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Protein

Probable ATP-dependent RNA helicase DDX4

Gene

DDX4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable ATP-dependent RNA helicase required during spermatogenesis (PubMed:10920202, PubMed:21034600). Required to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle (By similarity).By similarity2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi332 – 3398ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Helicase, Hydrolase

Keywords - Biological processi

Differentiation, Meiosis, RNA-mediated gene silencing, Spermatogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.4.13. 2681.
ReactomeiR-HSA-5601884. PIWI-interacting RNA (piRNA) biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ATP-dependent RNA helicase DDX4 (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 4
Vasa homolog
Gene namesi
Name:DDX4
Synonyms:VASA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:18700. DDX4.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmperinuclear region By similarity

  • Note: Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis.By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • perinuclear region of cytoplasm Source: GO_Central
  • P granule Source: GO_Central
  • pi-body Source: UniProtKB
  • piP-body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38646.

Polymorphism and mutation databases

BioMutaiDDX4.
DMDMi20138033.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 724724Probable ATP-dependent RNA helicase DDX4PRO_0000054977Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei222 – 2221PhosphoserineBy similarity
Modified residuei226 – 2261PhosphoserineBy similarity
Modified residuei722 – 7221PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NQI0.
MaxQBiQ9NQI0.
PaxDbiQ9NQI0.
PRIDEiQ9NQI0.

2D gel databases

REPRODUCTION-2DPAGEIPI00456933.

PTM databases

iPTMnetiQ9NQI0.
PhosphoSiteiQ9NQI0.

Expressioni

Tissue specificityi

Expressed only in ovary and testis. Expressed in migratory primordial germ cells in the region of the gonadal ridge in both sexes.1 Publication

Gene expression databases

BgeeiQ9NQI0.
CleanExiHS_DDX4.
ExpressionAtlasiQ9NQI0. baseline and differential.
GenevisibleiQ9NQI0. HS.

Organism-specific databases

HPAiCAB026170.
HPA037763.
HPA037764.

Interactioni

Subunit structurei

Found in a mRNP complex, at least composed of TDRD1, TDRD6, TDRD7 and DDX4. N-terminus interacts with RANBP9. Interacts with PIWIL2 and MAEL. Interacts with ARNTL/BMAL1 and CLOCK.By similarity

Protein-protein interaction databases

BioGridi120009. 9 interactions.
IntActiQ9NQI0. 3 interactions.
MINTiMINT-3072085.
STRINGi9606.ENSP00000424838.

Structurei

3D structure databases

ProteinModelPortaliQ9NQI0.
SMRiQ9NQI0. Positions 246-675.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini319 – 502184Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini530 – 675146Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi288 – 31629Q motifAdd
BLAST
Motifi446 – 4494DEAD box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi58 – 234177Gly-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0335. Eukaryota.
ENOG410XNTI. LUCA.
GeneTreeiENSGT00770000120531.
HOGENOMiHOG000268804.
HOVERGENiHBG015893.
InParanoidiQ9NQI0.
KOiK13982.
OMAiMQSNSRN.
OrthoDBiEOG7B5WV8.
PhylomeDBiQ9NQI0.
TreeFamiTF300364.

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.
IPR000629. RNA-helicase_DEAD-box_CS.
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. 2 hits.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NQI0-1) [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
MGDEDWEAEI NPHMSSYVPI FEKDRYSGEN GDNFNRTPAS SSEMDDGPSR
60 70 80 90 100
RDHFMKSGFA SGRNFGNRDA GECNKRDNTS TMGGFGVGKS FGNRGFSNSR
110 120 130 140 150
FEDGDSSGFW RESSNDCEDN PTRNRGFSKR GGYRDGNNSE ASGPYRRGGR
160 170 180 190 200
GSFRGCRGGF GLGSPNNDLD PDECMQRTGG LFGSRRPVLS GTGNGDTSQS
210 220 230 240 250
RSGSGSERGG YKGLNEEVIT GSGKNSWKSE AEGGESSDTQ GPKVTYIPPP
260 270 280 290 300
PPEDEDSIFA HYQTGINFDK YDTILVEVSG HDAPPAILTF EEANLCQTLN
310 320 330 340 350
NNIAKAGYTK LTPVQKYSIP IILAGRDLMA CAQTGSGKTA AFLLPILAHM
360 370 380 390 400
MHDGITASRF KELQEPECII VAPTRELVNQ IYLEARKFSF GTCVRAVVIY
410 420 430 440 450
GGTQLGHSIR QIVQGCNILC ATPGRLMDII GKEKIGLKQI KYLVLDEADR
460 470 480 490 500
MLDMGFGPEM KKLISCPGMP SKEQRQTLMF SATFPEEIQR LAAEFLKSNY
510 520 530 540 550
LFVAVGQVGG ACRDVQQTVL QVGQFSKREK LVEILRNIGD ERTMVFVETK
560 570 580 590 600
KKADFIATFL CQEKISTTSI HGDREQRERE QALGDFRFGK CPVLVATSVA
610 620 630 640 650
ARGLDIENVQ HVINFDLPST IDEYVHRIGR TGRCGNTGRA ISFFDLESDN
660 670 680 690 700
HLAQPLVKVL TDAQQDVPAW LEEIAFSTYI PGFSGSTRGN VFASVDTRKG
710 720
KSTLNTAGFS SSQAPNPVDD ESWD
Length:724
Mass (Da):79,308
Last modified:January 23, 2002 - v2
Checksum:i6D313DD98B177067
GO
Isoform 2 (identifier: Q9NQI0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     132-166: GYRDGNNSEASGPYRRGGRGSFRGCRGGFGLGSPN → D

