ZC3HD_HUMAN
ID ZC3HD_HUMAN Reviewed; 1668 AA.
AC Q5T200; A2A323; O94936; Q5T1Z9; Q7Z7J3; Q8NDT6; Q9H0L6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Zinc finger CCCH domain-containing protein 13 {ECO:0000305};
GN Name=ZC3H13 {ECO:0000303|PubMed:29507755, ECO:0000312|HGNC:HGNC:20368};
GN Synonyms=KIAA0853 {ECO:0000303|PubMed:10048485};
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] (ISOFORM 2), AND VARIANT ASP-1429.
RA Shan Y.X., Yu L.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-971, AND VARIANT ASP-1429.
RC TISSUE=Fetal brain;
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 MRNA] OF 298-1668 (ISOFORM 2), AND VARIANT
RP ASP-1429.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 702-1668 (ISOFORM 1), AND VARIANT
RP ASP-1429.
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-263 AND SER-265, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; THR-263 AND SER-265, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242; THR-263; SER-265 AND
RP SER-993, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1382, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [10]
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-209; SER-242;
RP SER-316; SER-318; SER-325; THR-354; THR-364; SER-370; SER-372; SER-381;
RP SER-831; SER-833; SER-837; SER-845; SER-848; SER-853; SER-875; SER-877;
RP SER-986; SER-993; SER-1010; SER-1014 AND SER-1017, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-1453; SER-1456 AND SER-1466 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242; THR-263; SER-986;
RP SER-993; SER-1014 AND SER-1017, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-198; SER-207;
RP SER-209; SER-242; THR-263; SER-265; SER-370; SER-372; SER-381; SER-845;
RP SER-848; SER-853; SER-877; SER-993; SER-1010; SER-1014; SER-1017; THR-1170;
RP SER-1208; SER-1230; SER-1364; SER-1366 AND SER-1438, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; THR-237; SER-242;
RP THR-263; SER-265; SER-325; SER-328; SER-370; SER-372; SER-381; SER-845;
RP SER-848; SER-853; SER-877; THR-882; SER-986; SER-993; SER-1010; SER-1017;
RP SER-1191; SER-1194; SER-1208; SER-1210 AND SER-1465, AND IDENTIFICATION BY
RP 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 [16]
RP IDENTIFICATION IN A MACOM-LIKE COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=24100041; DOI=10.1074/jbc.m113.500397;
RA Horiuchi K., Kawamura T., Iwanari H., Ohashi R., Naito M., Kodama T.,
RA Hamakubo T.;
RT "Identification of Wilms' tumor 1-associating protein complex and its role
RT in alternative splicing and the cell cycle.";
RL J. Biol. Chem. 288:33292-33302(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-198; SER-207;
RP SER-209; SER-211; SER-238; SER-242; THR-263; SER-265; SER-318; SER-325;
RP SER-370; SER-372; SER-381; SER-643; SER-873; SER-875; SER-877; SER-943;
RP SER-986; SER-993; THR-1033; THR-1170; SER-1364; SER-1366; SER-1386;
RP SER-1406 AND SER-1409, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242; SER-370; SER-372;
RP SER-877; SER-1010; SER-1014; SER-1017 AND SER-1210, 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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-194, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-194, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-194, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-194, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [23]
RP FUNCTION, AND IDENTIFICATION IN THE WMM COMPLEX.
RX PubMed=29507755; DOI=10.1038/s41421-018-0019-0;
RA Yue Y., Liu J., Cui X., Cao J., Luo G., Zhang Z., Cheng T., Gao M., Shu X.,
RA Ma H., Wang F., Wang X., Shen B., Wang Y., Feng X., He C., Liu J.;
RT "VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near stop
RT codon and associates with alternative polyadenylation.";
RL Cell Discov. 4:10-10(2018).
CC -!- FUNCTION: Associated component of the WMM complex, a complex that
CC mediates N6-methyladenosine (m6A) methylation of RNAs, a modification
CC that plays a role in the efficiency of mRNA splicing and RNA processing
CC (PubMed:29507755). Acts as a key regulator of m6A methylation by
CC promoting m6A methylation of mRNAs at the 3'-UTR (By similarity).
CC Controls embryonic stem cells (ESCs) pluripotency via its role in m6A
CC methylation (By similarity). In the WMM complex, anchors component of
CC the MACOM subcomplex in the nucleus (By similarity). Also required for
CC bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B) (By
CC similarity). {ECO:0000250|UniProtKB:E9Q784}.
CC -!- SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex
CC composed of a catalytic subcomplex, named MAC, and of an associated
CC subcomplex, named MACOM (PubMed:29507755). The MAC subcomplex is
CC composed of METTL3 and METTL14. The MACOM subcomplex is composed of
CC WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or
CC RBM15B) (PubMed:29507755). Also a component of a MACOM-like complex,
CC named WTAP complex, composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA,
CC RBM15, BCLAF1 and THRAP3 (PubMed:24100041).
