位置:首页 > 蛋白库 > TET3_HUMAN
TET3_HUMAN
ID   TET3_HUMAN              Reviewed;        1795 AA.
AC   O43151; A6NEI3; J3KNF3; K9JJH7; Q86Z24; Q8TBM9;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2019, sequence version 4.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Methylcytosine dioxygenase TET3 {ECO:0000305};
DE            EC=1.14.11.n2 {ECO:0000269|PubMed:31928709};
GN   Name=TET3 {ECO:0000312|HGNC:HGNC:28313}; Synonyms=KIAA0401;
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] {ECO:0000312|EMBL:ADU77107.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND FUNCTION.
RX   PubMed=23217707; DOI=10.1016/j.cell.2012.11.014;
RA   Xu Y., Xu C., Kato A., Tempel W., Abreu J.G., Bian C., Hu Y., Hu D.,
RA   Zhao B., Cerovina T., Diao J., Wu F., He H.H., Cui Q., Clark E., Ma C.,
RA   Barbara A., Veenstra G.J.C., Xu G., Kaiser U.B., Liu X.S., Sugrue S.P.,
RA   He X., Min J., Kato Y., Shi Y.G.;
RT   "Tet3 CXXC domain and dioxygenase activity cooperatively regulate key genes
RT   for Xenopus eye and neural development.";
RL   Cell 151:1200-1213(2012).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 421-1795 (ISOFORM 3).
RA   Kim N.-S., Shon H.-Y., Oh J.-H., Lee J.-Y., Kim J.-M., Hahn Y., Kim Y.;
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 849-1795 (ISOFORM 4).
RC   TISSUE=Duodenum;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1336-1795 (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA   Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT   new cDNA clones from brain which code for large proteins in vitro.";
RL   DNA Res. 4:307-313(1997).
RN   [6]
RP   IDENTIFICATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12646957; DOI=10.1038/sj.leu.2402834;
RA   Lorsbach R.B., Moore J., Mathew S., Raimondi S.C., Mukatira S.T.,
RA   Downing J.R.;
RT   "TET1, a member of a novel protein family, is fused to MLL in acute myeloid
RT   leukemia containing the t(10;11)(q22;q23).";
RL   Leukemia 17:637-641(2003).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH HCFC1 AND OGT.
RX   PubMed=23353889; DOI=10.1038/emboj.2012.357;
RA   Deplus R., Delatte B., Schwinn M.K., Defrance M., Mendez J., Murphy N.,
RA   Dawson M.A., Volkmar M., Putmans P., Calonne E., Shih A.H., Levine R.L.,
RA   Bernard O., Mercher T., Solary E., Urh M., Daniels D.L., Fuks F.;
RT   "TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and
RT   SET1/COMPASS.";
RL   EMBO J. 32:645-655(2013).
RN   [8]
RP   INTERACTION WITH OGT.
RX   PubMed=23222540; DOI=10.1038/nature11742;
RA   Chen Q., Chen Y., Bian C., Fujiki R., Yu X.;
RT   "TET2 promotes histone O-GlcNAcylation during gene transcription.";
RL   Nature 493:561-564(2013).
RN   [9]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1397, 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   [10]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-491; LYS-1188; LYS-1219; LYS-1397
RP   AND LYS-1561, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [11] {ECO:0007744|PDB:4Z3C}
RP   X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 49-98 IN COMPLEX WITH DNA,
RP   FUNCTION, DOMAIN CXXC-TYPE ZINC-FINGER, AND ZINC-BINDING.
RX   PubMed=29276034; DOI=10.1016/j.str.2017.11.022;
RA   Xu C., Liu K., Lei M., Yang A., Li Y., Hughes T.R., Min J.;
RT   "DNA Sequence Recognition of Human CXXC Domains and Their Structural
RT   Determinants.";
RL   Structure 26:85-95.e3(2018).
RN   [12]
RP   INVOLVEMENT IN BEFAHRS, VARIANTS BEFAHRS CYS-752; MET-851; LEU-908;
RP   CYS-1072; THR-1076; MET-1089; LEU-1677 AND 1695-GLN--ILE-1795 DEL,
RP   CHARACTERIZATION OF VARIANTS BEFAHRS CYS-752; LEU-908; CYS-1072; THR-1076
RP   AND MET-1089, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP   1077-HIS--ASP-1079.
