ZRAB3_HUMAN
ID ZRAB3_HUMAN Reviewed; 1079 AA.
AC Q5FWF4; B3KYA1; B4E375; B5MDI3; D3DP76; E9PBP0; Q53SM1; Q6P2C4; Q8N1P4;
AC Q9H0E8;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=DNA annealing helicase and endonuclease ZRANB3 {ECO:0000305};
DE AltName: Full=Annealing helicase 2 {ECO:0000303|PubMed:21078962};
DE Short=AH2 {ECO:0000303|PubMed:21078962};
DE AltName: Full=Zinc finger Ran-binding domain-containing protein 3 {ECO:0000305};
DE Includes:
DE RecName: Full=DNA annealing helicase ZRANB3 {ECO:0000305};
DE EC=3.6.4.- {ECO:0000269|PubMed:22704558, ECO:0000269|PubMed:22705370};
DE Includes:
DE RecName: Full=Endonuclease ZRANB3 {ECO:0000305};
DE EC=3.1.-.- {ECO:0000269|PubMed:22759634};
GN Name=ZRANB3 {ECO:0000303|PubMed:22759634, ECO:0000312|HGNC:HGNC:25249};
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 MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 248-1079 (ISOFORM 1).
RC TISSUE=Teratocarcinoma, Tongue, and Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Lymph, and 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
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 [8]
RP FUNCTION.
RX PubMed=21078962; DOI=10.1073/pnas.1011196107;
RA Yusufzai T., Kadonaga J.T.;
RT "Annealing helicase 2 (AH2), a DNA-rewinding motor with an HNH motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:20970-20973(2010).
RN [9]
RP FUNCTION AS ENDONUCLEASE, SUBCELLULAR LOCATION, INTERACTION WITH PCNA,
RP DOMAIN, AND MUTAGENESIS OF LYS-65; GLN-519; 525-PHE-PHE-526; TRP-625;
RP THR-631; TYR-632; ASN-634; MET-643 AND HIS-1021.
RX PubMed=22759634; DOI=10.1101/gad.193516.112;
RA Weston R., Peeters H., Ahel D.;
RT "ZRANB3 is a structure-specific ATP-dependent endonuclease involved in
RT replication stress response.";
RL Genes Dev. 26:1558-1572(2012).
RN [10]
RP FUNCTION AS ANNEALING HELICASE, SUBCELLULAR LOCATION, INTERACTION WITH
RP PCNA, DOMAIN, AND MUTAGENESIS OF GLN-519 AND PHE-525.
RX PubMed=22705370; DOI=10.1016/j.molcel.2012.05.025;
RA Yuan J., Ghosal G., Chen J.;
RT "The HARP-like domain-containing protein AH2/ZRANB3 binds to PCNA and
RT participates in cellular response to replication stress.";
RL Mol. Cell 47:410-421(2012).
RN [11]
RP FUNCTION AS ANNEALING HELICASE, SUBCELLULAR LOCATION, INTERACTION WITH
RP PCNA, DOMAIN, AND MUTAGENESIS OF 157-ASP-GLU-158; GLN-519; ILE-522;
RP 525-PHE-PHE-526; 631-THR-TYR-631 AND PHE-1075.
RX PubMed=22704558; DOI=10.1016/j.molcel.2012.05.024;
RA Ciccia A., Nimonkar A.V., Hu Y., Hajdu I., Achar Y.J., Izhar L.,
RA Petit S.A., Adamson B., Yoon J.C., Kowalczykowski S.C., Livingston D.M.,
RA Haracska L., Elledge S.J.;
RT "Polyubiquitinated PCNA recruits the ZRANB3 translocase to maintain genomic
RT integrity after replication stress.";
RL Mol. Cell 47:396-409(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
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 [13]
RP FUNCTION, AND MUTAGENESIS OF LYS-163; 762-LEU--ILE-764 AND
RP 792-TRP--SER-794.
RX PubMed=26884333; DOI=10.1074/jbc.m115.709733;
RA Badu-Nkansah A., Mason A.C., Eichman B.F., Cortez D.;
RT "Identification of a substrate recognition domain in the replication stress
RT response protein zinc finger Ran-binding domain-containing protein 3
RT (ZRANB3).";
RL J. Biol. Chem. 291:8251-8257(2016).