CC {ECO:0000269|PubMed:24100041, ECO:0000269|PubMed:29507755}.
CC -!- INTERACTION:
CC Q5T200; P0DPB3: SCHIP1; NbExp=2; IntAct=EBI-2679720, EBI-1397509;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:24100041}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:24100041}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5T200-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T200-2; Sequence=VSP_027202, VSP_014252, VSP_014253;
CC -!- SIMILARITY: Belongs to the ZC3H13 family. {ECO:0000305}.
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DR EMBL; AY283618; AAP37483.1; -; mRNA.
DR EMBL; AL157758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL831833; CAD38544.1; -; mRNA.
DR EMBL; AL136745; CAB66679.2; -; mRNA.
DR EMBL; AB020660; BAA74876.1; -; mRNA.
DR CCDS; CCDS81766.1; -. [Q5T200-1]
DR CCDS; CCDS9400.1; -. [Q5T200-2]
DR RefSeq; NP_001070256.1; NM_001076788.1.
DR RefSeq; NP_001317493.1; NM_001330564.1.
DR RefSeq; NP_001317494.1; NM_001330565.1. [Q5T200-1]
DR RefSeq; NP_001317495.1; NM_001330566.1. [Q5T200-1]
DR RefSeq; NP_001317496.1; NM_001330567.1. [Q5T200-1]
DR RefSeq; NP_055885.3; NM_015070.5. [Q5T200-2]
DR RefSeq; XP_005266369.1; XM_005266312.1.
DR AlphaFoldDB; Q5T200; -.
DR BioGRID; 116719; 112.
DR ComplexPortal; CPX-1605; WMM N6-adenosine-methyltransferase complex.
DR CORUM; Q5T200; -.
DR IntAct; Q5T200; 28.
DR MINT; Q5T200; -.
DR STRING; 9606.ENSP00000282007; -.
DR GlyGen; Q5T200; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5T200; -.
DR PhosphoSitePlus; Q5T200; -.
DR BioMuta; ZC3H13; -.
DR DMDM; 68052314; -.
DR EPD; Q5T200; -.
DR jPOST; Q5T200; -.
DR MassIVE; Q5T200; -.
DR MaxQB; Q5T200; -.
DR PaxDb; Q5T200; -.
DR PeptideAtlas; Q5T200; -.
DR PRIDE; Q5T200; -.
DR ProteomicsDB; 64298; -. [Q5T200-1]
DR ProteomicsDB; 64299; -. [Q5T200-2]
DR Antibodypedia; 23654; 112 antibodies from 22 providers.
DR DNASU; 23091; -.
DR Ensembl; ENST00000242848.8; ENSP00000242848.4; ENSG00000123200.17. [Q5T200-1]
DR Ensembl; ENST00000282007.7; ENSP00000282007.3; ENSG00000123200.17. [Q5T200-2]
DR GeneID; 23091; -.
DR KEGG; hsa:23091; -.
DR UCSC; uc001vas.3; human. [Q5T200-1]
DR CTD; 23091; -.
DR DisGeNET; 23091; -.
DR GeneCards; ZC3H13; -.
DR HGNC; HGNC:20368; ZC3H13.
DR HPA; ENSG00000123200; Low tissue specificity.
DR MIM; 616453; gene.
DR neXtProt; NX_Q5T200; -.
DR OpenTargets; ENSG00000123200; -.
DR PharmGKB; PA134907656; -.
DR VEuPathDB; HostDB:ENSG00000123200; -.
DR eggNOG; KOG1874; Eukaryota.
DR GeneTree; ENSGT00730000111163; -.
DR HOGENOM; CLU_003683_0_0_1; -.
DR InParanoid; Q5T200; -.
DR OrthoDB; 248688at2759; -.
DR PhylomeDB; Q5T200; -.
DR TreeFam; TF332670; -.
DR PathwayCommons; Q5T200; -.
DR SignaLink; Q5T200; -.
DR BioGRID-ORCS; 23091; 228 hits in 1085 CRISPR screens.
DR ChiTaRS; ZC3H13; human.
DR GeneWiki; ZC3H13; -.
DR GenomeRNAi; 23091; -.
DR Pharos; Q5T200; Tbio.
DR PRO; PR:Q5T200; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q5T200; protein.
DR Bgee; ENSG00000123200; Expressed in sural nerve and 212 other tissues.
DR ExpressionAtlas; Q5T200; baseline and differential.