RX   PubMed=31928709; DOI=10.1016/j.ajhg.2019.12.007;
RA   Beck D.B., Petracovici A., He C., Moore H.W., Louie R.J., Ansar M.,
RA   Douzgou S., Sithambaram S., Cottrell T., Santos-Cortez R.L.P.,
RA   Prijoles E.J., Bend R., Keren B., Mignot C., Nougues M.C., Ounap K.,
RA   Reimand T., Pajusalu S., Zahid M., Saqib M.A.N., Buratti J., Seaby E.G.,
RA   McWalter K., Telegrafi A., Baldridge D., Shinawi M., Leal S.M.,
RA   Schaefer G.B., Stevenson R.E., Banka S., Bonasio R., Fahrner J.A.;
RT   "Delineation of a Human Mendelian Disorder of the DNA Demethylation
RT   Machinery: TET3 Deficiency.";
RL   Am. J. Hum. Genet. 106:234-245(2020).
CC   -!- FUNCTION: Dioxygenase that catalyzes the conversion of the modified
CC       genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC)
CC       and plays a key role in epigenetic chromatin reprogramming in the
CC       zygote following fertilization (PubMed:31928709). Also mediates
CC       subsequent conversion of 5hmC into 5-formylcytosine (5fC), and
CC       conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into
CC       5hmC, 5fC and 5caC probably constitutes the first step in cytosine
CC       demethylation (By similarity). Selectively binds to the promoter region
CC       of target genes and contributes to regulate the expression of numerous
CC       developmental genes (PubMed:23217707). In zygotes, DNA demethylation
CC       occurs selectively in the paternal pronucleus before the first cell
CC       division, while the adjacent maternal pronucleus and certain
CC       paternally-imprinted loci are protected from this process. Participates
CC       in DNA demethylation in the paternal pronucleus by mediating conversion
CC       of 5mC into 5hmC, 5fC and 5caC. Does not mediate DNA demethylation of
CC       maternal pronucleus because of the presence of DPPA3/PGC7 on maternal
CC       chromatin that prevents TET3-binding to chromatin (By similarity). In
CC       addition to its role in DNA demethylation, also involved in the
CC       recruitment of the O-GlcNAc transferase OGT to CpG-rich transcription
CC       start sites of active genes, thereby promoting histone H2B
CC       GlcNAcylation by OGT (PubMed:23353889). Binds preferentially to DNA
CC       containing cytidine-phosphate-guanosine (CpG) dinucleotides over CpH
CC       (H=A, T, and C), hemimethylated-CpG and hemimethylated-hydroxymethyl-
CC       CpG (PubMed:29276034). {ECO:0000250|UniProtKB:Q8BG87,
CC       ECO:0000269|PubMed:23217707, ECO:0000269|PubMed:23353889,
CC       ECO:0000269|PubMed:29276034, ECO:0000269|PubMed:31928709}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + a 5-methyl-2'-deoxycytidine in DNA + O2 = a
CC         5-hydroxymethyl-2'-deoxycytidine in DNA + CO2 + succinate;
CC         Xref=Rhea:RHEA:52636, Rhea:RHEA-COMP:11370, Rhea:RHEA-COMP:13315,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:85454, ChEBI:CHEBI:136731;
CC         EC=1.14.11.n2; Evidence={ECO:0000269|PubMed:31928709};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52637;
CC         Evidence={ECO:0000305|PubMed:31928709};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q6N021};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6N021};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q6N021};
CC       Note=The zinc ions have a structural role.
CC       {ECO:0000250|UniProtKB:Q6N021};
CC   -!- SUBUNIT: Interacts with HCFC1 and OGT. {ECO:0000269|PubMed:23222540,
CC       ECO:0000269|PubMed:23353889}.