RN [14]
RP METHYLATION AT CYS-630 (MICROBIAL INFECTION).
RX PubMed=25412445; DOI=10.1371/journal.ppat.1004522;
RA Yao Q., Zhang L., Wan X., Chen J., Hu L., Ding X., Li L., Karar J.,
RA Peng H., Chen S., Huang N., Rauscher F.J. III, Shao F.;
RT "Structure and specificity of the bacterial cysteine methyltransferase
RT effector NleE suggests a novel substrate in human DNA repair pathway.";
RL PLoS Pathog. 10:e1004522-e1004522(2014).
RN [15]
RP METHYLATION (MICROBIAL INFECTION).
RX PubMed=27445336; DOI=10.1074/jbc.m116.734079;
RA Zhang Y., Muehlen S., Oates C.V., Pearson J.S., Hartland E.L.;
RT "Identification of a distinct substrate-binding domain in the bacterial
RT cysteine methyltransferase effectors NleE and OspZ.";
RL J. Biol. Chem. 291:20149-20162(2016).
CC -!- FUNCTION: DNA annealing helicase and endonuclease required to maintain
CC genome stability at stalled or collapsed replication forks by
CC facilitating fork restart and limiting inappropriate recombination that
CC could occur during template switching events (PubMed:21078962,
CC PubMed:22704558, PubMed:22705370, PubMed:22759634, PubMed:26884333).
CC Recruited to the sites of stalled DNA replication by polyubiquitinated
CC PCNA and acts as a structure-specific endonuclease that cleaves the
CC replication fork D-loop intermediate, generating an accessible 3'-OH
CC group in the template of the leading strand, which is amenable to
CC extension by DNA polymerase (PubMed:22759634). In addition to
CC endonuclease activity, also catalyzes the fork regression via annealing
CC helicase activity in order to prevent disintegration of the replication
CC fork and the formation of double-strand breaks (PubMed:22705370,
CC PubMed:22704558). {ECO:0000269|PubMed:21078962,
CC ECO:0000269|PubMed:22704558, ECO:0000269|PubMed:22705370,
CC ECO:0000269|PubMed:22759634, ECO:0000269|PubMed:26884333}.
CC -!- SUBUNIT: Interacts (via PIP-box and RanBP2-type zinc finger) with PCNA
CC (when PCNA is polyubiquitinated via 'Lys-63'-linked polyubiquitin).
CC {ECO:0000269|PubMed:22704558, ECO:0000269|PubMed:22705370,
CC ECO:0000269|PubMed:22759634}.
CC -!- INTERACTION:
CC Q5FWF4; O00629: KPNA4; NbExp=2; IntAct=EBI-13954615, EBI-396343;
CC Q5FWF4; P12004: PCNA; NbExp=8; IntAct=EBI-13954615, EBI-358311;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22704558,
CC ECO:0000269|PubMed:22705370, ECO:0000269|PubMed:22759634}. Chromosome
CC {ECO:0000269|PubMed:22704558, ECO:0000269|PubMed:22705370,
CC ECO:0000269|PubMed:22759634}. Note=Following DNA damage, recruited to
CC sites of DNA damage and stalled replication forks by polyubiquitinated
CC PCNA (PubMed:22704558, PubMed:22705370, PubMed:22759634).
CC {ECO:0000269|PubMed:22704558, ECO:0000269|PubMed:22705370,
CC ECO:0000269|PubMed:22759634}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q5FWF4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5FWF4-2; Sequence=VSP_023138, VSP_023139, VSP_023140;
CC Name=3;
CC IsoId=Q5FWF4-3; Sequence=VSP_023139;
CC Name=4;
CC IsoId=Q5FWF4-4; Sequence=VSP_044175, VSP_023139;
CC Name=5;
CC IsoId=Q5FWF4-5; Sequence=VSP_044176, VSP_044177, VSP_044178;
CC -!- DOMAIN: The PIP-box mediates the interaction with PCNA, while the
CC RanBP2-type zinc finger mediates binding to 'Lys-63'-linked
CC polyubiquitin (PubMed:22704558, PubMed:22705370 and PubMed:22759634).