DR Genevisible; Q5T200; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Developmental protein; Isopeptide bond;
KW Metal-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1668
FT /note="Zinc finger CCCH domain-containing protein 13"
FT /id="PRO_0000050778"
FT ZN_FING 36..64
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 645..789
FT /evidence="ECO:0000255"
FT COILED 1300..1366
FT /evidence="ECO:0000255"
FT COMPBIAS 13..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1081
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
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 263
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 354
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 364
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 848
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 877
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 882
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 943
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 986
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 993
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
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 1010
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 1033
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1170
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 1386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 194
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1440
FT /note="E -> EA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.1"
FT /id="VSP_027202"
FT VAR_SEQ 1558..1563
FT /note="DADNLF -> GSFILL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.1"
FT /id="VSP_014252"
FT VAR_SEQ 1564..1668
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.1"
FT /id="VSP_014253"
FT VARIANT 1429
FT /note="E -> D (in dbSNP:rs9534264)"
FT /evidence="ECO:0000269|PubMed:10048485,
FT ECO:0000269|PubMed:11230166, ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.1"
FT /id="VAR_022727"
FT CONFLICT 702..704
FT /note="EKE -> KAR (in Ref. 5; BAA74876)"
FT /evidence="ECO:0000305"
FT CONFLICT 967
FT /note="I -> K (in Ref. 3; CAD38544)"
FT /evidence="ECO:0000305"
FT MOD_RES Q5T200-2:1453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q5T200-2:1456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q5T200-2:1466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
SQ SEQUENCE 1668 AA; 196635 MW; B7E8118D3B5954D6 CRC64;
MSKIRRKVTV ENTKTISDST SRRPSVFERL GPSTGSTAET QCRNWLKTGN CLYGNTCRFV
HGPSPRGKGY SSNYRRSPER PTGDLRERMK NKRQDVDTEP QKRNTEESSS PVRKESSRGR
HREKEDIKIT KERTPESEEE NVEWETNRDD SDNGDINYDY VHELSLEMKR QKIQRELMKL
EQENMEKREE IIIKKEVSPE VVRSKLSPSP SLRKSSKSPK RKSSPKSSSA SKKDRKTSAV
SSPLLDQQRN SKTNQSKKKG PRTPSPPPPI PEDIALGKKY KEKYKVKDRI EEKTRDGKDR
GRDFERQREK RDKPRSTSPA GQHHSPISSR HHSSSSQSGS SIQRHSPSPR RKRTPSPSYQ
RTLTPPLRRS ASPYPSHSLS SPQRKQSPPR HRSPMREKGR HDHERTSQSH DRRHERREDT
RGKRDREKDS REEREYEQDQ SSSRDHRDDR EPRDGRDRRD ARDTRDRREL RDSRDMRDSR
EMRDYSRDTK ESRDPRDSRS TRDAHDYRDR EGRDTHRKED TYPEESRSYG RNHLREESSR
TEIRNESRNE SRSEIRNDRM GRSRGRVPEL PEKGSRGSRG SQIDSHSSNS NYHDSWETRS
SYPERDRYPE RDNRDQARDS SFERRHGERD RRDNRERDQR PSSPIRHQGR NDELERDERR
EERRVDRVDD RRDERARERD RERERDRERE RERERERDRE REKERELERE RARERERERE
KERDRERDRD RDHDRERERE RERDREKERE REREERERER ERERERERER ERERERARER
DKERERQRDW EDKDKGRDDR REKREEIRED RNPRDGHDER KSKKRYRNEG SPSPRQSPKR
RREHSPDSDA YNSGDDKNEK HRLLSQVVRP QESRSLSPSH LTEDRQGRWK EEDRKPERKE
SSRRYEEQEL KEKVSSVDKQ REQTEILESS RMRAQDIIGH HQSEDRETSD RAHDENKKKA
KIQKKPIKKK KEDDVGIERG NIETTSEDGQ VFSPKKGQKK KSIEKKRKKS KGDSDISDEE
AAQQSKKKRG PRTPPITTKE ELVEMCNGKN GILEDSQKKE DTAFSDWSDE DVPDRTEVTE
AEHTATATTP GSTPSPLSSL LPPPPPVATA TATTVPATLA ATTAAAATSF STSAITISTS
ATPTNTTNNT FANEDSHRKC HRTRVEKVET PHVTIEDAQH RKPMDQKRSS SLGSNRSNRS
HTSGRLRSPS NDSAHRSGDD QSGRKRVLHS GSRDREKTKS LEITGERKSR IDQLKRGEPS
RSTSSDRQDS RSHSSRRSSP ESDRQVHSRS GSFDSRDRLQ ERDRYEHDRE RERERRDTRQ
REWDRDADKD WPRNRDRDRL RERERERERD KRRDLDRERE RLISDSVERD RDRDRDRTFE
SSQIESVKRC EAKLEGEHER DLESTSRDSL ALDKERMDKD LGSVQGFEET NKSERTESLE
GDDESKLDDA HSLGSGAGEG YEPISDDELD EILAGDAEKR EDQQDEEKMP DPLDVIDVDW
SGLMPKHPKE PREPGAALLK FTPGAVMLRV GISKKLAGSE LFAKVKETCQ RLLEKPKDAD
NLFEHELGAL NMAALLRKEE RASLLSNLGP CCKALCFRRD SAIRKQLVKN EKGTIKQAYT
SAPMVDNELL RLSLRLFKRK TTCHAPGHEK TEDNKLSQSS IQQELCVS