CC   -!- INTERACTION:
CC       O43151; O15294: OGT; NbExp=7; IntAct=EBI-2831148, EBI-539828;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8BG87}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8BG87}. Chromosome
CC       {ECO:0000250|UniProtKB:Q8BG87}. Note=At the zygotic stage, localizes in
CC       the male pronucleus, while it localizes to the cytoplasm at other
CC       preimplantation stages. Binds to the promoter of target genes, close to
CC       the transcription start site. {ECO:0000250|UniProtKB:Q8BG87}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=4;
CC         IsoId=O43151-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O43151-2; Sequence=VSP_021628;
CC       Name=3;
CC         IsoId=O43151-3; Sequence=VSP_034192;
CC   -!- TISSUE SPECIFICITY: Expressed in colon, muscle, adrenal gland and
CC       peripheral blood lymphocytes. {ECO:0000269|PubMed:12646957}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in fetal brain but not adult brain.
CC       {ECO:0000269|PubMed:12646957}.
CC   -!- DOMAIN: The CXXC zinc finger mediates binding to CpG-DNA
CC       (PubMed:29276034). It mediates binding to DNA sequences containing
CC       unmethylated cytosine or 5-carboxylcytosine in 5'-CCG-3' DNA sequence
CC       motifs (By similarity). {ECO:0000250|UniProtKB:Q8BG87,
CC       ECO:0000269|PubMed:29276034}.
CC   -!- DISEASE: Beck-Fahrner syndrome (BEFAHRS) [MIM:618798]: A developmental
CC       disorder characterized by mild to severe intellectual disability,
CC       global developmental delay, hypotonia, autistic traits, movement
CC       disorders, growth abnormalities including overgrowth or poor growth,
CC       and facial dysmorphism. Both autosomal dominant and autosomal recessive
CC       inheritance has been reported. {ECO:0000269|PubMed:31928709}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the TET family. {ECO:0000305}.
CC   -!- CAUTION: Subsequent steps in cytosine demethylation are subject to
CC       discussion. According to a first model cytosine demethylation occurs
CC       through deamination of 5hmC into 5-hydroxymethyluracil (5hmU) and
CC       subsequent replacement by unmethylated cytosine by the base excision
CC       repair system. According to another model, cytosine demethylation is
CC       rather mediated via conversion of 5hmC into 5fC and 5caC, followed by
CC       excision by TDG. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH22243.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAO33386.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAX93057.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HQ220209; ADU77107.1; -; mRNA.
DR   EMBL; AC110801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC073263; AAX93057.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC073046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF466365; AAO33386.1; ALT_INIT; mRNA.
DR   EMBL; BC022243; AAH22243.1; ALT_INIT; mRNA.
DR   EMBL; AB007861; BAA23697.1; -; mRNA.
DR   CCDS; CCDS46339.2; -. [O43151-1]
DR   RefSeq; NP_001274420.1; NM_001287491.1. [O43151-1]
DR   RefSeq; XP_005264244.1; XM_005264187.3.
DR   PDB; 4Z3C; X-ray; 1.57 A; C=49-98.
DR   PDBsum; 4Z3C; -.
DR   AlphaFoldDB; O43151; -.
DR   SMR; O43151; -.
DR   BioGRID; 128327; 18.
DR   IntAct; O43151; 32.
DR   MINT; O43151; -.
DR   STRING; 9606.ENSP00000386869; -.
DR   GlyGen; O43151; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O43151; -.
DR   PhosphoSitePlus; O43151; -.
DR   BioMuta; TET3; -.
DR   jPOST; O43151; -.
DR   MassIVE; O43151; -.
DR   MaxQB; O43151; -.
DR   PaxDb; O43151; -.
DR   PeptideAtlas; O43151; -.
DR   PRIDE; O43151; -.
DR   ProteomicsDB; 48772; -. [O43151-1]
DR   ProteomicsDB; 48773; -. [O43151-2]
DR   ProteomicsDB; 48774; -. [O43151-3]
DR   Antibodypedia; 31410; 380 antibodies from 30 providers.
DR   DNASU; 200424; -.
DR   Ensembl; ENST00000409262.8; ENSP00000386869.3; ENSG00000187605.16. [O43151-1]
DR   GeneID; 200424; -.