Note: No experimental confirmation available.
Show »
Length:690
Mass (Da):75,821
Checksum:i8D37259B5DED0EBD
GO
Isoform 3 (identifier: Q9NQI0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-111: MGDEDWEAEI...EDGDSSGFWR → MGSRNLFLTNSP
     132-166: GYRDGNNSEASGPYRRGGRGSFRGCRGGFGLGSPN → D
     209-225: GGYKGLNEEVITGSGKN → D

Note: No experimental confirmation available.
Show »
Length:575
Mass (Da):63,211
Checksum:i04F943C83BD71828
GO
Isoform 4 (identifier: Q9NQI0-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     112-131: Missing.

Note: No experimental confirmation available. Gene prediction based on cDNA data.
Show »
Length:704
Mass (Da):77,056
Checksum:iA1A44F186461C9D6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti240 – 2401Q → R in BAG52716 (PubMed:14702039).Curated
Sequence conflicti380 – 3801Q → K in AAH47455 (PubMed:15489334).Curated
Sequence conflicti556 – 5561I → T in AAF86585 (PubMed:10920202).Curated
Sequence conflicti713 – 7131Q → R in AAF86585 (PubMed:10920202).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti148 – 1481G → D.
Corresponds to variant rs2306259 [ dbSNP | Ensembl ].
VAR_019574
Natural varianti287 – 2871I → V.
Corresponds to variant rs2305123 [ dbSNP | Ensembl ].
VAR_052159

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 111111MGDED…SGFWR → MGSRNLFLTNSP in isoform 3. 1 PublicationVSP_046132Add
BLAST
Alternative sequencei112 – 13120Missing in isoform 4. CuratedVSP_047177Add
BLAST
Alternative sequencei132 – 16635GYRDG…LGSPN → D in isoform 2 and isoform 3. 2 PublicationsVSP_011197Add
BLAST
Alternative sequencei209 – 22517GGYKG…GSGKN → D in isoform 3. 1 PublicationVSP_046133Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY004154 mRNA. Translation: AAF86585.1.
AF262962 mRNA. Translation: AAF72705.1.
AK093439 mRNA. Translation: BAG52716.1.
AK292417 mRNA. Translation: BAF85106.1.
AC016632 Genomic DNA. No translation available.
CH471123 Genomic DNA. Translation: EAW54929.1.
BC047455 mRNA. Translation: AAH47455.1.
BC088362 mRNA. Translation: AAH88362.1.
AL137462 mRNA. Translation: CAB70750.1.
CCDSiCCDS3969.1. [Q9NQI0-1]
CCDS47208.1. [Q9NQI0-2]
CCDS54854.1. [Q9NQI0-4]
CCDS54855.1. [Q9NQI0-3]
PIRiT46407.
RefSeqiNP_001136021.1. NM_001142549.1. [Q9NQI0-2]
NP_001160005.1. NM_001166533.1. [Q9NQI0-4]
NP_001160006.1. NM_001166534.1. [Q9NQI0-3]
NP_077726.1. NM_024415.2. [Q9NQI0-1]
UniGeneiHs.223581.