CC {ECO:0000269|PubMed:22704558, ECO:0000269|PubMed:22705370,
CC ECO:0000269|PubMed:22759634}.
CC -!- PTM: (Microbial infection) Methylation at Cys-630 by enteropathogenic
CC E.coli protein NleE or S.flexneri protein OspZ: methylation disrupts
CC ability to bind 'Lys-63'-linked ubiquitin.
CC {ECO:0000269|PubMed:25412445, ECO:0000269|PubMed:27445336}.
CC -!- MISCELLANEOUS: In contrast to classical helicases that unwing DNA,
CC annealing helicases rewind it. {ECO:0000305|PubMed:21078962}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX93066.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAG54763.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG65387.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAX11631.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAX11633.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL136824; CAB66758.1; -; mRNA.
DR EMBL; AK095362; BAC04536.1; -; mRNA.
DR EMBL; AK131303; BAG54763.1; ALT_INIT; mRNA.
DR EMBL; AK304601; BAG65387.1; ALT_INIT; mRNA.
DR EMBL; BX647838; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC012450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC017031; AAX93066.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC020602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC064850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471058; EAX11631.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471058; EAX11633.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC064616; AAH64616.1; -; mRNA.
DR EMBL; BC089429; AAH89429.2; -; mRNA.
DR CCDS; CCDS46419.1; -. [Q5FWF4-1]
DR CCDS; CCDS67963.1; -. [Q5FWF4-3]
DR RefSeq; NP_001273497.1; NM_001286568.1. [Q5FWF4-3]
DR RefSeq; NP_115519.2; NM_032143.3. [Q5FWF4-1]
DR RefSeq; XP_005263866.1; XM_005263809.1. [Q5FWF4-1]
DR RefSeq; XP_006712851.1; XM_006712788.1. [Q5FWF4-1]
DR RefSeq; XP_011510260.1; XM_011511958.2. [Q5FWF4-1]
DR RefSeq; XP_011510262.1; XM_011511960.1. [Q5FWF4-1]
DR RefSeq; XP_011510265.1; XM_011511963.1. [Q5FWF4-3]
DR PDB; 5MKW; X-ray; 2.00 A; A/B=948-1067.
DR PDB; 5MLO; X-ray; 1.96 A; B/D/F=515-529.
DR PDB; 5MLW; X-ray; 2.45 A; B/D/F=1069-1079.
DR PDB; 5YD8; X-ray; 2.30 A; U/V/W=1069-1079.
DR PDBsum; 5MKW; -.
DR PDBsum; 5MLO; -.
DR PDBsum; 5MLW; -.
DR PDBsum; 5YD8; -.
DR AlphaFoldDB; Q5FWF4; -.
DR SMR; Q5FWF4; -.
DR BioGRID; 123877; 26.
DR IntAct; Q5FWF4; 13.
DR STRING; 9606.ENSP00000264159; -.
DR iPTMnet; Q5FWF4; -.
DR PhosphoSitePlus; Q5FWF4; -.
DR BioMuta; ZRANB3; -.
DR DMDM; 74741477; -.
DR EPD; Q5FWF4; -.
DR jPOST; Q5FWF4; -.
DR MassIVE; Q5FWF4; -.
DR MaxQB; Q5FWF4; -.
DR PaxDb; Q5FWF4; -.
DR PeptideAtlas; Q5FWF4; -.
DR PRIDE; Q5FWF4; -.
DR ProteomicsDB; 19263; -.
DR ProteomicsDB; 62811; -. [Q5FWF4-1]
DR ProteomicsDB; 62812; -. [Q5FWF4-2]
DR ProteomicsDB; 62813; -. [Q5FWF4-3]
DR Antibodypedia; 56175; 79 antibodies from 18 providers.
DR DNASU; 84083; -.