DR   KEGG; hsa:200424; -.
DR   MANE-Select; ENST00000409262.8; ENSP00000386869.3; NM_001287491.2; NP_001274420.1.
DR   UCSC; uc002skb.6; human. [O43151-1]
DR   UCSC; uc061kse.1; human.
DR   CTD; 200424; -.
DR   DisGeNET; 200424; -.
DR   GeneCards; TET3; -.
DR   HGNC; HGNC:28313; TET3.
DR   HPA; ENSG00000187605; Tissue enhanced (bone).
DR   MalaCards; TET3; -.
DR   MIM; 613555; gene.
DR   MIM; 618798; phenotype.
DR   neXtProt; NX_O43151; -.
DR   OpenTargets; ENSG00000187605; -.
DR   PharmGKB; PA162405645; -.
DR   VEuPathDB; HostDB:ENSG00000187605; -.
DR   eggNOG; ENOG502QURD; Eukaryota.
DR   GeneTree; ENSGT00940000157631; -.
DR   HOGENOM; CLU_001618_3_0_1; -.
DR   InParanoid; O43151; -.
DR   OMA; PDSQWGL; -.
DR   PhylomeDB; O43151; -.
DR   TreeFam; TF342373; -.
DR   PathwayCommons; O43151; -.
DR   Reactome; R-HSA-5221030; TET1,2,3 and TDG demethylate DNA.
DR   SignaLink; O43151; -.
DR   SIGNOR; O43151; -.
DR   BioGRID-ORCS; 200424; 16 hits in 1091 CRISPR screens.
DR   ChiTaRS; TET3; human.
DR   GenomeRNAi; 200424; -.
DR   Pharos; O43151; Tbio.
DR   PRO; PR:O43151; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; O43151; protein.
DR   Bgee; ENSG00000187605; Expressed in oocyte and 183 other tissues.
DR   ExpressionAtlas; O43151; baseline and differential.
DR   Genevisible; O43151; HS.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0001939; C:female pronucleus; IEA:Ensembl.
DR   GO; GO:0001940; C:male pronucleus; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
DR   GO; GO:0070579; F:methylcytosine dioxygenase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0006211; P:5-methylcytosine catabolic process; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0080111; P:DNA demethylation; ISS:UniProtKB.
DR   GO; GO:0044727; P:DNA demethylation of male pronucleus; ISS:UniProtKB.
DR   GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
DR   GO; GO:0070989; P:oxidative demethylation; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IMP:UniProtKB.
DR   InterPro; IPR024779; 2OGFeDO_noxygenase_dom.
DR   InterPro; IPR040175; TET1/2/3.
DR   InterPro; IPR002857; Znf_CXXC.
DR   PANTHER; PTHR23358; PTHR23358; 1.
DR   Pfam; PF12851; Tet_JBP; 1.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   SMART; SM01333; Tet_JBP; 1.
DR   PROSITE; PS51058; ZF_CXXC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromatin regulator; Chromosome;
KW   Cytoplasm; Developmental protein; Dioxygenase; Disease variant;
KW   DNA-binding; Intellectual disability; Iron; Isopeptide bond; Metal-binding;
KW   Nucleus; Oxidoreductase; Reference proteome; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1795
FT                   /note="Methylcytosine dioxygenase TET3"
FT                   /id="PRO_0000050750"
FT   ZN_FING         50..90
FT                   /note="CXXC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT                   ECO:0000269|PubMed:29276034"
FT   REGION          142..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          985..998
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   REGION          1345..1366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1395..1430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1608..1638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..570
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..666
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..694
