ZRAB2_HUMAN
ID ZRAB2_HUMAN Reviewed; 330 AA.
AC O95218; D3DQ75; Q53GS3; Q59F92; Q5VV33; Q5VV34; Q8IXN6; Q9UP63;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Zinc finger Ran-binding domain-containing protein 2;
DE AltName: Full=Zinc finger protein 265;
DE AltName: Full=Zinc finger, splicing;
GN Name=ZRANB2; Synonyms=ZIS, ZNF265;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Fetal brain;
RX PubMed=9931435; DOI=10.1016/s0378-1119(98)00536-8;
RA Nakano M., Yoshiura K., Oikawa M., Miyoshi O., Yamada K., Kondo S.,
RA Miwa N., Soeda E., Jinno Y., Fujii T., Niikawa N.;
RT "Identification, characterization and mapping of the human ZIS (zinc-
RT finger, splicing) gene.";
RL Gene 225:59-65(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-207.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-207.
RC TISSUE=Skin;
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SNRNP70; U2AF1 AND
RP CLK1.
RX PubMed=11448987; DOI=10.1083/jcb.200010059;
RA Adams D.J., van der Weyden L., Mayeda A., Stamm S., Morris B.J.,
RA Rasko J.E.J.;
RT "ZNF265 -- a novel spliceosomal protein able to induce alternative
RT splicing.";
RL J. Cell Biol. 154:25-32(2001).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-153; SER-181;
RP SER-188 AND SER-193, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP INTERACTION WITH AKAP17A.
RX PubMed=16982639; DOI=10.1093/nar/gkl660;
RA Mangs A.H., Speirs H.J.L., Goy C., Adams D.J., Markus M.A., Morris B.J.;
RT "XE7: a novel splicing factor that interacts with ASF/SF2 and ZNF265.";
RL Nucleic Acids Res. 34:4976-4986(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305; SER-307 AND SER-310
RP (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-153; SER-181 AND
RP SER-188, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303; SER-305;
RP SER-307 AND SER-310 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-153, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-188,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305 AND SER-307 (ISOFORM 2),
RP AND 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-120; SER-153; SER-181;
RP SER-188 AND SER-193, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305;
RP SER-307 AND SER-310 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [19]
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).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-153; SER-181;
RP SER-188 AND SER-193, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303;
RP SER-305 AND SER-307 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-153; SER-181 AND
RP SER-188, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [23]
RP STRUCTURE BY NMR OF 1-40, AND RNA-BINDING.
RX PubMed=12657633; DOI=10.1074/jbc.m301896200;
RA Plambeck C.A., Kwan A.H.Y., Adams D.J., Westman B.J., van der Weyden L.,
RA Medcalf R.L., Morris B.J., Mackay J.P.;
RT "The structure of the zinc finger domain from human splicing factor ZNF265
RT fold.";
RL J. Biol. Chem. 278:22805-22811(2003).
CC -!- FUNCTION: Splice factor required for alternative splicing of
CC TRA2B/SFRS10 transcripts. May interfere with constitutive 5'-splice
CC site selection. {ECO:0000269|PubMed:11448987}.
CC -!- SUBUNIT: Interacts with the C-terminal half of SNRNP70, the Arg/Ser-
CC rich domain of AKAP17A as well as with U2AF1 and CLK1.
CC {ECO:0000269|PubMed:11448987, ECO:0000269|PubMed:16982639}.
CC -!- INTERACTION:
CC O95218; Q02040: AKAP17A; NbExp=4; IntAct=EBI-1051583, EBI-1042725;
CC O95218; P49407: ARRB1; NbExp=4; IntAct=EBI-1051583, EBI-743313;
CC O95218; P32121: ARRB2; NbExp=4; IntAct=EBI-1051583, EBI-714559;
CC O95218; Q5S007: LRRK2; NbExp=2; IntAct=EBI-1051583, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11448987}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=ZIS-1;
CC IsoId=O95218-1; Sequence=Displayed;
CC Name=2; Synonyms=ZIS-2;
CC IsoId=O95218-2; Sequence=VSP_024945;
CC -!- DOMAIN: The RanBP2-type zinc fingers mediate binding to RNA.
CC -!- PTM: Isoform 2 is phosphorylated on Ser-310 upon DNA damage, probably
CC by ATM or ATR.
CC -!- SIMILARITY: Belongs to the ZRANB2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD09746.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD09747.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD92805.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=CAB66879.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF065391; AAD09746.1; ALT_FRAME; mRNA.
DR EMBL; AF065392; AAD09747.1; ALT_FRAME; mRNA.
DR EMBL; AL136945; CAB66879.1; ALT_FRAME; mRNA.
DR EMBL; AB209568; BAD92805.1; ALT_SEQ; mRNA.
DR EMBL; AK222858; BAD96578.1; -; mRNA.
DR EMBL; AL512443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06433.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06435.1; -; Genomic_DNA.
DR EMBL; BC039814; AAH39814.1; -; mRNA.
DR CCDS; CCDS659.1; -. [O95218-1]
DR CCDS; CCDS660.1; -. [O95218-2]
DR RefSeq; NP_005446.2; NM_005455.4. [O95218-2]
DR RefSeq; NP_976225.1; NM_203350.2. [O95218-1]
DR PDB; 1N0Z; NMR; -; A=1-40.
DR PDB; 2K1P; NMR; -; A=65-95.
DR PDB; 3G9Y; X-ray; 1.40 A; A=65-95.
DR PDBsum; 1N0Z; -.
DR PDBsum; 2K1P; -.
DR PDBsum; 3G9Y; -.