DR Ensembl; ENST00000264159.11; ENSP00000264159.6; ENSG00000121988.18. [Q5FWF4-1]
DR Ensembl; ENST00000401392.5; ENSP00000383979.1; ENSG00000121988.18. [Q5FWF4-3]
DR Ensembl; ENST00000619650.4; ENSP00000480120.1; ENSG00000121988.18. [Q5FWF4-2]
DR GeneID; 84083; -.
DR KEGG; hsa:84083; -.
DR MANE-Select; ENST00000264159.11; ENSP00000264159.6; NM_032143.4; NP_115519.2.
DR UCSC; uc002tul.5; human. [Q5FWF4-1]
DR CTD; 84083; -.
DR DisGeNET; 84083; -.
DR GeneCards; ZRANB3; -.
DR HGNC; HGNC:25249; ZRANB3.
DR HPA; ENSG00000121988; Low tissue specificity.
DR MalaCards; ZRANB3; -.
DR MIM; 615655; gene.
DR neXtProt; NX_Q5FWF4; -.
DR OpenTargets; ENSG00000121988; -.
DR PharmGKB; PA134871612; -.
DR VEuPathDB; HostDB:ENSG00000121988; -.
DR eggNOG; KOG1000; Eukaryota.
DR GeneTree; ENSGT00940000158559; -.
DR HOGENOM; CLU_004251_0_0_1; -.
DR InParanoid; Q5FWF4; -.
DR OMA; PGFSEWF; -.
DR OrthoDB; 1082831at2759; -.
DR PhylomeDB; Q5FWF4; -.
DR TreeFam; TF354227; -.
DR PathwayCommons; Q5FWF4; -.
DR SignaLink; Q5FWF4; -.
DR BioGRID-ORCS; 84083; 15 hits in 1081 CRISPR screens.
DR ChiTaRS; ZRANB3; human.
DR GenomeRNAi; 84083; -.
DR Pharos; Q5FWF4; Tbio.
DR PRO; PR:Q5FWF4; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q5FWF4; protein.
DR Bgee; ENSG00000121988; Expressed in pancreatic ductal cell and 142 other tissues.
DR ExpressionAtlas; Q5FWF4; baseline and differential.
DR Genevisible; Q5FWF4; HS.
DR GO; GO:0043596; C:nuclear replication fork; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; IDA:UniProtKB.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
DR GO; GO:0036292; P:DNA rewinding; IDA:UniProtKB.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IDA:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; IDA:UniProtKB.
DR GO; GO:0048478; P:replication fork protection; IDA:UniProtKB.
DR GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR CDD; cd00085; HNHc; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR002711; HNH.
DR InterPro; IPR003615; HNH_nuc.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF01844; HNH; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00507; HNHc; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Chromosome; DNA damage;
KW DNA repair; Endonuclease; Helicase; Hydrolase; Metal-binding; Methylation;
KW Multifunctional enzyme; Nuclease; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1079
FT /note="DNA annealing helicase and endonuclease ZRANB3"
FT /id="PRO_0000278182"
FT DOMAIN 46..208
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 325..481
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1011..1051
FT /note="HNH"
FT ZN_FING 621..650
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 46..481
FT /note="DNA annealing helicase activity"
FT REGION 582..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1079
FT /note="Endonuclease activity"
FT MOTIF 157..160
FT /note="DEAH box"
FT MOTIF 519..526
FT /note="PIP-box"
FT MOTIF 1074..1078
FT /note="APIM motif"
FT BINDING 59..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 630
FT /note="(Microbial infection) S-methylcysteine"
FT /evidence="ECO:0000269|PubMed:25412445"
FT VAR_SEQ 1..642
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044175"
FT VAR_SEQ 1..535
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_023138"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044176"
FT VAR_SEQ 403..428
FT /note="GLTFTAASHVVFAELYWDPGHIKQAE -> DLYDKVAWGKRTLVSGLFMECF
FT CFVP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044177"
FT VAR_SEQ 429..1079
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044178"
FT VAR_SEQ 718..719
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_023139"
FT VAR_SEQ 1077..1079
FT /note="VKK -> ETSKLHESHKVTGAEQGLQVSGLPDSAAPEGGAAHTNDQRRCQRM
FT KQPLTEVQILSHSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_023140"
FT VARIANT 541
FT /note="E -> K (in dbSNP:rs935615)"
FT /id="VAR_030671"
FT VARIANT 546
FT /note="R -> Q (in dbSNP:rs7608121)"
FT /id="VAR_030672"
FT VARIANT 637
FT /note="E -> V (in dbSNP:rs59900519)"
FT /id="VAR_061237"
FT MUTAGEN 65
FT /note="K->R: Abolishes ATPase activity. Abolishes
FT endonuclease activity; when associated with A-1021."