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT                   ECO:0000269|PubMed:29276034, ECO:0007744|PDB:4Z3C"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT                   ECO:0000269|PubMed:29276034, ECO:0007744|PDB:4Z3C"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT                   ECO:0000269|PubMed:29276034, ECO:0007744|PDB:4Z3C"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT                   ECO:0000269|PubMed:29276034, ECO:0007744|PDB:4Z3C"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT                   ECO:0000269|PubMed:29276034, ECO:0007744|PDB:4Z3C"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT                   ECO:0000269|PubMed:29276034, ECO:0007744|PDB:4Z3C"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT                   ECO:0000269|PubMed:29276034, ECO:0007744|PDB:4Z3C"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT                   ECO:0000269|PubMed:29276034, ECO:0007744|PDB:4Z3C"
FT   BINDING         828
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         830
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         888
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         914
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         916
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         956
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         966
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         968
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         984
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         993
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         1053
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         1069
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         1075
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         1077
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         1079
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         1082
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         1111
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         1673
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         1688..1690
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         1694..1696
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   BINDING         1704
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q6N021"
FT   CROSSLNK        491
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1188
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1219
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1397
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1561
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         863..1795
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_034192"
FT   VAR_SEQ         1575..1690
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9455477"
FT                   /id="VSP_021628"
FT   VARIANT         712
FT                   /note="R -> Q (in dbSNP:rs57955681)"
FT                   /id="VAR_062235"
FT   VARIANT         752
FT                   /note="R -> C (in BEFAHRS; unknown pathological
FT                   significance; no effect on methylcytosine dioxygenase
FT                   activity; dbSNP:rs534089911)"
FT                   /evidence="ECO:0000269|PubMed:31928709"
FT                   /id="VAR_083831"
FT   VARIANT         851
FT                   /note="T -> M (in BEFAHRS; dbSNP:rs1573856970)"
FT                   /evidence="ECO:0000269|PubMed:31928709"
FT                   /id="VAR_083832"
FT   VARIANT         908
FT                   /note="V -> L (in BEFAHRS; decreases methylcytosine
FT                   dioxygenase activity; dbSNP:rs1227643933)"
FT                   /evidence="ECO:0000269|PubMed:31928709"
FT                   /id="VAR_083833"
FT   VARIANT         1072
FT                   /note="F -> C (in BEFAHRS; decreases methylcytosine
FT                   dioxygenase activity; dbSNP:rs1573906351)"
FT                   /evidence="ECO:0000269|PubMed:31928709"
FT                   /id="VAR_083834"