DR AlphaFoldDB; O95218; -.
DR SMR; O95218; -.
DR BioGRID; 114802; 191.
DR CORUM; O95218; -.
DR IntAct; O95218; 53.
DR MINT; O95218; -.
DR STRING; 9606.ENSP00000359958; -.
DR GlyGen; O95218; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95218; -.
DR MetOSite; O95218; -.
DR PhosphoSitePlus; O95218; -.
DR BioMuta; ZRANB2; -.
DR EPD; O95218; -.
DR jPOST; O95218; -.
DR MassIVE; O95218; -.
DR MaxQB; O95218; -.
DR PaxDb; O95218; -.
DR PeptideAtlas; O95218; -.
DR PRIDE; O95218; -.
DR ProteomicsDB; 50722; -. [O95218-1]
DR ProteomicsDB; 50723; -. [O95218-2]
DR TopDownProteomics; O95218-1; -. [O95218-1]
DR Antibodypedia; 19679; 296 antibodies from 30 providers.
DR DNASU; 9406; -.
DR Ensembl; ENST00000254821.10; ENSP00000254821.6; ENSG00000132485.14. [O95218-2]
DR Ensembl; ENST00000370920.8; ENSP00000359958.3; ENSG00000132485.14. [O95218-1]
DR Ensembl; ENST00000611683.1; ENSP00000482026.1; ENSG00000132485.14. [O95218-2]
DR GeneID; 9406; -.
DR KEGG; hsa:9406; -.
DR MANE-Select; ENST00000370920.8; ENSP00000359958.3; NM_203350.3; NP_976225.1.
DR UCSC; uc001dfs.4; human. [O95218-1]
DR CTD; 9406; -.
DR DisGeNET; 9406; -.
DR GeneCards; ZRANB2; -.
DR HGNC; HGNC:13058; ZRANB2.
DR HPA; ENSG00000132485; Low tissue specificity.
DR MIM; 604347; gene.
DR neXtProt; NX_O95218; -.
DR OpenTargets; ENSG00000132485; -.
DR PharmGKB; PA37636; -.
DR VEuPathDB; HostDB:ENSG00000132485; -.
DR eggNOG; KOG1995; Eukaryota.
DR GeneTree; ENSGT00730000111078; -.
DR HOGENOM; CLU_061048_0_0_1; -.
DR InParanoid; O95218; -.
DR OMA; DLWGDNE; -.
DR OrthoDB; 1399319at2759; -.
DR PhylomeDB; O95218; -.
DR TreeFam; TF105996; -.
DR PathwayCommons; O95218; -.
DR SignaLink; O95218; -.
DR BioGRID-ORCS; 9406; 218 hits in 1083 CRISPR screens.
DR ChiTaRS; ZRANB2; human.
DR EvolutionaryTrace; O95218; -.
DR GeneWiki; ZRANB2; -.
DR GenomeRNAi; 9406; -.
DR Pharos; O95218; Tbio.
DR PRO; PR:O95218; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O95218; protein.
DR Bgee; ENSG00000132485; Expressed in epithelial cell of pancreas and 182 other tissues.
DR Genevisible; O95218; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0001530; F:lipopolysaccharide binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR InterPro; IPR017337; ZRANB2.
DR Pfam; PF00641; zf-RanBP; 2.
DR PIRSF; PIRSF037956; UCP037956_ZnF_Ran; 1.
DR SMART; SM00547; ZnF_RBZ; 2.
DR SUPFAM; SSF90209; SSF90209; 2.
DR PROSITE; PS01358; ZF_RANBP2_1; 2.
DR PROSITE; PS50199; ZF_RANBP2_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Metal-binding;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..330
FT /note="Zinc finger Ran-binding domain-containing protein 2"
FT /id="PRO_0000066585"
FT ZN_FING 9..40
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 65..94
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 117..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..324
FT /note="Required for nuclear targeting"
FT COMPBIAS 117..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..309
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 18
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R020"
FT MOD_RES 54
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R020"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT VAR_SEQ 310..330
FT /note="RRHRSSSGSSHSGSRSSSKKK -> SQVIGENTKQP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9931435,
FT ECO:0000303|Ref.3, ECO:0000303|Ref.4"
FT /id="VSP_024945"
FT VARIANT 207
FT /note="R -> G (in dbSNP:rs11583800)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.6"
FT /id="VAR_030783"
FT CONFLICT 41
FT /note="E -> G (in Ref. 4; BAD96578)"
FT /evidence="ECO:0000305"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1N0Z"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:1N0Z"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1N0Z"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2K1P"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:3G9Y"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:3G9Y"
FT MOD_RES O95218-2:303
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES O95218-2:305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES O95218-2:307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES O95218-2:310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
SQ SEQUENCE 330 AA; 37404 MW; 99BE2D12EBE0FF8E CRC64;
MSTKNFRVSD GDWICPDKKC GNVNFARRTS CNRCGREKTT EAKMMKAGGT EIGKTLAEKS
RGLFSANDWQ CKTCSNVNWA RRSECNMCNT PKYAKLEERT GYGGGFNERE NVEYIEREES
DGEYDEFGRK KKKYRGKAVG PASILKEVED KESEGEEEDE DEDLSKYKLD EDEDEDDADL
SKYNLDASEE EDSNKKKSNR RSRSKSRSSH SRSSSRSSSP SSSRSRSRSR SRSSSSSQSR
SRSSSRERSR SRGSKSRSSS RSHRGSSSPR KRSYSSSSSS PERNRKRSRS RSSSSGDRKK
RRTRSRSPER RHRSSSGSSH SGSRSSSKKK