FT /evidence="ECO:0000269|PubMed:22759634"
FT MUTAGEN 157..158
FT /note="DE->AA: Abolishes fork regression activity."
FT /evidence="ECO:0000269|PubMed:22704558"
FT MUTAGEN 163
FT /note="K->D: Loss of DNA-dependent ATPase activity."
FT /evidence="ECO:0000269|PubMed:26884333"
FT MUTAGEN 519
FT /note="Q->A: Abolishes interaction with PCNA; when
FT associated with A-522; 525-A-A-526 and A-1075. Abolishes
FT interaction with PCNA; when associated with A-525."
FT /evidence="ECO:0000269|PubMed:22704558,
FT ECO:0000269|PubMed:22705370, ECO:0000269|PubMed:22759634"
FT MUTAGEN 522
FT /note="I->A: Abolishes interaction with PCNA; when
FT associated with A-519; 525-A-A-526 and A-1075."
FT /evidence="ECO:0000269|PubMed:22704558"
FT MUTAGEN 525..526
FT /note="FF->AA: Abolishes interaction with PCNA; when
FT associated with A-519; A-522 and A-1075."
FT /evidence="ECO:0000269|PubMed:22704558,
FT ECO:0000269|PubMed:22759634"
FT MUTAGEN 525
FT /note="F->A: Abolishes interaction with PCNA; when
FT associated with A-519."
FT /evidence="ECO:0000269|PubMed:22705370"
FT MUTAGEN 625
FT /note="W->A: Abolishes interaction with 'Lys-63'-linked
FT polyubiquitin."
FT /evidence="ECO:0000269|PubMed:22759634"
FT MUTAGEN 631..632
FT /note="TY->AA: Abolishes interaction with 'Lys-63'-linked
FT polyubiquitin."
FT MUTAGEN 631
FT /note="T->A: Impaired interaction with 'Lys-63'-linked
FT polyubiquitin."
FT /evidence="ECO:0000269|PubMed:22704558,
FT ECO:0000269|PubMed:22759634"
FT MUTAGEN 632
FT /note="Y->A: Abolishes interaction with 'Lys-63'-linked
FT polyubiquitin."
FT /evidence="ECO:0000269|PubMed:22759634"
FT MUTAGEN 634
FT /note="N->A: Abolishes interaction with 'Lys-63'-linked
FT polyubiquitin."
FT /evidence="ECO:0000269|PubMed:22759634"
FT MUTAGEN 643
FT /note="M->A: Impaired interaction with polyubiquitin."
FT /evidence="ECO:0000269|PubMed:22759634"
FT MUTAGEN 762..764
FT /note="LDI->AAA: Loss of DNA-binding, DNA-dependent ATPase
FT and nuclease activities."
FT /evidence="ECO:0000269|PubMed:26884333"
FT MUTAGEN 792..794
FT /note="WSS->AAA: Loss of DNA-dependent ATPase activity."
FT /evidence="ECO:0000269|PubMed:26884333"
FT MUTAGEN 1021
FT /note="H->A: Does not affect endonuclease. Abolishes
FT endonuclease activity; when associated with R-65."
FT /evidence="ECO:0000269|PubMed:22759634"
FT MUTAGEN 1075
FT /note="F->A: Abolishes interaction with PCNA; when
FT associated with A-519; A-522 and 525-A-A-526."