Genome annotation databases

EnsembliENST00000353507; ENSP00000334167; ENSG00000152670. [Q9NQI0-2]
ENST00000354991; ENSP00000347087; ENSG00000152670. [Q9NQI0-2]
ENST00000505374; ENSP00000424838; ENSG00000152670. [Q9NQI0-1]
ENST00000511853; ENSP00000423123; ENSG00000152670. [Q9NQI0-3]
ENST00000514278; ENSP00000425359; ENSG00000152670. [Q9NQI0-4]
GeneIDi54514.
KEGGihsa:54514.
UCSCiuc003jqg.5. human. [Q9NQI0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY004154 mRNA. Translation: AAF86585.1.
AF262962 mRNA. Translation: AAF72705.1.
AK093439 mRNA. Translation: BAG52716.1.
AK292417 mRNA. Translation: BAF85106.1.
AC016632 Genomic DNA. No translation available.
CH471123 Genomic DNA. Translation: EAW54929.1.
BC047455 mRNA. Translation: AAH47455.1.
BC088362 mRNA. Translation: AAH88362.1.
AL137462 mRNA. Translation: CAB70750.1.
CCDSiCCDS3969.1. [Q9NQI0-1]
CCDS47208.1. [Q9NQI0-2]
CCDS54854.1. [Q9NQI0-4]
CCDS54855.1. [Q9NQI0-3]
PIRiT46407.
RefSeqiNP_001136021.1. NM_001142549.1. [Q9NQI0-2]
NP_001160005.1. NM_001166533.1. [Q9NQI0-4]
NP_001160006.1. NM_001166534.1. [Q9NQI0-3]
NP_077726.1. NM_024415.2. [Q9NQI0-1]
UniGeneiHs.223581.

3D structure databases

ProteinModelPortaliQ9NQI0.
SMRiQ9NQI0. Positions 246-675.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120009. 9 interactions.
IntActiQ9NQI0. 3 interactions.
MINTiMINT-3072085.
STRINGi9606.ENSP00000424838.

PTM databases

iPTMnetiQ9NQI0.
PhosphoSiteiQ9NQI0.

Polymorphism and mutation databases

BioMutaiDDX4.
DMDMi20138033.

2D gel databases

REPRODUCTION-2DPAGEIPI00456933.

Proteomic databases

EPDiQ9NQI0.
MaxQBiQ9NQI0.
PaxDbiQ9NQI0.
PRIDEiQ9NQI0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000353507; ENSP00000334167; ENSG00000152670. [Q9NQI0-2]
ENST00000354991; ENSP00000347087; ENSG00000152670. [Q9NQI0-2]
ENST00000505374; ENSP00000424838; ENSG00000152670. [Q9NQI0-1]
ENST00000511853; ENSP00000423123; ENSG00000152670. [Q9NQI0-3]
ENST00000514278; ENSP00000425359; ENSG00000152670. [Q9NQI0-4]
GeneIDi54514.
KEGGihsa:54514.
UCSCiuc003jqg.5. human. [Q9NQI0-1]

Organism-specific databases

CTDi54514.
GeneCardsiDDX4.
HGNCiHGNC:18700. DDX4.
HPAiCAB026170.
HPA037763.
HPA037764.
MIMi605281. gene.
neXtProtiNX_Q9NQI0.
PharmGKBiPA38646.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0335. Eukaryota.
ENOG410XNTI. LUCA.
GeneTreeiENSGT00770000120531.
HOGENOMiHOG000268804.
HOVERGENiHBG015893.
InParanoidiQ9NQI0.
KOiK13982.
OMAiMQSNSRN.
OrthoDBiEOG7B5WV8.
PhylomeDBiQ9NQI0.
TreeFamiTF300364.

Enzyme and pathway databases

BRENDAi3.6.4.13. 2681.
ReactomeiR-HSA-5601884. PIWI-interacting RNA (piRNA) biogenesis.

Miscellaneous databases

GenomeRNAii54514.
NextBioi56900.
PROiQ9NQI0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NQI0.
CleanExiHS_DDX4.
ExpressionAtlasiQ9NQI0. baseline and differential.
GenevisibleiQ9NQI0. HS.

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.
IPR000629. RNA-helicase_DEAD-box_CS.
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. 2 hits.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human VASA gene is specifically expressed in the germ cell lineage."
    Castrillon D.H., Quade B.J., Wang T.Y., Quigley C., Crum C.P.
    Proc. Natl. Acad. Sci. U.S.A. 97:9585-9590(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "Cloning and characterization of the human VASA gene."
    Rocha D., Affara N.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "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 AND 3).
    Tissue: Testis.
  4. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 2).
    Tissue: Testis.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-724 (ISOFORM 1).
    Tissue: Testis.
  8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Spermatozoal protein profiles in male infertility with asthenozoospermia."
    Li H.J., Yu N., Zhang X.Y., Jin W., Li H.Z.
    Chin. Med. J. 123:2879-2882(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "NANOS3 function in human germ cell development."
    Julaton V.T., Reijo Pera R.A.
    Hum. Mol. Genet. 20:2238-2250(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiDDX4_HUMAN
AccessioniPrimary (citable) accession number: Q9NQI0
Secondary accession number(s): A8K8Q2
, B3KSF4, D6RDK4, E9PCD8, Q5M7Z3, Q86VX0, Q9NT92, Q9NYB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2002
Last modified: May 11, 2016
This is version 142 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.