D11L8_HUMAN
ID D11L8_HUMAN Reviewed; 907 AA.
AC A8MPP1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Putative ATP-dependent RNA helicase DDX11-like protein 8;
DE EC=3.6.4.13;
DE AltName: Full=DEAD/H box protein 11-like 8;
GN Name=DDX11L8;
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).
CC -!- FUNCTION: Putative DNA helicase. {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 -!- INTERACTION:
CC A8MPP1; PRO_0000308465 [P29991]; Xeno; NbExp=3; IntAct=EBI-5463183, EBI-8826747;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX11/CHL1 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: Defined as a pseudogene by HGNC. However, proteomics data
CC suggest the existence of the protein. {ECO:0000305}.
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DR EMBL; AC009533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A8MPP1; -.
DR IntAct; A8MPP1; 13.
DR GlyGen; A8MPP1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; A8MPP1; -.
DR PhosphoSitePlus; A8MPP1; -.
DR BioMuta; HGNC:37101; -.
DR EPD; A8MPP1; -.
DR jPOST; A8MPP1; -.
DR MassIVE; A8MPP1; -.
DR MaxQB; A8MPP1; -.
DR PeptideAtlas; A8MPP1; -.
DR PRIDE; A8MPP1; -.
DR ProteomicsDB; 1904; -.
DR GeneCards; DDX11L8; -.
DR HGNC; HGNC:37101; DDX11L8.
DR neXtProt; NX_A8MPP1; -.
DR InParanoid; A8MPP1; -.
DR PhylomeDB; A8MPP1; -.
DR PathwayCommons; A8MPP1; -.
DR Pharos; A8MPP1; Tdark.
DR PRO; PR:A8MPP1; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; A8MPP1; protein.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..907
FT /note="Putative ATP-dependent RNA helicase DDX11-like
FT protein 8"
FT /id="PRO_0000349360"
FT DOMAIN 9..447
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 202..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 395..398
FT /note="DEAH"
FT COMPBIAS 202..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FC9"
SQ SEQUENCE 907 AA; 101811 MW; AFB568D7B8725EB8 CRC64;
MANETQKVGA IHFPFPFTPY SIQEDFMAEL YRVLEAGKIG IFESPTGTGK SLSLICGALS
WLRDFEQKKR EEEARLLETG TGPLHDEKDE SLCLSSSCEG AAGTPRPAGE PAWVTQFVQK
KEERDLVDRL KVEQARRKQR EERLQQLQHR VQLKYAAKRL RQEEEETENL LRLSREMLET
GPEAERLEQL ESGEEELVLA EYESDEEKKV ASGHRVDEDE DDLEEEHITK IYHCSRTHSQ
LAQFVHEVKK SPFGKDVRLV SLGSRQNLCV NEDVRSLGSV QLINDRCVDM QRSRHEKKKG
AEEEKPKRRR QEKQAACPFY NHEQMGLLRD EALAEVKDME QLLALGKEAR ACPYYRSRLA
IPAAKLVVLP YQMLLHAATR QAAGIRLQDQ VVIIDEAHNL IDTITGMHSV EVSGSQLCQA
HSQLLQYMER YGKRLKAKNL MYLKQILYLL EKFVAVLGGN IKQNPNTQSL SQTGTELKTI
NDFLFQSQID NINLFKVQRY CEKSMISRKL FGFTERYGAV FSSREQPKLA GFQQFLQSLQ
PRTTEALAAP ADESQASVPQ PASPLMHIEG FLAALTTANQ DGRVILSRQG SLSESTLKFL
LLNPAVHFAQ VVKECRAVVI AGGTMQPVSD FRQQLLACAG VEAERVVEFS CGHVIPPDNI
PLVICSGISN QPLEFTFQKR DLPQMMDEVG RILCNLCGVV SGGVVCFFSS YEYLRQVHAH
WEKGGLLGRL AARKKIFQEP KSAHQVEQVL LAYSRCIQAC GQERGQVTEA LLLSVVGGKM
SEGINFSDNL GRCVVMVGMP FPNIRSAELQ EKMAYLDQTL PRAPGQAPPG KALVENLCMK
AVNQSIGRAI RHQKDFASIV LLDQRYARPP VLAKLPAWIR ASVEVKATFG PAIAAVQKFH
REKSASS