FT /evidence="ECO:0000269|PubMed:22704558"
FT CONFLICT 366
FT /note="I -> T (in Ref. 2; BAC04536)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="S -> I (in Ref. 2; BAG65387)"
FT /evidence="ECO:0000305"
FT CONFLICT 847
FT /note="V -> A (in Ref. 2; BAG54763)"
FT /evidence="ECO:0000305"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:5MLO"
FT HELIX 950..961
FT /evidence="ECO:0007829|PDB:5MKW"
FT TURN 966..968
FT /evidence="ECO:0007829|PDB:5MKW"
FT HELIX 972..981
FT /evidence="ECO:0007829|PDB:5MKW"
FT HELIX 984..992
FT /evidence="ECO:0007829|PDB:5MKW"
FT HELIX 995..998
FT /evidence="ECO:0007829|PDB:5MKW"
FT HELIX 1001..1009
FT /evidence="ECO:0007829|PDB:5MKW"
FT HELIX 1013..1015
FT /evidence="ECO:0007829|PDB:5MKW"
FT STRAND 1017..1023
FT /evidence="ECO:0007829|PDB:5MKW"
FT HELIX 1034..1036
FT /evidence="ECO:0007829|PDB:5MKW"
FT STRAND 1037..1041
FT /evidence="ECO:0007829|PDB:5MKW"
FT HELIX 1042..1063
FT /evidence="ECO:0007829|PDB:5MKW"
FT HELIX 1073..1075
FT /evidence="ECO:0007829|PDB:5YD8"
SQ SEQUENCE 1079 AA; 123248 MW; 7B65AB9568B15AAE CRC64;
MPRVHNIKKS LTPHISCVTN ESDNLLDFLP DRLRAKLLPF QKDGIIFALK RNGRCMVADE
MGLGKTIQAI GITYFYKEEW PLLIVVPSSL RYPWTEEIEK WIPELSPEEI NVIQNKTDVR
RMSTSKVTVL GYGLLTADAK TLIDALNNQN FKVVIVDESH YMKSRNATRS RILLPIVQKA
RRAILLTGTP ALGRPEELFM QIEALFPQKF GRWTDYAKRY CNAHIRYFGK RPQWDCRGAS
NLNELHQLLS DIMIRRLKTE VLTQLPPKVR QRIPFDLPSA AAKELNTSFE EWEKIMRTPN
SGAMETVMGL ITRMFKQTAI AKAGAVKDYI KMMLQNDSLK FLVFAHHLSM LQACTEAVIE
NKTRYIRIDG SVSSSERIHL VNQFQKDPDT RVAILSIQAA GQGLTFTAAS HVVFAELYWD
PGHIKQAEDR AHRIGQCSSV NIHYLIANGT LDTLMWGMLN RKAQVTGSTL NGRKEKIQAE
EGDKEKWDFL QFAEAWTPND SSEELRKEAL FTHFEKEKQH DIRSFFVPQP KKRQLMTSCD
ESKRFREENT VVSSDPTKTA ARDIIDYESD VEPETKRLKL AASEDHCSPS EETPSQSKQI
RTPLVESVQE AKAQLTTPAF PVEGWQCSLC TYINNSELPY CEMCETPQGS AVMQIDSLNH
IQDKNEKDDS QKDTSKKVQT ISDCEKQALA QSEPGQLADS KEETPKIEKE DGLTSQPGNE
QWKSSDTLPV YDTLMFCASR NTDRIHIYTK DGKQMSCNFI PLDIKLDLWE DLPASFQLKQ
YRSLILRFVR EWSSLTAMKQ RIIRKSGQLF CSPILALEEI TKQQTKQNCT KRYITKEDVA
VASMDKVKNV GGHVRLITKE SRPRDPFTKK LLEDGACVPF LNPYTVQADL TVKPSTSKGY
LQAVDNEGNP LCLRCQQPTC QTKQACKANS WDSRFCSLKC QEEFWIRSNN SYLRAKVFET
EHGVCQLCNV NAQELFLRLR DAPKSQRKNL LYATWTSKLP LEQLNEMIRN PGEGHFWQVD
HIKPVYGGGG QCSLDNLQTL CTVCHKERTA RQAKERSQVR RQSLASKHGS DITRFLVKK
