIEKIAN
	Isoform 4 [UniParc]. Checksum: 6D543611ED7E4BFE	FASTA	453	51,063
	10 20 30 40 50 60 MAGAAGRVQD RALRRFPITL PVGDLSNLHL KEEKIKPDTN GAVVKTNANA EKTDEEEKED 70 80 90 100 110 120 RAAQSLLNKL IRSNLVDNTN QVEVLQRDPN SPLYSVKSFE ELRLPQNLIA QSQSGTGKTA 130 140 150 160 170 180 AFVLAMLSQV EPANKYPQCL CLSPTYELAL QTGKVIEQMG KFYPELKLAY AVRGNKLERG 190 200 210 220 230 240 QKISEQIVIG TPGTVLDWCS KLKFIDPKKI KVFVLDEADV MIATQGHQDQ SIRIQRMLPR 250 260 270 280 290 300 NCQMLLFSAT FEDSVWKFAQ KVVPDPNVIK LKREEETLDT IKQYYVLCSS RDEKFQALCN 310 320 330 340 350 360 LYGAITIAQA MIFCHTRKTA SWLAAELSKE GHQVALLSGE MMVEQRAAVI ERFREGKEKV 370 380 390 400 410 420 LVTTNVCARG IDVEQVSVVI NFDLPVDKDG NPDNETYLHR IGRTGRFGKR GLAVNMVDSK 430 440 450 HSMNILNRIQ EHFNKKIERL DTDDLDEIEK IAN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"The DEXD/H-box RNA helicase DDX19 is regulated by an alpha-helical switch." Collins R., Karlberg T., Lehtio L., Schutz P., van den Berg S., Dahlgren L.G., Hammarstrom M., Weigelt J., Schuler H. J. Biol. Chem. 284:10296-10300(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 54-475 ALONE AND IN COMPLEX WITH RNA, REGULATION BY N-TERMINAL HELIX DOMAIN.
[10]	"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.
[11]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00008943.
IPI00027599.
IPI00556368.
IPI00939593.

RefSeq

NP_001014449.1. NM_001014449.2.
NP_001014451.1. NM_001014451.2.
NP_001244101.1. NM_001257172.1.
NP_001244102.1. NM_001257173.1.
NP_001244103.1. NM_001257174.1.
NP_009173.1. NM_007242.5.

UniGene

Hs.221761.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9UMR2.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48486N.

IntAct

Q9UMR2. 11 interactions.

MINT

MINT-4831823.

STRING

9606.ENSP00000288071.

PTM databases

PhosphoSite

Q9UMR2.

Polymorphism databases

DMDM

10719979.

Proteomic databases

PaxDb

Q9UMR2.

PRIDE

Q9UMR2.

Protocols and materials databases

DNASU

11269.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000288071; ENSP00000288071; ENSG00000157349.
ENST00000355992; ENSP00000348271; ENSG00000157349.
ENST00000393657; ENSP00000377267; ENSG00000157349.
ENST00000451014; ENSP00000392639; ENSG00000157349.
ENST00000563392; ENSP00000456574; ENSG00000157349.
ENST00000568625; ENSP00000456757; ENSG00000157349.

GeneID

11269.

KEGG

hsa:11269.

UCSC

uc002eyo.3. human.
uc002eyp.3. human.
uc010vlv.2. human.

Organism-specific databases

CTD

11269.

GeneCards

GC16P070328.

HGNC

HGNC:2742. DDX19B.

HPA

CAB037284.

MIM

605812. gene.

neXtProt

NX_Q9UMR2.

PharmGKB

PA27208.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0513.

HOGENOM

HOG000268797.

HOVERGEN

HBG107989.

InParanoid

Q9UMR2.

OMA

HETIFEV.

OrthoDB

EOG46MBJK.

PhylomeDB

Q9UMR2.

Gene expression databases

ArrayExpress

Q9UMR2.

Bgee

Q9UMR2.

CleanEx

HS_DDX19B.

Genevestigator

Q9UMR2.

GermOnline

ENSG00000157349. Homo sapiens.

Family and domain databases

InterPro

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]

Pfam

PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

SUPFAM

SSF52540. SSF52540. 1 hit.

PROSITE

PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DDX19B. human.

EvolutionaryTrace

Q9UMR2.

GenomeRNAi

11269.

NextBio

42879.

SOURCE

Search...

Entry information

Entry name

DD19B_HUMAN

Accession

Primary (citable) accession number: Q9UMR2
Secondary accession number(s): B3KNE9 , B4DXS6, E7EMK4, Q6FIB7, Q6IAE0, Q96KE7, Q9H0U0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.