ID J3QS41_HUMAN Unreviewed; 1943 AA.
AC J3QS41;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Helicase with zinc finger {ECO:0000313|Ensembl:ENSP00000464512.1};
GN Name=HELZ {ECO:0000313|Ensembl:ENSP00000464512.1};
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 {ECO:0000313|Ensembl:ENSP00000464512.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000464512.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [2] {ECO:0007829|PubMed:18669648}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [3] {ECO:0007829|PubMed:19413330}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [4] {ECO:0007829|PubMed:19690332}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [5] {ECO:0007829|PubMed:20068231}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6] {ECO:0007829|PubMed:21269460}
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., Burckstummer 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).
RN [7] {ECO:0007829|PubMed:21406692}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9] {ECO:0007829|PubMed:24275569}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10] {ECO:0007829|PubMed:24129315}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24129315;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11] {ECO:0000313|Ensembl:ENSP00000464512.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AC005544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EPD; J3QS41; -.
DR MassIVE; J3QS41; -.
DR MaxQB; J3QS41; -.
DR PeptideAtlas; J3QS41; -.
DR Antibodypedia; 31693; 122 antibodies from 14 providers.
DR Ensembl; ENST00000580168.5; ENSP00000464512.1; ENSG00000198265.12.
DR UCSC; uc010wqk.3; human.
DR HGNC; HGNC:16878; HELZ.
DR VEuPathDB; HostDB:ENSG00000198265; -.
DR GeneTree; ENSGT00940000156686; -.
DR HOGENOM; CLU_237325_0_0_1; -.
DR OrthoDB; 5405202at2759; -.
DR PhylomeDB; J3QS41; -.
DR ChiTaRS; HELZ; human.
DR Proteomes; UP000005640; Chromosome 17.
DR Bgee; ENSG00000198265; Expressed in colonic epithelium and 213 other cell types or tissues.
DR ExpressionAtlas; J3QS41; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18077; DEXXQc_HELZ; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR049569; HELZ_DEAD-box_1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF365; HELICASE WITH ZINC FINGER DOMAIN-RELATED; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF04851; ResIII; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723};
KW Proteomics identification {ECO:0007829|EPD:J3QS41,
KW ECO:0007829|MaxQB:J3QS41};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 178..206
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 178..206
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1118..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1528..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1609..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1730..1780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1793..1844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1871..1943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1732..1746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1760..1780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1793..1827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1875..1893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1918..1943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1943 AA; 219057 MW; 5D5EE85F38850E0E CRC64;
MEDRRAEKSC EQACESLKRQ DYEMALKHCT EALLSLGQYS MADFTGPCPL EIERIKIESL
LYRIASFLQL KNYVQADEDC RHVLGEGLAK GEDAFRAVLC CMQLKGKLQP VSTILAKSLT
GESLNGMVTK DLTRLKTLLS ETETATSNAL SGYHVEDLDE GSCNGWHFRP PPRGITSSEE
YTLCKRFLEQ GICRYGAQCT SAHSQEELAE WQKRYASRLI KLKQQNENKQ LSGSYMETLI
EKWMNSLSPE KVLSECIEGV KVEHNPDLSV TVSTKKSHQT WTFALTCKPA RMLYRVALLY
DAHRPHFSII AISAGDSTTQ VSQEVPENCQ EWIGGKMAQN GLDHYVYKVG IAFNTEIFGT
FRQTIVFDFG LEPVLMQRVM IDAASTEDLE YLMHAKQQLV TTAKRWDSSS KTIIDFEPNE
TTDLEKSLLI RYQIPLSADQ LFTQSVLDKS LTKSNYQSRL HDLLYIEEIA QYKEISKFNL
KVQLQILASF MLTGVSGGAK YAQNGQLFGR FKLTETLSED TLAGRLVMTK VNAVYLLPVP
KQKLVQTQGT KEKVYEATIE EKTKEYIFLR LSRECCEELN LRPDCDTQVE LQFQLNRLPL
CEMHYALDRI KDNGVLFPDI SMTPTIPWSP NRQWDEQLDP RLNAKQKEAV LAITTPLAIQ
LPPVLIIGPY GTGKTFTLAQ AVKHILQQQE TSRILICTHS NSAADLYIKD YLHPYVEAGN
PQARPLRVYF RNRWVKTVHP VVHQYCLISS AHSTFQMPQK EDILKHRVVV VTLNTSQYLC
QLDLEPGFFT HILLDEAAQA MECETIMPLA LATQNTRIVL AGDHMQLSPF VYSEFARERN
LHVSLLDRLY EHYPAEFPCR ILLCENYRSH EAIINYTSEL FYEGKLMASG KQPAHKDFYP
LTFFTARGED VQEKNSTAFY NNAEVFEVVE RVEELRRKWP VAWGKLDDGS IGVVTPYADQ
VFRIRAELRK KRLSDVNVER VLNVQGKQFR VLFLSTVRTR HTCKHKQTPI KKKEQLLEDS
TEDLDYGFLS NYKLLNTAIT RAQSLVAVVG DPIALCSIGR CRKFWERFIA LCHENSSLHG
ITFEQIKAQL EALELKKTYV LNPLAPEFIP RALRLQHSGS TNKQQQSPPK GKSLHHTQND
HFQNDGIVQP NPSVLIGNPI RAYTPPPPLG PHPNLGKSPS PVQRIDPHTG TSILYVPAVY
GGNVVMSVPL PVPWTGYQGR FAVDPRIITH QAAMAYNMNL LQTHGRGSPI PYGLGHHPPV
TIGQPQNQHQ EKDQHEQNRN GKSDTNNSGP EINKIRTPEK KPTEPKQVDL ESNPQNRSPE
SRPSVVYPST KFPRKDNLNP RHINLPLPAP HAQYAIPNRH FHPLPQLPRP PFPIPQQHTL
LNQQQNNLPE QPNQIPPQPN QVVQQQSQLN QQPQQPPPQL SPAYQAGPNN AFFNSAVAHR
PQSPPAEAVI PEQQPPPMLQ EGHSPLRAIA QPGPILPSHL NSFIDENPSG LPIGEALDRI
HGSVALETLR QQQARFQQWS EHHAFLSQGS APYPHHHHPH LQHLPQPPLG LHQPPVRADW
KLTSSAEDEV ETTYSRFQDL IRELSHRDQS ETRELAEMPP PQSRLLQYRQ VQSRSPPAVP
SPPSSTDHSS HFSNFNDNSR DIEVASNPAF PQRLPPQIFN SPFSLPSEHL APPPLKYLAP
DGAWTFANLQ QNHLMGPGFP YGLPPLPHRP PQNPFVQIQN HQHAIGQEPF HPLSSRTVSS
SSLPSLEEYE PRGPGRPLYQ RRISSSSVQP CSEEVSTPQD SLAQCKELQD HSNQSSFNFS
SPESWVNTTS STPYQNIPCN GSSRTAQPRE LIAPPKTVKP PEDQLKSENL EVSSSFNYSV
LQHLGQFPPL MPNKQIAESA NSSSPQSSAG GKPAMSYASA LRAPPKPRPP PEQAKKSSDP
LSLFQELSLG SSSGSNGFYS YFK
//