FT   VARIANT         1076
FT                   /note="A -> T (in BEFAHRS; decreases methylcytosine
FT                   dioxygenase activity; dbSNP:rs1573906389)"
FT                   /evidence="ECO:0000269|PubMed:31928709"
FT                   /id="VAR_083835"
FT   VARIANT         1089
FT                   /note="V -> M (in BEFAHRS; decreases methylcytosine
FT                   dioxygenase activity; dbSNP:rs1174857008)"
FT                   /evidence="ECO:0000269|PubMed:31928709"
FT                   /id="VAR_083836"
FT   VARIANT         1677
FT                   /note="P -> L (in BEFAHRS)"
FT                   /evidence="ECO:0000269|PubMed:31928709"
FT                   /id="VAR_083837"
FT   VARIANT         1695..1795
FT                   /note="Missing (in BEFAHRS)"
FT                   /evidence="ECO:0000269|PubMed:31928709"
FT                   /id="VAR_083838"
FT   MUTAGEN         1077..1079
FT                   /note="HKD->YKA: Abolishes methylcytosine dioxygenase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:31928709"
FT   HELIX           61..64
FT                   /evidence="ECO:0007829|PDB:4Z3C"
FT   STRAND          70..72
FT                   /evidence="ECO:0007829|PDB:4Z3C"
FT   HELIX           73..76
FT                   /evidence="ECO:0007829|PDB:4Z3C"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:4Z3C"
FT   TURN            85..87
FT                   /evidence="ECO:0007829|PDB:4Z3C"
FT   TURN            90..93
FT                   /evidence="ECO:0007829|PDB:4Z3C"
SQ   SEQUENCE   1795 AA;  193705 MW;  7D1041E2C45C4F18 CRC64;
     MSQFQVPLAV QPDLPGLYDF PQRQVMVGSF PGSGLSMAGS ESQLRGGGDG RKKRKRCGTC
     EPCRRLENCG ACTSCTNRRT HQICKLRKCE VLKKKVGLLK EVEIKAGEGA GPWGQGAAVK
     TGSELSPVDG PVPGQMDSGP VYHGDSRQLS ASGVPVNGAR EPAGPSLLGT GGPWRVDQKP
     DWEAAPGPAH TARLEDAHDL VAFSAVAEAV SSYGALSTRL YETFNREMSR EAGNNSRGPR
     PGPEGCSAGS EDLDTLQTAL ALARHGMKPP NCNCDGPECP DYLEWLEGKI KSVVMEGGEE
     RPRLPGPLPP GEAGLPAPST RPLLSSEVPQ ISPQEGLPLS QSALSIAKEK NISLQTAIAI
     EALTQLSSAL PQPSHSTPQA SCPLPEALSP PAPFRSPQSY LRAPSWPVVP PEEHSSFAPD
     SSAFPPATPR TEFPEAWGTD TPPATPRSSW PMPRPSPDPM AELEQLLGSA SDYIQSVFKR
     PEALPTKPKV KVEAPSSSPA PAPSPVLQRE APTPSSEPDT HQKAQTALQQ HLHHKRSLFL
     EQVHDTSFPA PSEPSAPGWW PPPSSPVPRL PDRPPKEKKK KLPTPAGGPV GTEKAAPGIK
     PSVRKPIQIK KSRPREAQPL FPPVRQIVLE GLRSPASQEV QAHPPAPLPA SQGSAVPLPP
     EPSLALFAPS PSRDSLLPPT QEMRSPSPMT ALQPGSTGPL PPADDKLEEL IRQFEAEFGD
     SFGLPGPPSV PIQDPENQQT CLPAPESPFA TRSPKQIKIE SSGAVTVLST TCFHSEEGGQ
     EATPTKAENP LTPTLSGFLE SPLKYLDTPT KSLLDTPAKR AQAEFPTCDC VEQIVEKDEG
     PYYTHLGSGP TVASIRELME ERYGEKGKAI RIEKVIYTGK EGKSSRGCPI AKWVIRRHTL
     EEKLLCLVRH RAGHHCQNAV IVILILAWEG IPRSLGDTLY QELTDTLRKY GNPTSRRCGL
     NDDRTCACQG KDPNTCGASF SFGCSWSMYF NGCKYARSKT PRKFRLAGDN PKEEEVLRKS
     FQDLATEVAP LYKRLAPQAY QNQVTNEEIA IDCRLGLKEG RPFAGVTACM DFCAHAHKDQ
     HNLYNGCTVV CTLTKEDNRC VGKIPEDEQL HVLPLYKMAN TDEFGSEENQ NAKVGSGAIQ
     VLTAFPREVR RLPEPAKSCR QRQLEARKAA AEKKKIQKEK LSTPEKIKQE ALELAGITSD
     PGLSLKGGLS QQGLKPSLKV EPQNHFSSFK YSGNAVVESY SVLGNCRPSD PYSMNSVYSY
     HSYYAQPSLT SVNGFHSKYA LPSFSYYGFP SSNPVFPSQF LGPGAWGHSG SSGSFEKKPD
     LHALHNSLSP AYGGAEFAEL PSQAVPTDAH HPTPHHQQPA YPGPKEYLLP KAPLLHSVSR
     DPSPFAQSSN CYNRSIKQEP VDPLTQAEPV PRDAGKMGKT PLSEVSQNGG PSHLWGQYSG
     GPSMSPKRTN GVGGSWGVFS SGESPAIVPD KLSSFGASCL APSHFTDGQW GLFPGEGQQA
     ASHSGGRLRG KPWSPCKFGN STSALAGPSL TEKPWALGAG DFNSALKGSP GFQDKLWNPM
     KGEEGRIPAA GASQLDRAWQ SFGLPLGSSE KLFGALKSEE KLWDPFSLEE GPAEEPPSKG
     AVKEEKGGGG AEEEEEELWS DSEHNFLDEN IGGVAVAPAH GSILIECARR ELHATTPLKK
     PNRCHPTRIS LVFYQHKNLN QPNHGLALWE AKMKQLAERA RARQEEAARL GLGQQEAKLY
     GKKRKWGGTV VAEPQQKEKK GVVPTRQALA VPTDSAVTVS SYAYTKVTGP YSRWI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024