DDX3Y_HUMAN
ID DDX3Y_HUMAN Reviewed; 660 AA.
AC O15523; B4DK29; B4DXX7; Q8IYV7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=ATP-dependent RNA helicase DDX3Y;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 3, Y-chromosomal;
GN Name=DDX3Y;
GN Synonyms=DBY {ECO:0000303|PubMed:15294876, ECO:0000303|PubMed:9381176};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9381176; DOI=10.1126/science.278.5338.675;
RA Lahn B.T., Page D.C.;
RT "Functional coherence of the human Y chromosome.";
RL Science 278:675-680(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12815422; DOI=10.1038/nature01722;
RA Skaletsky H., Kuroda-Kawaguchi T., Minx P.J., Cordum H.S., Hillier L.W.,
RA Brown L.G., Repping S., Pyntikova T., Ali J., Bieri T., Chinwalla A.,
RA Delehaunty A., Delehaunty K., Du H., Fewell G., Fulton L., Fulton R.,
RA Graves T.A., Hou S.-F., Latrielle P., Leonard S., Mardis E., Maupin R.,
RA McPherson J., Miner T., Nash W., Nguyen C., Ozersky P., Pepin K., Rock S.,
RA Rohlfing T., Scott K., Schultz B., Strong C., Tin-Wollam A., Yang S.-P.,
RA Waterston R.H., Wilson R.K., Rozen S., Page D.C.;
RT "The male-specific region of the human Y chromosome is a mosaic of discrete
RT sequence classes.";
RL Nature 423:825-837(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Testis, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=15383328; DOI=10.1016/j.yexcr.2004.07.005;
RA Sekiguchi T., Iida H., Fukumura J., Nishimoto T.;
RT "Human DDX3Y, the Y-encoded isoform of RNA helicase DDX3, rescues a hamster
RT temperature-sensitive ET24 mutant cell line with a DDX3X mutation.";
RL Exp. Cell Res. 300:213-222(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15294876; DOI=10.1093/hmg/ddh240;
RA Ditton H.J., Zimmer J., Kamp C., Rajpert-De Meyts E., Vogt P.H.;
RT "The AZFa gene DBY (DDX3Y) is widely transcribed but the protein is limited
RT to the male germ cells by translation control.";
RL Hum. Mol. Genet. 13:2333-2341(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Probable ATP-dependent RNA helicase. During immune response,
CC may enhance IFNB1 expression via IRF3/IRF7 pathway (By similarity).
CC {ECO:0000250|UniProtKB:Q62095}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15294876,
CC ECO:0000269|PubMed:15383328}. Nucleus {ECO:0000269|PubMed:15383328}.
CC Note=Shuttles between the nucleus and the cytoplasm in an XPO1-
CC dependent manner.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O15523-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15523-2; Sequence=VSP_055456;
CC Name=3;
CC IsoId=O15523-3; Sequence=VSP_055457, VSP_055458;
CC -!- TISSUE SPECIFICITY: Widely expressed at the mRNA level, with highest
CC levels in testis (PubMed:9381176). Testis-specific (at protein level).
CC Expressed predominantly in spermatogonia, but occasionally detected in
CC some pre-leptotene/leptotene spermatocytes (PubMed:15294876).
CC {ECO:0000269|PubMed:15294876, ECO:0000269|PubMed:9381176}.
CC -!- DISEASE: Note=Located in the 'azoospermia factor a' (AZFa) region on
CC chromosome Y which is deleted in Sertoli cell-only syndrome. This is an
CC infertility disorder in which no germ cells are visible in seminiferous
CC tubules leading to azoospermia.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC subfamily. {ECO:0000305}.
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DR EMBL; AF000984; AAC51831.1; -; mRNA.
DR EMBL; AF000985; AAC51832.1; -; mRNA.
DR EMBL; AK296366; BAG59041.1; -; mRNA.
DR EMBL; AK302172; BAG63539.1; -; mRNA.
DR EMBL; AC004474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034942; AAH34942.1; -; mRNA.
DR CCDS; CCDS14782.1; -. [O15523-1]
DR RefSeq; NP_001116137.1; NM_001122665.3. [O15523-1]
DR RefSeq; NP_001289481.1; NM_001302552.2. [O15523-2]
DR RefSeq; NP_004651.2; NM_004660.4. [O15523-1]
DR AlphaFoldDB; O15523; -.
DR SMR; O15523; -.
DR BioGRID; 114204; 114.
DR ELM; O15523; -.
DR IntAct; O15523; 27.
DR MINT; O15523; -.
DR GlyGen; O15523; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15523; -.
DR PhosphoSitePlus; O15523; -.
DR SwissPalm; O15523; -.
DR BioMuta; DDX3Y; -.
DR EPD; O15523; -.
DR jPOST; O15523; -.
DR MassIVE; O15523; -.
DR MaxQB; O15523; -.
DR PaxDb; O15523; -.
DR PeptideAtlas; O15523; -.
DR PRIDE; O15523; -.
