DDX12_HUMAN
ID DDX12_HUMAN Reviewed; 950 AA.
AC Q92771;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Putative ATP-dependent RNA helicase DDX12;
DE EC=3.6.4.13;
DE AltName: Full=CHL1-related protein 2;
DE Short=hCHLR2;
DE AltName: Full=DEAD/H box protein 12;
GN Name=DDX12P; Synonyms=CHLR2, DDX12;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 168-901, AND TISSUE SPECIFICITY.
RX PubMed=9013641; DOI=10.1074/jbc.272.6.3823;
RA Amann J., Kidd V.J., Lahti J.M.;
RT "Characterization of putative human homologues of the yeast chromosome
RT transmission fidelity gene, CHL1.";
RL J. Biol. Chem. 272:3823-3832(1997).
CC -!- FUNCTION: DNA helicase involved in cellular proliferation. Probably
CC required for maintaining the chromosome segregation (By similarity).
CC {ECO:0000250}.
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: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Only expressed in proliferating tissues.
CC {ECO:0000269|PubMed:9013641}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX11/CHL1 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AC092821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC141557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U33834; AAB06963.1; -; mRNA.
DR AlphaFoldDB; Q92771; -.
DR SMR; Q92771; -.
DR IntAct; Q92771; 3.
DR iPTMnet; Q92771; -.
DR PhosphoSitePlus; Q92771; -.
DR BioMuta; HGNC:2737; -.
DR DMDM; 182705254; -.
DR EPD; Q92771; -.
DR jPOST; Q92771; -.
DR MassIVE; Q92771; -.
DR MaxQB; Q92771; -.
DR PeptideAtlas; Q92771; -.
DR PRIDE; Q92771; -.
DR ProteomicsDB; 75455; -.
DR GeneCards; DDX12P; -.
DR HGNC; HGNC:2737; DDX12P.
DR MIM; 601151; gene.
DR neXtProt; NX_Q92771; -.
DR InParanoid; Q92771; -.
DR PhylomeDB; Q92771; -.
DR SignaLink; Q92771; -.
DR ChiTaRS; DDX12P; human.
DR Pharos; Q92771; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q92771; protein.
DR GO; GO:0005634; C:nucleus; 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:0003678; F:DNA helicase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0034085; P:establishment of sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR028331; CHL1/DDX11.
DR InterPro; IPR010614; DEAD_2.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR PANTHER; PTHR11472; PTHR11472; 1.
DR PANTHER; PTHR11472:SF41; PTHR11472:SF41; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00604; rad3; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 5: Uncertain;
KW ATP-binding; Cell cycle; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..950
FT /note="Putative ATP-dependent RNA helicase DDX12"
FT /id="PRO_0000307815"
FT DOMAIN 28..464
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 191..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 412..415
FT /note="DEAH"
FT COMPBIAS 191..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63..70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 205..206
FT /note="RP -> WL (in Ref. 2; AAB06963)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="H -> Y (in Ref. 2; AAB06963)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="R -> Q (in Ref. 2; AAB06963)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="N -> D (in Ref. 2; AAB06963)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="G -> R (in Ref. 2; AAB06963)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="P -> S (in Ref. 2; AAB06963)"
FT /evidence="ECO:0000305"
FT CONFLICT 421..423
FT /note="TTS -> ITG (in Ref. 2; AAB06963)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="N -> D (in Ref. 2; AAB06963)"
FT /evidence="ECO:0000305"
FT CONFLICT 684
FT /note="S -> I (in Ref. 2; AAB06963)"
FT /evidence="ECO:0000305"
FT CONFLICT 716
FT /note="G -> S (in Ref. 2; AAB06963)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="R -> H (in Ref. 2; AAB06963)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="L -> I (in Ref. 2; AAB06963)"
FT /evidence="ECO:0000305"
FT CONFLICT 846
FT /note="H -> P (in Ref. 2; AAB06963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 950 AA; 106006 MW; EE9417A878ACAE85 CRC64;
MRSGGGCSGS LSLRGPASFK FSGVCPDSRG LAFSVAILPA KKEDFMAELY RVLEAGKIGI
FESPTGTGKS LSLICGALSW LRDFEQKKRE EEARLLETGT GPLHDEKDES LCLSSSCEGA
AGTPRPAGEP AWVTQFVQKK EERDLVNRLK AEQARRKQRE ERLQQLQHRV QLKYAAKRLR
QEEEERENLL RLSREMLETG PEAERPEQLE SGEEELVLAE YESDEEKKVA SGVDEDEDDL
EEEHITKIYH CSRTHSQLAQ FVHEVKKSPF GKDVRLVSLG SRQNLCVNED VRSLGSVQLI
NNRCVDMQRS RHEKKKGAEE EKPKRRRQEK QAACPFYNHE QMGLLRDEAL AEVKDMEQLL
ALGKEARACP YYGSRLAIPA AQLVVLPYQM LLHAATRQAA GIRLQDQVVI IDEAHNLIDT
TTSMHSVEVS GSQLCQAHSQ LLQYMERYGK RLKAKNLMYL KQILYLLEKF VAVLGGNIKQ
NPNTQSLSQT GMELKTINDF LFQSQIDNIN LFKVQRYCEK SMISRKLFGF TERYGAVFSS
REQPKLAGFQ QFLQSLQPRT TEALAAPADE SQASVPQPAS PLMHIEGFLA ALTTANQDGR
VILSRQGSLS QSTLKFLLLN PAVHFAQVVK ECRAVVIAGG TMQPVSNFRQ QLLACAGVEA
ERVVEFSCGH VIPPDNILPL VICSGVSNQP LEFTFQKRDL PQMMDEVGRI LCNLCGVVSG
GVVCFFPSYE YLRQVHAHWE KGGLLGRLAA RKKIFQEPKS AHQVEQVLLA YSRCLQACGQ
ERGPVTGALL LSVVGGKMSE GINFSDNLGR CVVMVGMPFP NIRSAELQEK MAYLDQTLPR
APGQAHPGKA LVENLCMKAV NQSIGRAIRH QKDFASIVLL DQRYARPPVL AKLPAWIRAR
VEVKATFGPA IAAVQKVSPT FFFLRASQPR DHISHCLLSA QFHREKSASS