DR ProteomicsDB; 48723; -. [O15523-1]
DR ProteomicsDB; 5478; -.
DR Antibodypedia; 5485; 227 antibodies from 30 providers.
DR DNASU; 8653; -.
DR Ensembl; ENST00000336079.8; ENSP00000336725.3; ENSG00000067048.17. [O15523-1]
DR Ensembl; ENST00000360160.8; ENSP00000353284.4; ENSG00000067048.17. [O15523-1]
DR GeneID; 8653; -.
DR KEGG; hsa:8653; -.
DR MANE-Select; ENST00000336079.8; ENSP00000336725.3; NM_004660.5; NP_004651.2.
DR UCSC; uc004fsu.2; human. [O15523-1]
DR CTD; 8653; -.
DR DisGeNET; 8653; -.
DR GeneCards; DDX3Y; -.
DR GeneReviews; DDX3Y; -.
DR HGNC; HGNC:2699; DDX3Y.
DR HPA; ENSG00000067048; Tissue enhanced (bone).
DR MalaCards; DDX3Y; -.
DR MIM; 400010; gene.
DR neXtProt; NX_O15523; -.
DR OpenTargets; ENSG00000067048; -.
DR Orphanet; 1646; Partial chromosome Y deletion.
DR PharmGKB; PA27168; -.
DR VEuPathDB; HostDB:ENSG00000067048; -.
DR GeneTree; ENSGT00940000154443; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; O15523; -.
DR OMA; NHGNSRL; -.
DR PhylomeDB; O15523; -.
DR TreeFam; TF300364; -.
DR BRENDA; 3.6.4.13; 2681.
DR PathwayCommons; O15523; -.
DR SignaLink; O15523; -.
DR BioGRID-ORCS; 8653; 13 hits in 697 CRISPR screens.
DR ChiTaRS; DDX3Y; human.
DR GeneWiki; DDX3Y; -.
DR GenomeRNAi; 8653; -.
DR Pharos; O15523; Tbio.
DR PRO; PR:O15523; -.
DR Proteomes; UP000005640; Chromosome Y.
DR RNAct; O15523; protein.
DR Bgee; ENSG00000067048; Expressed in sperm and 190 other tissues.
DR ExpressionAtlas; O15523; baseline and differential.
DR Genevisible; O15523; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007276; P:gamete generation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm; DNA-binding;
KW Helicase; Hydrolase; Isopeptide bond; Methylation; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT CHAIN 2..660
FT /note="ATP-dependent RNA helicase DDX3Y"
FT /id="PRO_0000055011"
FT DOMAIN 209..401
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 412..573
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 178..206
FT /note="Q motif"
FT MOTIF 345..348
FT /note="DEAD box"
FT COMPBIAS 15..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 198..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 222..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 100
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 103
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 109
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62095"
FT MOD_RES 590
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 615
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 630
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT VAR_SEQ 1..15
FT /note="MSHVVVKNDPELDQQ -> MEIGRPRKDTWK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055456"
FT VAR_SEQ 287..291
FT /note="FSYRS -> VKYSF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055457"
FT VAR_SEQ 292..660
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055458"
FT CONFLICT 46
FT /note="R -> K (in Ref. 1; AAC51832/AAC51831)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="M -> V (in Ref. 1; AAC51832/AAC51831)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="N -> D (in Ref. 1; AAC51832/AAC51831)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 73154 MW; 0C370E9367952AB6 CRC64;
MSHVVVKNDP ELDQQLANLD LNSEKQSGGA STASKGRYIP PHLRNREASK GFHDKDSSGW
SCSKDKDAYS SFGSRDSRGK PGYFSERGSG SRGRFDDRGR SDYDGIGNRE RPGFGRFERS
GHSRWCDKSV EDDWSKPLPP SERLEQELFS GGNTGINFEK YDDIPVEATG SNCPPHIENF
SDIDMGEIIM GNIELTRYTR PTPVQKHAIP IIKGKRDLMA CAQTGSGKTA AFLLPILSQI
YTDGPGEALK AVKENGRYGR RKQYPISLVL APTRELAVQI YEEARKFSYR SRVRPCVVYG
GADIGQQIRD LERGCHLLVA TPGRLVDMME RGKIGLDFCK YLVLDEADRM LDMGFEPQIR
RIVEQDTMPP KGVRHTMMFS ATFPKEIQML ARDFLDEYIF LAVGRVGSTS ENITQKVVWV
EDLDKRSFLL DILGATGSDS LTLVFVETKK GADSLEDFLY HEGYACTSIH GDRSQRDREE
ALHQFRSGKS PILVATAVAA RGLDISNVRH VINFDLPSDI EEYVHRIGRT GRVGNLGLAT
SFFNEKNMNI TKDLLDLLVE AKQEVPSWLE NMAYEHHYKG GSRGRSKSNR FSGGFGARDY
RQSSGSSSSG FGASRGSSSR SGGGGYGNSR GFGGGGYGGF YNSDGYGGNY NSQGVDWWGN
